ID PUR9_NEIMF Reviewed; 526 AA. AC A1KTP9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 04-NOV-2026, entry version 95. 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=NMC0963; OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM OS 15464 / FAM18). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=272831; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700532 / DSM 15464 / FAM18; RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023; RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.; RT "Meningococcal genetic variation mechanisms viewed through comparative RT analysis of serogroup C strain FAM18."; RL PLoS Genet. 3:230-240(2007). 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; AM421808; CAM10236.1; -; Genomic_DNA. DR RefSeq; WP_002226408.1; NC_008767.1. DR AlphaFoldDB; A1KTP9; -. DR SMR; A1KTP9; -. DR KEGG; nmc:NMC0963; -. DR HOGENOM; CLU_016316_5_2_4; -. DR OMA; AAAMKPY; -. 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; purH; 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..526 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000018918" FT DOMAIN 1..147 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 526 AA; 57026 MW; E125CF52F1694623 CRC64; MPSIKRALIS LSDKTGAVEF AQTLTKLGVE ILSTGGTAKL LADAGVPVIE VADYTGFPEM LDGRVKTLHP KIHGGILGRR DLDEHVAKME EHGIGNIDLV CVNLYPFAAT IAKPNCTLED AIENIDIGGP TMVRSAAKNW KHVAIVTDTA DFPAIAAELE ANNGALSDKT RFNLSRKAFS HTAQYDGMIS NYLTSLSDDV LSGEPEIGEF PSQFNQSWIK VQDMRYGENP HQRAAFYRDI DPAAGSLSAY KQLQGKELSY NNIADADAAW EAVKSFDAPA CVIVKHANPC GVAVAADTLT AYKLAYVTDT TSAFGGIIAF NREVDGETVK QITDNQFMEV LMAPKFTAEA LEIAAAKKNV RVLEVPLEAG ANRFELKRVG GGLLVQTPDI HRLNRADLKV VSKRQPTEQE WNDLMFVWNV AKYVKSNAIV FGKGGQTYGI GAGQMSRVDS TRIAARKAQD ANLDLNGACA ASDAFFPFRD GVDVIAEQGI KAIIHPAGSM RDQEVFDAAD EHGIAMVVTD VRHFRH //