ID A0A2N5EQ84_9GAMM Unreviewed; 935 AA.
AC A0A2N5EQ84;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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=CYR34_05650 {ECO:0000313|EMBL:PLR51749.1};
OS Chimaeribacter arupi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chimaeribacter.
OX NCBI_TaxID=2060066 {ECO:0000313|EMBL:PLR51749.1, ECO:0000313|Proteomes:UP000234626};
RN [1] {ECO:0000313|EMBL:PLR51749.1, ECO:0000313|Proteomes:UP000234626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2016Iso1 {ECO:0000313|EMBL:PLR51749.1,
RC ECO:0000313|Proteomes:UP000234626};
RA Rossi A., Fisher M.;
RT "Characterization of six clinical isolates of Enterochimera gen. nov., a
RT novel genus of the Yersiniaciae family and the three species Enterochimera
RT arupensis sp. nov., Enterochimera coloradensis sp. nov, and Enterochimera
RT californica sp. nov.";
RL Submitted (DEC-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:PLR51749.1}.
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DR EMBL; PJZK01000004; PLR51749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5EQ84; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000234626; 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:UP000234626};
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; 105342 MW; EB1077DD2B1A6DD9 CRC64;
MQNGAMKAWL DSSYLAGANQ SYIEQLYEDF LTDPGSVEDS WRSIFQQLPT AGVKPDQLHS
KTRDYFRRLA KDASRYSAAI NDPDTDAKQV KVLQLINAFR FRGHQQANLD PLGLWKQDEV
PDLDPAYHNL TEADFQETFN VGSFAIGKDT MQLGELYQAL KQTYCGSIGA EYMHITNTDE
KRWIQQRIES AVGRATFSPE EKKRFLKELT AAEGLERYLG AKFPGAKRFS LEGGDALVPM
LKEMIRHAGK NGTREVVLGM AHRGRLNVLI NVLGKKTEEL FDEFAGKHKE HLGTGDVKYH
MGFSSDVETE GGMVHLALAF NPSHLEIVSP VVMGSVRARR DRLDEARSNM VLPITIHGDA
AITGQGVVQE TLNMSQARGY EVGGTVRIVI NNQVGFTTSN PQDARSTQYC TDIAKMVQSP
IFHVNADDPE AVAFVTRLAL DFRNTFKRDV MIDLVCYRRH GHNEADEPSA TQPLMYAKIK
KHPTPRKLYA DRLSETEVAS LEDATEMINL YRDALDRGDC VVEEWRPMNM HSFTWSPYLN
HEWDEPYPST VDMKRLQELA RRISTIPDAI EVQSRVAKIY NDRKEMAEGN KAFDWGGAEN
LAYATLVDEG VPVRLSGEDS GRGTFFHRHA VIHNQKNGAV YVPLANIHNS QGEFRVWDSV
LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLIVMSP
KSLLRHPLAV SSLDELANGT FEPAIGEVDA LDPKQVKRVV MCSGKVYYDL LEQRRKNEQT
NVAIIRIEQL YPFPHQAMQA VLAQYAHVHD FVWCQEEPLN QGAWYCSQHN FREVIPFGAS
LRYAGRAASA SPAVGYMSVH QKQQQDLVND ALNVD
//