ID PUR9_POLAQ Reviewed; 526 AA. AC A4T025; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 96. 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=Pnuc_1877; OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 / OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=312153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1; RX PubMed=22675600; DOI=10.4056/sigs.2395367; RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T., RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.; RT "Complete genome sequence of Polynucleobacter necessarius subsp. RT asymbioticus type strain (QLW-P1DMWA-1(T))."; RL Stand. Genomic Sci. 6:74-83(2012). 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; CP000655; ABP35089.1; -; Genomic_DNA. DR RefSeq; WP_011903712.1; NC_009379.1. DR AlphaFoldDB; A4T025; -. DR SMR; A4T025; -. DR GeneID; 31482267; -. DR KEGG; pnu:Pnuc_1877; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_4; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000231; 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_1000076488" FT DOMAIN 1..145 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 526 AA; 56551 MW; 0C816811F14922EB CRC64; MIRTALLSVS DKNGIVPFAK SLHEQGIKLI STGGTAKLLA ENNLPVVEVS SLTKFPEMLD GRVKTLHPMV HGGLLARRDF PEHMAALEEH GIDTIDMLVI NLYPFNETVA KENCSFEDAV ENIDIGGPAM LRAAAKNHQD VTVLISPEDY APVLAEMKAN QNVVSYKTNL ALAKKVFAHT AQYDGSIANY LSALGDDLDH KARSAYPETL HLAFEKVQEM RYGENPHQSA AFYKDIYPVN GALANYKQLQ GKELSYNNIA DADSAWECVK SFAGNSGGAA ACVIIKHANP CGVAVGASAL EAYQKAFKTD PSSAFGGIIA FNIPCDGAAA QEISKQFVEV LIAPSFTDEA KAIFAAKQNV RLLEIPLGNA FNTFDFKRVG GGLLVQSPDA KNVLQNEMRV VSQRQPTPSE MNDMMFAWRV AKFVKSNAIV YCSNGMTLGI GAGQMSRVDS ARMASIKAEN AGLSLKGSAV ASDAFFPFRD GLDVVVNGGA SCAIQPGGSM RDDEIIAAAN EHGIAMIFTG TRHFRH //