ID   E1SH12_PANVC            Unreviewed;       935 AA.
AC   E1SH12;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:ADO08753.1};
GN   OrderedLocusNames=Pvag_0548 {ECO:0000313|EMBL:ADO08753.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08753.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO08753.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO08753.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
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; CP002206; ADO08753.1; -; Genomic_DNA.
DR   RefSeq; WP_013357145.1; NC_014562.1.
DR   AlphaFoldDB; E1SH12; -.
DR   KEGG; pva:Pvag_0548; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006631; 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:ADO08753.1};
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;  105061 MW;  A5F20F4CE5CEB8D6 CRC64;
     MQNSAMKPWL DSSWLAGANQ SYIEQLYEDF LTDPDSVDAV WRSMFQQLPG TGMKPEQFHS
     TTREYFRRLA KDASRYTSSV SDPETNSKQV KVLQLINAFR FRGHQHANLD PLGLWKQDRV
     ADLDPAFHDL TEADFQESFN VGSFAIGKET MKLADLFDAL TQTYCGSIGA EYMHINNTDE
     KRWIQQRLES VAGRAAFSNE EKKGFLKELT AAEGLEKYLG AKFPGAKRFS LEGGDALVPM
     LREMIRHAGK SGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFAGKHKE HLGTGDVKYH
     MGFSSDVETE GGLVHLALAF NPSHLEIVSP VVMGSVRARL DRLDEPASNK VLPITIHGDA
     AVIGQGVVQE TLNMSQARGY EVGGTVRIVI NNQVGFTTSN PKDARSTPYC TDIGKMVLAP
     IFHVNADDPE AVAFVTRLAL DYRNTFKRDV FIDLVCYRRH GHNEADEPSA TQPLMYQKIK
     KHPTPRKIYA DRLEGEAVAT QEDATEMVNL YRDALDAGEC VVPEWRPMSL HSFTWSPYLN
     HEWDEPYPAQ VDMKRLKELA LRISQVPEEV EVQSRVAKIY NDRRLMAEGE KAFDWGGAEN
     LAYATLVDEG IPVRLSGEDT GRGTFFHRHA VVHNQANGST YTPLHHVHSG QGQFKVWDSV
     LSEEAVLAFE YGYATAEPRI LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
     PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLIVMSP
     KSLLRHPLAI STLDELANGS FQPAIGEVDN LDAQGVKRVV LCSGKVYYDL LEQRRKNEQT
     DVAIVRIEQL YPFPHHAVQE ALQAYSHVQD FVWCQEEPLN QGAWYCSQHH FREVVPFGAT
     LRYAGRPASA SPAVGYMSVH QQQQQDLVND ALNVN
//