GenomeNet

Database: UniProt
Entry: Q8TJC6
LinkDB: Q8TJC6
Original site: Q8TJC6 
ID   ACDA2_METAC             Reviewed;         805 AA.
AC   Q8TJC6;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 106.
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=MA_3860;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC       cleavage of acetyl-CoA, allowing growth on acetate as sole source
CC       of carbon and energy. The alpha-epsilon subcomponent functions as
CC       a carbon monoxide dehydrogenase. {ECO:0000255|HAMAP-
CC       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   -!- 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
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; AE010299; AAM07211.1; -; Genomic_DNA.
DR   RefSeq; WP_011023758.1; NC_003552.1.
DR   ProteinModelPortal; Q8TJC6; -.
DR   SMR; Q8TJC6; -.
DR   PRIDE; Q8TJC6; -.
DR   EnsemblBacteria; AAM07211; AAM07211; MA_3860.
DR   GeneID; 1475753; -.
DR   KEGG; mac:MA_3860; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   InParanoid; Q8TJC6; -.
DR   KO; K00192; -.
DR   OMA; NSHIAGA; -.
DR   OrthoDB; 1404at2157; -.
DR   PhylomeDB; Q8TJC6; -.
DR   BioCyc; MACE188937:G1FZT-4109-MONOMER; -.
DR   UniPathway; UPA00642; -.
DR   Proteomes; UP000002487; 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:0050418; F:hydroxylamine reductase activity; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; PF13187; Fer4_9; 1.
DR   Pfam; PF03063; Prismane; 2.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00314; cdhA; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Methanogenesis; Nickel; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    805       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha 2.
FT                                /FTId=PRO_0000155075.
FT   DOMAIN      407    435       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      445    474       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        72     72       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        75     75       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        76     76       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        78     78       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        83     83       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        93     93       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       249    249       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL       277    277       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       322    322       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       416    416       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       419    419       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       422    422       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       426    426       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       454    454       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       457    457       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       460    460       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       464    464       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       522    522       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       551    551       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       586    586       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   BINDING     116    116       Carbon monoxide; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
SQ   SEQUENCE   805 AA;  87955 MW;  BBC8DF01BF79D604 CRC64;
     MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELG PMGPTAMAGL ASYRSWNLLL
     LDRYEPVLTP MCDQCCYCTY GPCDLSGNKR GACGIDMAGQ TGREFFLRVI TGTACHAAHG
     RHLLDHVIEV FGEDLPLNLG ESNVLTPNVT ICTGLSPKTL GECRAPMEYV EEQLTQLLAT
     IHAGQESAEI DYDSKALFSG SLDHVGMEVS DIAQVSAYDF PKADPEAPLI EIGMGSIDKS
     KPLIVAIGHN VAGVTYIMDY MEENNLTDKM EIAGLCCTAF DMTRYKEADR RAPYAKIVGS
     LAKELKVIRS GMPDVIVVDE QCVRGDVLSE SQKLKIPVIA SNEKIMMGLP DRTDADVDSI
     VEEIKSGAIP GCVMLDYDKL GELIPKIAEV MAPIRDAEGI TAIPTDEEFK VYIDKCVKCG
     ECMLACPEEL DIPEALEYAA KGSYEYLEAL HDVCIGCRRC EQVCKKEIPI LNVLEKAAQK
     SISEEKGWVR SGRGQASDAE IRKEGLNLVM GTTPGIIAII GCPNYPAGTK DVYLIAEEFL
     KRNYLLAVSG CSAMDIGMFK DEDGKTLYEK YPGTFAGGGL LNTGSCVSNA HISGAAEKVA
     GIFAQRTLAG NLAEIADYTL NRVGACGLAW GAYSQKAASI GTGCNIYGIP AVLGPHSSKY
     RRALIAKNYD ESKWKVYDGR DGSEMTIPPA PEFLLTTAET WQEAIPMMAK ACIRPSDNNM
     GRSIKLTHWM ELSKKYLGVE PEDWWKFVRN EADLPLAKRE ELLKRLEAEH GWEIDWKRKK
     IISGPKIKFD VSAQPTNLKR LCKEA
//
DBGET integrated database retrieval system