(data stored in ACNUC7421 zone)

SWISSPROT: A8FQC1_SHESH

ID   A8FQC1_SHESH            Unreviewed;       888 AA.
AC   A8FQC1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   OrderedLocusNames=Ssed_0431 {ECO:0000313|EMBL:ABV35044.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35044.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35044.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35044.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
CC       that catalyzes the overall conversion of pyruvate to acetyl-CoA
CC       and CO(2). {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000156};
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DR   EMBL; CP000821; ABV35044.1; -; Genomic_DNA.
DR   RefSeq; WP_012140781.1; NC_009831.1.
DR   ProteinModelPortal; A8FQC1; -.
DR   STRING; 425104.Ssed_0431; -.
DR   EnsemblBacteria; ABV35044; ABV35044; Ssed_0431.
DR   KEGG; sse:Ssed_0431; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; REPWFPG; -.
DR   OrthoDB; POG091H046S; -.
DR   BioCyc; SSED425104:GH7Q-453-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR004660; 2-oxoA_DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   Pfam; PF00456; Transketolase_N; 2.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   4: Predicted;
DR   PRODOM; A8FQC1.
DR   SWISS-2DPAGE; A8FQC1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000313|EMBL:ABV35044.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:ABV35044.1};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT   DOMAIN      105    292       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      361    408       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
SQ   SEQUENCE   888 AA;  99464 MW;  23A521326286D488 CRC64;
     MSEHMLQDLD PLETQEWVDS LQAVLEQEGP ERAHYLLEKL IDKARRNGTH LPYKATTAYL
     NTIPAGQEPH VPGNQEMERR IRAIVRWNAL AMVLRGSKKD LELGGHISSF ASSATIYDVC
     FNHFFRGPNE KDGGDLVYFQ GHIAPGIYSR SFLEGRLTED QMNSFRQEVD GKGLPSYPHP
     KLMPDYWQFP TVSMGLGPIQ AIYQARFLKY LTDRGLKDCS EQTVYCFLGD GECDEPETLG
     AIGLAAREEL DNLVFIVNCN LQRLDGPVRG NGKIIQELEG EFRGAGWEAV KVIWGRYWDP
     LLARDTSGKL LQLMEETVDG EYQNCKAKGG AYTREHFFGK YPETAEMVAN MSDDDIWRLN
     RGGHDPVKIF AALQHAKDTK GRPTVILAKT VKGYGMGDAG EGKNIAHNVK KMGVESLKYF
     RDRFNIPISD DQLEDIPFYH PGADSEEVKY LKARRAELHG AMPARREKFS EELEVPSLKI
     FDSVLKGSNG REISSTMAFV RILTALLKDK KIGKQIVPII PDEARTFGME GLFRQVGIYA
     HEGQKYVPQD SDQVAYYRED KSGQVLQEGI NELGAMSSWV AAATSYSVND TPMIPFYIYY
     SMFGFQRIGD MAWAAGDMRA RGFMVGGTSG RTTLNGEGLQ HQDGHSHVLA NTIPSCVSYD
     PTYGYEIAVV VQDGIRRMYG EQQEDIFYYL TTMNENYEQP AMPEGAEEGI VKGIYKLETV
     EGSGKGKVQL MGCGTILEQV RKAAQALAKD FGISADVFSV TSFNELTRDG QAAERYNMLH
     PTETPQEAYI SQVISSESPA IVATDYMKIY GEQLRAYIPT DYKVLGTDGF GRSDSRENLR
     HHFEVDAKFI VIASLKSLVD RNELPVDVLT KAISEYGIDV DKINPQYA
//

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