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Entry
EC 1.2.7.4                  Enzyme                                 

Name
anaerobic carbon-monoxide dehydrogenase;
Ni-CODH;
carbon-monoxide dehydrogenase (ferredoxin)
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy
Sysname
carbon-monoxide,water:ferredoxin oxidoreductase
Reaction(IUBMB)
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+ [RN:R07157]
Reaction(KEGG)
R07157;
(other) R08034 R09317
Show
Substrate
CO [CPD:C00237];
H2O [CPD:C00001];
oxidized ferredoxin [CPD:C00139]
Product
CO2 [CPD:C00011];
reduced ferredoxin [CPD:C00138];
H+ [CPD:C00080]
Comment
This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase.
History
EC 1.2.7.4 created 2003 (EC 1.2.99.2 created 1982, modified 1990, modified 2003, incorporated 2015), modified 2016
Pathway
Nitrotoluene degradation
Methane metabolism
Carbon fixation pathways in prokaryotes
Microbial metabolism in diverse environments
Orthology
K00192  
acetyl-CoA decarbonylase/synthase complex subunit alpha
K00198  
anaerobic carbon-monoxide dehydrogenase catalytic subunit
Genes
CAMA: 
AVN: 
AVL: 
AVD: 
ACX: 
Achr_4450(cooS)
TMB: 
CCV: 
CCO: 
CGRA: 
GSU: 
GSU2098(cooS)
GME: 
Gmet_1902(cooS)
GUR: 
GBM: 
Gbem_0072(cooS-2) Gbem_1736(cooS-1)
GEO: 
Geob_0362(cooS-1) Geob_1046(cooS-2)
GPI: 
GSB: 
PCA: 
Pcar_0057(cooS-2) Pcar_0888(cooS-1)
PEF: 
DES: 
DEU: 
DVU: 
DVU2098(cooS)
DVL: 
DVM: 
DVG: 
DDE: 
DDS: 
DDN: 
DMA: 
DSA: 
DAF: 
DAS: 
DPI: 
BN4_11760(cooS) BN4_20190(cooS)
DEJ: 
DBA: 
DRT: 
DAK: 
DSF: 
DOL: 
DML: 
Dmul_09300(cooS1) Dmul_19100(cooS2) Dmul_30840(cdhA)
DAL: 
DAT: 
HRM2_16670(cdhA) HRM2_41010(cdh1) HRM2_43440(cdh2)
DTO: 
DAO: 
DTI: 
SFU: 
DBR: 
RPC: 
RRU: 
RRF: 
GMC: 
GTH: 
PTL: 
PDU: 
CAC: 
CAE: 
CAY: 
CTC: 
CTET: 
CNO: 
CBO: 
CBA: 
CBH: 
CBY: 
CBL: 
CBB: 
CBI: 
CBN: 
CbC4_2402(cooS)
CBF: 
CBM: 
CBJ: 
CBE: 
CBZ: 
CBEI: 
CKL: 
CKR: 
CLJ: 
CLJU_c09110(cooS1) CLJU_c17910(cooS2) CLJU_c37670(codH)
CCB: 
CLB: 
CSR: 
Cspa_c16740(cooS1) Cspa_c21120(cooS2) Cspa_c57670(cooS3)
CPAS: 
CPAT: 
CPAE: 
CSB: 
CLSA_c11710(cooS1) CLSA_c14830(cooS2)
CAH: 
CLT: 
CSQ: 
CLD: 
CACE: 
CCK: 
CTYK: 
CEU: 
CFM: 
AMT: 
GFE: 
CTH: 
CTX: 
CCE: 
CCL: 
CSS: 
Cst_c19650(cooS1)
CSD: 
RAL: 
RUM: 
ROB: 
BYL: 
LACY: 
CSH: 
HSD: 
CDF: 
PDC: 
CDC: 
CDL: 
PDF: 
CST: 
DSY: 
DHD: 
DDH: 
DDL: 
DMT: 
DRM: 
DAE: 
DCA: 
DKU: 
DRU: 
DGI: 
DFG: 
DAU: 
TJR: 
SGY: 
DOR: 
DAI: 
DMI: 
DED: 
DEC: 
DCF50_p290(cooS1)
DRS: 
ELM: 
AWO: 
CAD: 
TTE: 
TKI: 
CHY: 
CHY_0034(cooSV) CHY_0085(cooSII) CHY_0736(cooSIV) CHY_1824(cooSI)
TEP: 
TAE: 
MTA: 
ADG: 
TPZ: 
Tph_c05730(cooS1) Tph_c13580(cooS) Tph_c15180(acsB)
CSC: 
CHD: 
CKI: 
CLC: 
TOC: 
TNR: 
NTH: 
AAR: 
HHL: 
VPR: 
VAT: 
SSG: 
SRI: 
PUF: 
PFT: 
TAZ: 
TREAZ_1535(cooS_2) TREAZ_1650(cooS_1)
TPI: 
CPOR: 
TOH: 
CPC: 
CPH: 
PROS: 
PMX: 
TAM: 
DTE: 
DIN: 
TID: 
TOP: 
CTHI: 
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MJH: 
MIG: 
MMP: 
MMP0985(cdhA)
MMQ: 
MMX: 
MMZ: 
MMD: 
MMAK: 
MMAO: 
MAE: 
MVN: 
MVO: 
MOK: 
MAC: 
MA_1016(cdhA) MA_1309(cooS) MA_3282(cooS) MA_3860(cdhA) MA_4399(cdhA)
MBA: 
MBY: 
MBW: 
MBAR: 
MBAK: 
MMA: 
MMAZ: 
MMJ: 
MMAC: 
MVC: 
MEK: 
MLS: 
METM: 
MEF: 
MEQ: 
MSJ: 
MSZ: 
MSW: 
MTHE: 
MTHR: 
MHOR: 
MBU: 
MMET: 
MMH: 
MHAZ: 
MEV: 
MZH: 
MPY: 
MHZ: 
MTP: 
MCJ: 
MCON_1332(cdhA) MCON_2865(cooS)
MHI: 
MHU: 
MBG: 
MEMA: 
MPI: 
MBN: 
MFO: 
MPL: 
RCI: 
LRC456(cdhA)
MTH: 
MMG: 
METC: 
MWO: 
MWSIV6_0249(cdhA1) MWSIV6_0986(cdhA3) MWSIV6_0987(cdhA5)
MEL: 
MEW: 
METH: 
MFC: 
BRM9_0801(cdhA)
MFI: 
MCUB: 
MCBB_1821(cdhA)
MFV: 
MKA: 
MK0536 MK0717(cdhA_1) MK0719(cdhA_1)
AFU: 
AFG: 
AVE: 
AST: 
FPL: 
GAC: 
GAH: 
MEAR: 
TON: 
TGA: 
TGAM_0824(cooS)
TBA: 
THA: 
THS: 
TGY: 
TCB: 
KCR: 
BARC: 
AOA65_0464(cdhA2) AOA65_1716(cdhA)
BARB: 
AOA66_1428(cdhA2)
 » show all
Taxonomy
Reference
1  [PMID:6687389]
  Authors
Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL.
  Title
Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein.
  Journal
J. Biol. Chem. 258 (1983) 2364-9.
Reference
2  [PMID:6687458]
  Authors
Diekert G, Ritter M.
  Title
Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum.
  Journal
FEBS. Lett. 151 (1983) 41-4.
Reference
3  [PMID:3029096]
  Authors
Bonam D, Ludden PW.
  Title
Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.
  Journal
J. Biol. Chem. 262 (1987) 2980-7.
Reference
4  [PMID:11593006]
  Authors
Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW.
  Title
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11973-8.
  Sequence
[rru:Rru_A1427]
Reference
5  [PMID:11509720]
  Authors
Dobbek H, Svetlitchnyi V, Gremer L, Huber R, Meyer O.
  Title
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.
  Journal
Science. 293 (2001) 1281-5.
  Sequence
[chy:CHY_0085]
Reference
6  [PMID:12386327]
  Authors
Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL.
  Title
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.
  Journal
Science. 298 (2002) 567-72.
  Sequence
[mta:Moth_1203]
Reference
7  [PMID:24521136]
  Authors
Can M, Armstrong FA, Ragsdale SW
  Title
Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.
  Journal
Chem. Rev. 114 (2014) 4149-74.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system