ID PUR9_PHOLL Reviewed; 529 AA. AC Q7N954; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 115. 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=plu0495; OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / OS TT01) (Photorhabdus luminescens subsp. laumondii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., RA Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). 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; BX571860; CAE12790.1; -; Genomic_DNA. DR RefSeq; WP_011144880.1; NC_005126.1. DR AlphaFoldDB; Q7N954; -. DR SMR; Q7N954; -. DR STRING; 243265.plu0495; -. DR GeneID; 24168160; -. DR KEGG; plu:plu0495; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000002514; 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..529 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000018924" FT DOMAIN 2..148 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 529 AA; 57683 MW; 3680DA643CC313F8 CRC64; MQQLRPIHRA LLSVSDKSGV VEFAKALSQR GVELLSTGGT ARLLAESDLK VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDEIM AQHQISPIDM VVVNLYPFAQ TVAKPDCTLA DAVENIDIGG PTMVRSAAKN HKDVAIVVNS KDYKKIIEEM DNNQGSLTQS TRFDLAIKAF EHTAAYDSMI ANYFGKLVPP YHGDTTQPSG RFPRTLNLNF IKKQDMRYGE NSHQDAAFYI EENLSESSIA TATQLQGKAL SYNNIADTDA ALECVKEFVE PACVIVKHAN PCGVAIGKDI HEAYDSAFKT DPTSAFGGII AFNRELDIKT AQAIIDRQFV EVIIAPSVNK DVLPVLATKQ NIRVLVCGEW EDRAAGLDFK RVNGGLLVQD RDLGMVAVTN LRVVSKRHPT EQEMKDALFC WKVAKFVKSN AIVYAKNDMT IGIGAGQMSR VYSAKIAGIK AADEGLEVQG CAMASDAFFP FRDGIDAAAA VGVSCIIQPG GSIRDDEVIT AADEHGIAMI FTGMRHFRH //