(data stored in SCRATCH zone)

SWISSPROT: Q3IIH8_PSEHT

ID   Q3IIH8_PSEHT            Unreviewed;       888 AA.
AC   Q3IIH8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   Name=aceE {ECO:0000313|EMBL:CAI85489.1};
GN   OrderedLocusNames=PSHAa0391 {ECO:0000313|EMBL:CAI85489.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85489.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85489.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85489.1; -; Genomic_DNA.
DR   RefSeq; WP_011327102.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIH8; -.
DR   STRING; 326442.PSHAa0391; -.
DR   EnsemblBacteria; CAI85489; CAI85489; PSHAa0391.
DR   KEGG; pha:PSHAa0391; -.
DR   PATRIC; fig|326442.8.peg.375; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; REPWFPG; -.
DR   OrthoDB; POG091H046S; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IIH8.
DR   SWISS-2DPAGE; Q3IIH8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000313|EMBL:CAI85489.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:CAI85489.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT   DOMAIN      104    292       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      361    427       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
SQ   SEQUENCE   888 AA;  99525 MW;  37BD4F9EC7DBEACB CRC64;
     MSEVNKIDVD ALETQEWLQA LESVVREEGV ERAQFLLEQV LEQARLDGVD MPTGITTNYV
     NTIPVEQEPA YPGDVNIERR IRSIIRWNAI MIVLRASKKD LDLGGHMASY QSSAAFYEVC
     FNHFFKAPND VDGGDLVYYQ GHISPGIYAR AFVEGRLSAS QLDNFRQEVG GEGLPSYPHP
     KLMPEFWQFP TVSMGLGPIS SIYQARFLKY LDGRGLKDTK NQRVYAFLGD GEMDEPESRG
     AISFAAREKL DNLCYLVNCN LQRLDGPVMG NGKIIQELEG LFKGAGWNVI KLVWGSGWDI
     LLAKDKTGKL LQLMNETVDG DYQTYKAKNG AYVREHFFGR YPETAALVAD MTDDEIFALK
     RGGHEPSKLF AAFKKAEETK GRPTVILAKT VKGYGMGEAA EGKNIAHQVK KMDMSHVAHL
     RSRLGLDDLI SEEQLTELPY LTLEEGTPEH TYLHARREEL KGYTPKRIAR FSEKLTVPEV
     EAFNPLLEEQ KRDISTTMGF VRALNILLKD KGIGKNIVPI IADEARTFGM EGLFRQIGIY
     NPHGQNYTPQ DRDIVSYYKE ATSGQVLQEG INELGAMSSW VAAATSYSTN DLPMIPFYIY
     YSMFGFQRVG DMAWMAGDQQ ARGFLLGATA GRTTLNGEGL QHEDGHSHIL ASTVPNCISY
     DPTYAYEVAV IIQDGIRRMY GDDQENIYYY LTLMNENYHQ PAMPEGAEEG IRKGIYKLES
     YAGKKANVQL LSSGTIMTEV RKAAKVLSED YGVASDVFSV TSFNELTRDG QDVERFNMLN
     PEGEQKTAYI TSVLNDSVTV AATDYMKNYA EQARSFIPSN NYKVLGTDGY GRSDSRENLR
     RHFEVNADYV VVATLSELAK RGEVEKSVVI EALKKFNIDT NKLNPLYA
//

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