ID Q87DC5_XYLFT Unreviewed; 938 AA.
AC Q87DC5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=odhA {ECO:0000313|EMBL:AAO28629.1};
GN OrderedLocusNames=PD_0760 {ECO:0000313|EMBL:AAO28629.1};
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190 {ECO:0000313|EMBL:AAO28629.1, ECO:0000313|Proteomes:UP000002516};
RN [1] {ECO:0000313|EMBL:AAO28629.1, ECO:0000313|Proteomes:UP000002516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964 {ECO:0000313|Proteomes:UP000002516};
RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E., da Silva A.C., Moon D.H., Takita M.A.,
RA Lemos E.G., Machado M.A., Ferro M.I., da Silva F.R., Goldman M.H.,
RA Goldman G.H., Lemos M.V., El-Dorry H., Tsai S.M., Carrer H., Carraro D.M.,
RA de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T.,
RA Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E.,
RA Abreu I.L., Alves L.M., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S.,
RA Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A.,
RA Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E.Jr.,
RA Sassaki F.T., Sena J.A., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M.,
RA Zaros L.G., Civerolo E.L., Simpson A.J., Almeida N.F.Jr., Setubal J.C.,
RA Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO28629.1; -; Genomic_DNA.
DR RefSeq; WP_011097772.1; NC_004556.1.
DR AlphaFoldDB; Q87DC5; -.
DR GeneID; 58016309; -.
DR KEGG; xft:PD_0760; -.
DR HOGENOM; CLU_004709_1_0_6; -.
DR Proteomes; UP000002516; 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:UP000002516};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 590..783
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 938 AA; 104768 MW; 5B6802DD04C86A3E CRC64;
MDNLIKQFTQ SSPLAGGNAA YIEDLYEQYL VLPNSVDPKW KAYFDGFKGR DAGDIPHSAV
IAHITDTAKQ SVKQGPSDER ERNIGRLITA YRSRGHLGAR IDPLGLTPPS NPPDLDLPFH
NLSQADLDNE FSTGGIGGQP RMKLRNLLAH LKATYTDTIG TEFMHISEFE QRQWIYRRLE
NVGGKIASNA TNRKRILERL TAAEGLERYL HTKYVGQKRF SLEGGDALIP LMDTLVRQAG
NNDVKDIVVG MAHRGRLNVL VNTLGKNPRK LFDEFEGKFE HAHHDRAHTG DVKYHMGFSA
DIAVSDGKQV HLALAFNPSH LEIVDPVVAG SVRSRQERFG DTERKTVLPI LIHGDAAFAG
QGVVMELLQM SQARGFAVGG TLHVIINNQI GFTTSARDDA RSTPYCTDVA KMIGAPVFHV
NGDDPDAVVF VAQLAYEFRQ QFKKDVVIDL VCYRRWGHNE ADEPAATQPV MYQTIRKHKT
TRELYATKLE GEGVIAAGEA KAMVDDYRAK LDSGKFTTEL ASKHTDEFVI DWSKYLSGKL
EDTVKTSVKR QTLNKLAALI NTIPPTVELH PRVAKIYEDR IKMAAGEQPC DWGFAENLAY
ATLLAEGHKL RLVGQDAGRG TFFHRHAILH DQKTDSYYLP LHQLVSNPDD ATVIDSLLSE
EAVMGFEYGY STTDPNTLCI WEAQFGDFAN GAQVVIDQFI AAGEVKWGRI SGLSLFLPHG
YEGQGPEHSS ARLERFLQLC ALENMLVCVP TTPAQAFHMI RRQMRMSTRK PLIVMTPKSL
LRHKLAVSTL DELANGKFQH IIPDDAADPK HVKRIVMCAG KVYYDLFENQ QKRSQNDVAI
IRIEQLYPFP RALLASELKR FNKATDVVWC QEEPQNQGAW YQIKHHLQAV LAHAQRLHYA
GRSSSPSPAV GHMAEHMAEQ ESLVADALLN PFNNHVAE
//
