ID H9XQ39_PHYIN Unreviewed; 440 AA.
AC H9XQ39;
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:AFH01350.1};
DE Flags: Fragment;
GN Name=UMP {ECO:0000313|EMBL:AFH01350.1};
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:AFH01350.1};
RN [1] {ECO:0000313|EMBL:AFH01350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01350.1};
RA Garcia Bayona L., Restrepo S., Zimmernann B.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH01350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01350.1};
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:AFH01350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T30-4 {ECO:0000313|EMBL:AFH01350.1};
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; JQ087258; AFH01350.1; -; Genomic_DNA.
DR AlphaFoldDB; H9XQ39; -.
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:AFH01350.1}.
FT DOMAIN 1..234
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH01350.1"
FT NON_TER 440
FT /evidence="ECO:0000313|EMBL:AFH01350.1"
SQ SEQUENCE 440 AA; 46282 MW; C4C8E96370C4AC18 CRC64;
LCVGLDPHVA ELPEATAAAA QAFCLNIIEQ THHVAAAYKP NSAFFEAFGA EGITALHSVI
KAIPSGIPVL LDAKRGDIST TAAAYAVSAF DKLEAHAITL APYMGADSID PFVRGHPERG
CFVLCKTSNP SANDFQTLSV GSRALFEEVA AKCEQWNSED NVGLVVGATD VKALRRVRAV
TPNLWILAPG IGAQGGNLEE AVTAGLSSDG LGLLVPVSRG ISKAANPKEA AESLRDAINA
ARKTKFALSF GVLKFGDFTL KSGRQSPYFF NAGLFRTGRA LGQLGQFYAQ AIHDSGVEFD
VLFGPAYKGI TLAAAVAIAY ADMYGVDLPF AYNRKEAKDH GEGGVLVGAD MTGKKVLIID
DVITAGTAIR EAFGILEKTN AQVSGVCISL DRQEKVSIED TRSAIDQVRE SFGIPVVSIA
TLDNLVGYLE TVDTATDANA
//
