ID A7I830_METB6 Unreviewed; 786 AA.
AC A7I830;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=Mboo_1373 {ECO:0000313|EMBL:ABS55891.1};
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS55891.1, ECO:0000313|Proteomes:UP000002408};
RN [1] {ECO:0000313|Proteomes:UP000002408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8
RC {ECO:0000313|Proteomes:UP000002408};
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS55891.1; -; Genomic_DNA.
DR AlphaFoldDB; A7I830; -.
DR STRING; 456442.Mboo_1373; -.
DR KEGG; mbn:Mboo_1373; -.
DR eggNOG; arCOG02428; Archaea.
DR HOGENOM; CLU_361186_0_0_2; -.
DR Proteomes; UP000002408; 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 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; PF13187; Fer4_9; 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:ABS55891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002408};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 400..430
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 439..468
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 767..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 251
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 279
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 318
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
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 416
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 420
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 454
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 458
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 516
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 545
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
FT BINDING 580
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01137"
SQ SEQUENCE 786 AA; 84588 MW; F2DB20A3559ABBAB CRC64;
MLLVTEKKVS LSIKELDAGF GRIRDLSVSI GKLSAGDWAE EKGPTPYPSL ATLREWDHTL
LSRYQPFYMP FCDLCCLCTY GKCDLTGTKK GACGISMPAQ QARTVLLTAC IGAATHTSHA
RELVTYAIKR SGRDCEIDPG GNAIGVEAPV IRLVCGEKPQ ILADLETVLD YCESQITSLL
AATHTGQEGK YLDFESKVLH AGMIDQVGME VADLAQISAL GYPKADPDAP LAALGMGTVE
TTKPVILVIG HNVPPAVAII DYLAEENLTD QVEVTGICCT SVDATRYSPR AKIIGPMSWQ
LRYIRSGIPD VIVVDEQCVR TDAFDEAVAA GTPFIATSDK NCMGLPDRTR DPVDAIVADL
SSGRAKGALI LDSEKAGEVA VRVARTVMPA RRKTSTALSP EAVREKAADC TRCRLCQRAC
PNDLAIPQGM KAAAEGDLSL LSLLYETCVG CGRCEHACTQ DIPVHSLIVA AAAEKIKNEK
FVIRTGRGAI QDVEIRNVGG PIVLGEIPGV VAFVGCSNFA NGGKEIAEMS VEFAKRRYIV
CTSGCAAMSI GMYRDEEGKT PYEQFPGSFT AGGIVNVGSC VANAHIAGAT IKIASIFARR
NLRGNYAEIA DYVHNRVGAV GVAWGAMSQK AAAIASGFWR LGIPVVVGPH GTKYRRMLLG
RADRDEDWYV HDQRTGEKVY AGPAPEHLFV AAETKEEAMV LVAKLCMRPN DTTRGRAMKL
THYIDLYQRS HGALPEDIPR YIRTTADIPV TLKGEITGIL SQSGWKEQPI PDPTLLTRDM
PGEGRL
//
