ID PUR5_ANADE Reviewed; 345 AA. AC Q2IQE7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 25. 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=Adeh_1255; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; 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., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) 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; CP000251; ABC81029.1; -; Genomic_DNA. DR RefSeq; YP_464466.1; -. DR GeneID; 3888824; -. DR GenomeReviews; CP000251_GR; Adeh_1255. DR KEGG; ade:Adeh_1255; -. DR HOGENOM; Q2IQE7; -. DR OMA; Q2IQE7; CGKLDPE. DR BioCyc; ADEH290397:ADEH_1255-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 1 345 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_0000258326. SQ SEQUENCE 345 AA; 36501 MW; B436F7CF742A231C CRC64; MSLTYRDAGV DIDEGDRLVD LIKPHARPTL RPEVLGGIGG FGGLFALDVK KYREPVLVSG TDGVGTKLKV AFAADRHDTV GIDLVAMCVN DIAVVGAEPL FFLDYYATGK LSAEQGAEVV KGIAEGCRQA GCALIGGETA ELPGFYARGE YDLAGFAVGC VDRPRIVDGT RVARGDVVIG IASSGLHSNG FSLARKALLD RYPLDHRFEG LGGRTLADAL LEPTRIYAKD VLALLDQVPV RAFAHITGGG LPGNVPRTLP DGTRAVLEEK RWPRPAIFDV VEREGQVPRD EMYRTFNMGL GLVAVVAPGD EAAAHAALRA RGLEAWTVGA IEAGGPGEAT CEVVR //