ID E4UCX8_LIBSC Unreviewed; 350 AA.
AC E4UCX8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=CKC_02335 {ECO:0000313|EMBL:ADR52218.1};
OS Liberibacter solanacearum (strain CLso-ZC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52218.1, ECO:0000313|Proteomes:UP000007038};
RN [1] {ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RT "Complete genome sequence of Candidatus Liberibacter solanacearum CLso-
RT ZC1.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLso-ZC1;
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADR52218.1, ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52218.1,
RC ECO:0000313|Proteomes:UP000007038};
RX PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA Duan Y., Zhou L., Vahling C.M.;
RT "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum',
RT the Bacterium Associated with Potato Zebra Chip Disease.";
RL PLoS ONE 6:E19135-E19135(2011).
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}.
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DR EMBL; CP002371; ADR52218.1; -; Genomic_DNA.
DR AlphaFoldDB; E4UCX8; -.
DR STRING; 658172.CKC_02335; -.
DR KEGG; lso:CKC_02335; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_2_5; -.
DR Proteomes; UP000007038; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 44..340
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 350 AA; 38573 MW; 7C07F6A645F8D8E6 CRC64;
MALNTSISGK ENGISSVDHM DISFFKEFKV SEFDKTQELS AYQKMLLIRR FEEKTGQLYG
MGLIGGFCHL CIGQEAVIIG MKMAMAEGDQ MITAYRDHGH ILSCGVEASK VMAELTGRQG
GISKGKGGSM HMFSTENGFY GGHGIVGAQV SLGTGIAFAN KYRKSDKVCV VCLGDGAANQ
GQVYESFNMA ELWKLGVIYV IENNQYAMGT SVARASAQPN LSKRGISFNI PGIQVDGMDV
RSVKAAIEKA TAYCRANKGP IILEMLTYRY RGHSMSDPAT YRTRDEVNDM RTNHDPIEQV
RERLLQKKWA SESDLKAIEM SVRKIVNDSV EFAQSDEEPN SSELYSDILI
//
