ID   A0A1F3H1M9_9BACT        Unreviewed;       907 AA.
AC   A0A1F3H1M9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=A2W86_10245 {ECO:0000313|EMBL:OFX85006.1};
OS   Bacteroidetes bacterium GWD2_45_23.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797330 {ECO:0000313|EMBL:OFX85006.1, ECO:0000313|Proteomes:UP000178053};
RN   [1] {ECO:0000313|EMBL:OFX85006.1, ECO:0000313|Proteomes:UP000178053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFX85006.1}.
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DR   EMBL; MENT01000013; OFX85006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3H1M9; -.
DR   Proteomes; UP000178053; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          571..764
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   907 AA;  103528 MW;  F6F81615FCD6C48A CRC64;
     MNDQNEFSTM DIEAIEALYQ KYKEDPDNVD ESFRYFFQGF DLATSHFPVK PMDGKTALEH
     SPKELSVMRL ITAYRRRGHL FTKTNPVRTR RSYTPTLEIE NFDLTQDDLN TLFEAGKEIG
     IGRASLKDIV DHLDETYCKS IGVEYRYMTK PEVVKWLQEK MESSRNQESF SNEAKLRILD
     RLVEASGFED YLHKKFVGQK RFSLEGSESI IPALDAILAQ GRDYEVNEIV IGMAHRGRLN
     VLTNIMEKPY SQIFREFNAQ NYEEEIKYGD VKYHLGYDNI IDYEGRSISV SLAPNPSHLE
     AVGPVMEGIA RARLENEHAY HYEEVLPILV HGDAAIAGQG VVYETIQFSK LEGYKTGGTI
     HIVINNQVGF TTNYLQARSS TYCTDVAKVT QSPVFHVNGD DIEAMVYVAK LALEFRQKFH
     IDVFIDLLSY RKYGHNEGDE PRFTQPELYD IIARHKNPRD IYAEKLMKEG VLTPQAFESR
     LSDFHQLLEK AYEESQATSS LNLHLFLANR FPEIRLPEAG DFESPSDTAV SKELFLQLTK
     SITALPEDKK FFNKTIRLFQ QRAAMIEADA YDWAMGELMA YATLAWEKHS VRLSGQDSER
     GTFSHRHAEI ITEDGKEKYF PLKNLGGEQE PVRVYNSPLN EYGILGFEYG YSLAHPDGLT
     VWEAQFGDFY NVGQVIVDQY ISAAQEKWGL KSGLVMLLPH GYEGQGAEHS SGRLERFLSL
     CANLNMQVVN CTTPANFFHA LRRQLHRDIR VPLIVFTPKS LLRHPACISS LADFTEGGFR
     EVMEDVQHDE YTKVKRILLC TGKIYYELEA ARKETQTADV SIIRIEQLYP FPDKQLRNLL
     NRYAANVELV WVQEEPANMG AANYMKEYLS DLALQVISRP ASGVTAEGLT ALHKINQALI
     INQALSV
//