ID   A0A1T5P2L1_9BACT        Unreviewed;       800 AA.
AC   A0A1T5P2L1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:SKD06559.1};
GN   ORFNames=SAMN05660461_3474 {ECO:0000313|EMBL:SKD06559.1};
OS   Chitinophaga ginsengisegetis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD06559.1, ECO:0000313|Proteomes:UP000190166};
RN   [1] {ECO:0000313|EMBL:SKD06559.1, ECO:0000313|Proteomes:UP000190166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD06559.1,
RC   ECO:0000313|Proteomes:UP000190166};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUZZ01000002; SKD06559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5P2L1; -.
DR   STRING; 393003.SAMN05660461_3474; -.
DR   Proteomes; UP000190166; 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; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SKD06559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190166}.
FT   DOMAIN          476..650
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   800 AA;  89513 MW;  6A95AEBF55983D22 CRC64;
     MIENNELAMN LESRLSFEEF RKEVLNDYRL ACESREVSLL ARKEVLTGKA KFGIFGDGKE
     VAQIAMSKYF QPGDFRSGYY RDQTVAFATG IATPEQFFSQ LYADPDLEND PFSGGRQMNS
     HYATPNLDQD GNWLNLTQMK NSAADMAPTA GQMPRALGLA YASKMFREVE ALHSYKNLSN
     NGNEICFATI GDASTSEGHF WETMNAAGVL QVPLAVFVWD DGYGISVPRK YQTTKGSISA
     ALEGFRKTEE SNGFDIYNVK GWDYAGMCEV FEAAIRKIRE THIPALFHVE EITQPQGHST
     SGSHERYKSK ERLSWEREFD CNVKMRSWII ENALCEEETL RAVEAEAKVK AQNARKAAWE
     KYITPIKEQV QSFTALAAPV AAIEGADANM INTFIRDLQN NREPLRRDIL KASAMILLKH
     RHLKSDAAIQ ALQQYYDTYL AGEKEVYNTL LHATGVNSAL NVPVVPAAYE ADSITVNGYE
     ILNKYFDQLF TNNDRVFAFG EDVGKIGDVN QGFAGLQQKH GKVRIADTGI RELTIMGQGI
     GLALRGLRPI AEIQYLDYLL YGLQPLSDDV ASLQYRTKGI MHCPLIVRTR GHRLEGIWHS
     GSPMGMIINS LRGMHVCVPR NMVQAAGMYN TLLQANEPAL VIESLNGYRL KEKLPANLET
     YTVPLGIPEI LHEGTDVTIV TYGSMTRIVE EAMVTLAETG ISCELIDVQT LLPFDIHHSI
     VESLQKTNRI LFIDEDVPGG GTAYMFQQVI EKQGGYRWLD VSPRTMSAQA HRPAYGSDGD
     YFSKPNTEDV VKVIMEMMQE
//