ID PUR9_AERHH Reviewed; 530 AA. AC A0KGJ2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 29-MAY-2013, entry version 49. 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=ATIC; DE AltName: Full=IMP synthase; DE AltName: Full=Inosinicase; GN Name=purH; OrderedLocusNames=AHA_0841; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / NCIB 9240; RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000462; ABK36339.1; -; Genomic_DNA. DR RefSeq; YP_855383.1; NC_008570.1. DR ProteinModelPortal; A0KGJ2; -. DR STRING; 380703.AHA_0841; -. DR PRIDE; A0KGJ2; -. DR EnsemblBacteria; ABK36339; ABK36339; AHA_0841. DR GeneID; 4487128; -. DR KEGG; aha:AHA_0841; -. DR PATRIC; 20779202; VBIAerHyd135212_0840. DR eggNOG; COG0138; -. DR HOGENOM; HOG000230373; -. DR KO; K00602; -. DR OMA; DLLFAWK; -. DR ProtClustDB; PRK00881; -. DR BioCyc; AHYD380703:GH2M-842-MONOMER; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00139; PurH; 1; -. DR InterPro; IPR024051; AICAR_Tfase_dom. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR PANTHER; PTHR11692; PTHR11692; 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 SMART; SM00851; MGS; 1. DR SUPFAM; SSF53927; Cytidine_deaminase-like; 1. DR SUPFAM; SSF52335; MGS-like_dom; 1. DR TIGRFAMs; TIGR00355; purH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Transferase. FT CHAIN 1 530 Bifunctional purine biosynthesis protein FT PurH. FT /FTId=PRO_1000018832. SQ SEQUENCE 530 AA; 56898 MW; 9EA6E3286CCD0888 CRC64; MEQARPIRRA LLSVSDKTGI LEFAKALNER GVALLSTGGT AKLLADAGLP VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRREQDDAIM AQHAISPIDM VVVNLYPFAA TVAKPGCTLA DAVENIDIGG PTMVRSAAKN HKDVAIVVKA ADYDRVIREM DGNGNSLKLA TRFDLAIAAF EHTAAYDGMI ANYFGTMVPS YGDNKEGDEE SRFPRTFNSQ FIKKQDMRYG ENSHQAAAFY AEEQAAPGSV ASAIQLQGKA LSYNNIADTD AALECVKEFD QPACVIVKHA NPCGVAIGSD LLSAYERAWQ TDPTSAFGGI IAFNRELDGA TAKAIVERQF VEVIIAPTVS QAARDAVAAK QNVRLLECGQ WTAPAQGFDF KRVNGGLLVQ ERDLGMVTLG DLTVVSKRQP TEAELNDLLF CWKVAKFVKS NAIVYAKDGQ TIGVGAGQMS RVYSAKIAGI KAEDEGLTVA GSVMASDAFF PFRDGIDAAA AAGISCVIQP GGSMRDQEVI DAADEHGMCM LFTNMRHFRH //