ID A0A0G9MXQ5_9SPHN Unreviewed; 361 AA.
AC A0A0G9MXQ5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=AAW00_03375 {ECO:0000313|EMBL:KLE35480.1};
OS Aurantiacibacter luteus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE35480.1, ECO:0000313|Proteomes:UP000053464};
RN [1] {ECO:0000313|EMBL:KLE35480.1, ECO:0000313|Proteomes:UP000053464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA37 {ECO:0000313|EMBL:KLE35480.1,
RC ECO:0000313|Proteomes:UP000053464};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter luteus KA37.";
RL Submitted (APR-2015) 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|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU361139}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLE35480.1}.
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DR EMBL; LBHB01000001; KLE35480.1; -; Genomic_DNA.
DR RefSeq; WP_047002882.1; NZ_LBHB01000001.1.
DR AlphaFoldDB; A0A0G9MXQ5; -.
DR STRING; 1581420.AAW00_03375; -.
DR PATRIC; fig|1581420.6.peg.684; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000053464; 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 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:UP000053464};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 52..349
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 361 AA; 39420 MW; 14CFD34042857540 CRC64;
MAKAATPKAA KGAAAPSADD AADFALRSLQ QALEKQKRFK ADGDDLLHFY EQMLLIRRFE
EKAGQLYGLG LIGGFCHLYI GQEAVAVGLQ SALTEGLDSV ITGYRDHGHM LAYGIDPKVI
MAELTGRAAG ISKGKGGSMH MFSTEHKFYG GHGIVGAQVS LGGGLALAHQ YNDDGGLCLA
YFGDGAANQG QVYETMNMAS LWKLPIVFVV ENNQYAMGTA VKRSSAETEF YRRGTAFRIP
GMEVNGMDVL EVRQAAEIAF AHVRGGNGPV LMECNTYRYR GHSMSDPAKY RTREEVQEQR
DHHDPIERVK KDLTEAGVNE DKLKEIDRAI RATVAEAADF AEQSPEPQAS ELYTDVLVEE
Y
//