ID ACDA_METBU Reviewed; 802 AA.
AC Q12XL7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE EC=1.2.7.4 {ECO:0000255|HAMAP-Rule:MF_01137};
DE AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS CODH subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
GN Name=cdhA {ECO:0000255|HAMAP-Rule:MF_01137}; OrderedLocusNames=Mbur_0858;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
CC -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC cleavage of acetyl-CoA, allowing growth on acetate as sole source of
CC carbon and energy. The alpha-epsilon subcomponent functions as a carbon
CC monoxide dehydrogenase. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01137};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_01137};
CC -!- COFACTOR:
CC Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC {ECO:0000255|HAMAP-Rule:MF_01137};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01137}.
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_01137}.
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DR EMBL; CP000300; ABE51809.1; -; Genomic_DNA.
DR RefSeq; WP_011498962.1; NC_007955.1.
DR AlphaFoldDB; Q12XL7; -.
DR SMR; Q12XL7; -.
DR STRING; 259564.Mbur_0858; -.
DR GeneID; 3996856; -.
DR KEGG; mbu:Mbur_0858; -.
DR HOGENOM; CLU_361186_0_0_2; -.
DR OrthoDB; 35334at2157; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000001979; 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 GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
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; PF13237; Fer4_10; 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; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW Oxidoreductase; Repeat.
FT CHAIN 1..802
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha"
FT /id="PRO_1000164093"
FT DOMAIN 404..432
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 442..473
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 69
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:0000255|HAMAP-Rule:MF_01137"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 73
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:0000255|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:0000255|HAMAP-Rule:MF_01137"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 113
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 246
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 274
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 319
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01137"
FT BINDING 419
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 423
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01137"
FT BINDING 457
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 461
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 519
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 548
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 583
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ SEQUENCE 802 AA; 87795 MW; 2A40A6661CCC9010 CRC64;
MSELTTGRFS ISDLDNVQIT INNIVGAIEK QSDDIDVEMG PTVKPGVSSL RDWDHNILDR
YNPVYTPMCD QCCYCTFGPC DLSGNKEGAC GINLEGHNAR EFMLRVITGA AAHSGHGRHL
LHHLIGLYGK DHPLDVGATN IIAPNVQLVT GVQPKTLGDL DSVLSYVEEQ ITQLLAAIHV
GQEGAAIDFE SKALHGGMID HVGMEISDIA QISCLDFPKS DEEAPLADIG MGCLDASKPT
LIVIGHNVAA VTDIIDYMED KGLNDKIELG GLCCTALDMT RYKTGDRTLP RAKVVGTLAK
ELKTIRSGIP DVIIVDEQCI RADVLKEASK LMIPVITTND KVMYGLKDRS NDSIEDILED
LTTGKEKGAL MFDYVKLGEL APRLTMMMSE IRKQKGIKAL PTDEELKELA DSCVHCLKCE
VACPNSLPIS EAMTALSEGD LSKFELLHDK CIACGRCEYA CPKDIDIVNV IEKSSQRVIS
EEVGKVRVGR GPISDPEIRE EGVNLVLGTT PGIVALVGCS NYPDGTKDLF TIADEMLRRS
YIVVVSGCSA MDLGMYKGED GLTLYEKYPS RFKSGGLLNT GSCVSNAHIT GAVIKVASIF
AQKNISGNYE EIADYTLNRV GAVGVAWGAY SQKAASIGTG CSRLGIPVIL GPHGSKYRRA
LIAKPYEEEK WKVYDARNGS EMQIPAAPDY LLTTAETVEE MMPMLAKSCI RPSDNNMGRM
IKLTHYMELS QKYLGIMPED WYKFVRTETD LPLAKREKLL KILEEEHGWE IDWKRKKILS
GPTMKSDVSA QPTNLKRLCK EA
//
