ID L0EWS5_LIBCB Unreviewed; 349 AA.
AC L0EWS5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|ARBA:ARBA00014159, ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU361139};
GN Name=pdhA {ECO:0000256|RuleBase:RU361139};
GN OrderedLocusNames=B488_11010 {ECO:0000313|EMBL:AGA65093.1};
OS Liberibacter crescens (strain BT-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA65093.1, ECO:0000313|Proteomes:UP000010799};
RN [1] {ECO:0000313|EMBL:AGA65093.1, ECO:0000313|Proteomes:UP000010799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-1 {ECO:0000313|EMBL:AGA65093.1,
RC ECO:0000313|Proteomes:UP000010799};
RX PubMed=23408754; DOI=10.4056/sigs.3326772;
RA Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT "Complete genome sequence of Liberibacter crescens BT-1.";
RL Stand. Genomic Sci. 7:271-283(2012).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361139}.
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:RU361139};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU361139};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU361139}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003789; AGA65093.1; -; Genomic_DNA.
DR AlphaFoldDB; L0EWS5; -.
DR STRING; 1215343.B488_11010; -.
DR KEGG; lcc:B488_11010; -.
DR PATRIC; fig|1215343.11.peg.1133; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_2_5; -.
DR Proteomes; UP000010799; Chromosome.
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 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 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:UP000010799};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 43..338
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 349 AA; 38929 MW; 3E03D74A94F5B4F8 CRC64;
MVLNKTHPVL KCKNEKELIA TNYFDNSMII DLNCQQELFA YREMLLIRRF EEKAGQLYGM
GLIGGFCHLY IGQEAVAVGV KMSLEEGDQM ITGYRDHGHI LACSVDASTV MAELTGRRNG
ISKGKGGSMH MFSKKHGFYG GHGIVGAQVS LGTGIAFANK YRNTDRVCAV YFGDGAANQG
QVYESFNMAA LWNLGVIYII ENNQYAMGTS VKRASAQSDL SKRGDSFGIP SMKIDGMDIR
AVKGATDKAV QHCRLGNGPI IIEMLTYRYR GHSMSDPASY RAREEVEMMR SEHDPIEKVR
MRLLEKEWAS ENDLKIIESE VRKIITASAN FAQNDMEPDE SELYLDILL
//
