PYRF_HALMA
ID PYRF_HALMA Reviewed; 277 AA.
AC Q5V216;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=rrnAC1515;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(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|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; AY596297; AAV46436.1; -; Genomic_DNA.
DR RefSeq; WP_004957213.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V216; -.
DR SMR; Q5V216; -.
DR STRING; 272569.rrnAC1515; -.
DR EnsemblBacteria; AAV46436; AAV46436; rrnAC1515.
DR GeneID; 40152476; -.
DR GeneID; 64821893; -.
DR KEGG; hma:rrnAC1515; -.
DR PATRIC; fig|272569.17.peg.2203; -.
DR eggNOG; arCOG00081; Archaea.
DR HOGENOM; CLU_060704_1_0_2; -.
DR OMA; QSAFFER; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001169; Chromosome I.
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..277
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000066472"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 277 AA; 29996 MW; 13192063BFC9E6BE CRC64;
MHFFDRLADR IATADSVVSV GLDPDPARLP DSVLDADLPR WQFNRRIIDA THEHAACYKP
NAAFYEDPDG WRALEETIAY AHGKNVPVLL DAKRGDIGNT ARQYAQILDE DEGPAADAIT
VNPFLGRDSL EPFLQRADRG VFVLGRTSNP GGEDLQDLEL ASGEKLYERV VHLADLWNGN
GNVGLVVGAT NPDELEEIRE LVPDIPFLVP GVGAQGGDAE AAVEHGLADG VGLVNSSRGI
IFAGEDAATR RDDSGDAFFK AAGQSAKQLK QRLNQFR
