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Entry: A0A091V9S0_PHORB
LinkDB: A0A091V9S0_PHORB
Original site: A0A091V9S0_PHORB 
ID   A0A091V9S0_PHORB        Unreviewed;       374 AA.
AC   A0A091V9S0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
DE   Flags: Fragment;
GN   ORFNames=N337_05913 {ECO:0000313|EMBL:KFQ86443.1};
OS   Phoenicopterus ruber ruber.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC   Phoenicopterus.
OX   NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ86443.1, ECO:0000313|Proteomes:UP000053700};
RN   [1] {ECO:0000313|EMBL:KFQ86443.1, ECO:0000313|Proteomes:UP000053700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ86443.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK420522; KFQ86443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091V9S0; -.
DR   Proteomes; UP000053700; Unassembled WGS sequence.
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:UP000053700};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          51..345
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ86443.1"
FT   NON_TER         374
FT                   /evidence="ECO:0000313|EMBL:KFQ86443.1"
SQ   SEQUENCE   374 AA;  41934 MW;  04659A4ECBB9C178 CRC64;
     ASRVMVASRN YADFASEATF EIKKCDLHRL EEGPSTTAVM TREEGLHYYK TMQTIRRMEL
     KSDQLYKQKI IRGFCHLYDG QEACCVGLEV AIKPTDHVIT AYRAHGFTYA RGVPVREILA
     ELTGRKGGCV KGKGGSMHMY TKNFYGGNGI VGAQVPLGAG IALACKYFGK NEVCLTLYGD
     GAANQGQIFE TYNMAALWKL PCVFICENNR YGMGTSVERA AASTDYYKRG DFIPGLRVDG
     MDVLCVREAA KFAVEYCRAG KGPILMELQT YRYHGHSMSD PGISYRTREE IQEVRSKSDP
     ITLLKDRMVN NNLASIEELK EIDVAVRKEI EEAAQFATTD PEPPLEELGN HIYFNEPPFE
     VRGPNQWIRY KSVS
//
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