ID   PUR5_BORA1              Reviewed;         349 AA.
AC   Q2KX26;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE            EC=6.3.3.1;
DE   AltName: Full=AIRS;
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE   AltName: Full=AIR synthase;
GN   Name=purM; OrderedLocusNames=BAV0723;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D-
CC       ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
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DR   EMBL; AM167904; CAJ48333.1; -; Genomic_DNA.
DR   RefSeq; YP_785256.1; -.
DR   GeneID; 6264932; -.
DR   GenomeReviews; AM167904_GR; BAV0723.
DR   KEGG; bav:BAV0723; -.
DR   NMPDR; fig|521.1.peg.900; -.
DR   HOGENOM; Q2KX26; -.
DR   OMA; Q2KX26; CGKLDPE.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-lig...; IEA:HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00741; -; 1.
DR   InterPro; IPR000728; AIR_synth.
DR   InterPro; IPR010918; AIR_synth_C.
DR   InterPro; IPR004733; PurM_cligase.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   TIGRFAMs; TIGR00878; purM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    349       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258335.
SQ   SEQUENCE   349 AA;  36806 MW;  96A469B4F964F477 CRC64;
     MTNEHSAPLT YRDAGVDIDA GDALVDRIKP LAARTMRPGV LAGIGGFGAL FEVPKKYREP
     VLVSGTDGVG TKLRLAFDWN RHDTVGIDLV AMSVNDILVQ GAEPLFFLDY FACGKLSVDT
     AAAVVGGIAR GCELAGCALI GGETAEMPGM YPDGEYDLAG FAVGAVEKTA IIDGKSIQPG
     DVVLGLASSG AHSNGYSLVR KILERAGARP DQDFHGQPLV DVVMAPTRIY VKQVLAALAE
     HGTAIKGLAH ITGGGLLDNV PRILQQGLSA KLYRDGWQMP QLFQWLQQQG AVADTEMYRV
     FNCGIGMVLV VAADQADAIS ATLRAQGEAV SRLGEIVPQQ DGMAQTFVV
//