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ACDA3_METAC
ID   ACDA3_METAC             Reviewed;         805 AA.
AC   Q8THW2;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 3 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 3 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA3 {ECO:0000255|HAMAP-Rule:MF_01137}; OrderedLocusNames=MA_4399;
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., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   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 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; AE010299; AAM07741.1; -; Genomic_DNA.
DR   RefSeq; WP_011024278.1; NC_003552.1.
DR   AlphaFoldDB; Q8THW2; -.
DR   SMR; Q8THW2; -.
DR   STRING; 188937.MA_4399; -.
DR   EnsemblBacteria; AAM07741; AAM07741; MA_4399.
DR   GeneID; 1476293; -.
DR   KEGG; mac:MA_4399; -.
DR   HOGENOM; CLU_361186_0_0_2; -.
DR   InParanoid; Q8THW2; -.
DR   OrthoDB; 1404at2157; -.
DR   PhylomeDB; Q8THW2; -.
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: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:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; 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; 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; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..805
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   alpha 3"
FT                   /id="PRO_0000155076"
FT   DOMAIN          407..435
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   DOMAIN          445..474
FT                   /note="4Fe-4S ferredoxin-type 2"
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="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         76
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         78
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         83
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         93
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         116
FT                   /ligand="CO"
FT                   /ligand_id="ChEBI:CHEBI:17245"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         249
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         277
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         322
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
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         422
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         426
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         460
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         464
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         522
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         551
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         586
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ   SEQUENCE   805 AA;  87993 MW;  8B1B9B32B56C56CD 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 SMKLKIPVIA SNEKIMMGLP DRTDADVDSI
     VEEIKSGAIP GCVMLDYDKL GELIPKIAEV MAPIRDAEGI TAIPTDEEFK VYIDKCVKCG
     ECMLACPEEL DIPEALEYAA KGSYEYLEAL HDVCIGCRRC EQVCKKEIPI LNVLEKAAQK
     SISEEKGWVR SGRGQASDAE IRAEGLNLVM GTTPGIIAII GCPNYPAGTK DVYNIAEEFL
     KRNYLVVVSG CSAMDIGMYK DDDGKTLYER YPGTFSGGGL LNTGSCVSNA HITGAAEKVA
     GIFAQRTLAG NLAEVADYTL NRVGACGLAW GAYSQKAASI GTGCNIYGIP AVLGPHSSKY
     RRALIAKTYE EDKWKVFDAR DGSEMNIPPA PEFLLTTAET WQEALPMMAK ACIRPSDNNM
     GRSIKLTHWM ELSKKYLGVE PEDWWKFVRN EADLPLAKRE ELLKRLEAEQ GWEIDWKRKK
     IISGPKIKFD VSAQPTNLKR LCKEA
 
 
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