ID A0A0P7B1Q1_9HYPO Unreviewed; 368 AA.
AC A0A0P7B1Q1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
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=AK830_g11950 {ECO:0000313|EMBL:KPM34622.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM34622.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM34622.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM34622.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPM34622.1}.
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DR EMBL; LKCW01000317; KPM34622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B1Q1; -.
DR STRING; 78410.A0A0P7B1Q1; -.
DR OrthoDB; 922at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000050424; Unassembled WGS sequence.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
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:UP000050424}.
FT DOMAIN 36..355
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT REGION 165..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40125 MW; FFC5DDD1C59F8FF0 CRC64;
MSPHPTLKAT FASRSATATH PLNAYLFKLM DLKASNLCLS ADVATARELL YFADKIGPSI
VVLKTHYDMI SGWDFHPQTG TGAKLASLAR KHGFLIFEDR KFGDIGNTVE LQYTSGAARI
IEWAHITNVN MVPGKASVTS LSNAAAKWLK RRDYEVKTSV SVGTPTISNA DYDSERSDAE
RTDGSDEAEP PRPDNGRKGS IVSTTTVTQQ YEAADSPRHV KTIAEGDDNH FPGIDDAPVE
RGLLILAQMS TEGNFMNKEY TQACVEAARE HKDFVMGFIS QESLNSKPDD AFIHMTPGCQ
LPPDGEDVNA DVKGDGKGQQ YNTPQKIVGI AGADIAIVGR GIIKAGDPEE EAERYRSAAW
KAYTERVR
//
