ID Q7T368_DANRE Unreviewed; 359 AA.
AC Q7T368; A0A8M1PEP2;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 149.
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=pdhb {ECO:0000313|EMBL:AAH53233.1,
GN ECO:0000313|Ensembl:ENSDARP00000002122,
GN ECO:0000313|RefSeq:NP_998319.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-2173};
GN Synonyms=wu:fc76a05 {ECO:0000313|RefSeq:NP_998319.1}, zgc:64062
GN {ECO:0000313|RefSeq:NP_998319.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH53233.1};
RN [1] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9007256;
RA Kelsh R.N., Brand M., Jiang Y.J., Heisenberg C.P., Lin S., Haffter P.,
RA Odenthal J., Mullins M.C., van Eeden F.J., Furutani-Seiki M., Granato M.,
RA Hammerschmidt M., Kane D.A., Warga R.M., Beuchle D., Vogelsang L.,
RA Nusslein-Volhard C.;
RT "Zebrafish pigmentation mutations and the processes of neural crest
RT development.";
RL Development 123:369-389(1996).
RN [2] {ECO:0000313|EMBL:AAH53233.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH53233.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16109975;
RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL Genome Res. 15:1307-1314(2005).
RN [4] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18803863;
RA Kolmakov N.N., Kube M., Reinhardt R., Canario A.V.;
RT "Analysis of the goldfish Carassius auratus olfactory epithelium
RT transcriptome reveals the presence of numerous non-olfactory GPCR and
RT putative receptors for progestin pheromones.";
RL BMC Genomics 9:429-429(2008).
RN [5] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20826660;
RA Maurer C.M., Schonthaler H.B., Mueller K.P., Neuhauss S.C.;
RT "Distinct retinal deficits in a zebrafish pyruvate dehydrogenase-deficient
RT mutant.";
RL J. Neurosci. 30:11962-11972(2010).
RN [6] {ECO:0000313|Ensembl:ENSDARP00000002122}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000002122};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [7] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23117182;
RA Chen K., Cole R.B., Rees B.B.;
RT "Hypoxia-induced changes in the zebrafish (Danio rerio) skeletal muscle
RT proteome.";
RL J. Proteomics 78:477-485(2013).
RN [8] {ECO:0000313|Ensembl:ENSDARP00000002122, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000002122};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [9] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [10] {ECO:0000313|RefSeq:NP_998319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [11] {ECO:0000313|RefSeq:NP_998319.1}
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; BX649457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053233; AAH53233.1; -; mRNA.
DR RefSeq; NP_998319.1; NM_213154.1.
DR STRING; 7955.ENSDARP00000002122; -.
DR PaxDb; 7955-ENSDARP00000002122; -.
DR Ensembl; ENSDART00000006513.9; ENSDARP00000002122.7; ENSDARG00000021346.9.
DR GeneID; 406428; -.
DR KEGG; dre:406428; -.
DR AGR; ZFIN:ZDB-GENE-040426-2173; -.
DR CTD; 5162; -.
DR ZFIN; ZDB-GENE-040426-2173; pdhb.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR OMA; SRMRHHC; -.
DR OrthoDB; 5473567at2759; -.
DR TreeFam; TF105674; -.
DR Reactome; R-DRE-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DRE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DRE-5362517; Signaling by Retinoic Acid.
DR Reactome; R-DRE-70268; Pyruvate metabolism.
DR Proteomes; UP000000437; Chromosome 22.
DR Bgee; ENSDARG00000021346; Expressed in muscle tissue and 37 other cell types or tissues.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0004738; F:pyruvate dehydrogenase activity; IMP:ZFIN.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043473; P:pigmentation; IMP:ZFIN.
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 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 Proteomics identification {ECO:0007829|PeptideAtlas:Q7T368};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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; 39308 MW; 06B31C8784F75DE4 CRC64;
MASLRCFLRS GKSAVSAVLR REFHRTPPAA VQVTVRDALN QAMDEELERD ERVFLLGEEV
AQYDGAYKVS RGLWKKYGDK RIIDTPITEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
DQVINSAAKT YYMSAGLQAV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVLSPWNS
EDARGLLKAA IRDDNPVVFL ENELMYGVPF EMSEEVQSKD FVIPIGKAKI ERQGNHITLV
SHSRMVGLCL DAAAVLAKEG IECEVINLRS IRPLDADTIE TSITKTNHLV TVEGGWPQFG
VGAEILARIM EGPAFNYLDA PAVRVTGVDI PMPYAKILED NSIPQIKDII FSVKKTLNV
//
