SWISSPROT: A0A0F6BI21_GEOS0

ID   A0A0F6BI21_GEOS0        Unreviewed;       360 AA.
AC   A0A0F6BI21;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, 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   OrderedLocusNames=GY4MC1_0223 {ECO:0000313|EMBL:ADP73072.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73072.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73072.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73072.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000256|RuleBase:RU366007}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine
CC         + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111;
CC         EC=1.2.4.1; Evidence={ECO:0000256|RuleBase:RU366007};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={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; CP002293; ADP73072.1; -; Genomic_DNA.
DR   RefSeq; WP_013399876.1; NC_014650.1.
DR   EnsemblBacteria; ADP73072; ADP73072; GY4MC1_0223.
DR   KEGG; gmc:GY4MC1_0223; -.
DR   KO; K00161; -.
DR   OMA; YGMKGVL; -.
DR   OrthoDB; 1248201at2; -.
DR   BioCyc; GSP581103:G1GOQ-266-MONOMER; -.
DR   Proteomes; UP000002034; 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   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF41; PTHR11516:SF41; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE   4: Predicted;
DR   PRODOM; A0A0F6BI21.
DR   SWISS-2DPAGE; A0A0F6BI21.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Glycolysis {ECO:0000256|RuleBase:RU366007};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366007,
KW   ECO:0000313|EMBL:ADP73072.1};
KW   Pyruvate {ECO:0000256|RuleBase:RU366007, ECO:0000313|EMBL:ADP73072.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT   DOMAIN       38    323       E1_dh. {ECO:0000259|Pfam:PF00676}.
SQ   SEQUENCE   360 AA;  39965 MW;  7C75E3AA326DAAAD CRC64;
     MFDQDQLQFE MVQLLDENGN GDEKTLASFS DEFLVALYRW MRKARVIDER LLKMQRQGRI
     GTYAPFGGQE AAQIGSVFAL ESNDWIFPTY REIAACLAHG LPLAQIFRYL RGHLSGGRTP
     EHLNIFPIQI IIGAQTLHAT GCAWATKLKG ETQVSVCYFG DGATSQGDFH EALNFASVYQ
     VPVIFFCQNN QYAISVPVHK QTASRTIAQK AVAYGMKGVL VDGNDALAVY KTVKEAADAA
     RNGGGPVLIE AFTYRLGPHT TSDDPAKYRN AEEAEKWRRK KDPLHRLRVL LEKRGIWTEG
     EEEEWVAQVN GEVTAAYEEA AADGSGSIVD ALSCVYGKPS KLLQEQKQEA ARRKQGKEGK
//