PYRFE_NOSS1
ID PYRFE_NOSS1 Reviewed; 477 AA.
AC Q8YSY4;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bifunctional enzyme PyrF/PyrE;
DE Includes:
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
DE Includes:
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRT;
DE Short=OPRTase;
DE EC=2.4.2.10;
GN Name=pyrFE; OrderedLocusNames=alr2945;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to orotate, leading to the formation of
CC orotidine monophosphate (OMP). {ECO:0000250}.
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine monophosphate
CC (OMP) to uridine monophosphate (UMP). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SIMILARITY: In the N-terminal section; belongs to the OMP decarboxylase
CC family. Type 2 subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB74644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000019; BAB74644.1; ALT_INIT; Genomic_DNA.
DR PIR; AB2174; AB2174.
DR RefSeq; WP_044523080.1; NZ_RSCN01000003.1.
DR AlphaFoldDB; Q8YSY4; -.
DR SMR; Q8YSY4; -.
DR STRING; 103690.17132039; -.
DR EnsemblBacteria; BAB74644; BAB74644; BAB74644.
DR KEGG; ana:alr2945; -.
DR eggNOG; COG0284; Bacteria.
DR eggNOG; COG0461; Bacteria.
DR OMA; PNPEMMP; -.
DR OrthoDB; 1181405at2; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Glycosyltransferase; Lyase; Magnesium;
KW Multifunctional enzyme; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..477
FT /note="Bifunctional enzyme PyrF/PyrE"
FT /id="PRO_0000134638"
FT REGION 1..273
FT /note="OMP decarboxylase"
FT REGION 274..477
FT /note="Orotate phosphoribosyltransferase"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 400..408
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52826 MW; 157D608B39BF23B4 CRC64;
MIFFDKLHQN ISQNQSLLFV GLDPNPEMMP GRYSSQDIID GLWDWLQFII AETADFVCAY
KPTLGFYEAL GVPGLELLQK TLAAIPSHIP IILDAKHSDL NTSTIFAKTV FTQWGVDAIT
LSPYTGQDHV APFLVYPDKA VFILCSTSNP GAEALQQYPT RESPLYLQVV QESKNWGTPE
QLGLEVGTTN AEVLARIRQV APERMIMVRS IWAEGGNLNR ILEVGLNTDG NGLLIPVPQD
MLASANLSKE IQSLRAEINQ VRDITVRDVA SCSVWLPDVF TVKQHPLHDL ILQLYDIDCI
MFGNFVQASG AVFPYYIDLR KIISNPQVFN QVLSGYENIV KNLTFDRLAG IPYGSLPTAT
GLALRLNCPM IFPRKEVKAH GTRRLIEGNF RTGEVVVVVD DILISGKSVM EGADKLKSAG
LNVHDIVVFI DHEQGVKDKL QANGYRGHAV LTISEITSVL HQAGRINDEQ FLALTAE
