ID   A0A1I4WLA4_9GAMM        Unreviewed;       961 AA.
AC   A0A1I4WLA4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05216289_105150 {ECO:0000313|EMBL:SFN14591.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN14591.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFN14591.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN14591.1,
RC   ECO:0000313|Proteomes:UP000198575};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOVF01000005; SFN14591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4WLA4; -.
DR   STRING; 578942.SAMN05216289_105150; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000198575; 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:UP000198575};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          612..804
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   961 AA;  105933 MW;  90ECEC7D2551D4FC CRC64;
     MTSSTLLEQF QTTSALSGGN AAFIEELYER WLDDPNAVAP SWNTYFTSLK GRANGEVGHS
     GVIARIEAAQ RSGPKRRAAS SAVDNVEAQK QAGVLKLVTA YRSRGHLAAN LDPLDLANTY
     GQEELEALGL LPRPAAPDLE LAFHGLSNAD LDTEFNTGSL SGPQRLKLRD LIALLKATYA
     TTIGVEFMHI SDASQRQWMH EKMERAGGRF GLSADEKKHL LGKLTQADGL ERYLHTKYVG
     QKRFALEGGD SLIPMLDEML RRGGSAGLKD MVIGMAHRGR LNVLVNILGK PPSKLFDEFE
     GRFEHSEDPA HSGDVKYHMG FSANVRTPGR TVHVALAFNP SHLEIVDPVV AGSVRARQTH
     RADSDREHVV PVLIHGDAAF AGQGVVMELF NMSQANGFCV GGTIHIVVNN QVGFTISNPH
     DARSTLYCTD VAKMVNAPVF HVNGDDPEAV LFVSRLAFDY RQKFKRDVVI DLVCYRRHGH
     NEADEPAATQ PLMYQVIRAR KPLRELYSET LVAEGVLAAA DATAMVDDYR KLLEAGAPIP
     GVDADYHDPH GVDWSKHLAN DIFEVVKTGI SKKSMTAVNA ELLRVPPGIT LHSRVAKIYA
     DRDKMAAGKQ EIDWGFAENL AYGSLVADGY NLRLVGQDAG RGTFFHRHAV MHDQKSGSHH
     VPLKTIRADA SVEVIDSLLS EEAVMAFEYG YATAKPNTLV IWEAQFGDFA NGAQVVIDQF
     ISSGEAKWGR LCGIVLLLPH GYEGQGPEHS SARLERYLQL CAVENMQVCV PTTPAQMFHM
     MRRQMLRAAR KPLIVMTPKS LLRHKMAVSS LDDLVNGRFH LVIPDLTAKN AKKVKRVVFC
     AGKVYYDLVE EAARREISDV AILRVEQLYP FPRTEVKAEL EKYPAAKEVI WCQEEPMNQG
     AWYQIKHHFQ AVVAERHTVA YAGRPRSPAP ACGHLGRHLA EQAALVELAL VSPISSDYAL
     E
//