ID   Q1YT51_9GAMM            Unreviewed;       945 AA.
AC   Q1YT51;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=GB2207_02492 {ECO:0000313|EMBL:EAS47636.1};
OS   gamma proteobacterium HTCC2207.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS47636.1, ECO:0000313|Proteomes:UP000005555};
RN   [1] {ECO:0000313|EMBL:EAS47636.1, ECO:0000313|Proteomes:UP000005555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS47636.1,
RC   ECO:0000313|Proteomes:UP000005555};
RA   Giovannoni S.J., Cho J.-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 (MAR-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:EAS47636.1}.
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DR   EMBL; AAPI01000002; EAS47636.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YT51; -.
DR   STRING; 314287.GB2207_02492; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000005555; 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;  106195 MW;  EF5F41974CDF5075 CRC64;
     MPEGPMEQFL RSSHFSGGNA AYIEDLYDTY LHDRNAVPEQ WSSFFDTLPR TNGSTAPDIS
     HATIVQHFEL LGRRQARPTP APGSGGIHLE HERKQVKVVQ LISSYRFRGH QKANLDPLGL
     MVREHVPDLD LHFHGLTDAD LDTTFQTGPL YFGKQEATLR EIVESLEETY CGSLGAEYMH
     ITSFSEKQWL AQRFESVRSK PTYGDEARVD VLNRLTAAEG LEKHLDSKYP GTKRFGLEGG
     ESLIPLLDCL VRRAGEYGGK EIVMAMAHRG RLNVLVNILG KNPAELFEEF EGKRLVNTSG
     DVKYHQGFSS NVMTPGGEVH MALGFNPSHL EISCPVVIGS GRARQDRRDD KTGEKVVPIL
     MHGDAAFAGQ GVVMETFQLS QTRAYKTGGS IHIVINNQVG FTTSRQEDAR STEYCTDIAK
     MVQAPILHVN GDNPDAVMFA AMLATDYRYE FGKDVVIDLV CYRRRGHNET DEPSSTQPLM
     YDVIRKHSTT RELYSQKLVA EGVVTQDQSN EMSNDYRARL DKGEFVVHNL VREPDTSLFV
     DWEPYLGHDW RTPANTGLKL KNLQDVAAKI IDIPDGIKVQ RQVSKIYDDR RKMAGGALPL
     NWGMAELLAY GTLLDEGYPI RFTGQDVRRG TFSHRHAVVF NQKDGEAYLP LANLSDDQPQ
     FDIYDSVLSE EAVLAFEYGY ATTAPKGLII WEAQFGDFAN GAQVVIDQFI ASGEHKWGRL
     SGLTMLLPHG FEGQGPEHSS ARLERFLQLC AEHNMQVVNP TTPAQIFHLL RRQAIRPMRR
     PLVIMSPKWI LRHKLATSSL EELAGGKFQD VIGENELDAD KVTRVVLCSG KVYYHLLEER
     MARGIDNIAL VRIEQLYPFP DVELEAALKP FTNVKDVIWC QEEPMNQGAW YSSQHHMRHV
     LQGIDPMLHL RYVGRISSAA PACGYMSTHL EEQKQFIDEA LAPDA
//