ID A0A222FJZ0_9GAMM Unreviewed; 355 AA.
AC A0A222FJZ0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:ASP39365.1};
GN ORFNames=CHH28_12085 {ECO:0000313|EMBL:ASP39365.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP39365.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP39365.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP39365.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-2017) 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}.
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DR EMBL; CP022530; ASP39365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FJZ0; -.
DR KEGG; bsan:CHH28_12085; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000202440; Chromosome.
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};
KW Pyruvate {ECO:0000256|RuleBase:RU366007, ECO:0000313|EMBL:ASP39365.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000202440};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 35..323
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 355 AA; 39323 MW; 19808C1FF38FB34A CRC64;
MESLATVIRY LDDDGQACHE LPLWAHEMEP LLECYRWMVL TRLFDQKAIA LQRTGQCGTY
PSSLGQEAIS VSLGQAMEAE DIFVPYYRDH GTQLMRGCGM HELLLYWGGD ERGSAGGPAQ
DFPICVPIAT QCGHAVGAAR ALQLQNKPQA VVCTLGDGAS SKGDFLEALN LAGVWQLPVV
FVLNNNQWAI SVSRQQQCGA TALALKGIGA GIPSLQVDGN DTIAMMDEVT RALERARSGG
GATLIEAISY RLSDHTTADD ASRYRPDDEV QQAWKREPIA RLKQFLMRQG AWSDALEQQW
QEHCQHAVAA AVKHYLEMPE QPPEAMFDYL YADWPSVLDG QLQTFAERRQ RRLGE
//
