(data stored in ACNUC7421 zone)

SWISSPROT: PYRF_STRM5

ID   PYRF_STRM5              Reviewed;         241 AA.
AC   B4SRN9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE   AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200};
GN   OrderedLocusNames=Smal_0054;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-
CC       monophosphate (OMP) to uridine 5'-monophosphate (UMP).
CC       {ECO:0000255|HAMAP-Rule:MF_01200}.
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_01200};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01200}.
DR   EMBL; CP001111; ACF49759.1; -; Genomic_DNA.
DR   RefSeq; WP_012509634.1; NC_011071.1.
DR   SMR; B4SRN9; -.
DR   STRING; 391008.Smal_0054; -.
DR   EnsemblBacteria; ACF49759; ACF49759; Smal_0054.
DR   KEGG; smt:Smal_0054; -.
DR   eggNOG; ENOG4106EG9; Bacteria.
DR   eggNOG; COG0284; LUCA.
DR   HOGENOM; HOG000226070; -.
DR   KO; K01591; -.
DR   OMA; NFKIFLD; -.
DR   OrthoDB; 1150446at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00270-MONOMER; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001867; 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_01200_B; OMPdecase_type1_B; 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;
DR   PRODOM; B4SRN9.
DR   SWISS-2DPAGE; B4SRN9.
KW   Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN         1    241       Orotidine 5'-phosphate decarboxylase.
FT                                /FTId=PRO_1000138560.
FT   REGION       69     78       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   ACT_SITE     71     71       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING      19     19       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     124    124       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     185    185       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     194    194       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     214    214       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01200}.
FT   BINDING     215    215       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
SQ   SEQUENCE   241 AA;  25630 MW;  E7E94319016C0430 CRC64;
     MSRAPLPLRD DERLIFALDV PDRVQALDWV ERLGDSVAFY KIGMELLASG EYFQVLDELA
     RRDKRVFVDL KFFDIPATAA AVIKRLSQWP VSYATIHGWH PAMMEACAAA NSSDMRLLAV
     TVLTSMGRPD LAQMGIDREP VDVVVERALA AQAAGIDGVI ASGQEAGPIR AATGAGFSIV
     CPGIRPGGPV GDDQKRTVGV AQAFADGADA IVIGRPIRLA ADPQAAARAI QQEIASALAA
     R
//

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