1.97.1.1: chlorate reductase
This is an abbreviated version!
For detailed information about chlorate reductase, go to the full flat file.
Word Map on EC 1.97.1.1
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1.97.1.1
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nitrate
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perchlorate-reducing
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dissimilatory
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chlorate-reducing
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dechloromonas
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dechloratans
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ideonella
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denitrification
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pantotrophus
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hoqno
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menaquinol
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azospira
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bromate
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biotechnology
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stigmatellin
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degradation
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analysis
- 1.97.1.1
- nitrate
-
perchlorate-reducing
-
dissimilatory
-
chlorate-reducing
- dechloromonas
- dechloratans
-
ideonella
-
denitrification
- pantotrophus
-
hoqno
- menaquinol
- azospira
- bromate
- biotechnology
- stigmatellin
- degradation
- analysis
Reaction
Synonyms
chlorate reductase, chlorate reductase C, clr, ClrA, NarGH, PCR, perchlorate reductase, reductase, chlorate
ECTree
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General Information
General Information on EC 1.97.1.1 - chlorate reductase
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evolution
physiological function
additional information
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the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and a subfamily that participates in a key step of the chlorine cycle
evolution
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the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and a subfamily that participates in a key step of the chlorine cycle
evolution
-
the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and group 3 ClrA proteins subfamily that participates in a key step of the chlorine cycle. The Rhodoplanes roseus chlorate reductase has other substantial differences to previously characterized chlorate reductases
evolution
Rhodoplanes elegans DSM 11970
-
the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and a subfamily that participates in a key step of the chlorine cycle
-
evolution
Rhodoplanes roseus DSM 5909
-
the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and group 3 ClrA proteins subfamily that participates in a key step of the chlorine cycle. The Rhodoplanes roseus chlorate reductase has other substantial differences to previously characterized chlorate reductases
-
evolution
Rhodoplanes piscinae DSM 19946
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the enzyme belongs to the dimethylsulfoxide (DMSO) reductase family, and a subfamily that participates in a key step of the chlorine cycle
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P60068; P60069; P60000
a soluble periplasmic c-type cytochrome from Ideonella dechloratans donates electrons to Clr in vitro
physiological function
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the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
Stutzerimonas chloritidismutans
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the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
Acinetobacter thermotoleranticus
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the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
Dechlorospirillum anomalous
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the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
Vibrio dechloraticans
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment.Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
physiological function
-
the enzyme participates in a key step of the chlorine cycle, perchlorate and chlorate being used as respiratory electron acceptors
physiological function
-
the enzyme participates in a key step of the chlorine cycle, perchlorate is used as respiratory electron acceptor
physiological function
-
the enzyme participates in a key step of the chlorine cycle, perchlorate is used as respiratory electron acceptors
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Wolinella succinogenes HAP-1
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the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Moorella humiferrea 64-FGQ
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the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Moorella glycerini JW/AS-Y6
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the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment.Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Stutzerimonas chloritidismutans AW1
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
Rhodoplanes elegans DSM 11970
-
the enzyme participates in a key step of the chlorine cycle, perchlorate is used as respiratory electron acceptor
-
physiological function
Azospirillum lipoferum VPI Sp 59b
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Vibrio dechloraticans Cuznesove B-1168
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Stutzerimonas chloritidismutans ASK1
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
Dechlorospirillum anomalous 7JB116
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Azospira sp. Perc1ace
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Rhodoplanes roseus DSM 5909
-
the enzyme participates in a key step of the chlorine cycle, perchlorate and chlorate being used as respiratory electron acceptors
-
physiological function
Rhodoplanes piscinae DSM 19946
-
the enzyme participates in a key step of the chlorine cycle, perchlorate is used as respiratory electron acceptors
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment.Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
Sporomusa ovata An4
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
physiological function
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment
-
physiological function
Moorella stamsii E3-O
-
the reduction of chlorate is one alternative to derive energy in an anoxic environment. Perchlorate reductases are periplasmic heterodimers of PcrA and PcrB, carrying a Mo-bis (pyranopterin guanine dinucleotide) cofactor and iron-sulfur clusters. Electrons are transferred from a membrane-associated, proton pumping c cytochrome of the NapC/NrfH family to PcrA. PcrC, a soluble multiheme c cytochrome, is predicted to participate in electron transport reactions
-
P60068; P60069; P60000
the genes for the enzymes chlorate reductase (clrABDC) and chlorite dismutase, necessary for chlorate metabolism and probably acquired by lateral gene transfer, are located in a gene cluster that also includes other genes potentially important for chlorate metabolism. Among those are a gene for cytochrome c (cyc) whose gene product may serve as an electron carrier during chlorate reduction, a cofactor biosynthesis gene (mobB) and a predicted transcriptional regulator (arsR)
additional information
-
the genes for the enzymes chlorate reductase (clrABDC) and chlorite dismutase, necessary for chlorate metabolism and probably acquired by lateral gene transfer, are located in a gene cluster that also includes other genes potentially important for chlorate metabolism. Among those are a gene for cytochrome c (cyc) whose gene product may serve as an electron carrier during chlorate reduction, a cofactor biosynthesis gene (mobB) and a predicted transcriptional regulator (arsR)