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ACDB2_METMA
ID   ACDB2_METMA             Reviewed;         470 AA.
AC   Q8PV85;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2;
DE            Short=ACDS complex subunit beta 2;
DE            EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE   AltName: Full=ACDS complex acyltransferase 2;
GN   Name=cdhC2; OrderedLocusNames=MM_2087;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC       acetyl-CoA, allowing growth on acetate as sole source of carbon and
CC       energy. The alpha-epsilon complex generates CO from CO(2), while the
CC       beta subunit (this protein) combines the CO with CoA and a methyl group
CC       to form acetyl-CoA. The methyl group, which is incorporated into
CC       acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-
CC       sulfur protein (the gamma-delta complex). {ECO:0000255|HAMAP-
CC       Rule:MF_01138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA
CC         + methyl-Co(III)-[corrinoid Fe-S protein]; Xref=Rhea:RHEA:45212,
CC         Rhea:RHEA-COMP:11110, Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.3.1.169;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01138};
CC   -!- COFACTOR:
CC       Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC       Note=Binds 1 [Ni-Fe-S] cluster.;
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC   -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, beta,
CC       gamma and delta chains with a probable stoichiometry of
CC       (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}.
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DR   EMBL; AE008384; AAM31783.1; -; Genomic_DNA.
DR   RefSeq; WP_011034018.1; NC_003901.1.
DR   AlphaFoldDB; Q8PV85; -.
DR   SMR; Q8PV85; -.
DR   STRING; 192952.MM_2087; -.
DR   PRIDE; Q8PV85; -.
DR   EnsemblBacteria; AAM31783; AAM31783; MM_2087.
DR   GeneID; 1480429; -.
DR   KEGG; mma:MM_2087; -.
DR   PATRIC; fig|192952.21.peg.2396; -.
DR   eggNOG; arCOG04360; Archaea.
DR   HOGENOM; CLU_613408_0_0_2; -.
DR   OMA; FMHLNQR; -.
DR   UniPathway; UPA00642; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR   GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1650.10; -; 1.
DR   HAMAP; MF_01138; CdhC; 1.
DR   InterPro; IPR045822; ACS_CODH_B_C.
DR   InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR   InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR   InterPro; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR42281; PTHR42281; 1.
DR   Pfam; PF19436; ACS_CODH_B_C; 1.
DR   Pfam; PF03598; CdhC; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00316; cdhC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW   Reference proteome; Transferase.
FT   CHAIN           1..470
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   beta 2"
FT                   /id="PRO_0000155105"
FT   BINDING         190
FT                   /ligand="[Ni-Fe-S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60400"
FT                   /evidence="ECO:0000255"
FT   BINDING         193
FT                   /ligand="[Ni-Fe-S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60400"
FT                   /evidence="ECO:0000255"
FT   BINDING         279
FT                   /ligand="[Ni-Fe-S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60400"
FT                   /evidence="ECO:0000255"
FT   BINDING         281
FT                   /ligand="[Ni-Fe-S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60400"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   470 AA;  52364 MW;  A6D00D6AA42F7503 CRC64;
     MADEFPFEIS PMFEGERVRK EGMFVELGGP KSLGLELVRA ADMDAIEDDK VTIIGPDLKD
     MEEGKTYPWA MIFNIGGELV EPDLESVVER RVHDFINYCQ GIMHLNQRYD VWMRVSKDTA
     AKMDSFEPFG KAVMMLFKTE LPFIEKMQVT FYTDKDEVEK QMETAKEIFK ARDARTKDLH
     DEDVEVFYGC TLCQSFAPTN VCVVSPDRIS LCGAINWFDG RAAAKVDPEG PQFEIAKGDL
     IDAVTGEYTG VNEIAKKLSS GEFDKIKLHS FFDCPHTSCG CFEVVGFYIP EVDGIGWVDR
     EYQGMAPNGI GFSTMAGQTG GGKQIVGFLG IGVNYFYSPK FIQADGGWNR VVWLPSKLKE
     KIDEAIPADL KDKIATENDA SDIESLKAFL QEKNHPVVAT WAAAEEEEEE EEEEEEVAVA
     AAPMMMPAAG FQMPAMPMMS GGSSGGIKLT FKNAKITIDR MIISEKKEKK
 
 
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