ID   A0A0Q5TUK4_9BACT        Unreviewed;       920 AA.
AC   A0A0Q5TUK4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=ASG33_09000 {ECO:0000313|EMBL:KQS34139.1};
OS   Dyadobacter sp. Leaf189.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS34139.1, ECO:0000313|Proteomes:UP000051810};
RN   [1] {ECO:0000313|EMBL:KQS34139.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS34139.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS34139.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS34139.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS34139.1}.
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DR   EMBL; LMPS01000001; KQS34139.1; -; Genomic_DNA.
DR   RefSeq; WP_056282827.1; NZ_LMPS01000001.1.
DR   AlphaFoldDB; A0A0Q5TUK4; -.
DR   STRING; 1736295.ASG33_09000; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000051810; 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   Reference proteome {ECO:0000313|Proteomes:UP000051810};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          586..779
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   920 AA;  104937 MW;  AEA3550E5B2CB4B1 CRC64;
     MDKYTYIANS DAAYIEELYN SYKQDATSVD EGWQKFFEGF DFYQKYPVNG NGHTNGAAAG
     KEAATVGKSD PGRIRKEMEV VHLIRGYRSR GHLMATTNPI QKRKDRRPQL DISDFNLGLE
     DLDTVFEAGV EVFGRPASLR EIVESLKTIY TRNIGFEYLY IRDREQKSWL RKKIEKEALN
     MDFSIDEKKH ILSKLNEAVV FENFLHTKYL GQKRFSLEGG ETTIPALDAM INKAAEMGVV
     EVMIGMAHRG RLNVLANVMQ KTYGQIFNEF EGNLPDQVWG DGDVKYHMGF ASQITTKDGH
     KVHMKLAPNP SHLEAVNPVV EGYIRARADG MYDSDYDRVL PVLIHGDAAV AGQGIVYEVT
     QMSALNGYYT GGTIHFVINN QVGFTTDFID ARSSIYCTDI AKIVDAPVLH VNGDDPEAVV
     FCMRLAVEYR QKFNKDIFID MVCYRRHGHN EADEPKFTQP VLYKSIETHQ NPREIYQKTL
     ADRGDVDAQL AANMDKEFKQ LLQERLDMVK QKALPYTLPK LEQEWHTLRK SKPEDFEKSP
     ETGVPLDILE KIGKALISTP ENFNRLKQID KLLKDREQMI FDKKEVNWAT AELLAYGSIL
     TEGNIVRLSG QDVQRGTFSH RHAVLRDVET NAAYNSLQHI QEGQGQFMIY NSLLSEYGVL
     GFEFGYSMAN PNALVIWEAQ FGDFANGTQV IIDQFVTSSE TKWDRWTGLV MLLPHGYEGQ
     GPEHSNARPE RYLQLSANYN IIVANVTTPA NFFHLLRRQL KFPFRKPLIV MSPKSMLRHP
     LCVSPIDSLV SGSFQETIGD TYADPKKVKK VLLCTGKLYY ELYEKQQAEK RDDVAIIRLE
     QMHPFPQTQI DAHLNQYPDA KVYWVQEEPF NMGGWTFMLR MYKGAKPLQV IARESSASPS
     TGFAKIHAKE QAEIIRRAFE
//