ID A0A091BD91_9GAMM Unreviewed; 357 AA.
AC A0A091BD91;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU366007};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU366007};
GN Name=pdhA {ECO:0000256|RuleBase:RU366007};
GN ORFNames=N790_11575 {ECO:0000313|EMBL:KFN42370.1};
OS Arenimonas malthae CC-JY-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1384054 {ECO:0000313|EMBL:KFN42370.1, ECO:0000313|Proteomes:UP000029392};
RN [1] {ECO:0000313|EMBL:KFN42370.1, ECO:0000313|Proteomes:UP000029392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-JY-1 {ECO:0000313|EMBL:KFN42370.1,
RC ECO:0000313|Proteomes:UP000029392};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas malthae.";
RL Submitted (SEP-2013) 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). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|RuleBase:RU366007}.
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:RU366007};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU366007};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|RuleBase:RU366007}.
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:KFN42370.1}.
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DR EMBL; AVCH01000200; KFN42370.1; -; Genomic_DNA.
DR RefSeq; WP_043805027.1; NZ_AVCH01000200.1.
DR AlphaFoldDB; A0A091BD91; -.
DR STRING; 1384054.N790_11575; -.
DR PATRIC; fig|1384054.3.peg.2507; -.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000029392; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|RuleBase:RU366007};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366007}; Pyruvate {ECO:0000256|RuleBase:RU366007};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 41..325
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 357 AA; 39683 MW; 0E3D2B2612A69932 CRC64;
MSTVATFEIE YLQYLGQDGR LVREDLPEFA RDRRNLVELF KQMLLVRTFD TKAVALQRTG
KLGTYASCLG HEAAHIGIGS AMQYDDVFAP SYREYGAQFM RGVKPRDVLM YWGGDERGND
FSGPPHDYPW CVPIATQCLH AAGAALAFKL RGEPRVAVTC VGDGGSSKTD TYAAINSAGA
YSLPFVLCII NNQWAISVPR KSQTGAKTLA QKGLAGGLDC VQVDGNDIIA VRAAMDHALK
RARNGHGGSV LELVTYRLSD HTTADDARRY RDDAEVKAAW EREPMSRLRT FLINDGMWSE
AEEAAWKEEC GKRVDEEVNA YLETKVQPVE AMFDYLYAEL PADYEAQRAD AIKWEGR
//
