ID   A0A1Q3PYM1_9BACT        Unreviewed;       903 AA.
AC   A0A1Q3PYM1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=BGO32_02260 {ECO:0000313|EMBL:OJV26250.1};
OS   Bacteroidetes bacterium 37-13.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1895921 {ECO:0000313|EMBL:OJV26250.1, ECO:0000313|Proteomes:UP000185627};
RN   [1] {ECO:0000313|EMBL:OJV26250.1, ECO:0000313|Proteomes:UP000185627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37-13 {ECO:0000313|EMBL:OJV26250.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV26250.1}.
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DR   EMBL; MKTC01000027; OJV26250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3PYM1; -.
DR   STRING; 1895921.BGO32_02260; -.
DR   Proteomes; UP000185627; 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          570..763
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   903 AA;  102281 MW;  92A40ECF8579AB25 CRC64;
     MDKYSYLSNA TPEYIENLYL DFKANPASVD VEFKKFFEGF DYASSSANGN GKATSVSLDE
     IKVYKLITDY RDKAHLISTT NPLQPRKDRK ANLELENFGL SEKDLERRFQ IGNEIGLPNA
     TLSEIIAKLK AVYAGNIGFE FGYVRTKEER DWLLERIEKP AQLYNYNIGK KEQIFRALNR
     ASVFEKFLGT KYIGEKRFSL EGGETTIPAL EAIINKSAEL GAEEVIFGMA HRGRLNVLAN
     IIGKTYEEIF NEFEGNIVGD PIFGDGDVKY HLGYTSLFKA AKGKSVYLKL MPNPSHLEAV
     SPVIAGFCRA KANTIYNEHF EKILPIAIHG DAALAGQGII YEVLQMEKLP GYHIGGTLHF
     VINNQIGFTT GFEEARSSDY STSIAATIEA PVFHVNGDDA EATVFVSELA AEYRQTFKKD
     VFVDMVCYRK WGHNESDDPK FTQPLMYQLI DKHVNPRDVY SKVLEQQGKM GADLAKKLEK
     EFWAELQERL DLVKQKPLPY KPQPTEEAWN SLRSATGKDF EQSPETGVKE ATLLALAATM
     NTIPQDFSPL KKMKKYLAER QTLMVEEKRL DWAAGELLAY ASILNDGKDV RFSGEDVERG
     TFTHRHAVIY DENNGNGYNR LSKLSPTQGK FRIYNSHLSE YGVLGFEYGY SMVHPEPLVI
     WEAQFGDFNN GAQIMIDQFI AAAESKWQRC SGLVMLLPHG YEGQGPEHSS ARLERFLQLC
     AELNMVVTNI SSPANYFHAM RRQLAWEFRK PLIVMSPKSL LRHPQCVSDL SEITTGTFRE
     IIADEPQSKN IRRILFCSGK IYFDLKNKQT QKAANDVLIV RIEQLYPIPE KQMQEVVKKY
     PKAEVVWVQE EPLNMGAWSF LIGRLYDVLP MKVVARKNSA SPATGYKKQH LKEQEAILEA
     AFA
//