ID PUR9_PSYA2 Reviewed; 526 AA. AC Q4FRN8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 112. 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=Psyc_1472; OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=259536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / VKM B-2377 / 273-4; RX PubMed=20154119; DOI=10.1128/aem.02101-09; RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., RA Murray A., Thomashow M., Tiedje J.M.; RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low- RT temperature growth."; RL Appl. Environ. Microbiol. 76:2304-2312(2010). 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; CP000082; AAZ19320.1; -; Genomic_DNA. DR RefSeq; WP_011280738.1; NC_007204.1. DR AlphaFoldDB; Q4FRN8; -. DR SMR; Q4FRN8; -. DR STRING; 259536.Psyc_1472; -. DR KEGG; par:Psyc_1472; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000546; 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..526 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000057906" FT DOMAIN 1..145 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 526 AA; 56508 MW; 95388A5911545799 CRC64; MSKAPLALLS VSDKSNIVEF AQGLIQAGFG LLSTGGTFRL LTEHNVAVTE VSDYTGFPEM MDGRVKTLHP KIHGGILGRR GTDDMVMSEH AIERIDLVVV NLYPFAETIA RSDVTMNDAI ENIDIGGPTM VRSAAKNHAH VGIVTDPADY TRVLEALGDS TALTATLRYD LAVKAFEHTA QYDGMIANFL GSRVNESQEP ESFSRTFNVQ LEKVQDLRYG ENPHQKAAFY VENNSSKSKQ ASIATAKQLQ GKALSYNNIA DTDAALECVK AFSTPACVIV KHANPCGVAV DIDQVAAYRT AFSTDPESSF GGIIAFNRPL TLAAATAIID NQFVEVIIAP SVEDGVLEAT ASKKNVRVLV CGDLPAPELR DRQLDYKRVN GGLLVQEQDL GLITAHDLKI VTDVQPTEAQ IADLLFSWNV AKYVKSNAIV YAKGQRTIGV GAGQMSRVNS ARIAAIKAEH AGLATEGAVM ASDAFFPFRD GIDNAAEVGI AAIIQPGGSM RDDETIAAAN EHGIAMVFTG MRHFRH //