ID F0C0J8_9XANT Unreviewed; 942 AA.
AC F0C0J8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=XGA_0358 {ECO:0000313|EMBL:EGD20934.1};
OS Xanthomonas hortorum ATCC 19865.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD20934.1, ECO:0000313|Proteomes:UP000005023};
RN [1] {ECO:0000313|EMBL:EGD20934.1, ECO:0000313|Proteomes:UP000005023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD20934.1,
RC ECO:0000313|Proteomes:UP000005023};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD20934.1}.
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DR EMBL; AEQX01000036; EGD20934.1; -; Genomic_DNA.
DR RefSeq; WP_006448692.1; NZ_AEQX01000036.1.
DR AlphaFoldDB; F0C0J8; -.
DR GeneID; 55511107; -.
DR PATRIC; fig|925777.8.peg.5459; -.
DR Proteomes; UP000005023; Unassembled WGS sequence.
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:EGD20934.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 942 AA; 104585 MW; A705CDB821ADCC51 CRC64;
MDNLLKQFAQ SSQLAGGNAA YIEDLYEQYL VAPDSVDPKW KSYFDDFKGR DAGDVPHSAA
IAHILTASKQ AANAGTGAGA SDERERNVGR LITAYRARGH LGAQLDPLGL TPPVNPPDLD
LPFHSLSQAD MDSEFSTGGV GGQPRMKLKD LLARLKATYA STIGAEFMHI QEFDQRQWIY
KRLEDAGGKI AGDAASRKRT LERLTAAEGL ERYLHTKYVG QKRFSLEGGD ALIPMMDEII
RQSGNDQVKD IVIGMAHRGR LNVLVNTLGK NPRKLFDEFE GKFEHAHDDR AHTGDVKYHM
GFSADIAVGT DKQVHLALAF NPSHLEIVDP VVVGSVRSRQ ERFGDAERKT VLPILIHGDA
AFAGQGVVME LFQMSQARGF AVGGTVHIVI NNQIGFTTSA RDDARSTLYC TDVAKMIGAP
VFHVNGDDPD AVMFVSKLAY EFRQQFKKDV VIDLVCYRRW GHNEADEPAA TQPVMYQTIR
KHKTTRELYA NKLESDGVLS ADEAKALVDG YRNKLDSGEY TTELATRKPD EFAIDWSKYL
VGTAADPVDT RVKREQLDRL AKLITTIPEG VELHARVAKI YDDRVKMAAG QQAGDWGFAE
NLAYATLLAE GHKLRLVGQD AGRGTFFHRH AILHDQKNDN YYLPLRQLVE NPEDATIIDS
LLSEEAVMGF EYGYSTTDPN ALCIWEAQFG DFANGAQVVI DQFIAAGEAK WGRIAGLSLF
LPHGYEGQGP EHSSARLERF LQLCALENML VCVPTTPAQC FHMIRRQMRM TTRKPLVVMT
PKSLLRHKLA VSSLEELAEG EFQHLIPDAK ADAGKVKRVV LCSGKVYYDL LEDQTKRDQD
DVAILRVEQL YPFPRAQLAA ELKAYANATD VVWCQEEPQN QGAWYQIRHH LNFCLTGAQS
LHYAGRARSP SPAAGHMADH IVEQQKLVAD ALLNPFNDQV AE
//
