ID A0A2D0LGB6_9GAMM Unreviewed; 935 AA.
AC A0A2D0LGB6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=Xkoz_00671 {ECO:0000313|EMBL:PHM74739.1};
OS Xenorhabdus kozodoii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351676 {ECO:0000313|EMBL:PHM74739.1, ECO:0000313|Proteomes:UP000221101};
RN [1] {ECO:0000313|EMBL:PHM74739.1, ECO:0000313|Proteomes:UP000221101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17907 {ECO:0000313|EMBL:PHM74739.1,
RC ECO:0000313|Proteomes:UP000221101};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM74739.1}.
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DR EMBL; NJCX01000003; PHM74739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D0LGB6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000221101; 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 593..786
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 105278 MW; 6847E7963DA5E641 CRC64;
MQNGAMKDWL DSSFLAGANQ SYIEQIYEDY ITDPNSVDAS WREIFQQLPD AGLSGEQLHS
QTRDYFRRLA KDATRYHTSV SDPAMDAKQV KVLQLINAFR FRGHQHANLD PLGLWKQEPV
PDLDPAFHNL TKADFEETFN VGSFAIGKET MKLADLYDAL KRIYCGSIGA EYMHITNTEE
KRWIQQRLES VAVSSQFSAE EKRRFLKELT SAEGLERYLG AKFPGAKRFS LEGGDALIPM
LKELIRHAGK QNTREVVLGM AHRGRLNVLV NLLGKKPADL FDEFAGKHKE HLGTGDVKYH
QGFSSDFETE GGLVHLALAF NPSHLEIVSP VVIGSVRARR DRLNEGRSNM VLPVTIHGDA
AVTGQGIVQE TLNMSQARGY EVGGTIRIVV NNQVGFTTSN PKDARSTQYC TDIVKMVQAP
IFHVNADDPE AVAFVTRLAL DFRNTFKRDV MIDLVCYRRH GHNEADEPSA TQPLMYQKIK
KLPTARKIYA DRLVAEGLLG ANDVTEMVNL YRDALDNGGC VVDEWRPMGL HSFTWEPYLD
HEWDEEYPHK MDMKRLQDLG KSISTVPAEV AMHSRVAKIY GDRADMANGN KLFDWGAAET
LAYATLVDEG IPVRISGEDA GRGTFFHRHA VIHDQNNASV YVPLANIHNG QGTFNVWDSV
LSEEAVLAFE YGYATTEPRV LTIWEAQFGD FANVAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLIVMSP
KSLLRHPLAV STMDELANGK FEPVIGEIDG LDPKDVKRVV LCSGKVYYDL LEQRRKNEQT
NVAIVRIEQL YPFPRQHLQA QFEQYAHVHD FVWCQEEPLN QGAWYCSQHN FREAIPFGAS
LRYAGRPASA SPAVGYPSVH QQQQQALVND ALNVE
//