ID D3S710_METSF Unreviewed; 773 AA.
AC D3S710;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01137};
DE Short=ACDS complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01137};
DE EC=1.2.7.4 {ECO:0000256|HAMAP-Rule:MF_01137};
DE AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01137};
DE Short=ACDS CODH subunit alpha {ECO:0000256|HAMAP-Rule:MF_01137};
GN Name=cdhA {ECO:0000256|HAMAP-Rule:MF_01137};
GN OrderedLocusNames=MFS40622_0120 {ECO:0000313|EMBL:ADC68820.1};
OS Methanocaldococcus sp. (strain FS406-22).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=644281 {ECO:0000313|EMBL:ADC68820.1, ECO:0000313|Proteomes:UP000002189};
RN [1] {ECO:0000313|EMBL:ADC68820.1, ECO:0000313|Proteomes:UP000002189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS406-22 {ECO:0000313|EMBL:ADC68820.1,
RC ECO:0000313|Proteomes:UP000002189};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The
CC alpha-epsilon subcomponent functions as a carbon monoxide
CC dehydrogenase. {ECO:0000256|HAMAP-Rule:MF_01137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2
CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01137};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01137};
CC Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000256|HAMAP-
CC Rule:MF_01137};
CC -!- COFACTOR:
CC Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01137};
CC Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC {ECO:0000256|HAMAP-Rule:MF_01137};
CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits. The ACDS
CC complex is made up of alpha, epsilon, beta, gamma and delta subunits
CC with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-
CC (gamma(1)delta(1))(8). {ECO:0000256|HAMAP-Rule:MF_01137}.
CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster
CC C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation.
CC Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges
CC the two subunits of the CODH dimer. Contains two additional 4Fe-4S
CC clusters, dubbed E and F, that probably transport electrons from
CC ferredoxin to the B cluster. {ECO:0000256|HAMAP-Rule:MF_01137}.
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_01137}.
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DR EMBL; CP001901; ADC68820.1; -; Genomic_DNA.
DR AlphaFoldDB; D3S710; -.
DR STRING; 644281.MFS40622_0120; -.
DR KEGG; mfs:MFS40622_0120; -.
DR eggNOG; arCOG02428; Archaea.
DR HOGENOM; CLU_361186_0_0_2; -.
DR Proteomes; UP000002189; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR CDD; cd01916; ACS_1; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.2030; -; 2.
DR Gene3D; 1.10.8.190; Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1; 1.
DR HAMAP; MF_01137; CdhA; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004460; CdhA.
DR InterPro; IPR004137; HCP/CODH.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR NCBIfam; TIGR00314; cdhA; 1.
DR PANTHER; PTHR30109:SF6; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF03063; Prismane; 2.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01137};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01137};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01137};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01137};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01137};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01137,
KW ECO:0000313|EMBL:ADC68820.1}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 397..426
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 435..465
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 116
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 250
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 278
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 317
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 407
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 413
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 417
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 445
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 455
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 513
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 542
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 577
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
SQ SEQUENCE 773 AA; 85746 MW; EB3B1B7F1BE8FEC4 CRC64;
MGNNVEMDIK KLLTPLVKMK NANISMSIKF GEAEGEEEWE PMGPTPMPKI PTLRHWDFKL
LERYPPFYMP ICDLCCLCTF GKCDLSRGKK GACGLNIKAQ QARIVLIACC IGAACHAGHS
RHLVHHLIEK LGRDYPIDLG NEIEVEAPIA RTVTGIKPKT LGDLEKILDY CEEQITHLLS
AAHTGQEGNY LDFESKALHA GMIDDLAREA GDIAQIVAYN MPKGDEDAPL IELGFGCIDK
SKPVILCIGH NVVPGSYILE YLEDNNMEDE VEVCGICCTA IDITRVSDKP KVVGPLSRQL
MFVRSGVADV VIVDEQCIRT DILEEVLKTG AVLIATNEKM CLGLEDVSHM DEDEIIGYIL
RNRAALLLDE EKVGKVAVEL AKIVAKERKD KKTLPNLNEV VELAKQCTEC GWCNRNCPNA
FKVKEAMVLA KQGNFEGFID LYKRCYGCGR CEAICPRNLP IVSMTTKVGE AYYKDLKFKI
RAGRGPIKDV EIRSVGAPIV FGDIPGVVAL VGCSNHPNGE EEVAMIAKEF LERKYIVVAT
GCAAMAIGMW KDKDGKTLYE KYPGEFRAGG LVNCGSCLSN CHITGAAIKI ANIFAKVPLR
GNYAEVADYI LNKVGAVGVA WGAMSQKAAA IATGVNRWGI PVILGPHGAK YRRLYLSNGE
KFKVKDKKTG EILEIEPVPE HLIVTAENVK ECICMIPKLC MRPNDNPKGR ANKIYHYVDV
YEKYFGRMPP DLEKFVRTEK DIPFMMKDKI MAYLEEKGWK PLEKYPQDPT ILY
//
