ID   A0A1S9ZL36_9GAMM        Unreviewed;       948 AA.
AC   A0A1S9ZL36;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=B0180_04725 {ECO:0000313|EMBL:OOR84235.1};
OS   Moraxella canis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR84235.1, ECO:0000313|Proteomes:UP000190322};
RN   [1] {ECO:0000313|EMBL:OOR84235.1, ECO:0000313|Proteomes:UP000190322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR84235.1,
RC   ECO:0000313|Proteomes:UP000190322};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Moore E.;
RT   "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
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:OOR84235.1}.
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DR   EMBL; MUXT01000005; OOR84235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9ZL36; -.
DR   Proteomes; UP000190322; 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          597..790
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   948 AA;  105746 MW;  16B05071FB08CB31 CRC64;
     MTNSKDTVAF SNTELAADSA AYVEALYEQY MADSQSVSEE WQKYFETYRQ DTDAPHNAIK
     EQFLLLARNQ AAAGQAGPSS DCNPKQMAVQ ALISAYRRRG HRKANLDPLG LHPRPEVEDL
     TLAFHGLSES DLDTVFPTND LAIGKSEAKL REIIEILERV YCQSIGYEYM HVFKAAEKRW
     IENYIESNHG HIKFSKDKKL EILERLTAAE GLEKYLARKY TGVKRFGLEG GESFIPAVHE
     IVQRAGGQGS KEVVIGMAHR GRLNLLVNIL GKNPGDLFDE FDGKVQPVNG SGDVKYHNGF
     SSNVMTPGGE MHLALAFNPS HLEIVSPVLQ GSVRARQARR SEKYGLEIDN STVLPLVVHG
     DAALAGQGVN QETFQMSQTR AYKTGGTVHI VINNQVGFTT SRIEDARSTE YCTDVAKMVH
     APILHVNGDD PEAVVFASQL AVDYRREFGK DVMLDIFCYR RNGHNESDEP SATQPLMYAV
     IKKLPTTRTQ YVEQLVQEGI ITHEQGAQFE DDYRESLDRG EFVAGGLVSE PNTELFVDWK
     PYLGHDLEDD WETGVDIEKL KSYGRAMAKI PEGFTLQRQV AKVVEQRLAM QTGEEPLNWG
     AAETLAYASL AAEGSLVRIT GEDVGRGTFS HRHSELYNMN DGSMYIPLQH ITEDQARFAT
     YNSLLSEEAV LAFEYGYATT VPNALIIWEA QFGDFVNGAQ VVIDQFISSG ETKWQRVCGL
     TMLLPHGFEG QGPEHSSARL ERFLQLCAED NMQVITPTTP AQIFHALRRQ VVRPIRKPLI
     VMSPKSLLRH PLATSNLEEL ASGKFETVLP EIDSINNEKV TRLVLCGGKV YYDLLDQRRK
     LGQEHIAIVR IEQLYPLPEE RILAEIDKYP NLEEIMWAQE EPLNQGAWYY LAPELFRMVV
     PAPTKAKIIP PSARPAAAAP ATGSPKLHAE QQKALIAEAL GVTVEALK
//