(data stored in ACNUC16935 zone)

SWISSPROT: F6HI27_VITVI

ID   F6HI27_VITVI            Unreviewed;       405 AA.
AC   F6HI27;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   30-AUG-2017, entry version 41.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   OrderedLocusNames=VIT_04s0043g00720 {ECO:0000313|EMBL:CCB51874.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; Vitales; Vitaceae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C.,
RA   Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A.,
RA   Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D.,
RA   Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M.,
RA   Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C.,
RA   Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I.,
RA   Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G.,
RA   Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D.,
RA   Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F.,
RA   Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F.,
RA   Weissenbach J., Quetier F., Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in
RT   major angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
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DR   EMBL; FN595763; CCB51874.1; -; Genomic_DNA.
DR   RefSeq; XP_002269441.1; XM_002269405.4.
DR   UniGene; Vvi.1484; -.
DR   ProteinModelPortal; F6HI27; -.
DR   STRING; 29760.VIT_04s0043g00720.t01; -.
DR   PRIDE; F6HI27; -.
DR   EnsemblPlants; VIT_04s0043g00720.t01; VIT_04s0043g00720.t01; VIT_04s0043g00720.
DR   GeneID; 100250049; -.
DR   Gramene; VIT_04s0043g00720.t01; VIT_04s0043g00720.t01; VIT_04s0043g00720.
DR   KEGG; vvi:100250049; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   eggNOG; COG0022; LUCA.
DR   InParanoid; F6HI27; -.
DR   KO; K00162; -.
DR   OrthoDB; EOG09360DU7; -.
DR   Proteomes; UP000009183; Chromosome 4.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:InterPro.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624:SF90; PTHR11624:SF90; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
DR   PRODOM; F6HI27.
DR   SWISS-2DPAGE; F6HI27.
KW   Complete proteome {ECO:0000313|Proteomes:UP000009183};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN       85    260       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   405 AA;  43926 MW;  A3080BD2CC672673 CRC64;
     MAAIFQGIGA AAAAAALPPA EKFHSQSPRF VSARKGSLFV VRSDGRPSLG SSPRSRGAQR
     LITNAVAAKA DASVTSTASK PGHELLLFEA LREGLEEEMD RDPRVCVMGE DVGHYGGSYK
     VTKGLATKYG DLRVLDTPIA ENSFTGMGIG AAMTGLRPII EGMNMGFLLL AFNQISNNCG
     MLHYTSGGQF KIPVVIRGPG GVGRQLGAEH SQRLESYFQS IPGIQMVACS TPYNAKGLMK
     AAIRSENPVI LFEHVLLYNL KERIPDEEYV LSLEEAEMVR PGEHVTILTY SRMRYHVMQA
     AKTLVNKGYD PEVIDIRSLK PFDLYTIGNS VKKTHRVLIV EECMRTGGIG ASLTAAITEN
     FIDYLDAPIV CLSSQDVPTP YAGTLEEWTV VQPSQIVTAV EQLCQ
//

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