ID PUR5_BART1 Reviewed; 363 AA. AC A9IVF6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 12. 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=BT_1341; OS Bartonella tribocorum (strain CIP 105476 / IBS 506). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=382640; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18037886; DOI=10.1038/ng.2007.38; RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.; RT "Genomic analysis of Bartonella identifies type IV secretion systems RT as host adaptability factors."; RL Nat. Genet. 39:1469-1476(2007). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM260525; CAK01703.1; -; Genomic_DNA. DR RefSeq; YP_001609698.1; -. DR GeneID; 5830178; -. DR GenomeReviews; AM260525_GR; BT_1341. DR OMA; A9IVF6; 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 1 363 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_1000083450. SQ SEQUENCE 363 AA; 38539 MW; 215D535BE70E7D3A CRC64; MSNQDLINNK SKAGLTYAKA GVNIDMGNAM VEKIKPFIRA TKRAGADAEI GGFGGLFDLK AAGFTDPILV AANDGVGTKL KIAIEVGHHN TVGIDLVAMC VNDLLVQGAE PLFFLDYFAT GKLDPEQGAA IVSGIAEGCK QSGAALIGGE TAEMPGMYAE GDYDLAGFAV GACERSMLLP SKNLTEGDII LGLSASGIHS NGFSLVRRII EQNDLKWNDP APFDPSNNLG VALLTPTRIY VKSLLPIMRK YEGVKALAHI TGGGFLENIP RVIPSSLCAE INLSTINVPS VFSWIAKQGK IEETEMLRTF NCGIGMIIIV GQHTAEAVTQ ALEKNGETVT PLGILTKRQD QNKGILYRGV LHL //