ID   A0A3N4MT01_9BACT        Unreviewed;       915 AA.
AC   A0A3N4MT01;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=EG028_05700 {ECO:0000313|EMBL:RPD42659.1};
OS   Chitinophaga barathri.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD42659.1, ECO:0000313|Proteomes:UP000279089};
RN   [1] {ECO:0000313|Proteomes:UP000279089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA   Zong Y.;
RT   "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL   Submitted (NOV-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:RPD42659.1}.
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DR   EMBL; RMBX01000002; RPD42659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4MT01; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000279089; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:RPD42659.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279089};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          580..773
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   915 AA;  103033 MW;  F609049A1D90D824 CRC64;
     MKDFSFVTNS HPAYIESLYQ QYRADASSVD PEWIKFFEGF DFAVSTTNGK AAAPASGASS
     LPVSSDQLVK ELGVFRLIQA YRKKGHLIAK TNPIRERKDR QPNLDLKFFG LADADLKTEF
     FAGQVIGLGK APLEKIVQHL QEVYASKVGL EFTYINDAAR MEWLQKEMET TIRKPLTVDQ
     KKRILSKLNQ GVMFEKFLHT KYIGQKRFSL EGGETTIPAL DAMISTAAEY GVQEAVIGMA
     HRGRLNILAN ILGKTYEQIF SEFEGTAIPD TTMGSGDVKY HLGFRASIQT PAGKEVNVQL
     TPNPSHLEVV DPVVIGFSRS KADVIYNSDY DKILPILIHG DAAVAGQGVV YEVAQMSKLK
     GYYTGGTMHF VINNQIGFTT DFEDARSSDY CTSVASIVQA PVFHVNGDDV EATVKVAEIA
     TRYRQEFNSD IYIDMVCYRK HGHNEGDDPK FTQPKLYSAI DKHPNPREIY SQQLIANGDV
     DAALATEMEK TFWADLQERL DDIKQHPLPY KYQTPDLWWK ELRKSTPEDF AASPATAIPQ
     ADLDQLFAAI MAIPQGFKPL RKVEKLLQDK QKLFTEQGLL DWASGELLAY ASILKDGRDV
     RLSGQDVKRG TFSHRHAVLR NEETDEEYSR LSNLSDTQGK FRIYNSLLSE FAVLGFEYGY
     SIANPYALTI WEAQFGDFMN GAQTLIDQFI TSAETKWQKQ SGLVLLLPHG YEGQGPEHSS
     ARLERFLQQC AEQNIFVTNC TTAASFFHAL RRQLAWPFRK PMINFSPKAN LRHVRSYSPV
     ADFVQGGFKE VLDDPFITDA SRVKKVLLCS GKMYFDLSEK QMKEDRKDVA IVRMEQLYPL
     PVGQLEAIQQ KYKGATWFWV QEEPLNMGAA GFLQMNLKQF NYGVISRNPS AATATGYSKV
     HAQEQQEIID TAFNI
//