ID PUR9_CORA7 Reviewed; 510 AA. AC C3PF03; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 28-JAN-2026, entry version 84. 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=cauri_0810; OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / OS CN-1) (Corynebacterium nigricans). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=548476; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1; RX PubMed=20137072; DOI=10.1186/1471-2164-11-91; RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R., RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H., RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.; RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a RT vaginal swab of a woman with spontaneous abortion."; RL BMC Genomics 11:91-91(2010). 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; CP001601; ACP32407.1; -; Genomic_DNA. DR RefSeq; WP_010187644.1; NC_012590.1. DR AlphaFoldDB; C3PF03; -. DR SMR; C3PF03; -. DR STRING; 548476.cauri_0810; -. DR GeneID; 31923435; -. DR KEGG; car:cauri_0810; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_11; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000002077; 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; 3.40.50.1380: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..510 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000122955" FT DOMAIN 2..150 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 510 AA; 54834 MW; AA6592523844B7A6 CRC64; MSEDPKNIKR ALISVYDKTG LEDLARALDN AGVEIVSTGS TAKKIADLGI DVTPVEKLTG FPECLEGRVK TLHPRVHAGI LADTRKEDHL KQLEELEVEP FQLVVVNLYP FRETVASGAD FDGCVEQIDI GGPSMVRAAA KNHPSVAVVV DPARYGDVAD AVANGGFTLE ERRGLARDAF LHTADYDAAV SAWFVDQLSD GDVTTPLRYG ENSHQSATVT RIGTTGLANA KQFNGKEMSY NNYQDADAAW RAAWDHERPC VAIIKHANPC GIAVSEESIA AAHRAAHACD PMSAFGGVIA VNREVTVEMA EQVKEIFTEV IVAPSYEEGA IEVLKAKKNL RVLQAEHEAP KEEVKYISGG MLTQEPDTYQ AEGDNPANWT LAAGEALNES DLAQLEFAWR SVRAVKSNAI LLAKDNATVG VGMGQVNRVD SAKLAVERAN TLADGANRAE GSFAASDAFF PFADGLEVLL EAGVKAVVQP GGSIRDEEVI EAAKKAGVTM YFTGTRHFFH //