GenomeNet

Database: UniProt
Entry: A0A3P3DAF7_9RHOB
LinkDB: A0A3P3DAF7_9RHOB
Original site: A0A3P3DAF7_9RHOB 
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}.
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; 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
//
DBGET integrated database retrieval system