ID A4Z4U5_KLUMA Unreviewed; 267 AA.
AC A4Z4U5;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 Name=URA3 {ECO:0000313|EMBL:ABB69700.1};
GN Synonyms=Ura3 {ECO:0000313|EMBL:AOP17589.1};
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911 {ECO:0000313|EMBL:ABB69700.1};
RN [1] {ECO:0000313|EMBL:ABB69700.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1777 {ECO:0000313|EMBL:ABB69700.1};
RX PubMed=17433483; DOI=10.1016/j.jbiotec.2007.03.008;
RA Hong J., Wang Y., Kumagai H., Tamaki H.;
RT "Construction of thermotolerant yeast expressing thermostable cellulase
RT genes.";
RL J. Biotechnol. 130:114-123(2007).
RN [2] {ECO:0000313|EMBL:AOP17589.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IIPE453 {ECO:0000313|EMBL:AOP17589.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; DQ234267; ABB69700.1; -; Genomic_DNA.
DR EMBL; KX453285; AOP17589.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Z4U5; -.
DR SMR; A4Z4U5; -.
DR VEuPathDB; FungiDB:KLMA_10731; -.
DR UniPathway; UPA00070; UER00120.
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}.
FT DOMAIN 31..251
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 267 AA; 29295 MW; 3B0281C40E3EE735 CRC64;
MSTKSYSERA AAHRSPVAAK LLNLMEEKKS NLCASLDVRK TAELLRLVEV LGPYICLLKT
HVDILEDFSF ENTIVPLKQL AEKHKFLIFE DRKFADIGNT VKLQYTSGVY RIAEWSDITN
AHGVTGAGIV AGLKQGAEEV TKEPRGLLML AELSSKGSLA HGEYTRGTVE IAKSDKDFVI
GFIAQNDMGG REEGYDWLIM TPGVGLDDKG DALGQQYRTV DEVVAGGSDI IIVGRGLFAK
GRDPVVEGER YRKAGWDAYL KRVGRSA
//
