ID PUR5_DECAR Reviewed; 347 AA. AC Q47B77; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, 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=Daro_3174; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.; RT "Complete sequence of Dechloromonas aromatica RCB."; RL Submitted (AUG-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. 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; CP000089; AAZ47904.1; -; Genomic_DNA. DR RefSeq; YP_286374.1; -. DR GeneID; 3567174; -. DR GenomeReviews; CP000089_GR; Daro_3174. DR KEGG; dar:Daro_3174; -. DR NMPDR; fig|159087.4.peg.3469; -. DR HOGENOM; Q47B77; -. DR OMA; Q47B77; CGKLDPE. DR BioCyc; DARO159087:DARO_3174-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 1 347 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_0000258349. SQ SEQUENCE 347 AA; 36611 MW; 33DC0FAAD30878E0 CRC64; MTQNTSLSYR DAGVDIDAGD ALVERIKPLA KKTLREGVLG GIGGFGALFE VPKRYKEPVL VSGTDGVGTK LRLAFDLNRH DTVGQDLVAM SVNDILVLGA ESLFFLDYFA CGKLDVDTAA AVVGGIAKGC ELAGCALIGG ETAEMPGMYP AGEYDLAGFA VGVVEKSKAI DGKASITPGD VVLGLASSGA HSNGYSLVRK IIERSKPDMN AKFDGERTLA DVVMAPTRIY VKQVLATMQK VTIKGMAHIT GGGLLENVPR VLPENTVAEL EKAAWPRPKL FDWMQAEGNV AENEMHRVFN CGIGLVIVVA AADADAAMAE LKAQGEAVYR IGKIRARSGD EAQTLVV //