ID PUR9_LEPIN Reviewed; 511 AA. AC Q8F3W6; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 105. 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=LA_2283; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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; AE010300; AAN49482.1; -; Genomic_DNA. DR RefSeq; NP_712464.1; NC_004342.2. DR RefSeq; WP_000614727.1; NC_004342.2. DR AlphaFoldDB; Q8F3W6; -. DR SMR; Q8F3W6; -. DR STRING; 189518.LA_2283; -. DR PaxDb; 189518-LA_2283; -. DR EnsemblBacteria; AAN49482; AAN49482; LA_2283. DR KEGG; lil:LA_2283; -. DR PATRIC; fig|189518.3.peg.2269; -. DR HOGENOM; CLU_016316_5_2_12; -. DR InParanoid; Q8F3W6; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. 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; Reference proteome; KW Transferase. FT CHAIN 1..511 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192100" FT DOMAIN 1..147 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 511 AA; 56318 MW; 4E510B81D2909DD5 CRC64; MIQIKRALIS VSDKSGLVEF AKFLNQNGVE IISTGGTLKL LKDNGIAAIA IDDYTGFPEI LDGRVKTLHP KVHGGLLGVI SNPAHKQKME ELKIPKIDLV VVNLYPFLKT VSKPEVQLEE AIENIDIGGP SMIRSAAKNY KHTLVLTDPN DYKKIQNLIS SSGISEEISA SYMRKAFSHT AMYDAAISSW FYKQSGEVFP DVLNLSFIKK QKLRYGENPH QAASFYEPLF TKSDFSPLQG KELSFNNMLD FDAAFHISSL LPENTVCIIK HLNPCGIAYA DNPLEAFQLA RRTDPISAFG GVIGIKGQVN GELATSITEN FVEGVIAQKF TQEALEVFSK KPNIRLIEIQ DFKEALDELD LRPIHHGLLI QDRDYTTITE KDLKVVTKKQ PSPDDIRGLM FAWSCVRFIK SNAIVYTEEN ATLGIGAGQM SRVDSVQLGA NKALNVGLSV VGSYVASDAF FPFRDGIDAL AKAGAKAIIQ PGGSVRDEEV IQAADEHGLI MVFTGMRHFR H //