ID   A3Y7N9_9GAMM            Unreviewed;       945 AA.
AC   A3Y7N9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=MED121_12895 {ECO:0000313|EMBL:EAQ66825.1};
OS   Marinomonas sp. MED121.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ66825.1, ECO:0000313|Proteomes:UP000003436};
RN   [1] {ECO:0000313|EMBL:EAQ66825.1, ECO:0000313|Proteomes:UP000003436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED121 {ECO:0000313|EMBL:EAQ66825.1,
RC   ECO:0000313|Proteomes:UP000003436};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) 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:EAQ66825.1}.
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DR   EMBL; AANE01000002; EAQ66825.1; -; Genomic_DNA.
DR   RefSeq; WP_009831773.1; NZ_CH672429.1.
DR   AlphaFoldDB; A3Y7N9; -.
DR   STRING; 314277.MED121_12895; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000003436; 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          600..793
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   945 AA;  106085 MW;  4D1959F478FDB8C9 CRC64;
     MHESLMELLW STSHFSGGNL EYIEGLFESY LVDPNSVSEE WRKCFDQLPR VSEGQSTDVP
     HSVVQEQFLQ LAKNKYRFQP AAVSAAVSSG HEQKQIKVLQ LISAYQMRGH QHANLDPLGL
     QGRNQVPDLD LAFHQLTGAD LDEEFSTGPL FFSKDVMKLK DIIAGLEKTY CSSIGYEFMY
     LVDTQEKRWI QQRVESSLSD PQYSNETRKS LLERLTAAEG LEKYLGSRYP GAKRFGLEGA
     ESLIPMMNEL IQRSGALGAK EVVIGMAHRG RLNVLVNTLG KNPKDLFDEF EGKKLVNTSG
     DVKYHQGFSS NVVTDGGEVH IALSFNPSHL EIVSPVVEGS VRARQDRRND TTGKTVVPIS
     IHGDSAFAGQ GVVMETFQMS QTRGYKTGGT VHIVVNNQVG FTTNRQEDVR STQYSTDVAK
     MIQAPIFHVN GDDPEAVLFV TQLALDYRYE FGRDVVIDLV CYRRRGHNET DEPSGTQPLM
     YQVINKLKTT RTQYADKLVG LGVVSKAEEK QLVDENREDL DNGRHVSKSL VLESQTGSFV
     DWTPYIGADW TDEGDTTYPL AKLQELAKKL TQIPDGIVVQ RQVQKIYQDR DKMTAGALPI
     NWGYAETLAF ATLLEQDFPL RITGQDSGRG TFSHRHAVIH SQKDGSSYIP LKHLSEGQPP
     LDLYDSYLSE EAVLAFEYGY ATTSPKGMVI WEAQFGDFAN GAQVVIDQFI TSGEHKWGRL
     CGLTMLLPHG YEGQGPEHSS ARLERYMQLC AEFNIQVCVP TTPAQIYHIL RRQAIRPMRR
     PLIILSPKSL LRHKQAISSL EDLSEGSFKT VLPDSSSKAD PADVKRLVIC SGKIYYDLIN
     RREELAKDDV AVIRLEQLYP FPYKDFETVL APYKNVESLV WCQEEPKNQG AWHANRHRMN
     RVLEALYPQL KIRFAGRISS AAPAAGYMSI HIEEQEALVN DAIQG
//