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Database: UniProt
Entry: Q8TRZ4
LinkDB: Q8TRZ4
Original site: Q8TRZ4 
ID   ACDA1_METAC             Reviewed;         806 AA.
AC   Q8TRZ4;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   OrderedLocusNames=MA_1016;
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; AAM04446.1; -; Genomic_DNA.
DR   RefSeq; WP_011021051.1; NC_003552.1.
DR   ProteinModelPortal; Q8TRZ4; -.
DR   SMR; Q8TRZ4; -.
DR   PRIDE; Q8TRZ4; -.
DR   EnsemblBacteria; AAM04446; AAM04446; MA_1016.
DR   GeneID; 1472906; -.
DR   KEGG; mac:MA_1016; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   InParanoid; Q8TRZ4; -.
DR   KO; K00192; -.
DR   OMA; EVCGICC; -.
DR   OrthoDB; 1404at2157; -.
DR   PhylomeDB; Q8TRZ4; -.
DR   BioCyc; MACE188937:G1FZT-1088-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   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; 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    806       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha 1.
FT                                /FTId=PRO_0000155074.
FT   DOMAIN      407    436       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      446    475       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        76     76       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        77     77       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        84     84       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       250    250       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL       278    278       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       323    323       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       417    417       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       420    420       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       423    423       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       427    427       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       455    455       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       458    458       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       461    461       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       465    465       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       523    523       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       552    552       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       587    587       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   BINDING     117    117       Carbon monoxide; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
SQ   SEQUENCE   806 AA;  88694 MW;  4D7D376E7718B0B9 CRC64;
     MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELE KAGPTLFPGL ESYRDDWNFK
     LLDRYEPVIT PMCDQCCYCT YGPCDLSGNK RGACGIDMLG HNGREFFLRV ITGTACHAAH
     GRHLLDHLIE TFGEDLPLNL GQSNVLTPNI TISTGLSPKN LGEIKPAMEF VEEQLTQLLA
     TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDVVQVAAYD FPKADPEAPL IEIGMGTIDK
     SKPFLCVIGH NVGGVTYMMD YMEEHDLTDK MEIAGLCCTA IDLSRYKEAD RRPPYAKVIG
     SMSKELKVIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMYGL PNRTDANVDD
     VVEELKSGAI PGCVMLDYDK LGELCIRLTM EMGPIRDAEG ITAIPTDEEF ADWVAKCADC
     GACMIACPEE LDIPEAMGFA KEGDFSYLEE LHDQCIGCRR CEQVCKKEIP ILNIIEKVAQ
     KQIAEEKGWM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYAEGT KDVYYIAEEF
     LKRNFIVVTT GCGAMDIGMF KDEDGKTLYE RFPGGFECGG LVNIGSCVSN AHITGAAEKV
     AAIFAQRTLE GNLAEISDYI LNRVGACGLA WGAFSQKASS IGTGCNILGI PAVLGPHSSK
     YRRALIAKTY EEDKWKVYDA RNGQEMPIPP APEFLLTTAE TWQEAIPMMA KACIRPSDNS
     MGRSIKLTHW MELHKKYLGK DPEDWWKFVR NEADLPLAKR EALLKELESK HGWEIDWKKK
     KIISGPKIKF DVSAQPTNLK RLCKEA
//
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