ID PUR9_LISMF Reviewed; 509 AA. AC Q71YQ3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. 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=LMOf2365_1790; OS Listeria monocytogenes serotype 4b (strain F2365). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F2365; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H., RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., RA Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne RT pathogen Listeria monocytogenes reveal new insights into the core genome RT components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). 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; AE017262; AAT04561.1; -; Genomic_DNA. DR RefSeq; WP_003726208.1; NC_002973.6. DR AlphaFoldDB; Q71YQ3; -. DR SMR; Q71YQ3; -. DR KEGG; lmf:LMOf2365_1790; -. DR HOGENOM; CLU_016316_5_2_9; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. 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..509 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192102" FT DOMAIN 1..144 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 509 AA; 54911 MW; EE5D704F1A683D8F CRC64; MKRALISVSD KNGIVPFAEK LVELGVEIIS TGGTKAAFEQ AGVPVTGIEE VTEFPEMLDG RVKTLHPAIH GGLLARRDTA EHMEAIAAHD IKPIDLVVVN LYPFQETIQK SGVTLEEAIE NIDIGGPSML RSAAKNYAAV TVVVDTADYD TVLTELEEHG ATTFETRQRL AAKVFRHTAA YDALIAEYLT NITGETFPEK VTLTYNRKQV LRYGENPHQD AAFYTEPGTV ENSISSAKQL HGKELSYNNI RDADAALKIA SEFTEPVAVA VKHMNPCGVG VGENIEEAYL KAYEADETSI FGGIVALNKE VDAKTAEHMS KIFLEIIIAP SFSEEAFAIL AKKKNIRLLT VPFAGSVKGF EKTSVNGGLL IQASDSVIED TASYEVVTEK QPTEAEMKAL IAQWKIVKHV KSNAIVVGSD KQTLGIGAGQ MNRIGSALIA LKQAGEKAKG AVLASDAFFP MDDTVEAAAK AGITAIIQPG GSIKDKESIE MANKYGISMV LTHVRHFKH //