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Database: UniProt
Entry: A0A0K9RDF1_SPIOL
LinkDB: A0A0K9RDF1_SPIOL
Original site: A0A0K9RDF1_SPIOL 
ID   A0A0K9RDF1_SPIOL        Unreviewed;       364 AA.
AC   A0A0K9RDF1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 14.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=SOVF_079370 {ECO:0000313|EMBL:KNA17500.1};
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae;
OC   Anserineae; Spinacia.
OX   NCBI_TaxID=3562 {ECO:0000313|EMBL:KNA17500.1, ECO:0000313|Proteomes:UP000054095};
RN   [1] {ECO:0000313|EMBL:KNA17500.1, ECO:0000313|Proteomes:UP000054095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Viroflay {ECO:0000313|Proteomes:UP000054095};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KNA17500.1};
RX   PubMed=24352233; DOI=10.1038/nature12817;
RA   Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S.,
RA   Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R.,
RA   Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F.,
RA   Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.;
RT   "The genome of the recently domesticated crop plant sugar beet (Beta
RT   vulgaris).";
RL   Nature 505:546-549(2014).
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};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|RuleBase:RU364074}.
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DR   EMBL; KQ143728; KNA17500.1; -; Genomic_DNA.
DR   Proteomes; UP000054095; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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:SF94; PTHR11624:SF94; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054095};
KW   Glycolysis {ECO:0000256|RuleBase:RU364074};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364074};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054095};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074};
KW   Transit peptide {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN       37    212       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   364 AA;  39539 MW;  8BE7FD9415F8C9B7 CRC64;
     MSWLVRQVVN NGRLQSSSRI RALQHAARAY ATAGKEITVR EALNSALDEE MGADPRVFVM
     GEEVGEYQGA YKITKGLLDK YGPERVIDTP ITEAGFAGIG VGAAYKELRP VIEFMTFNFS
     MQAIDHIINS AAKSNYMSAG QISVPIVFRG PNGAAAGVGA QHSQCYAAWY GSCPGLKVLC
     PYSSEDARGL LKAAIRDPDP VVFLENELLY GESFPVSEEV LDSNFTVPIG KAKIERQGKD
     VTITAFSKMV GYALKAADIL AEEGISAEVV NLRSIRPLDR PTINESVRKT NRLVTVEEGF
     PQHGVGAEIC ASVIEDSFEY LDAPVERISG ADIPMPYAPN LERLAVPQIE DIVRAAKRAC
     YRSS
//
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