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 01-MAY-2013, entry version 74.
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 / 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 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA 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
CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation
CC of orotidine monophosphate (OMP) (By similarity).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine monophosphate
CC (OMP) to uridine monophosphate (UMP) (By similarity).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC + 5-phospho-alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 1/2.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 2/2.
CC -!- SIMILARITY: In the N-terminal section; belongs to the OMP
CC decarboxylase family. Type 2 subfamily.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC purine/pyrimidine phosphoribosyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB74644.1; Type=Erroneous initiation;
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DR EMBL; BA000019; BAB74644.1; ALT_INIT; Genomic_DNA.
DR PIR; AB2174; AB2174.
DR RefSeq; NP_486985.1; NC_003272.1.
DR ProteinModelPortal; Q8YSY4; -.
DR STRING; 103690.alr2945; -.
DR EnsemblBacteria; BAB74644; BAB74644; BAB74644.
DR GeneID; 1106543; -.
DR KEGG; ana:alr2945; -.
DR PATRIC; 22776188; VBINosSp37423_3554.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000256439; -.
DR KO; K13421; -.
DR OMA; VKAHGTR; -.
DR ProtClustDB; PRK05500; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:EC.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA: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 Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01208; PyrE; 1; fused.
DR HAMAP; MF_01215; OMPdecase_type2; 1; atypical/fused.
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; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR PROSITE; PS00156; OMPDECASE; FALSE_NEG.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Decarboxylase; Glycosyltransferase; Lyase;
KW Magnesium; Multifunctional enzyme; Pyrimidine biosynthesis;
KW Transferase.
FT CHAIN 1 477 Bifunctional enzyme PyrF/PyrE.
FT /FTId=PRO_0000134638.
FT REGION 1 273 OMP decarboxylase.
FT REGION 274 477 Orotate phosphoribosyltransferase.
FT REGION 400 408 5-phosphoribose 1-diphosphate binding (By
FT similarity).
FT ACT_SITE 96 96 Proton donor (By similarity).
FT BINDING 374 374 5-phosphoribose 1-diphosphate; shared
FT with dimeric partner (By similarity).
FT BINDING 375 375 5-phosphoribose 1-diphosphate (By
FT similarity).
FT BINDING 378 378 5-phosphoribose 1-diphosphate; shared
FT with dimeric partner (By similarity).
FT BINDING 380 380 5-phosphoribose 1-diphosphate; shared
FT with dimeric partner (By similarity).
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
//
