ID PUR9_STRM5 Reviewed; 527 AA. AC B4SL92; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 10-JUN-2026, entry version 90. 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=Smal_3662; OS Stenotrophomonas maltophilia (strain R551-3). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Lysobacterales; Lysobacteraceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=391008; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R551-3; RX PubMed=19060168; DOI=10.1128/aem.02239-08; RA Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N., RA Barac T., Vangronsveld J., van der Lelie D.; RT "Genome survey and characterization of endophytic bacteria exhibiting a RT beneficial effect on growth and development of poplar trees."; RL Appl. Environ. Microbiol. 75:748-757(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide + (6S)-5,6,7,8-tetrahydrofolate; 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=IMP + H2O = 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; CP001111; ACF53361.1; -; Genomic_DNA. DR RefSeq; WP_012512279.1; NC_011071.1. DR AlphaFoldDB; B4SL92; -. DR SMR; B4SL92; -. DR STRING; 391008.Smal_3662; -. DR PaxDb; 391008-Smal_3662; -. DR KEGG; smt:Smal_3662; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 FunFam; 3.40.140.20:FF:000001; Bifunctional purine biosynthesis protein PurH; 1. DR FunFam; 3.40.140.20:FF:000002; Bifunctional purine biosynthesis protein PurH; 1. DR FunFam; 3.40.50.1380:FF:000001; Bifunctional purine biosynthesis protein PurH; 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; NF002049; PRK00881.1; 1. 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_1000096098" FT DOMAIN 1..149 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 527 AA; 55804 MW; 4A9964CDC6A8CB9C CRC64; MTADLLPVRR ALLSVSDKTG LVELATALAA RGVELLSTGG TAKAIRDAGL AVKDVADVTG FPEMMDGRVK TLHPMVHGGL LGRSGLDDAV MAEHGIGAID LLVLNLYPFE SVTAKADCSL ADAVENIDIG GPAMLRSAAK NFARVAVATD PSQYAELLAS LEANNGQLTA ATRFAFSVAA FNRVAQYDAA ISNYLSAVTA TDTAVPVRAE YPAQMNSTFV KVMDLRYGEN PHQSGAFYRD LYPVPGTLAT FQQLQGKELS YNNLADADAA WECVRQFDAP ACVIVKHANP CGVAVGAGNG DAYELAYATD PTSAFGGIIA FNKPLDAATA KVILDRQFVE VLIAPDYEPA ALEYAQKKAN VRVLRIPHGD GLNNFDNKRV GSGLLLQSSD NRGMTRDELK VVSKLAPTDK QFTDLLFAWK VAKFVKSNAI VYAKDNRTIG VGAGQMSRVY SARIAGIKAA DANLVVEGSV MASDAFFPFR DGIDAAAAAG IKAVIQPGGS MRDAEVIAAA DEHGLAMVFT GVRHFRH //