ID E8N8X4_MICTS Unreviewed; 365 AA.
AC E8N8X4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN Name=pdhA {ECO:0000256|RuleBase:RU361139};
GN OrderedLocusNames=MTES_0219 {ECO:0000313|EMBL:BAJ73183.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ73183.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ73183.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ73183.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) 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).
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|RuleBase:RU361139}.
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DR EMBL; AP012052; BAJ73183.1; -; Genomic_DNA.
DR AlphaFoldDB; E8N8X4; -.
DR STRING; 979556.MTES_0219; -.
DR KEGG; mts:MTES_0219; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000008975; Chromosome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:SF72; DEHYDROGENASE-RELATED; 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 29..324
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 341..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 39304 MW; A2357D27FBB4CB8D CRC64;
MPTPRPPRST ARRATKRPTA VELRALYREM LLIRRFEERA ARAYSEAKIG GYCHLNLGEE
ATVVGLMAAL EPGDYLYANY REHGYALARG ISPERAMAEL YGRTDGVSKG WGGSMHMFDL
DARFMGGYGI VGGQVPLATG TALAIHYRGE DDVVMCLMGD GTTNIGAFHE SLNIAALWNL
PIVYVVNNNG LGMGTTVEQS SAEPELHRRA SSYRMPSARV DGFDPGAVRE AARIARDSAR
AGTPYLLETM TGRMKGHSVV DPARYRTAEE AAAAKAADPV AAFAARLRAD DVLSADDLDA
LDREVTAEVT AAAAFADASP HPDVSTLFDY TYATPVPNDA RRLPGEALFP AAPRPARSLP
EEVSA
//
