ID J9GVG7_9STAP Unreviewed; 370 AA.
AC J9GVG7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SOJ_20410 {ECO:0000313|EMBL:EJX17752.1};
OS Staphylococcus sp. OJ82.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1202667 {ECO:0000313|EMBL:EJX17752.1, ECO:0000313|Proteomes:UP000006164};
RN [1] {ECO:0000313|EMBL:EJX17752.1, ECO:0000313|Proteomes:UP000006164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ82 {ECO:0000313|EMBL:EJX17752.1,
RC ECO:0000313|Proteomes:UP000006164};
RX PubMed=23105083; DOI=10.1128/JB.01653-12;
RA Sung J.S., Chun J., Choi S., Park W.;
RT "Genome Sequence of the Halotolerant Staphylococcus sp. Strain OJ82,
RT Isolated from Korean Traditional Salt-Fermented Seafood.";
RL J. Bacteriol. 194:6353-6354(2012).
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|ARBA:ARBA00043719,
CC 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}.
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:EJX17752.1}.
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DR EMBL; ALPU01000010; EJX17752.1; -; Genomic_DNA.
DR RefSeq; WP_002508004.1; NZ_ALPU01000010.1.
DR AlphaFoldDB; J9GVG7; -.
DR PATRIC; fig|1202667.3.peg.2040; -.
DR Proteomes; UP000006164; 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|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU366007};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366007};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU366007};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 53..342
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 370 AA; 41424 MW; 8FA0A489E32968F9 CRC64;
MAPKLKAQFD AEKVLKDTES QFEMIQILDE DGNIVNEDLV PDLSDEQLVE LMERMVWTRI
LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALEQEDFI LPGYRDVPQL IWQGLPLTEA
FLFSRGHFKG NQMPEGVNAL SPQIIIGAQY VQTAGVALGI KKRGKSAVAI TYTGDGGSSQ
GDFYEGINFA SAYKAPAIFV IQNNNYAIST PRSKQTAAIT LAQKAIAVGI PGIQVDGMDA
LAVYQATKEA RDRAVNGEGP TLIETITYRY GPHTMAGDDP TKYRTSDEDS EWEKKDPLVR
FRKYLENKGL WTGDKENEVI DRAKSEIKVA IKEADNTEKQ KVTDLMENMY EEMPQHLAEQ
YEIYKEKESK
//
