ID   ODPB_BOVIN              Reviewed;         359 AA.
AC   P11966; A6QQW6; Q58CN6;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   24-JAN-2024, entry version 146.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 31-54.
RX   PubMed=2829898; DOI=10.1016/0006-291x(88)90714-0;
RA   Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E.,
RA   Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.;
RT   "Identification of a cDNA clone for the beta-subunit of the pyruvate
RT   dehydrogenase component of human pyruvate dehydrogenase complex.";
RL   Biochem. Biophys. Res. Commun. 150:904-908(1988).
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. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC       heterotetramer interacts with DLAT, and is part of the multimeric
CC       pyruvate dehydrogenase complex that contains multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC       E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to
CC       an inner core composed of about 48 DLAT and 12 PDHX molecules.
CC       Interacts with DLAT. {ECO:0000250|UniProtKB:P11177}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX46758.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BT021911; AAX46758.1; ALT_FRAME; mRNA.
DR   EMBL; BC150020; AAI50021.1; -; mRNA.
DR   PIR; B27712; B27712.
DR   RefSeq; NP_001030512.2; NM_001035435.3.
DR   AlphaFoldDB; P11966; -.
DR   SMR; P11966; -.
DR   CORUM; P11966; -.
DR   STRING; 9913.ENSBTAP00000058224; -.
DR   PaxDb; 9913-ENSBTAP00000028958; -.
DR   PeptideAtlas; P11966; -.
DR   Ensembl; ENSBTAT00000028958.5; ENSBTAP00000028958.4; ENSBTAG00000021724.6.
DR   GeneID; 613610; -.
DR   KEGG; bta:613610; -.
DR   CTD; 5162; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021724; -.
DR   VGNC; VGNC:49151; PDHB.
DR   eggNOG; KOG0524; Eukaryota.
DR   GeneTree; ENSGT00940000155146; -.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   InParanoid; P11966; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; 5473567at2759; -.
DR   TreeFam; TF105674; -.
DR   Reactome; R-BTA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-BTA-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-BTA-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-BTA-70268; Pyruvate metabolism.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000021724; Expressed in infraspinatus muscle and 105 other cell types or tissues.
DR   ExpressionAtlas; P11966; baseline and differential.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:UniProtKB.
DR   GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; 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   Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW   Glucose metabolism; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Pyruvate; Reference proteome; Thiamine pyrophosphate; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2829898"
FT   CHAIN           31..359
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000162216"
FT   BINDING         89
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   SITE            319
FT                   /note="Important for interaction with DLAT"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   MOD_RES         67
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D051"
FT   MOD_RES         354
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D051"
SQ   SEQUENCE   359 AA;  39126 MW;  584B86D36A233EFC CRC64;
     MAVVAVLVRK PLEQVSGLLR RRFHRTAPAA LQVTVREAIN QGMDEELERD EKVFLLGEEV
     AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
     DQVINSAAKT YYMSGGLQSV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWSS
     EDAKGLIKSA IRDNNPVVVL ENELMYGVPF ELPSEAQSKD FLIPIGKAKI ERQGTHVTIV
     AHSRPVGHCL EAATVLSKEG IECEVINLRT IRPMDIETIE GSVMKTNHLV TVEGGWPQFG
     VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSVPQVKDII FAIKKTLNI
//