位置:首页 > 蛋白库 > PORC_THEMA
PORC_THEMA
ID   PORC_THEMA              Reviewed;         192 AA.
AC   O05650;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Pyruvate synthase subunit PorC;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase gamma chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit gamma;
GN   Name=porC; Synonyms=porG; OrderedLocusNames=TM_0015;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20.
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA   Kletzin A., Adams M.W.W.;
RT   "Molecular and phylogenetic characterization of pyruvate and 2-
RT   ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT   pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL   J. Bacteriol. 178:248-257(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA
CC         + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:12765,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD35109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA59455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X85171; CAA59455.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE000512; AAD35109.1; ALT_INIT; Genomic_DNA.
DR   PIR; C59427; A72427.
DR   RefSeq; NP_227831.1; NC_000853.1.
DR   RefSeq; WP_004082456.1; NZ_CP011107.1.
DR   PDB; 2RAA; X-ray; 2.12 A; A=1-192.
DR   PDBsum; 2RAA; -.
DR   AlphaFoldDB; O05650; -.
DR   SMR; O05650; -.
DR   STRING; 243274.THEMA_04725; -.
DR   EnsemblBacteria; AAD35109; AAD35109; TM_0015.
DR   KEGG; tma:TM0015; -.
DR   eggNOG; COG1014; Bacteria.
DR   InParanoid; O05650; -.
DR   OMA; PDYVIVQ; -.
DR   OrthoDB; 1777574at2; -.
DR   BioCyc; MetaCyc:MON-425; -.
DR   BRENDA; 1.2.7.1; 6331.
DR   EvolutionaryTrace; O05650; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.920.10; -; 1.
DR   InterPro; IPR011894; PorC_KorC.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   TIGRFAMs; TIGR02175; PorC_KorC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8550425"
FT   CHAIN           2..192
FT                   /note="Pyruvate synthase subunit PorC"
FT                   /id="PRO_0000099917"
FT   CONFLICT        23
FT                   /note="A -> V (in Ref. 1; CAA59455)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           20..33
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          52..60
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           124..131
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           138..149
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:2RAA"
FT   HELIX           171..187
FT                   /evidence="ECO:0007829|PDB:2RAA"
SQ   SEQUENCE   192 AA;  21270 MW;  C58296B289254B70 CRC64;
     MPVAKKYFEI RWHGRAGQGA KSASQMLAEA ALEAGKYVQA FPEYGAERTG APMRAFNRIG
     DEYIRVRSAV ENPDVVVVID ETLLSPAIVE GLSEDGILLV NTVKDFEFVR KKTGFNGKIC
     VVDATDIALQ EIKRGIPNTP MLGALVRVTG IVPLEAIEKR IEKMFGKKFP QEVIDANKRA
     LRRGYEEVKC SE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024