ID PUR9_CALS4 Reviewed; 508 AA. AC Q8RC55; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 18-JUN-2025, entry version 113. 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=TTE0592; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis). OC Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., RA Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(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; AE008691; AAM23862.1; -; Genomic_DNA. DR RefSeq; WP_011025007.1; NC_003869.1. DR AlphaFoldDB; Q8RC55; -. DR SMR; Q8RC55; -. DR STRING; 273068.TTE0592; -. DR KEGG; tte:TTE0592; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_9; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000555; 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..508 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192143" FT DOMAIN 1..145 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 508 AA; 56362 MW; 42D2570B57C222A2 CRC64; MSRRALISVS KKDGIVEFAK KLEDLGYEII STGGTYNLLK ESGVKVIKVS EVTGFPEIMG GRVKTLHPKI HGGILAVRDK KEHLKDLNDH GIVPIDLVAI NLYPFKETIS REKVALEEAI ENIDIGGPAM IRAAAKNYKY VTVLVDPVDY EKVIEEIKLY GDTKEETRFY LAAKAFGHTA FYDSLIYEYF REKTNMEFPK VITFAYEKVQ DLRYGENPHQ KAAFYKNPVK SYGIAECLQL HGKELSFNNI NDANAAIELV REFSEPVAVA IKHTNPCGVA VGNSIYEAYL KAYEADPVSI FGGIVAFNGK VDVDTAKELV KIFLEIVIAP DFEEEALEIL MSKKNLRVLK LKEGYYREFD LKKVEGGVLV QQKDEIDLDE SSIKVVTKRA PTGKEMKDLK FAWKVVKHVK SNAIVLAKDG VTVGIGVGQV NRIWPTEQAI KQAGERAKGS VLASDAFFPF PDVVEAAARG GITAIIQPGG SQNDQLSIEA ADRAGIAMIF TGIRHFKH //