ID   D2UDU3_XANAP            Unreviewed;       941 AA.
AC   D2UDU3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:CBA16165.1};
GN   OrderedLocusNames=XALc_1668 {ECO:0000313|EMBL:CBA16165.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA16165.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA16165.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP565176; CBA16165.1; -; Genomic_DNA.
DR   RefSeq; WP_012916166.1; NC_013722.1.
DR   AlphaFoldDB; D2UDU3; -.
DR   STRING; 380358.XALC_1668; -.
DR   GeneID; 57876976; -.
DR   KEGG; xal:XALC_1668; -.
DR   PATRIC; fig|29447.3.peg.1629; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001890; 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:CBA16165.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
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   941 AA;  104281 MW;  24BA2C309B64A802 CRC64;
     MDNLLKQFAQ SSQLAAGNAA YIEDLYEQYL VSPDSIDPKW KTYFDGFQGR DAGDVPHSAV
     IAHIASAARQ AGNSGTGPSG DERERHVGRL ITAYRSRGHL GARLDPLGLT PPINPPDLGL
     PFHSLSESDL GSEFSTGGLG GQPRMKLRDL LARLKATYTG SIGSEFMHIS EFEQRQWIYQ
     RLENVGGQIT ADVASRRRIL ERITAAEGLE RYLHTKYVGQ KRFSLEGGDA LIPLMDVLVQ
     RGGSDAVKDI VIGMAHRGRL NVLVNTLGKN PRKLFDEFEG KFEHAHDDRA HTGDVKYHMG
     FSADVAVANG ASVHLALAFN PSHLEIVDPV VVGSVRSRQE RYGDAARKSV LPVIIHGDAA
     FAGQGVVMEL FQMSQARGFA VGGTVHIVIN NQIGFTTSAR DDARSTLYCT DVAKMIGAPV
     FHVNGDDPDA VAFVANIAYD FRQKFNKDVV IDLVCYRRWG HNEADEPAAT QPVMYQTIRK
     HKTTRELYAA QLESEGVLQP GEGQALVDAY RNKLDSGEYT TELAPRKHDE FAIDWSKYLS
     GKLSDKVNTT VKRKTLDQLA KIITTIPESV ELHPRVAKIY EDRVKMAAGE LPADWGFAEN
     LAYATLLNEG HKLRLVGQDA GRGTFFHRHA ILHDQKNDSY YLPLRQLVQN PEDATVIDSL
     LSEEAVMGFE YGYSTTDPNA LCIWEAQFGD FANGAQVVID QFIAAGEAKW GRIAGLSLFL
     PHGYEGQGPE HSSARLERFL QLCALENMLV CVPTTPAQAF HMIRRQMRMS TRKPLVVMTP
     KSLLRHKLAV SSLKELADGE FQHLIPDSKA EPKKVKRVIA CSGKVYYDLL EDQLKRGQED
     VAILRVEQLY PFPRALLAAE LKRYGNATDL VWCQEEPQNQ GAWYQIKHHL QACLADGQSL
     HYAGRPRSPS PAAGHLAEHL EEQLKLVADA LLNPFNDQVA E
//