ID E3TGJ6_ICTPU Unreviewed; 359 AA.
AC E3TGJ6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN Name=ODPB {ECO:0000313|EMBL:ADO29432.1};
GN Synonyms=odpb {ECO:0000313|RefSeq:NP_001188013.1}, pdhb
GN {ECO:0000313|RefSeq:NP_001188013.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:ADO29432.1};
RN [1] {ECO:0000313|EMBL:ADO29432.1, ECO:0000313|RefSeq:NP_001188013.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20634964; DOI=10.1371/journal.pone.0011546;
RA Chen F., Lee Y., Jiang Y., Wang S., Peatman E., Abernathy J., Liu H.,
RA Liu S., Kucuktas H., Ke C., Liu Z.;
RT "Identification and characterization of full-length cDNAs in channel
RT catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus).";
RL PLoS ONE 5:E11546-E11546(2010).
RN [2] {ECO:0000313|RefSeq:NP_001188013.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27307075;
RA Zeng Q., Liu S., Yao J., Zhang Y., Yuan Z., Jiang C., Chen A., Fu Q.,
RA Su B., Dunham R., Liu Z.;
RT "Transcriptome Display During Testicular Differentiation of Channel Catfish
RT (Ictalurus punctatus) as Revealed by RNA-Seq Analysis.";
RL Biol. Reprod. 95:19-19(2016).
RN [3] {ECO:0000313|RefSeq:NP_001188013.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the
CC glycolytic pathway to the tricarboxylic cycle.
CC {ECO:0000256|ARBA:ARBA00003754}.
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};
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DR EMBL; GU589482; ADO29432.1; -; mRNA.
DR RefSeq; NP_001188013.1; NM_001201084.1.
DR STRING; 7998.ENSIPUP00000015164; -.
DR GeneID; 100528814; -.
DR KEGG; ipu:100528814; -.
DR CTD; 5162; -.
DR OrthoDB; 5473567at2759; -.
DR Proteomes; UP000221080; Chromosome 21.
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 GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
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 33..208
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 359 AA; 39213 MW; 8928D41A6FB16D1D CRC64;
MASLRCFIRS GKNAVSVVLR REFHRTPSAA VQVTVRDALN QAMDEELERD ERVFLLGEEV
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQRSQ CFAAWYGHCP GLKVVSPWNA
EDARGLLKSA IRDDNPVVML ENELMYGMAF ELSAEALSKD FTIPIGKAKV ERSGSHITLT
SHSRMVGYCL DAAAVLAKEG IECEVVNLRT IRPLDVETIE TSVIKTNHLV TVEGGWPQFG
VGAEICARIM EGPAFNYLDA PAVRVTGVDI PMPYAKILED NSVPQIKDII FAVKKTLNV
//
