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ACDE_METTH
ID   ACDE_METTH              Reviewed;         173 AA.
AC   O27744;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS CODH subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
GN   Name=cdhB {ECO:0000255|HAMAP-Rule:MF_01134}; OrderedLocusNames=MTH_1709;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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 subcomponent functions as a carbon monoxide
CC       dehydrogenase. The precise role of the epsilon subunit is unclear; it
CC       may have a stabilizing role within the alpha(2)epsilon(2) component
CC       and/or be involved in electron transfer to FAD during a potential FAD-
CC       mediated CO oxidation. {ECO:0000255|HAMAP-Rule:MF_01134}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01134}.
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_01134}.
CC   -!- SIMILARITY: Belongs to the CdhB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01134}.
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DR   EMBL; AE000666; AAB86181.1; -; Genomic_DNA.
DR   PIR; F69095; F69095.
DR   AlphaFoldDB; O27744; -.
DR   SMR; O27744; -.
DR   STRING; 187420.MTH_1709; -.
DR   EnsemblBacteria; AAB86181; AAB86181; MTH_1709.
DR   KEGG; mth:MTH_1709; -.
DR   PATRIC; fig|187420.15.peg.1670; -.
DR   HOGENOM; CLU_123700_0_0_2; -.
DR   OMA; ITYYYLA; -.
DR   UniPathway; UPA00642; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01134; CdhB; 1.
DR   InterPro; IPR003704; CO_DH_CoA_synth.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   Pfam; PF02552; CO_dh; 1.
DR   PIRSF; PIRSF006035; CO_dh_b_ACDS_e; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   TIGRFAMs; TIGR00315; cdhB; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..173
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   epsilon"
FT                   /id="PRO_0000155097"
SQ   SEQUENCE   173 AA;  19558 MW;  CA692918D1A95AA6 CRC64;
     MIVLNDRIIP WQPTVIAGPK QAMLVTPETA TMMIKKARRP LMVVGPLAKR QEVLEHTVKI
     IRHFDLPVVA TADTYRALSE AGIESEPHGI VEITNLLKDP SWEGIRGEGQ HDLVIFIGCI
     YYIASQGLSS LKHFAPHIKT LTICKTFHSN ADASFPNMDD DEWFRYLEKM YAE
 
 
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