ID PUR9_XANC5 Reviewed; 527 AA. AC Q3BY85; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139}; GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; GN OrderedLocusNames=XCV0547; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10; RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S., RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., RA Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant pathogenic RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete RT genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, CC ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino- CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP- CC Rule:MF_00139}. 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; AM039952; CAJ22178.1; -; Genomic_DNA. DR RefSeq; WP_011346196.1; NZ_CP017190.1. DR AlphaFoldDB; Q3BY85; -. DR SMR; Q3BY85; -. DR STRING; 456327.BJD11_20135; -. DR KEGG; xcv:XCV0547; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000007069; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01421; IMPCH; 1. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR002695; PurH-like. DR NCBIfam; TIGR00355; purH; 1. DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1. DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 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; Methylglyoxal synthase-like; 1. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Transferase. FT CHAIN 1..527 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000018986" FT DOMAIN 1..149 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 527 AA; 55788 MW; CE12F763E04E098E CRC64; MASDFLPVRR ALLSVSDKTG LIDLARALVA RNVELLSTGG TAKAIREAGL PVKDVAELTG FPEMMDGRVK TLHPLVHGGL LGRAGVDEAV MAEHGIVPID LLVLNLYPFE SVTVKADCTL ADAVENIDIG GPAMLRSAAK NFARVAVATD PAQYADLLAE LEVNDGQLSA AKRFALSVAA FNRVAQYDAA ISNYLSAVAD SSEAVPTRSP FPAQINSNFV KVMDLRYGEN PHQSGAFYRD LYPVPGTLAT FQQLQGKELS YNNLADADAA WECVRQFDAP ACVIVKHANP CGVAVGAGCG DAYELAYATD PTSAFGGILA FNKTLDAATA KAILDRQFVE VLIAPDYEAG ALEYATRKAN VRVLKIPHGN GLNNYDTKRI GSGLLMQSAD NRSMSLGELS VVTQRAPNEA ELGDLLFAWR VAKYVKSNAI VYAKDSRTIG VGAGQMSRVV SAKIAALKAE EAKLTVAGSV MASDAFFPFR DGIDAAAAAG IKAVIQPGGS MRDGEVIAAA DEHGIAMVFT GVRHFRH //