PYRF_DEBHA
ID PYRF_DEBHA Reviewed; 267 AA.
AC Q6BY69; Q96VQ4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
DE AltName: Full=Uridine 5'-monophosphate synthase;
DE Short=UMP synthase;
GN Name=URA3; OrderedLocusNames=DEHA2A11968g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MTCC 234;
RX PubMed=11571754; DOI=10.1002/yea.774;
RA Bansal P.K., Sharma P., Mondal A.K.;
RT "A minisatellite sequence in the upstream region of DURA3 gene from
RT halotolerant yeast Debaryomyces hansenii.";
RL Yeast 18:1301-1307(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000255|PROSITE-ProRule:PRU10110};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}.
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DR EMBL; AY033329; AAK54442.1; -; Genomic_DNA.
DR EMBL; CR382133; CAG84825.1; -; Genomic_DNA.
DR RefSeq; XP_456850.1; XM_456850.1.
DR AlphaFoldDB; Q6BY69; -.
DR SMR; Q6BY69; -.
DR STRING; 4959.XP_456850.1; -.
DR EnsemblFungi; CAG84825; CAG84825; DEHA2A11968g.
DR GeneID; 2899491; -.
DR KEGG; dha:DEHA2A11968g; -.
DR VEuPathDB; FungiDB:DEHA2A11968g; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_030821_0_0_1; -.
DR InParanoid; Q6BY69; -.
DR OMA; KNFVMGF; -.
DR OrthoDB; 1303452at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000599; Chromosome A.
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 Gene3D; 3.20.20.70; -; 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:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..267
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134658"
FT ACT_SITE 94
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 3..4
FT /note="KT -> NK (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="N -> S (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> D (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="E -> D (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="F -> Y (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..76
FT /note="VV -> II (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..143
FT /note="SSK -> VSS (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..168
FT /note="EK -> GL (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="T -> S (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> I (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Q -> E (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="T -> S (in Ref. 1; AAK54442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29320 MW; D999613C57D2BEE0 CRC64;
MVKTQTYTER ASAHPSPVAQ RLFKLMDNKK TNLCASVDVK STEEFLTLIE KLGPYICLVK
THIDIIDDFS YEGTVVPLLA LAKKHNFMIF EDRKFADIGN TVKSQYSGGV YKIAQWSDIT
NAHGITGSGI VKGLKEAAQE SSKEPRGLLM LAELSSKGSL AYGEYTEKTI EIAKSDKEFV
IGFIAQRDMG GTDEGFDWIV MTPGVGLDDK GDGLGQQYRT VDQVVTTGTD IIIVGRGLFG
QGRDPTVEGK RYRDAGWNAY LKKTGSL
