ID   A0A2W7S9Q2_9BACT        Unreviewed;       795 AA.
AC   A0A2W7S9Q2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase E1 component {ECO:0000313|EMBL:PZX63749.1};
GN   ORFNames=LX80_01407 {ECO:0000313|EMBL:PZX63749.1};
OS   Hydrotalea sandarakina.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Hydrotalea.
OX   NCBI_TaxID=1004304 {ECO:0000313|EMBL:PZX63749.1, ECO:0000313|Proteomes:UP000249720};
RN   [1] {ECO:0000313|EMBL:PZX63749.1, ECO:0000313|Proteomes:UP000249720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23241 {ECO:0000313|EMBL:PZX63749.1,
RC   ECO:0000313|Proteomes:UP000249720};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PZX63749.1}.
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DR   EMBL; QKZV01000003; PZX63749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7S9Q2; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000249720; 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:PZX63749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249720}.
FT   DOMAIN          471..645
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   795 AA;  89205 MW;  9092EB5837179FFF CRC64;
     MEQTNTAIDT NVLSYEGFRQ QVLNDFKITV ISREASLLGR KEVLTGKAKF GIFGDGKELA
     QVAMARYFQP GDFRSGYYRD QTFMFATGLA TVDQFFSQLY ADPNIENDPF SAGRQMVSHF
     ATPNVDENGN WLDLANRKNI SSDIAPTAGQ MPRSLGLAFA SKCFRNTPVL QQFKHLSNNG
     NEICFCTIGD ASTSEGPFWE TINAAGVLQV PLAVFVWDDG YGISVPREYQ TTKGSISEAL
     QGMQKDEHTN GINIYKVKAW DYAGMCEVFE AALQKVRETH TPALFHVEEV TQPQGHSTSG
     SHERYKSAER LAWEREWDCI KKFREWIVLS GLATDDELNA IAQEAKILVK EARNNAWEKF
     IQPIKVQVQK TAELLNEMVV NDMDVYRTIQ QKVSELQKNI EPLRRDVLHT LHVAMEMAPH
     SPSYNDIQQY YNSLLHENNQ LYNSHLYNEG TASALKVETV KPLIPFDAPV LNGYEILNRY
     FDILFANNPK VLAFGEDVGN IGDVNQGFAG LQAKHGNTRI FDTGIRELTI MGQAIGLALR
     GLRPIAEIQY IDYLLYGLQT LSDDAATTHY RTFGRQSCPV IVRTRGHRLE GIWHSGSPMG
     LVIHALRGFH VCVPRNMVQA VGMYNTLLKG NDPGIVIECL NGYRLKEKLP ANLLEFTVPL
     GVPEIIRPGD DITLVSYGST LRIVEEAAER LAKLNVSCEV LDVQTLLPFD INHDILKSLK
     KTNRILFIDE DVPGGAAAYM FNKVMEEQGG YRWVDVAPRT LTAQAHRPAY GSDGDYFSKP
     NAEDVVRMVL TMMQE
//