ID PYRF_AZOSB Reviewed; 270 AA.
AC A1KBR9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=azo3659;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL96275.1; -; Genomic_DNA.
DR RefSeq; WP_011767381.1; NC_008702.1.
DR AlphaFoldDB; A1KBR9; -.
DR SMR; A1KBR9; -.
DR STRING; 62928.azo3659; -.
DR KEGG; azo:azo3659; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_1_0_4; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002588; 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 CDD; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR02127; pyrF_sub2; 1.
DR PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..270
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000066454"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 270 AA; 28828 MW; 47B6076A2BBD95F4 CRC64;
MHFMTALRAA WQQRDSLLCV GLDPDPARFP AHLQGRPDAI FEFCAAIVDA TADLVCSFKP
QIAYFAARRA EDQLEALIDH IHAHHPGVPV ILDAKRGDIG STAEQYAVEA FERFKADAIT
VNPYMGRDSV DPYLAYPDKG VILLCRTSNP GGSDLQFLDV GGEKLYERVA RLVAEDWNAS
GNCGLVVGAT FPAEIARVRA LTGEMPLLVP GIGAQGGDIE ATVKAGRTAA GGGLMINSSR
AILYAGKGED FAAAARAAAL QTRDAINAYR
//
