ID PUR9_STRP3 Reviewed; 515 AA. AC P0DD60; Q8K8Y6; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 10-JUN-2026, entry version 59. 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=SpyM3_0024; OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=198466; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-595 / MGAS315; RX PubMed=12122206; DOI=10.1073/pnas.152298499; RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.; RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage- RT encoded toxins, the high-virulence phenotype, and clone emergence."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002). 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; AE014074; AAM78631.1; -; Genomic_DNA. DR RefSeq; WP_011054093.1; NC_004070.1. DR AlphaFoldDB; P0DD60; -. DR SMR; P0DD60; -. DR KEGG; spg:SpyM3_0024; -. DR HOGENOM; CLU_016316_5_2_9; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000564; Chromosome. 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; Reference proteome; KW Transferase. FT CHAIN 1..515 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192136" FT DOMAIN 1..145 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 515 AA; 56217 MW; 58C11340BBB97049 CRC64; MTKRALISVS DKSGIVDFAK ELKNLGWDII STGGTKVALD NAGVETIAID DVTGFPEMMD GRVKTLHPNI HGGLLARRDA DSHLQAAKDN NIELIDLVVV NLYPFKETIL RPDITYDLAV ENIDIGGPSM LRSAAKNHAS VTVVVDPADY ATVLGELADA GQTTFETRQR LAAKVFRHTA AYDALIAEYF TTQVGEAKPE KLTITYDLKQ AMRYGENPQQ DADFYQKALP IDYSIASAKQ LNGKELSFNN IRDADAAIRI IRDFKDRPTV VVLKHMNPCG IGQADDIETA WDYAYEADPV SIFGGIVVLN REVDAATAKK MHPIFLEIII APSYSEEALA ILTNKKKNLR ILELPFDAQA ASEVEAEYTG VVGGLLVQNQ DVVAENPSDW QVVTDRQPTE QEATALEFAW KAIKYVKSNG IIITNDHMTL GLGAGQTNRV GSVKIAIEQA KDHLDGAVLA SDAFFPFADN IEEIAAAGIK AIIQPGGSVR DQDSIDAANK HGLTMIFTGV RHFRH //