ID A7E4B8_SCLS1 Unreviewed; 379 AA.
AC A7E4B8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 03-MAY-2023, entry version 82.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00021923};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
DE AltName: Full=OMP decarboxylase {ECO:0000256|ARBA:ARBA00033428};
DE AltName: Full=Uridine 5'-monophosphate synthase {ECO:0000256|ARBA:ARBA00031744};
GN ORFNames=SS1G_00140 {ECO:0000313|EMBL:EDN90740.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN90740.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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.
CC {ECO:0000256|ARBA:ARBA00011018}.
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DR EMBL; CH476621; EDN90740.1; -; Genomic_DNA.
DR RefSeq; XP_001598054.1; XM_001598004.1.
DR AlphaFoldDB; A7E4B8; -.
DR STRING; 665079.A7E4B8; -.
DR EnsemblFungi; EDN90740; EDN90740; SS1G_00140.
DR GeneID; 5494514; -.
DR KEGG; ssl:SS1G_00140; -.
DR VEuPathDB; FungiDB:sscle_03g029410; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_030821_1_1_1; -.
DR InParanoid; A7E4B8; -.
DR OMA; CLIKTHI; -.
DR OrthoDB; 922at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 39..365
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 379 AA; 42004 MW; BCC39C132A92EA5E CRC64;
MSPAASHPIA KTSFEDRASK TKHPLTAYLL RLMTLKQSNL CVSADVSTAG ELLRLANAVG
PSIVVLKTHY DLINNWDYSP TTGTGARLNR LARRHGFLIF EDRKFGDIGN TVQLQYTEGT
AKIIEWSHIT NVNMIPGKAS VDSLAEAAAR WRERKRYEVK TNISVGTPRP ESIEGDEDQI
TTPISLNNTC HEIPDGSHGL EAHNEANIGR KASIVSITTV SQHFEPADSP RSRIDFDIEE
EAYPGIDEAP LERGLLILAQ MSSAGNFMTR DYTNACVESA REHKQYVMGF ISQETLNTEA
DDDFISMTPG CQLPPENDEE AELEGDGKGQ QYNTPGKLVG LGCDIVIVGR GIIRAGDPEW
EAERYRRKAW EAYQERIKA
//
