ID A0A1G9NPD8_9RHOB Unreviewed; 331 AA.
AC A0A1G9NPD8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04488026_11267 {ECO:0000313|EMBL:SDL88448.1};
OS Aliiruegeria lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=571298 {ECO:0000313|EMBL:SDL88448.1, ECO:0000313|Proteomes:UP000199382};
RN [1] {ECO:0000313|EMBL:SDL88448.1, ECO:0000313|Proteomes:UP000199382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25294 {ECO:0000313|EMBL:SDL88448.1,
RC ECO:0000313|Proteomes:UP000199382};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEK01000126; SDL88448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9NPD8; -.
DR STRING; 571298.SAMN04488026_11267; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000199382; 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:UP000199382};
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 331 AA; 36680 MW; AFDCC26E1C928830 CRC64;
MAARRTTKKP NVSKEELLGY YKDMLLIRRF EEKAGQLYGM GLIGGFCHLY IGQEAVVVGL
EAATEEGDKR ITSYRDHGHM LACGMDPKGV MAELTGREGG YSKGKGGSMH MFSKEKHFYG
GHGIVGAQVP LGAGLAFADK YNENGRVTFT YFGDGAANQG QVYETFNMAA LWQLPVIFVI
ENNQYAMGTS QQRSTSSQEI YKRGEAFGIP GEAVDGMDVL AVKAASEKAV AHCRSGKGPY
ILEVKTYRYR GHSMSDPAKY RTREEVQKMR DERDPIEGVR QLLLTGKHAT EEELKAVDKE
IKDIVNESAE FSKQSPEPAL EELWTDIYAE A
//
