ODPB_BOVIN
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 03-AUG-2022, entry version 140.
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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.ENSBTAP00000028958; -.
DR PaxDb; P11966; -.
DR PeptideAtlas; P11966; -.
DR PRIDE; P11966; -.
DR Ensembl; ENSBTAT00000028958; ENSBTAP00000028958; ENSBTAG00000021724.
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; 875272at2759; -.
DR TreeFam; TF105674; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000021724; Expressed in infraspinatus muscle and 105 other tissues.
DR ExpressionAtlas; P11966; baseline.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
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: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 Gene3D; 3.40.50.920; -; 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; PTHR11624; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 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
