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Database: UniProt
Entry: A0A3P9Q6D7_POERE
LinkDB: A0A3P9Q6D7_POERE
Original site: A0A3P9Q6D7_POERE 
ID   A0A3P9Q6D7_POERE        Unreviewed;       390 AA.
AC   A0A3P9Q6D7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000029554.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000029554.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000029554.1};
RG   Ensembl;
RL   Submitted (SEP-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   -!- 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|ARBA:ARBA00033635,
CC         ECO:0000256|RuleBase:RU361139};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU361139};
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DR   RefSeq; XP_008425244.1; XM_008427022.2.
DR   AlphaFoldDB; A0A3P9Q6D7; -.
DR   STRING; 8081.ENSPREP00000029554; -.
DR   Ensembl; ENSPRET00000029888.1; ENSPREP00000029554.1; ENSPREG00000020018.1.
DR   GeneID; 103475424; -.
DR   KEGG; pret:103475424; -.
DR   CTD; 406702; -.
DR   GeneTree; ENSGT00530000063174; -.
DR   OMA; SKRDPIM; -.
DR   OrthoDB; 166915at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000020018; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
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; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361139};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          66..360
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   390 AA;  43330 MW;  FB4A689136D13110 CRC64;
     MLTNISNVLR TCAQRNGAAA VVSARTYSDF TTQATFEIKK CDVFKLDEAP ATQVVMTRDE
     GLQYYRTMQT MRRMELKADQ LYKQKIIRGF CHLYDGQEAC AVGIEASINL KDHLITAYRA
     HGYTLTRGGT VKEIMAELTG RRGGIAKGKG GSMHMYCKNF YGGNGIVGAQ VPLGAGVALA
     CKYKGTDELC VCLYGDGAAN QGQIFETYNM AALWKLPLIF ICENNRYGMG TSVERAAAST
     DYFKRGEFIP GLRVDGMDIL CVREATRFAA DHCRSGKGPI LMELQTYRYH GHSMSDPGVS
     YRTREEIQEV RSKSDPISLL KDRLLSNNMA SVEELKEIDV EVRKEIEDAA QFATTDPEPP
     LDELCNHIFS NSPPVEVRGT NPWTKLKSLS
//
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