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PORB_THEMA
ID   PORB_THEMA              Reviewed;         324 AA.
AC   Q56317;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Pyruvate synthase subunit PorB;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase beta chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta;
GN   Name=porB; OrderedLocusNames=TM_0018;
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 2-17 AND 20-44.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P94692};
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
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DR   EMBL; X85171; CAA59458.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35112.1; -; Genomic_DNA.
DR   PIR; B59427; D72427.
DR   RefSeq; NP_227834.1; NC_000853.1.
DR   RefSeq; WP_004082462.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q56317; -.
DR   SMR; Q56317; -.
DR   STRING; 243274.THEMA_04710; -.
DR   EnsemblBacteria; AAD35112; AAD35112; TM_0018.
DR   KEGG; tma:TM0018; -.
DR   eggNOG; COG1013; Bacteria.
DR   InParanoid; Q56317; -.
DR   OMA; ATGCMEV; -.
DR   OrthoDB; 981516at2; -.
DR   BioCyc; MetaCyc:MON-424; -.
DR   BRENDA; 1.2.7.1; 6331.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8550425"
FT   CHAIN           2..324
FT                   /note="Pyruvate synthase subunit PorB"
FT                   /id="PRO_0000099909"
FT   REGION          150..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         228
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
SQ   SEQUENCE   324 AA;  36385 MW;  2425239D778A6A0E CRC64;
     MPVNIKQLAQ EFDKKEIGIT QGHRLCPGCG APITVKFVMM IARHLGYEPV VGLATGCLEV
     STSIYPYTAW SVPYIHNAFE NVAATMSGVE TAYKALKNKG KIPEDKKYAF IAFGGDGGTY
     DIGLQSLSGM LERGHKVLYV LYDNEGYMNT GNQRSGSTPP GSDTTTAPVG KKLPGKVQLK
     KNIVEIVAAH ENVYAATASL SEPMDFFAKV EKALNFDGPS FLAVFSPCVR FWRVNDDKTV
     EISKLAVETK YWPLYEVERG VYRVTRKPRQ FKPVEEFLKA QGRFRKLLSR PDAKEIVDEL
     QEYVDRRWER LLTLEEVTKD KPIR
 
 
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