ID   PUR5_BURTA              Reviewed;         351 AA.
AC   Q2SYY5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-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=BTH_I1317;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000086; ABC39181.1; -; Genomic_DNA.
DR   RefSeq; YP_441864.1; -.
DR   GeneID; 3849468; -.
DR   GenomeReviews; CP000086_GR; BTH_I1317.
DR   KEGG; bte:BTH_I1317; -.
DR   TIGR; BTH_I1317; -.
DR   HOGENOM; Q2SYY5; -.
DR   OMA; Q2SYY5; VHGLAHI.
DR   BioCyc; BTHA271848:BTH_I1317-MON; -.
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    351       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258343.
SQ   SEQUENCE   351 AA;  36960 MW;  BB91A6134F011AB9 CRC64;
     MNPPKSAPDA QGLSYRDAGV DIDAGDALVD KIKPFAKKTL RDGVLGGIGG FGALFEVPKK
     YREPVLVSGT DGVGTKLKLA FHLNKHDTVG QDLVAMSVND ILVQGAEPLF FLDYFACGKL
     DVETAATVVK GIATGCELAG CALIGGETAE MPGMYPDGEY DLAGFAVGAV EKSKIIDGSA
     IAEGDVVLGL ASSGIHSNGF SLVRKIIERA NPDLSADFHG RSLADALMAP TRIYVKPLLA
     LMEKIAVKGM AHITGGGLVE NIPRVLRDGL TAELDQRAWP LPPLFQWLQQ HGGVADAEMH
     RVFNCGIGMA VIVSAADADE ALRQLTEAGE QVWKIGTVRA SREGEAQTVV V
//