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ACDA2_ARCFU
ID   ACDA2_ARCFU             Reviewed;         798 AA.
AC   O30274;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA2 {ECO:0000255|HAMAP-Rule:MF_01137}; OrderedLocusNames=AF_2397;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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: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   -!- 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; AE000782; AAB91266.1; -; Genomic_DNA.
DR   PIR; F69549; F69549.
DR   RefSeq; WP_010879884.1; NC_000917.1.
DR   AlphaFoldDB; O30274; -.
DR   SMR; O30274; -.
DR   STRING; 224325.AF_2397; -.
DR   PRIDE; O30274; -.
DR   EnsemblBacteria; AAB91266; AAB91266; AF_2397.
DR   GeneID; 1485627; -.
DR   KEGG; afu:AF_2397; -.
DR   eggNOG; arCOG02428; Archaea.
DR   HOGENOM; CLU_361186_0_0_2; -.
DR   OMA; NEREIPY; -.
DR   OrthoDB; 1404at2157; -.
DR   PhylomeDB; O30274; -.
DR   Proteomes; UP000002199; 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:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR   CDD; cd01916; ACS_1; 1.
DR   Gene3D; 1.20.1270.30; -; 1.
DR   Gene3D; 3.40.50.2030; -; 2.
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; IPR016101; CO_DH_a-bundle.
DR   InterPro; IPR004137; HCP/CODH.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF03063; Prismane; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00314; cdhA; 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; Nickel; Oxidoreductase;
KW   Reference proteome; Repeat.
FT   CHAIN           1..798
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   alpha 2"
FT                   /id="PRO_0000155073"
FT   DOMAIN          395..424
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   DOMAIN          434..463
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         65
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         68
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         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         71
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         76
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         86
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         109
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         313
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         405
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         408
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         411
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         415
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         443
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         446
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         449
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         453
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         511
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         540
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         575
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ   SEQUENCE   798 AA;  88378 MW;  FC3CBCCB41BD30A0 CRC64;
     MVLEFGKGAF VVDDLRNVTI KIGEIAEEEE EWAPMGPTPM PGIATLRDWD FFLLKRYKPF
     YAPACDMCCL CTMGKCDLTG NKRGACGIDL AAQTGRIVTI ACSIGVSAHT GHARHMLHDI
     EHMTGKKLSE IPVDLGPEID EVAPLTELIT GIKPKTLEDL ERALRYAEEQ IVQVVDAVHT
     GQEGSYLDYE SKALHLGMLD SLGKEIADIA QICAFGYPKG EDNQPLIEVG MGVMDRSKAM
     ILVIGHHAPP VLNIADYIEE NGLEDEVDLG GICCTANDMT RYYQKAKIVS ALGRQLKVIR
     AGLADVIVID EQCIRADILY HTKKLGIPVI CTNEKAMHAL PDMTKEEPKN IIKYLLDGNP
     GCVILDPLKV GEVAVEVARA RRKQRGDDIG PRLTEEQFME YARACTQCGN CTIACPQGIR
     IGEAMEAAEN GDRSKLEKEW DVCIACGRCE QVCPKGIPII DMYNYAAWNL IVNEKGKLRR
     GRGPIRDSEI RNVGAPIVLG TIPGIIAVIG CGNYPNGTRD AYTIMDEFAS RNYIVVTTGC
     MAFDAALYKD EEGQTVYEKY HDRFDGGGVV QIGSCVANAH IHGAAIKVAR IFAKRNIRAN
     YEEIADYILN RVGACGVAWG AYSQKAASIA TGFNRLGIPA VVGPHGSKYR RAFLGRPYND
     EDWMVYDART GEKVRIEPAP QDLLVAAETI EEAIPLMAKL CFRPNDTTQG RSIKLTHYID
     LSLKYLKRMP DDWHLFVRTE ADLPLAKKEE LLKELEDKHG WKIDWQKKKI VEGPIRGYHA
     GFNPTNLERC LRDGFMTV
 
 
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