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Database: UniProt
Entry: O30274
LinkDB: O30274
Original site: O30274 
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   10-APR-2019, entry version 119.
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};
GN   OrderedLocusNames=AF_2397;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing 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).
CC       The 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
CC         H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040,
CC         Rhea:RHEA-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.
CC       {ECO:0000255|HAMAP-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
CC       ACDS complex is made up of alpha, epsilon, beta, gamma and delta
CC       subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-
CC       beta(8)-(gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster;
CC       cluster C is a mixed Ni-Fe-S cluster which is the active site of
CC       CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S
CC       cluster that bridges the two subunits of the CODH dimer. Contains
CC       two additional 4Fe-4S clusters, dubbed E and F, that probably
CC       transport electrons from ferredoxin to the B cluster.
CC       {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01137}.
DR   EMBL; AE000782; AAB91266.1; -; Genomic_DNA.
DR   PIR; F69549; F69549.
DR   RefSeq; WP_010879884.1; NC_000917.1.
DR   ProteinModelPortal; O30274; -.
DR   SMR; O30274; -.
DR   STRING; 224325.AF_2397; -.
DR   EnsemblBacteria; AAB91266; AAB91266; AF_2397.
DR   GeneID; 1485627; -.
DR   KEGG; afu:AF_2397; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   KO; K00192; -.
DR   OMA; RNEREIP; -.
DR   OrthoDB; 1404at2157; -.
DR   BioCyc; AFUL224325:G1G17-2446-MONOMER; -.
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   CDD; cd01916; ACS_1; 1.
DR   Gene3D; 1.10.1060.10; -; 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; IPR004137; HCP/CODH.
DR   InterPro; IPR009051; Helical_ferredxn.
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; SSF46548; SSF46548; 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; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    798       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha 2.
FT                                /FTId=PRO_0000155073.
FT   DOMAIN      395    424       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      434    463       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        65     65       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        68     68       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        69     69       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        71     71       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        76     76       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        86     86       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       246    246       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL       274    274       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       313    313       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       405    405       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       408    408       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       411    411       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       415    415       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       443    443       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       446    446       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       449    449       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       453    453       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       511    511       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       540    540       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       575    575       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   BINDING     109    109       Carbon monoxide; via tele nitrogen.
FT                                {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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