ID H9XQ37_PHYIN Unreviewed; 439 AA.
AC H9XQ37;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Orotidine-5-monophosphate decarboxylase and orotate phosphoribosyl transferase {ECO:0000313|EMBL:AFH01348.1};
DE Flags: Fragment;
GN Name=UMP {ECO:0000313|EMBL:AFH01348.1};
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787 {ECO:0000313|EMBL:AFH01348.1};
RN [1] {ECO:0000313|EMBL:AFH01348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01348.1};
RA Garcia Bayona L., Restrepo S., Zimmernann B.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH01348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01348.1};
RA Garavito M., Vasquez J.J., Lozano G., Bernal A.;
RT "Towards a new control strategy of Phytophthora infestans by inhibition of
RT de novo pyrimidine biosynthesis: the big picture.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AFH01348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01348.1};
RX PubMed=24361203; DOI=10.1016/j.gene.2013.12.009;
RA Garcia-Bayona L., Garavito M.F., Lozano G.L., Vasquez J.J., Myers K.,
RA Fry W.E., Bernal A., Zimmermann B.H., Restrepo S.;
RT "De novo pyrimidine biosynthesis in the oomycete plant pathogen
RT Phytophthora infestans.";
RL Gene 537:312-321(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001419};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008847}.
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DR EMBL; JQ087256; AFH01348.1; -; Genomic_DNA.
DR AlphaFoldDB; H9XQ37; -.
DR VEuPathDB; FungiDB:PITG_09635; -.
DR UniPathway; UPA00070; UER00119.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04725; OMP_decarboxylase_like; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR00336; pyrE; 1.
DR NCBIfam; TIGR02127; pyrF_sub2; 1.
DR PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Transferase {ECO:0000313|EMBL:AFH01348.1}.
FT DOMAIN 1..233
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH01348.1"
FT NON_TER 439
FT /evidence="ECO:0000313|EMBL:AFH01348.1"
SQ SEQUENCE 439 AA; 46186 MW; 07EB8E4DF15D02E5 CRC64;
CVGLDPHVAE LPEATAAAAQ AFCLNIIEQT HHVAAAYKPN SAFFEAFGAE GITALHSVIK
AIPSGIPVLL DAKRGDISTT AAAYAVSAFD KLEAHAITLA PYMGADSIDP FVRGHPERGC
FVLCKTSNPS ANDFQTLSVG SRALFEEVAA KCEQWNSEDN VGLVVGATDV KALRRVRAVT
PNLWILAPGI GAQGGNLEEA VTAGLSSDGL GLLVPVSRGI SKAANPKEAA ESLRDAITAA
RKTKFALSFG VLKFGDFTLK SGRQSPYFFN AGLFRTGRAL GQLGKFYAQA IHDSGVEFDV
LFGPAYKGIT LAAAVAIAYA DMYGVDLPFA YNRKEAKDHG EGGVLVGADM TGKKVLIIDD
VITAGTAIRE AFGILEKTNA QVSGVCISLD RQEKVSIEDT RSAIDQVRES FGIPVVSIAT
LDNLVGYLET VDMATDANA
//
