ID Q8PAJ6_XANCP Unreviewed; 990 AA.
AC Q8PAJ6;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 101.
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:AAM40783.1};
GN OrderedLocusNames=XCC1487 {ECO:0000313|EMBL:AAM40783.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM40783.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM40783.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM40783.1; -; Genomic_DNA.
DR RefSeq; NP_636859.2; NC_003902.1.
DR AlphaFoldDB; Q8PAJ6; -.
DR STRING; 190485.XCC1487; -.
DR EnsemblBacteria; AAM40783; AAM40783; XCC1487.
DR KEGG; xcc:XCC1487; -.
DR PATRIC; fig|190485.4.peg.1594; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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:UP000001010};
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; 109387 MW; 30DB0DE91F3D2824 CRC64;
MVYPAGQLAD APSQAQGGII FRDLRSTDRA TRPAASAQSS PQQTRLTIVD NLLKQFAQSS
QLAGGNAAYI EDLYEQYLVA PDSVDPKWKA YFDGFNGRDA GDVPHSAAIA HILSASKQAA
NAGTGVGASD ERERNVGRLI TAYRSRGHLG AQLDPLGLTP PVNPPDLDLP FHSLSQADLD
SEFSTGGVGG QPRMKLKDLL ARLKATYAST IGAEFMHIPE FDQRQWIYKR LEDAGGKIAA
DAASRKRTLE RLTAAEGLER YLHTKYVGQK RFSLEGGDAL IPMMDTIIRQ SGNDQVKDIV
IGMAHRGRLN VLVNTLGKNP RKLFDEFEGK FEHAHDDRAH TGDVKYHMGF SADIAVGDDK
QVHLALAFNP SHLEIVDPVV VGSVRSRQER FGDADRKTVL PILIHGDAAF AGQGVVMELF
QMSQARGFAV GGTVHIVVNN QIGFTTSARD DARSTLYCTD VAKMIGAPVF HVNGDDPDAV
MFVSKLAYEF RQQFKKDVVI DLVCYRRWGH NEADEPAATQ PVMYQTIRKH KTTRELYATK
LESDGVLSAD EAKALVDGYR NKLDSGEYTT ELAKRKPDEF AIDWSKYLVG TAADPVDTRV
KRNELDRLAK LITTIPAGVE LHARVAKIYE DRVKMAAGNQ DGDWGFAENL AYATLLAEGH
KLRLVGQDAG RGTFFHRHAI LHDQKTDSYY LPLRQLVENP EDATIIDSLL SEEAVMGFEY
GYSTTDPNAL CVWEAQFGDF ANGAQVVIDQ FIAAGEAKWG RIAGLSLFLP HGYEGQGPEH
SSARLERFLQ LCALENMLVC VPTTPAQCFH MIRRQMRMTT RKPLVVMTPK SLLRHKLAVS
TLEELADGQF QHLIPDAKAD ASKVKRVVLC SGKVYYDLLE DQTKRGQDDV AILRVEQLYP
FPRAQLAAEL KRFGNAADVV WCQEEPQNQG AWYQIRHHLN FCLASGQSLH YAGRARSPSP
AAGHMADHIA EQQKLVADAL LNPFNDQVAE
//
