ID   Q3BVA4_XANC5            Unreviewed;       990 AA.
AC   Q3BVA4;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:CAJ23214.1};
GN   OrderedLocusNames=XCV1578 {ECO:0000313|EMBL:CAJ23214.1};
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN   [1] {ECO:0000313|EMBL:CAJ23214.1, ECO:0000313|Proteomes:UP000007069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10 {ECO:0000313|EMBL:CAJ23214.1,
RC   ECO:0000313|Proteomes:UP000007069};
RX   PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ23214.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3BVA4; -.
DR   STRING; 456327.BJD11_14735; -.
DR   KEGG; xcv:XCV1578; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000007069; 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   ECO:0000313|EMBL:CAJ23214.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          642..835
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   990 AA;  109298 MW;  C3999E7DC79252F6 CRC64;
     MVYPAGQLAD APSLAQGGII FRDLRPTDGA SRPAASAQSS PQQTRLTIVD NLLKQFAQSS
     QLAGGNAAYI EDLYEQYLVA PDSVDPKWKS YFDGFEGRGA GDVPHSAAIA HILTASKQAA
     NAGTGAGASD ERERNVGRLI TAYRARGHLG AQLDPLGLVP PVNPPDLDLP FHSLSQADLD
     SEFSTGGVGG QPRMKLKDLL TRLKATYASS IGAEFMHIQE FDQRQWIYKR LEDAGGKIAG
     DAASRKRTLE RLTAAEGLER YLHTKYVGQK RFSLEGGDSL IPMMDEIIRQ SGNDQVKDIV
     IGMAHRGRLN VLVNTLGKNP RKLFDEFEGK FEHAHDDRAH TGDVKYHMGF SADIAVGTDK
     QVHLALAFNP SHLEIVDPVV VGSVRSRQER FGDAERKSVL PILIHGDAAF AGQGVVMELF
     QMSQARGFAV GGTVHIVVNN QIGFTTSTRD DARSTLYCTD VAKMIGAPVF HVNGDDPDAV
     MFVSKLAYEF RQQFKKDVVI DLVCYRRWGH NEADEPAATQ PVMYQTIRKH KTTRELYAAK
     LESEGVLSAD EAKALVDGYR NKLDSGEYTT ELAKRKPDEF AIDWSKYLVG TAADPVDTRV
     KRDQLDRLAK LITTIPEGVE LHARVAKIYE DRVKMAAGDQ PGDWGFAENL AYATLLAEGH
     KLRLVGQDAG RGTFFHRHAI LHDQKTDDYY LPLRQLVQNP EDATVIDSLL SEEAVMGFEY
     GYSTTDPNAL CIWEAQFGDF ANGAQVVIDQ FIAAGEAKWG RIAGLSLFLP HGYEGQGPEH
     SSARLERFLQ LCALENMLVC VPTTPAQCFH MIRRQMRMTT RKPLVVMTPK SLLRHKLAVS
     SLEELADGQF QHLIPDAKAD AAKVKRVVLC SGKVYYDLLE DQTKRGQDDV AIVRIEQLYP
     FPRAQLAAEL KAYGNATDVV WCQEEPQNQG AWYQIRHHLN FCLAGGQSLH YAGRARSPSP
     AAGHMADHII EQQKLVADAL LNPFNDQVAE
//