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PYRF_HALLT
ID   PYRF_HALLT              Reviewed;         276 AA.
AC   B9LP84;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=Hlac_1586;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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; CP001365; ACM57172.1; -; Genomic_DNA.
DR   RefSeq; WP_015910312.1; NC_012029.1.
DR   AlphaFoldDB; B9LP84; -.
DR   SMR; B9LP84; -.
DR   STRING; 416348.Hlac_1586; -.
DR   EnsemblBacteria; ACM57172; ACM57172; Hlac_1586.
DR   GeneID; 7399534; -.
DR   KEGG; hla:Hlac_1586; -.
DR   eggNOG; arCOG00081; Archaea.
DR   HOGENOM; CLU_060704_1_0_2; -.
DR   OMA; QSAFFER; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000740; Chromosome 1.
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.
FT   CHAIN           1..276
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000164749"
FT   ACT_SITE        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   276 AA;  29838 MW;  C8412DCC9224E76D CRC64;
     MSFFETLADR IEATDSVVSV GLDPDPNRLP EFLANADLPR WAFNRRIIDA THEHAACYKP
     NAAFYEDADG WRALEETIAY AHGKDVPVLL DAKRADIGNT TRQYAAALDR ADAITVNPYL
     GRDSLQPFLD REEKGVFVLC RTSNPGGSDL QDLELASGEP LYERVAALAD VWNGNDNVGL
     VVGATAPEEL AEVREIVPEI PFLVPGVGAQ GGDAEAAVEH GLADRPDAAV DVGLVNSSRG
     IIFAGEESSR PDDEATYFGA AGDAAKRLKK RLNQYR
 
 
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