ID H2IWK0_RAHAC Unreviewed; 935 AA.
AC H2IWK0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Rahaq2_3180 {ECO:0000313|EMBL:AEX52995.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX52995.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX52995.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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; CP003244; AEX52995.1; -; Genomic_DNA.
DR RefSeq; WP_015698113.1; NZ_JMPO01000114.1.
DR AlphaFoldDB; H2IWK0; -.
DR STRING; 745277.Rahaq2_3180; -.
DR GeneID; 61513189; -.
DR KEGG; raq:Rahaq2_3180; -.
DR PATRIC; fig|745277.3.peg.3050; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000009010; Chromosome.
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:UP000009010};
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; 105563 MW; 3DCF9A24BC44D4FA CRC64;
MQNGAMKAWL DSSYLAGANQ SYIEQLYEDY LTDPGSVDDS WRSIFKQLPT VGVKPEQLHS
QTRDYFRRLA KDASRYNSSI SDPQTDAKQV KVLQLINAFR FRGHQNANLD PLGLWKLDDV
PDLDPAFHHL TEADFQETFN VGSFAIGKET MQLGELYKAL KQTYCGSIGA EYMHITNTEE
KRWIQQRIES VAGRASFTLD EKKTFLKELT AAEGLERYLG AKFPGAKRFS LEGGDALVPM
LKEMIRHAGK NGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFSGKHKE HLGTGDVKYH
MGYSSDVETE GGMVHLALAF NPSHLEIVSP VVIGSVRARR DRLDEARSNM VLPITIHGDA
AITGQGVVQE TLNMSLARGY EVGGTVRIVI NNQVGFTTSN PKDARSTDYC TDIAKMVQAP
IFHVNADDPE AVAFVTRLAL DFRNTFKRDV MIDLVCYRRH GHNEADEPSA TQPLMYNKIK
KHPTPRKIYA DVLTEQNVAS LEDATEMVNL YRDALDAGEC VVEEWRQNDM HTFTWSPYLN
HEWDEPYPNK VELKRLQELA RRVSHVPDAI EMQSRVAKIY GDRNEMAEGN KKFDWGGAEN
LAYATLVDEG IPIRLSGEDT GRGTFFHRHA VIHNQKNGSV YVPLANIHNS QGEFNVWDSV
LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CIPSTPAQVY HMIRRQALRG MRRPLIVMSP
KSLLRHPLAV STLDELANGS FLPAIGEVDE LEPKQVKRVV MCSGKVYYDL LEQRRKNEQT
DVAIVRIEQL YPFPHKAIQE VLEKFSHVHD FVWCQEEPLN QGAWYCSQHN FREVIPFGAS
LRYAGRPASA SPAVGYMSVH QKQQQDLVND ALNVK
//
