ID   A0A1I3QA41_9BACL        Unreviewed;       332 AA.
AC   A0A1I3QA41;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:SFJ29986.1};
GN   ORFNames=SAMN05421852_10754 {ECO:0000313|EMBL:SFJ29986.1};
OS   Thermoflavimicrobium dichotomicum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Thermoflavimicrobium.
OX   NCBI_TaxID=46223 {ECO:0000313|EMBL:SFJ29986.1, ECO:0000313|Proteomes:UP000199545};
RN   [1] {ECO:0000313|EMBL:SFJ29986.1, ECO:0000313|Proteomes:UP000199545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44778 {ECO:0000313|EMBL:SFJ29986.1,
RC   ECO:0000313|Proteomes:UP000199545};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FORR01000007; SFJ29986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3QA41; -.
DR   STRING; 46223.SAMN05421852_10754; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000199545; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SFJ29986.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199545}.
FT   DOMAIN          28..323
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   332 AA;  36813 MW;  0BCE62840FA85227 CRC64;
     MGQLLQFFEL GEQTWHGDQR KAEEAWRTMN LIRAFEEKCI ELYKQGLMGG SLHSYIGQEA
     VATGVCMNLN TDDYITISYR GRGQAIAKGA DPYKLFAEML GRKDGYCKGK GGPMHIACRE
     LGILGANGIV GAGIPIAVGA ALTAKNKKTG QIALTFFGDG ATNQGAFHEA LNLAAVLKLP
     VVFVCENNLY AEMTPIKHST LNEDLAERGA AYRIPSIVVD GNDVRAVHEA TKTAVDRARS
     GEGPTLIEAK TYRLVGHMFG DPETYRTKEE VAEWRQKEPI KRFRQVCLDE KLLDEDRLDE
     IQNQIYKEID TVAKRAMEAD QPGMEEIFTD VY
//