ID D6YBA2_THEBD Unreviewed; 324 AA.
AC D6YBA2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:ADG88462.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:ADG88462.1};
GN OrderedLocusNames=Tbis_1749 {ECO:0000313|EMBL:ADG88462.1};
OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS 10125 / KCTC 9307 / NBRC 14880 / R51).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermobispora.
OX NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG88462.1, ECO:0000313|Proteomes:UP000006640};
RN [1] {ECO:0000313|EMBL:ADG88462.1, ECO:0000313|Proteomes:UP000006640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermobispora bispora DSM 43833.";
RL Submitted (JAN-2010) 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; CP001874; ADG88462.1; -; Genomic_DNA.
DR RefSeq; WP_013131995.1; NC_014165.1.
DR AlphaFoldDB; D6YBA2; -.
DR STRING; 469371.Tbis_1749; -.
DR KEGG; tbi:Tbis_1749; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000006640; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ADG88462.1}; Pyruvate {ECO:0000313|EMBL:ADG88462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006640}.
FT DOMAIN 12..315
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 324 AA; 34764 MW; C41BADD9E4D88F82 CRC64;
MEPQVRLELY RTMVLIRTFE EAIRREYHAD KKPVFDIAAG LIPGEMHLAA GQEPVAAGVC
AHLTADDAVT ATHRPHHFAI AHGVNLNRLA AEIFGRVDGL GKGRGGHMHL FDPETHFSCS
GIIAEGYPPA LGQALAFKRR GTDRIAVAVT GEGAANQGAF HESLNLAALW KLPVVFIVED
NDWGISVPRS ASTSVPSNAV RAAAYGIPGE RVEDNSVEAV YRVAGEAIAR ARAGEGPSLI
EVHTVRLWGH FEGDAQGYRP DLAEVAERDP LPIYEAELRR AGVLDDDTVK AIAAEASERV
EAAIAFAKNS PEPDPATALD HVFA
//
