ID A0A1H7VS43_9BACI Unreviewed; 355 AA.
AC A0A1H7VS43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|ARBA:ARBA00014159, ECO:0000256|RuleBase:RU366007};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU366007};
GN Name=pdhA {ECO:0000256|RuleBase:RU366007};
GN ORFNames=SAMN05192533_10168 {ECO:0000313|EMBL:SEM11608.1};
OS Mesobacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=930146 {ECO:0000313|EMBL:SEM11608.1, ECO:0000313|Proteomes:UP000198553};
RN [1] {ECO:0000313|Proteomes:UP000198553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48,IBRC-M 10115,DSM 25386,CECT 8001
RC {ECO:0000313|Proteomes:UP000198553};
RA Varghese N., Submissions S.;
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). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211, 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|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU366007}.
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DR EMBL; FOBW01000001; SEM11608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7VS43; -.
DR STRING; 930146.SAMN05192533_10168; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000198553; 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};
KW Pyruvate {ECO:0000256|RuleBase:RU366007, ECO:0000313|EMBL:SEM11608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198553};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 38..324
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 355 AA; 39352 MW; AFD5AB22E1D9393A CRC64;
MWLEPNETIV NKVQVLDETG KLIGSHPDVN DDELLALYKW MVQARTFDQR ALKLQRQGRI
GTYAPMIGQE AAQVGSAFAL KKQDWIYPSY REVGACLVHG VSMENFFLYT MGHIKGGTSA
QGTNVFPVQI IIGAQCLHAV GSAWASKYKD ESSVSVAYIG DGGTSQGDFH EALNFAGVYK
LPTVFFVQNN QWAISVPRSK QTASATIAQK AAAYGITGIQ VDGNDVLAVY STMKEALRRA
REGKPVLVEA VTYRQGPHTT ADDPTKYRQN GELEQWLAKD PLKRMKAFLI ERGIWNEELE
QVEFETANDK VTKAFEIAAS TPSSKTVEVF DFVYEQKPSQ LAEQQNSIQV EGVVK
//
