ID PUR9_LACLS Reviewed; 518 AA. AC Q02Y66; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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=LACR_1605; OS Lactococcus lactis subsp. cremoris (strain SK11). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus; Lactococcus cremoris subsp. cremoris. OX NCBI_TaxID=272622; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK11; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). 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; CP000425; ABJ73106.1; -; Genomic_DNA. DR RefSeq; WP_011676465.1; NC_008527.1. DR AlphaFoldDB; Q02Y66; -. DR SMR; Q02Y66; -. DR KEGG; llc:LACR_1605; -. DR HOGENOM; CLU_016316_5_2_9; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000240; 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; Transferase. FT CHAIN 1..518 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000018901" FT DOMAIN 1..144 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 518 AA; 57140 MW; 0223F4472ED8AEA4 CRC64; MSKRALISVS DKEGIVEFAK KIQELGWEII STGGTKAVLD QEEIPNIAID EVTGFPEMMD GRVKTLHPLI HGALLGRRDL DSHMKSLAEH HISPIDLVVV NLYPFKETLL AGGSQAEMIE KIDIGGPSML RSAAKNHAAV TVVCDPMDYE KVEKELSADG ETSLELRQQL AAKVFRHTAS YDALIAQYLT EEFPVEDTKP EKLTLTYDLK QGMRYGENPQ QSADFYESGL PTTYSIAQSH QLHGKELSYN NVRDADAALQ IARDFDEPTV VALKHMNPCG IGTAKNIEQA WDYAYEADPV SIFGGIIVLN REVTEETAQK MSKIFLEIII APSYSKEALE ILSKKKNIRL LTVDFSKKEQ SEKEALVTGV LGGLLVQNQD VIVENPKEWT VATKVQPTDR QMEAMKFAWK AVKFVKSNGI IVTNDHQTLG VGPGQTNRVG SVKIALEATA DKDALLQENA VLGSDAFFPF ADNIDEIAKA GIKAIVQPGG SVRDQEVIEA CDKYGIAMVF TGLRHFRH //