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EC Tree
IUBMB Comments This radical AdoMet enzyme participates in a heme biosynthesis pathway found in archaea and sulfur-reducing bacteria. cf. EC 1.3.98.5, hydrogen peroxide-dependent heme synthase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ahbD , heme b synthase,
Mbar_A1458 , SAM-dependent heme synthase,
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SAM-dependent heme synthase
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ahbD
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Mbar_A1458
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Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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Fe-coproporphyrin III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)
This radical AdoMet enzyme participates in a heme biosynthesis pathway found in archaea and sulfur-reducing bacteria. cf. EC 1.3.98.5, hydrogen peroxide-dependent heme synthase.
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coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
Cu-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
Zn-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Cu-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Cu-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
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?
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
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?
Zn-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Zn-coproporphyrin III + 2 S-adenosyl-L-methionine
? + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
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Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine
protoheme + 2 CO2 + 2 5'-deoxyadenosine + 2 L-methionine
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?
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
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?
Fe-coproporphyrin III + S-adenosyl-L-methionine
protoheme + CO2 + 5'-deoxyadenosine + L-methionine
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?
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[4Fe-4S]-center
the enzyme contains two [4Fe-4S] clusters
4Fe-4S-center
isolated protein forms a brown solution with a broad peak between 340 to 400 nm in the UV-visible spectrum
4Fe-4S-center
presence of 2 [4Fe-4S]-clusters. The second cluster is not required for substrate binding and formation of the substrate radical but is involved in a late step of AhbD catalysis, most likely in electron transfer from the reaction intermediate to a final electron acceptor. The central iron ion of the porphyrin substrate also participates in the electron transfer from the reaction intermediate to the auxiliary [4Fe-4S] cluster
4Fe-4S-center
presence of two [4Fe-4S] clusters
S-adenosyl-L-methionine
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S-adenosyl-L-methionine
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Fe2+
contains 8.5 mol iron per mol enzyme
Iron
presence of 8.5 mol iron per mol AhbD and 5.1 mol sulfide per mol AhbD
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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AHBD_DESAG
Desulfovibrio alaskensis (strain ATCC BAA 1058 / DSM 17464 / G20)
388
0
43266
Swiss-Prot
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AHBD_DESVH
Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough)
367
0
40909
Swiss-Prot
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AHBD_METBF
Methanosarcina barkeri (strain Fusaro / DSM 804)
349
0
38631
Swiss-Prot
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A0A4P7UJ54_DESDE
407
0
44246
TrEMBL
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C19A/C23A
loss of the N-terminal 4Fe-4S-center, mutant is unable to cleave SAM
C321A/C324A
loss of the C-terminal 4Fe-4S-center, mutant cleaves SAM comparable to the wild-type enzyme
C19A/C23A
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loss of the N-terminal 4Fe-4S-center, mutant is unable to cleave SAM
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C321A/C324A
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loss of the C-terminal 4Fe-4S-center, mutant cleaves SAM comparable to the wild-type enzyme
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Blue Sepharose column chromatography and Mono Q column chromatography
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expresssion in Escherichia coli
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Kühner, M.; Haufschildt, K.; Neumann, A.; Storbeck, S.; Streif, J.; Layer, G.
The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri
Archaea
2014
327637
2014
Methanosarcina barkeri, Methanosarcina barkeri (Q46CH7), Methanosarcina barkeri DSM 804 (Q46CH7)
brenda
Bali, S.; Lawrence, A.; Lobo, S.; Saraiva, L.; Golding, B.; Palmer, D.; Howard, M.; Ferguson, S.; Warren, M.
Molecular hijacking of siroheme for the synthesis of heme and d1 heme
Proc. Natl. Acad. Sci. USA
108
18260-18265
2011
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans (A0A4P7UJ54)
brenda
Kuehner, M.; Schweyen, P.; Hoffmann, M.; Ramos, J.; Reijerse, E.; Lubitz, W.; Broering, M.; Layer, G.
The auxiliary [4Fe-4S] cluster of the radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer
Chem. Sci.
7
4633-4643
2016
Methanosarcina barkeri (Q46CH7), Methanosarcina barkeri DSM 804 (Q46CH7)
brenda
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History
Enzyme Nomenclature
1.3.98.6 AdoMet-dependent heme synthase
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