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ACDA1_METAC
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   03-AUG-2022, entry version 123.
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}; 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., 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; AAM04446.1; -; Genomic_DNA.
DR   RefSeq; WP_011021051.1; NC_003552.1.
DR   AlphaFoldDB; Q8TRZ4; -.
DR   SMR; Q8TRZ4; -.
DR   STRING; 188937.MA_1016; -.
DR   EnsemblBacteria; AAM04446; AAM04446; MA_1016.
DR   GeneID; 1472906; -.
DR   KEGG; mac:MA_1016; -.
DR   HOGENOM; CLU_361186_0_0_2; -.
DR   InParanoid; Q8TRZ4; -.
DR   OMA; LCIGHNV; -.
DR   OrthoDB; 1404at2157; -.
DR   PhylomeDB; Q8TRZ4; -.
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   CDD; cd01916; ACS_1; 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; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 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..806
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   alpha 1"
FT                   /id="PRO_0000155074"
FT   DOMAIN          407..436
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   DOMAIN          446..475
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         73
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         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         77
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         79
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         84
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         94
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         117
FT                   /ligand="CO"
FT                   /ligand_id="ChEBI:CHEBI:17245"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         250
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         278
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         323
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         417
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         420
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         423
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         427
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         455
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         458
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         461
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         465
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         523
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         552
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         587
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="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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