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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Phocaeicola dorei and UniProt Accession A0A076IP90

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.19 arginine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Phocaeicola dorei
UNIPROT: A0A076IP90
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Word Map
The taxonomic range for the selected organisms is: Phocaeicola dorei
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, atadc2, ptadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADC
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-
-
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ARGDC
-
-
-
-
bADC
-
-
-
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Biosynthetic arginine decarboxylase
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-
-
-
dADC
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-
-
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Decarboxylase, arginine
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-
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L-Arginine decarboxylase
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-
-
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Synthetic arginine decarboxylase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-77-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium. Disruption of polyamine biosynthetic genes including speA leads to delayed growth in various bacterial species. In contrast to the presence of intracellular spermidine as the sole polyamine in wild-type strain JCM 13471 and DELTA tdk mutant strain MS416, spermidine is barely detected in MS531. The remaining intracellular spermidine level in MS531 may be attributable to the spermidine import from polyamine-reduced medium via a predicted ATP-binding cassette transporter of spermidine, PotABCD
physiological function
gene speA encodes a putative arginine decarboxylase, an enzyme necessary for spermidine biosynthesis in cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A076IP90_9BACT
630
0
71488
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakanaka, M.; Sugiyama, Y.; Nara, M.; Kitakata, A.; Kurihara, S.
Functional analysis of arginine decarboxylase gene speA of Bacteroides dorei by markerless gene deletion
FEMS Microbiol. Lett.
365
fny003
2018
Phocaeicola dorei (A0A076IP90), Phocaeicola dorei, Phocaeicola dorei JCM 13471 (A0A076IP90)
Manually annotated by BRENDA team