ID   A0A1T4KTM9_9BACT        Unreviewed;       792 AA.
AC   A0A1T4KTM9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:SJZ45795.1};
GN   ORFNames=SAMN04488128_101297 {ECO:0000313|EMBL:SJZ45795.1};
OS   Chitinophaga eiseniae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=634771 {ECO:0000313|EMBL:SJZ45795.1, ECO:0000313|Proteomes:UP000190367};
RN   [1] {ECO:0000313|EMBL:SJZ45795.1, ECO:0000313|Proteomes:UP000190367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22224 {ECO:0000313|EMBL:SJZ45795.1,
RC   ECO:0000313|Proteomes:UP000190367};
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; FUWZ01000001; SJZ45795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4KTM9; -.
DR   STRING; 634771.SAMN04488128_101297; -.
DR   Proteomes; UP000190367; 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:SJZ45795.1}.
FT   DOMAIN          468..642
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   792 AA;  88637 MW;  4796E123E3FECE78 CRC64;
     MNIESRLSFE EFRKEVLNDY RLACESREVS LLARREVLTG KAKFGIFGDG KEVAQVAMSK
     YFKPGDFRSG YYRDQTVAFA TGIATPEQYF SQLYADPDQQ HDPFSGGRQM NSHFATPNLD
     KDGNWLNLME MKNSAADMAP TAGQMPRAVG LAYASKMFRE VEALHDLKHL SDNGNEICFA
     TIGDASTSEG HFWETMNAAG VLQVPLAVFV WDDGYGISVP RKYQTTKNSI SAALEGFRKT
     DGTNGFDIYN VKGWDYAGMC EVFEAAIRKI RETHIPALFH VEEITQPQGH STSGSHERYK
     SKERLSWEKE FDCNLKMRSW IMENALCDEE TLVKIEADAK TTAQNARKAA WEKYITPIKE
     EVQQFIALAT PVSTVAGANA ELVAQQLREL QANREPQRRD ILKTAATILL RHRQLKGEHA
     IQTLQQYYDQ YLQAEKENYS SLLHAVGANS VHNVPVVPVE YNDDATTLNG YEVLNKYFDQ
     LITNNPKVFA FGEDVGKIGD VNQAFAGLQQ KHGPLRITDT GIRELTIMGQ GIGMALRGLR
     PIAEIQYLDY VLYGLQPLSD DVASLQYRTK GIQHCPIIVR TRGHRLEGIW HSGSPMGMII
     HALRGMNVCV PRNMVQAAGM YNTLLQANEP ALVIESLNGY RLKEKLPSNL GTFTVPMGVP
     EVLKEGADVT LVTYGSMTRI VEEAMVTLEE LGISCELIDV QTLLPFDIHH SIVESLKKTN
     RIAFIDEDVP GGGSAFMFQQ VMEQQGGYRW LDVAPRTLSA QAHRPAYGSD GDYFSKPNAE
     DVVKMVIEMM EE
//