ID   D3PS46_MEIRD            Unreviewed;       344 AA.
AC   D3PS46;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=Mrub_1517 {ECO:0000313|EMBL:ADD28279.1};
GN   ORFNames=K649_14975 {ECO:0000313|EMBL:AGK06281.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS   ruber).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK06281.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:ADD28279.1, ECO:0000313|Proteomes:UP000006655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC   {ECO:0000313|EMBL:ADD28279.1};
RX   PubMed=21304689; DOI=10.4056/sigs.1032748;
RA   Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Meiothermus ruber type strain (21).";
RL   Stand. Genomic Sci. 3:26-36(2010).
RN   [2] {ECO:0000313|EMBL:AGK06281.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK06281.1};
RA   Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA   Eichler E., Turner S.W.;
RT   "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT   Sequencing Data.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGK06281.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC   {ECO:0000313|EMBL:AGK06281.1};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-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}.
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DR   EMBL; CP001743; ADD28279.1; -; Genomic_DNA.
DR   EMBL; CP005385; AGK06281.1; -; Genomic_DNA.
DR   RefSeq; WP_013013781.1; NC_021081.1.
DR   AlphaFoldDB; D3PS46; -.
DR   STRING; 504728.K649_14975; -.
DR   KEGG; mrb:Mrub_1517; -.
DR   KEGG; mre:K649_14975; -.
DR   PATRIC; fig|504728.9.peg.3074; -.
DR   eggNOG; COG1071; Bacteria.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000006655; Chromosome.
DR   Proteomes; UP000013026; 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:AGK06281.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT   DOMAIN          32..318
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   344 AA;  38284 MW;  3296FE3B54086031 CRC64;
     MDTIQYLDDQ GRPLRDLPLS PEELLQGYRA LRRARHFDER VLVLQRQGRL GVYPPFRGQE
     AAQVGVALCL RPDYDWLLPS YRESAAALTF GMPISKLILS WRADPAGWGA PPNVNMVQFY
     IPIATQIPQA AGVAHAQRLM GKDAVVAVFI GDGGTSEGDF HEGLNFAAVF EAPLVVVVQN
     NGWAISVPTY KQTKVQRIAQ KAQGYGIPGV TVDGNDLVAV WSVAREAVNR ARAGGGPTLI
     EALTYRVAPH TSSDDPSRYR SEEETERWLK RDPILRMKNC LLHLGLWSEA QEEALTEALE
     AEFLAAVEEA DRAPEPKPWE IVEQVYQKMQ PDQQAAWKYL RGEA
//