ID A0A059B4S3_EUCGR Unreviewed; 380 AA.
AC A0A059B4S3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=EUGRSUZ_H03385 {ECO:0000313|EMBL:KCW60660.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW60660.1};
RN [1] {ECO:0000313|EMBL:KCW60660.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW60660.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00043719,
CC ECO:0000256|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000256|ARBA:ARBA00011130}.
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DR EMBL; KK198760; KCW60660.1; -; Genomic_DNA.
DR RefSeq; XP_010024203.1; XM_010025901.2.
DR RefSeq; XP_010024204.1; XM_010025902.2.
DR AlphaFoldDB; A0A059B4S3; -.
DR STRING; 71139.A0A059B4S3; -.
DR EnsemblPlants; KCW60660; KCW60660; EUGRSUZ_H03385.
DR Gramene; KCW60660; KCW60660; EUGRSUZ_H03385.
DR eggNOG; KOG0524; Eukaryota.
DR InParanoid; A0A059B4S3; -.
DR OMA; VHEANTT; -.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 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; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 47..222
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 380 AA; 40418 MW; D4B36D01B87D433D CRC64;
MLSVLRRKAA AAAVGGSDAM LLGGRLRKSC AAAAAGLRGY ATAAKEMTVR EALNSALDEE
MSADPKVFLM GEEVGEYQGA YKVSKGFLPK FGPERVVDTP ITEAGFTGIG VGAAYYGLKP
VVEFMTFNFA MQAIDHIINS AAKTNYMSAG NISVPIVFRG PNGAAAGVGA QHSQCYAAWY
GSCPGLKVLA PYSSEDARGL LKAAIRDPDP VVFLENELMY GERFPVSAEA LDSSFCLPIG
KAKIEREGKD VTITAFSKMV GLSLEAAEIL AKEGITAEVI NLLSIRPLDR PTINASVRKT
NRLVTVEEGF PQHGVGAEIC MSIIEDSFGY LDAPIERITG ADVPMPYAAN LERMALPQIE
DIVRAAKRVC HRSVPMAATA
//
