ID A0A178EIE2_9PLEO Unreviewed; 221 AA.
AC A0A178EIE2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00021923, ECO:0000256|RuleBase:RU000512};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321, ECO:0000256|RuleBase:RU000512};
GN ORFNames=IQ07DRAFT_665511 {ECO:0000313|EMBL:OAL54989.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54989.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL54989.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54989.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000512};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC ECO:0000256|RuleBase:RU000512}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00011018, ECO:0000256|RuleBase:RU000512}.
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DR EMBL; KV441638; OAL54989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EIE2; -.
DR STRING; 765867.A0A178EIE2; -.
DR InParanoid; A0A178EIE2; -.
DR OrthoDB; 922at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000077535; 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 NCBIfam; TIGR01740; pyrF; 1.
DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 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 ECO:0000256|RuleBase:RU000512};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000512};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW ECO:0000256|RuleBase:RU000512};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 1..206
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 221 AA; 24203 MW; C28DE34A1EA6E725 CRC64;
MGSSCSFKTH VDVVDFNHDT AKGLKELAKK HDFLIFEDRK FVDIGNTVQK QYHGGALHIS
EFAHIVNVSI LGGEGIVEAL SQVVHAPELG YKDERAFILL AEMTSKGSLA TDNYTVKCVE
LARKQTSSII GWIANKSLES VPTQSSPSVS EDFLVFTTGV NQSSKGDKLG QQYQTPTIAI
EGGADFIISG RGIYAAQDPV QSARSYQREG WEAYLKRVSK E
//
