ID C0R516_WOLWR Unreviewed; 881 AA.
AC C0R516;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:ACN96008.1};
GN OrderedLocusNames=WRi_013360 {ECO:0000313|EMBL:ACN96008.1};
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=66084 {ECO:0000313|EMBL:ACN96008.1, ECO:0000313|Proteomes:UP000001293};
RN [1] {ECO:0000313|EMBL:ACN96008.1, ECO:0000313|Proteomes:UP000001293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wRi {ECO:0000313|Proteomes:UP000001293};
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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 -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR EMBL; CP001391; ACN96008.1; -; Genomic_DNA.
DR RefSeq; WP_012673421.1; NZ_MKIF01000115.1.
DR AlphaFoldDB; C0R516; -.
DR STRING; 66084.WRi_013360; -.
DR KEGG; wri:WRi_013360; -.
DR HOGENOM; CLU_004709_1_0_5; -.
DR Proteomes; UP000001293; 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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 538..731
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 881 AA; 99179 MW; 504671E1ECC19401 CRC64;
MSSLSCLYGD NAEFVEEMYS RYLQGDKSIG EDWNRIFSSN LEVNKAETCG AQHVTKVDDS
VANFFRSYGH FFADLNPLSP NVNKEVDYQK YSNLYPASDA GIYRDIYCKN IGFEFMHISS
YEERMWLQEK IENQTYTLSS QDKKEILRHL IESEMFEQFL HMKFPGYKRF SIEGGESAIV
AIEKIISDST VFGIEEIVLG MAHRGRLNVL TKVMGKEYAA MLSEFQGNLA YPSGLEVSGD
VKYHLGYSSD RALSGGKKIH LSLCPNPSHL EAVNPVLAGR IRAKQNIRSV LGISIHGDAA
FIGQGVVAET LTLSNIEGYR VDGIVHIVIN NQVGFTASPS CARSSFYCTD IAKSIEAPVF
HVNGDNPEAV SFVANLAMEY RQKFKKDVVI DIMCYRKYGH NEGDEPNFTQ PLMYKAISKH
KTPGTLYEEK LTAEKVLDDD EVNKLRSEFR AKLDKSLAES AAYTPKKADW FGGVWSKLRR
AKLNDLSEYY TDSGVPPDEL KKLGVHINSN IPSNFNINNK VRKILDGRID SINSGSNIDW
ATAESLAFAS LLTEGIGVRL SGQDSGRGTF SHRHSRLVDQ VTEEAFIPLN NINEKQAHFE
VIDSALSEYA VMGFEYGYSL DSPYSLVLWE GQFGDFANGA QIMIDQFIAS AETKWLRSSG
LVLLLPHGYE GQGPEHSSAR IERFLQLCAE DNMQVVNCST PANYFHVLRR QMHRDFRKPL
VVFTPKSLLR HKRAVSNLSD FEGKFLTVIP ECRKGLVSSD KVRKVVICSG KVYYDIIEML
ETQKINDIAV IRLEQFYPFP ADKLSNELEK YKNAEIIWCQ EEPKNMGGWF FVNPLIEEVL
SNLNIQAKRP KCIARPAAAS PACGYASVHA QQQEEILRQI A
//
