EC                  Enzyme                                 

anaerobic carbon monoxide dehydrogenase;
carbon-monoxide dehydrogenase (ferredoxin)
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
carbon-monoxide,water:ferredoxin oxidoreductase
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+ [RN:R07157]
(other) R08034 R09317
CO [CPD:C00237];
H2O [CPD:C00001];
oxidized ferredoxin [CPD:C00139]
CO2 [CPD:C00011];
reduced ferredoxin [CPD:C00138];
H+ [CPD:C00080]
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, 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, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC, aerobic carbon monoxide dehydrogenase.
EC created 2003 (EC created 1982, modified 1990, modified 2003, incorporated 2015), modified 2016
ec00633  Nitrotoluene degradation
ec00680  Methane metabolism
ec00720  Carbon fixation pathways in prokaryotes
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
K00192  anaerobic carbon-monoxide dehydrogenase, CODH/ACS complex subunit alpha
K00198  anaerobic carbon-monoxide dehydrogenase catalytic subunit
CAMA: F384_12620
AVN: Avin_04490(cooS)
AVL: AvCA_04490(cooS)
AVD: AvCA6_04490(cooS)
ACX: Achr_4450(cooS)
TMB: Thimo_0223
CCV: CCV52592_1131(codH)
CCO: CCC13826_0236(codH)
SULT: FA592_03290(cooS)
GSU: GSU2098(cooS)
GME: Gmet_1902(cooS)
GUR: Gura_0618
GBM: Gbem_0072(cooS-2) Gbem_1736(cooS-1)
GEO: Geob_0362(cooS-1) Geob_1046(cooS-2)
PCA: Pcar_0057(cooS-2) Pcar_0888(cooS-1)
DES: DSOUD_1182(cooS)
DEU: DBW_0138
DVU: DVU2098(cooS)
DVL: Dvul_1133
DVM: DvMF_2233
DDE: Dde_3028
DDS: Ddes_0382
DMA: DMR_25780
DEF: CNY67_12835(cooS)
DFL: DFE_2686
DCB: C3Y92_11905(cooS)
DMS: E8L03_07465(cooS)
DSD: GD606_18530(cooS)
DAS: Daes_0529
DPI: BN4_11760(cooS) BN4_20190(cooS)
PPRF: DPRO_1606(cooS) DPRO_3530
DBA: Dbac_0934
DRT: Dret_1234
DML: Dmul_09300(cooS1) Dmul_19100(cooS2) Dmul_30840(cdhA)
DAT: HRM2_16670(cdhA) HRM2_41010(cdh1) HRM2_43440(cdh2)
DTO: TOL2_C00990(cdh1) TOL2_C11820(cdhA) TOL2_C38110(cooS)
DOV: DSCO28_32360(cooS_1) DSCO28_36040(cooS_2) DSCO28_44770 DSCO28_59740(cooS_3)
DWD: DSCW_28520(cooS_1) DSCW_41580(cooS_2) DSCW_47510(cooS_3)
DALK: DSCA_26710(cooS_1) DSCA_27610(cooS_2) DSCA_28100(cooS_3)
DAX: FDQ92_02155(cooS) FDQ92_06245(cooS)
DBR: Deba_0241
RPC: RPC_4498
RRU: Rru_A1427
RRF: F11_07370
BBEV: BBEV_2326(cooS1)
CAE: SMB_G0117(cooS) SMB_G2533
CTC: CTC_01156
CNO: NT01CX_0669(cooS)
CBH: CLC_1369
CBN: CbC4_2402(cooS)
CKL: CKL_2148
CKR: CKR_1887
CLJ: CLJU_c09110(cooS1) CLJU_c17910(cooS2) CLJU_c37670(codH)
CSR: Cspa_c16740(cooS1) Cspa_c21120(cooS2) Cspa_c57670(cooS3)
CPAT: CLPA_c05080(cooS) CLPA_c34390(cooS1)
CPAE: CPAST_c05080(cooS) CPAST_c34390(cooS1)
CSB: CLSA_c11710(cooS1) CLSA_c14830(cooS2)
CLD: CLSPO_c13520(cooS1) CLSPO_c22620(cooS2)
CTYK: CTK_C21760(cooS)
CDY: F3K33_15405(cooS) F3K33_25905(cooS)
CCOH: SAMEA4530647_0946(cooS1_1)
HHW: NCTC503_01567(cooS1)
CAZO: G3A45_00240(cooS)
CTH: Cthe_2801
CSS: Cst_c19650(cooS1)
CSD: Clst_1883
CTHD: CDO33_08275(cooS)
RUM: CK1_12690
ROB: CK5_28700
BHAN: CGC63_06525(cooS) CGC63_07980(cooS)
BLAU: DQQ01_10205(cooS)
BPRO: PMF13cell1_00639(cooS1_1) PMF13cell1_04203(cooS) PMF13cell1_04285(cooS1_2)
BLAB: EYS05_16735(cooS)
EHL: EHLA_2243
RGN: RGna_12250(cooS)
CBOL: CGC65_03955(cooS) CGC65_24000(cooS)
CDF: CD630_01740(cooS) CD630_07160(cooS)
PDF: CD630DERM_01740(cooS) CD630DERM_07160(cooS1)
ROC: HF520_11320(cooS)
PHX: KGNDJEFE_00543(cooS)
DRM: Dred_0652
SGY: Sgly_2814
DED: DHBDCA_p230(cooS1)
DEC: DCF50_p290(cooS1)
TFR: BR63_06565(cooS)
ELM: ELI_3603
EMT: CPZ25_018705(cooS)
AWO: Awo_c10740(acsA) Awo_c19050(cooS)
AMIJ: EQM06_02755(cooS)
TTE: TTE1708
TKI: TKV_c08080(cooS) TKV_c20100(acsA)
CHY: CHY_0034(cooSV) CHY_0085(cooSII) CHY_0736(cooSIV) CHY_1824(cooSI)
ADG: Adeg_0335
TPZ: Tph_c05730(cooS1) Tph_c15180(acsB)
CSC: Csac_0400
TAE: TepiRe1_0598(cooS)
HALS: D7D81_07270(cooS) D7D81_07945(cooS)
CAD: Curi_c06440(cooS)
VPR: Vpar_0209
VRM: 44547418_00230(cooS2)
VDN: NCTC11831_00196(cooS1)
KST: KSMBR1_1326(cdh_acsA) KSMBR1_3765(acsA_2)
TAZ: TREAZ_1535(cooS_2) TREAZ_1650(cooS_1)
TPI: TREPR_3069(cooS)
TOH: BCB71_06635(cooS)
CPC: Cpar_1193
PMX: PERMA_0106(cooS)
CTHI: THC_1754
TAV: G4V39_00810(cooS) G4V39_01690(cooS)
TMAI: FVE67_00270(cooS)
MMP: MMP0985(cdhA)
MMD: GYY_05750
MMAK: MMKA1_10980(cdhA) MMKA1_11410(cdhA)
MMAO: MMOS7_10770(cdhA)
MMAD: MMJJ_00060
MVO: Mvol_0200
METF: CFE53_02830(cdhA)
MTH: MTH_1708
MMG: MTBMA_c02870(cdhA1) MTBMA_c14200(cdhA2) MTBMA_c14210(cdhA3)
MWO: MWSIV6_0249(cdhA1) MWSIV6_0986(cdhA3)
MTHM: FZP57_01125(cdhA)
METH: MBMB1_1565(cdhA)
MFC: BRM9_0801(cdhA)
MFI: DSM1535_0763(cdhA)
MCUB: MCBB_1821(cdhA)
METT: CIT01_07270(cdhA)
METO: CIT02_10120(cdhA)
MFV: Mfer_0527
MKA: MK0536 MK0717(cdhA_1) MK0719(cdhA_1)
TON: TON_1018
TGA: TGAM_0824(cooS)
THS: TES1_1211
THH: CDI07_07345(cooS)
MAC: MA_1016(cdhA) MA_1309(cooS) MA_3282(cooS) MA_3860(cdhA) MA_4399(cdhA)
MFZ: AOB57_003735(cdhA)
MBU: Mbur_0858
MMH: Mmah_1166
MZI: HWN40_01045(cooS) HWN40_08225(cdhA)
MCJ: MCON_1332(cdhA) MCON_2865(cooS)
MBG: BN140_2260(cooS)
MEMA: MMAB1_2986(cooS)
MPI: Mpet_0907
MPL: Mpal_0842
RCI: LRC456(cdhA)
HDF: AArcSl_0878(cooS)
KCR: Kcr_0762
BARC: AOA65_0464(cdhA2) AOA65_1716(cdhA)
BARB: AOA66_1428(cdhA2)
 » show all
1  [PMID:6687389]
Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL.
Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein.
J Biol Chem 258:2364-9 (1983)
2  [PMID:6687458]
Diekert G, Ritter M.
Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum.
FEBS Lett 151:41-4 (1983)
3  [PMID:3029096]
Bonam D, Ludden PW.
Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.
J Biol Chem 262:2980-7 (1987)
4  [PMID:11593006]
Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW.
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
Proc Natl Acad Sci U S A 98:11973-8 (2001)
5  [PMID:11509720]
Dobbek H, Svetlitchnyi V, Gremer L, Huber R, Meyer O.
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.
Science 293:1281-5 (2001)
6  [PMID:12386327]
Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL.
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.
Science 298:567-72 (2002)
7  [PMID:24521136]
Can M, Armstrong FA, Ragsdale SW
Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.
Chem Rev 114:4149-74 (2014)
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