ID A5GLH4_SYNPW Unreviewed; 327 AA.
AC A5GLH4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138, ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU364074};
GN Name=pdhB {ECO:0000313|EMBL:CAK23789.1};
GN OrderedLocusNames=SynWH7803_1363 {ECO:0000313|EMBL:CAK23789.1};
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK23789.1, ECO:0000313|Proteomes:UP000001566};
RN [1] {ECO:0000313|Proteomes:UP000001566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT971583; CAK23789.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GLH4; -.
DR STRING; 32051.SynWH7803_1363; -.
DR KEGG; syx:SynWH7803_1363; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_3; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000001566; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000001566};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 35810 MW; F32ABF964732FCE3 CRC64;
MAGTLLFNAL REAIDEEMAR DPHVCVMGED VGQYGGSYKV TKDLYEKYGE LRVLDTPIAE
NSFTGMAVGA AMTGLRPIVE GMNMGFLLLA FNQISNNMGM LRYTSGGNFT IPTVVRGPGG
VGRQLGAEHS QRLEAYFHAV PGIKIVACST PTNAKGLMKA AIRDNNPVLF FEHVLLYNLS
EELPAGDYTC ALDQADLVKE GSDVTILTYS RMRHHCLKAV EQLDADGINA ELIDLISLKP
FDMETIARSI RKTHRVIVVE ECMKTGGIGA ELIALITEHC FDDLDARPIR LSSQDIPTPY
NGNLENLTII QPHQIVEAAQ TIVRQGL
//
