PYRF_NATPD
ID PYRF_NATPD Reviewed; 269 AA.
AC Q3ISC9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=NP_1734A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48958.1; -; Genomic_DNA.
DR RefSeq; WP_011322591.1; NC_007426.1.
DR AlphaFoldDB; Q3ISC9; -.
DR SMR; Q3ISC9; -.
DR STRING; 348780.NP_1734A; -.
DR EnsemblBacteria; CAI48958; CAI48958; NP_1734A.
DR GeneID; 3703085; -.
DR KEGG; nph:NP_1734A; -.
DR eggNOG; arCOG00081; Archaea.
DR HOGENOM; CLU_060704_1_0_2; -.
DR OMA; QSAFFER; -.
DR OrthoDB; 54384at2157; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002698; 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..269
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000066482"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 269 AA; 29255 MW; D72248AD21ED11AB CRC64;
MSFFETLADR IDDRDSVVSV GLDPDPDRLP EFLDADLPRW AFNRRVIDAT HEHAACYKPN
AAFYEDSDGW RALEETIAYA HGKGVPVLLD AKRGDIGNTA RQYATLLDDD GLGADAITAN
PYMGRDTLEP YLSRADKGVF ILCRTSNSGG ADFQNLTVGN DKRLYEYVAQ RCQEWNEHEN
VGLVVGATAP EELESVRDLV DLPFLVPGVG AQGGDAAAAV DHGLADGVGL VNSSRGIIFA
GEGAADEDEY FRAVGAAAKR LKQRLNKHR
