ID PUR9_MAGMM Reviewed; 532 AA. AC A0LDB0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 28-JAN-2026, entry version 97. 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=Mmc1_3468; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Pseudomonadati; Pseudomonadota; Magnetococcia; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1; RX PubMed=19465526; DOI=10.1128/aem.02874-08; RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D., RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.; RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic RT coccus strain MC-1."; RL Appl. Environ. Microbiol. 75:4835-4852(2009). 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; CP000471; ABK45953.1; -; Genomic_DNA. DR RefSeq; WP_011715009.1; NC_008576.1. DR AlphaFoldDB; A0LDB0; -. DR SMR; A0LDB0; -. DR STRING; 156889.Mmc1_3468; -. DR KEGG; mgm:Mmc1_3468; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_5; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000002586; 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..532 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000192978" FT DOMAIN 1..147 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 532 AA; 57270 MW; 9B4C77A1369F150C CRC64; MAKIKRALIS VSDKTGLVPF CQGLAEHGVS FLSTGGTARL LRESGLDVMD VSEFTGFPEM LDGRVKTLHP KVHGGLLGLR DNASHQQQMG EHGIEPIDMV VVNLYPFEAT VAKEGCTLEE AIENIDIGGP SMLRSAAKNY RSVTVVTDPA DYARVLESLR AHDGQCDAGL NAQLARKVYA RTAAYDAAIS NWLSALDNEG RPGAFPETYT VQFKKVQGMR YGENPHQSAA FYAESPPSEE ASLATATQLQ GKELSFNNIH DANGALELVK EFSKPAAVVV KHANPCGVAV HDGDLLAAYR MARDTDPVSA FGGIIALNRC VDVAVAKEIA QLFVEVIIAP EYDEQALELF ATKKNLRLLR VPNIGVATAV STMDLKRVTG GLLLQDRDLK QLPEGSLKVV TERAPSEAEM RDLLFAWKVV KHVKSNAIVY AKEQRTLGVG AGQMSRVDAS RIAVWKAQDT AHTAGLRENP LLGAAMASDA FFPFRDGVDA AAKAGAKAVI QPGGSVRDEE VIAAANEHGM AMVFTGMRHF KH //