ID A0A3P3DAF7_9RHOB Unreviewed; 329 AA.
AC A0A3P3DAF7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ECO:0000313|EMBL:RRH69368.1};
GN ORFNames=EG244_18395 {ECO:0000313|EMBL:RRH69368.1};
OS Falsigemmobacter faecalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Falsigemmobacter.
OX NCBI_TaxID=2488730 {ECO:0000313|EMBL:RRH69368.1, ECO:0000313|Proteomes:UP000282125};
RN [1] {ECO:0000313|EMBL:RRH69368.1, ECO:0000313|Proteomes:UP000282125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102744-1 {ECO:0000313|EMBL:RRH69368.1,
RC ECO:0000313|Proteomes:UP000282125};
RA Li G., Jiang Y.;
RT "Gemmobacter sp. nov., YIM 102744-1 draft genome.";
RL Submitted (NOV-2018) 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:RRH69368.1}.
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DR EMBL; RRAZ01000044; RRH69368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3DAF7; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000282125; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 23..320
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 329 AA; 36451 MW; 0C7DD2DAB0EA7DDB CRC64;
MATRKSPEKA NVSKDELLKY YRDMLLIRRF EEKAGQLYGM GLIGGFCHLY IGQEAVVVGL
EASTKEGDKR ITSYRDHGHM LACGMEANGV MAELTGRIGG YSKGKGGSMH MFSKEKHFYG
GHGIVGAQVP LGAGLAFADK YLGNDNVTFT YFGDGAANQG QVYETYNMAE LWDLPVIFVI
ENNQYAMGTS MQRATKSTTL YERGLAYGIP GEQVDGMDVL AVKAAGEKAV AHCRAGKGPY
ILEMMTYRYR GHSMSDPAKY RTREEVQKMR DERDAIEQVR DLLLTGGHAT EDDLKQIDRD
IKTIVNASAE FSKDSPEPPV DELWTDIYA
//