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Database: UniProt
Entry: P73761
LinkDB: P73761
Original site: P73761 
ID   PYRF_SYNY3              Reviewed;         231 AA.
AC   P73761;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   26-NOV-2014, entry version 96.
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=sll0838;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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: Orotidine 5'-phosphate = UMP + CO(2).
CC       {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}.
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DR   EMBL; BA000022; BAA17813.1; -; Genomic_DNA.
DR   PIR; S74852; S74852.
DR   RefSeq; NP_441133.1; NC_000911.1.
DR   RefSeq; YP_005651190.1; NC_017277.1.
DR   RefSeq; YP_007451015.1; NC_020286.1.
DR   ProteinModelPortal; P73761; -.
DR   STRING; 1148.sll0838; -.
DR   PaxDb; P73761; -.
DR   EnsemblBacteria; BAA17813; BAA17813; BAA17813.
DR   GeneID; 954452; -.
DR   KEGG; syn:sll0838; -.
DR   PATRIC; 23839571; VBISynSp132158_1348.
DR   eggNOG; COG0284; -.
DR   HOGENOM; HOG000226070; -.
DR   InParanoid; P73761; -.
DR   KO; K01591; -.
DR   OMA; HAKEPRE; -.
DR   OrthoDB; EOG6N6815; -.
DR   PhylomeDB; P73761; -.
DR   UniPathway; UPA00070; UER00120.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-HAMAP.
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   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   Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    231       Orotidine 5'-phosphate decarboxylase.
FT                                /FTId=PRO_0000134594.
FT   REGION       59     68       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   ACT_SITE     61     61       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING      11     11       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING      32     32       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     118    118       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     180    180       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     189    189       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
FT   BINDING     209    209       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01200}.
FT   BINDING     210    210       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01200}.
SQ   SEQUENCE   231 AA;  24705 MW;  9772FCBBF7F3D4D2 CRC64;
     MTPDQVIVAL DVPDLPKAIA LVDRLPGVGF WKVGLELFVG AGPVILAELK DRGKRIFLDL
     KFHDIPNTML GACLSASRYE VDLLTLHATA GSQALTLAAQ AMAPLPHPPK LLAITLLTSI
     GDRQLREELQ QPLAVDDYVN AMARLARNAG IDGAVCSPQE VAKLRQTCGP EFLLVTPGVR
     PLWSAPGDQQ RVMIPAQAIA AGANYVVIGR PITADPSPEA AWERLCQDLA V
//
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