ID PUR9_LIMRD Reviewed; 512 AA. AC A5VHU2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 100. 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=Lreu_0144; OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Limosilactobacillus. OX NCBI_TaxID=557436; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20016; RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314; RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N., RA Kyrpides N.C., Walter J.; RT "The evolution of host specialization in the vertebrate gut symbiont RT Lactobacillus reuteri."; RL PLoS Genet. 7:E1001314-E1001314(2011). 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; CP000705; ABQ82416.1; -; Genomic_DNA. DR RefSeq; WP_003669729.1; NZ_AZDD01000012.1. DR AlphaFoldDB; A5VHU2; -. DR SMR; A5VHU2; -. DR STRING; 557436.Lreu_0144; -. DR KEGG; lre:Lreu_0144; -. DR PATRIC; fig|557436.17.peg.319; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_9; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000001991; 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; Reference proteome; KW Transferase. FT CHAIN 1..512 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000057899" FT DOMAIN 1..144 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 512 AA; 57033 MW; ECEC7A2970255506 CRC64; MKRALVSVSD KQNLVPFVKG LVENGFEIIS TGGTKRVLDE AGIETIGIED VTHFPEILDG RVKTLNPYVH GGLLARRNLP EHMATLEKLN ITPIDLVCVN LYPFKETIEK PGVEIADAIE NIDIGGPSMV RSAAKNYHDV TIVVDQADYD EVLAQIKEDG ETSLATRARL AAKAFRHTAA YDSLISQYLT KQTGLEDPEK LTLSWDLKET MRYGENSHQK AWLYEDALPK AFSVLQAKQL HGKKLSYNNI KDADEALRCI REFDEPTVVA MKHMNPCGIG RGDSLVQAWD RAYEADPVSI FGGVIALNRQ VDLVTAEKMH KIFLEIVIAP GFDDDAFELL AKKKNIRLLT LDFSKKDEPT KHEVVSVMGG MLLQEQDMLK EDYHDWQCVT EKQPTEEQLK TLMFAWKAVK HAKSNAIVLA NDERTLGVGE GQPNRIDSLK IAVKHAGEAI DDRTVMASDA FFPFGDCVEY AGQNGIKAIV QPGGSVRDQE SIEMANKYGI AMVTTGIRHF RH //