ID   ODPB_CAEEL              Reviewed;         352 AA.
AC   O44451;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   Name=pdhb-1; ORFNames=C04C3.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 130-137; 237-246 AND 262-272, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (SEP-2005) to UniProtKB.
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) (By similarity). {ECO:0000250|UniProtKB:P11177}.
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:0000250|UniProtKB:P11177};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P11177};
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR   EMBL; FO080230; CCD62196.1; -; Genomic_DNA.
DR   PIR; T32598; T32598.
DR   RefSeq; NP_500340.1; NM_067939.5.
DR   AlphaFoldDB; O44451; -.
DR   SMR; O44451; -.
DR   BioGRID; 42248; 15.
DR   DIP; DIP-24348N; -.
DR   IntAct; O44451; 6.
DR   STRING; 6239.C04C3.3.1; -.
DR   EPD; O44451; -.
DR   PaxDb; 6239-C04C3-3; -.
DR   PeptideAtlas; O44451; -.
DR   EnsemblMetazoa; C04C3.3.1; C04C3.3.1; WBGene00015413.
DR   GeneID; 177108; -.
DR   KEGG; cel:CELE_C04C3.3; -.
DR   UCSC; C04C3.3.1; c. elegans.
DR   AGR; WB:WBGene00015413; -.
DR   WormBase; C04C3.3; CE27647; WBGene00015413; pdhb-1.
DR   eggNOG; KOG0524; Eukaryota.
DR   GeneTree; ENSGT00940000155146; -.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   InParanoid; O44451; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; 5473567at2759; -.
DR   PhylomeDB; O44451; -.
DR   Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-CEL-70268; Pyruvate metabolism.
DR   PRO; PR:O44451; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00015413; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
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   GO; GO:0006096; P:glycolytic 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   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Oxidoreductase; Pyruvate;
KW   Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..352
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000042638"
FT   BINDING         81
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
SQ   SEQUENCE   352 AA;  38141 MW;  37F4A4A28C8ADECA CRC64;
     MALRKCGNLF VARLAGTSTR AASTMTVRDA LNQAMDEEIK RDDRVFLMGE EVAQYDGAYK
     ISKGLWKKHG DKRVVDTPIT EMGFAGIAVG AAFAGLRPIC EFMTFNFSMQ AIDQIINSAA
     KTYYMSAGRV PVPIVFRGPN GAAAGVAAQH SQDFSAWYAH CPGLKVVCPY SAEDAKGLLK
     AAIRDDNPVV FLENEILYGQ SFPVGDEVLS DDFVVPIGKA KIERAGDHVT IVSYSRGVEF
     SLEAAKQLEA IGVSAEVINL RSLRPFDFES IRQSVHKTHH LVSVETGWPF AGIGSEIAAQ
     VMESDVFDQL DAPLLRVTGV DVPMPYTQTL EAAALPTAEH VVKAVKKSLN IA
//