PYRF_BORA1
ID PYRF_BORA1 Reviewed; 272 AA.
AC Q2KY06;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01215};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01215};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01215}; OrderedLocusNames=BAV0575;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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|HAMAP-Rule:MF_01215};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01215}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01215}.
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DR EMBL; AM167904; CAJ48180.1; -; Genomic_DNA.
DR RefSeq; WP_012416271.1; NC_010645.1.
DR AlphaFoldDB; Q2KY06; -.
DR SMR; Q2KY06; -.
DR STRING; 360910.BAV0575; -.
DR EnsemblBacteria; CAJ48180; CAJ48180; BAV0575.
DR GeneID; 41392486; -.
DR KEGG; bav:BAV0575; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_1_0_4; -.
DR OMA; QSAFFER; -.
DR OrthoDB; 1181405at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01215; OMPdecase_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43375; PTHR43375; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..272
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000066456"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 272 AA; 29236 MW; EAC6F99B2F26D54E CRC64;
MNFLQKLEHA WATQNSLLQV GLDPDPARFP AELQGRPDAI LSFCRGIVDA TAPFASSFKP
QIAYFAAHRA EDQLEALCGH IRDKYPHLPI VLDAKRGDIG STAENYAREA FERYQAHAVT
VSPYMGLDSV EPYLAWRDRG VIVLCRTSNP GGSDLQFLPM ADGQPLYLHV AGLVADKWNA
HGQCGLVVGA TYPNELAAVR KRVGDSLPLL VPGIGAQGGD INATVQAGAN SARAGMMINS
SRAIIYASGG EDWREAAAEA ARGLRDAINA VR