ID PUR9_ANAVT Reviewed; 506 AA. AC Q3M6G3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Bifunctional purine biosynthesis protein purH; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase; DE EC=2.1.2.3; DE AltName: Full=AICAR transformylase; DE Includes: DE RecName: Full=IMP cyclohydrolase; DE EC=3.5.4.10; DE AltName: Full=Inosinicase; DE AltName: Full=IMP synthetase; DE AltName: Full=ATIC; GN Name=purH; OrderedLocusNames=Ava_3818; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; 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., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl CC THF route): step 1/1. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region (By similarity). CC -!- SIMILARITY: Belongs to the purH 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; CP000117; ABA23423.1; -; Genomic_DNA. DR RefSeq; YP_324318.1; -. DR GeneID; 3678750; -. DR GenomeReviews; CP000117_GR; Ava_3818. DR KEGG; ava:Ava_3818; -. DR NMPDR; fig|240292.3.peg.4110; -. DR HOGENOM; Q3M6G3; -. DR OMA; Q3M6G3; VVKHVKS. DR BioCyc; AVAR240292:AVA_3818-MON; -. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide for...; IEA:HAMAP. DR GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro. DR HAMAP; MF_00139; -; 1. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR013982; AICARFT_IMPCHas_formly. DR InterPro; IPR011607; MGS. DR PANTHER; PTHR11692; AICARFT_IMPCHas; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR TIGRFAMs; TIGR00355; purH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Transferase. FT CHAIN 1 506 Bifunctional purine biosynthesis protein FT purH. FT /FTId=PRO_1000018836. SQ SEQUENCE 506 AA; 54099 MW; 6B15CD33EA1B879F CRC64; MARLALLSVS NKTGLIDLAR RLVEEFEFDL ISSGGTAQAL KDAGLPVTKV ADYTGSPEIL GGRVKTLHPR IHGGILARRD VPSDLTDLEN NQIRPIDLVV VNLYPFEETI AKPGVTLAEA VEQIDIGGPA MLRASSKNFA HLTVLCDPAQ YDEYLQELRQ NNGVASLEFR QKAALKGFLH TASYDSAIAS YLSGTQQHTL NGTELQSLRY GENPHQPAAW YQTGTTPTGW TAAKKLQGKE LSYNNLVDLE AARRIIAEFT DTPAATIIKH TNPCGTALAD TIVEAYQKAF NADATSAFGG IVALNRPIDA ATASELTKTF LECVVAPDCD AEAQKILAKK SNVRVLTLAD LSTGPKTLVK QIAGGFLVQA ADDIAADTIQ WQVVTERQPT ADELAELLFA WKVCKHVKSN AIVVTSDRTT LGVGAGQMNR IGSTKIALEQ AGDKAKGAIL ASDGFFPFDD TVRTAAAAGI SAIVQPGGSL RDQDSVKAAN ELGLLMVLTG VRHFLH //