ID PUR9_CALS8 Reviewed; 513 AA. AC A4XKZ2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Csac_1992; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T OS 6331). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=351627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., RA Kengen S.M.W., Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000679; ABP67577.1; -; Genomic_DNA. DR RefSeq; WP_011917512.1; NC_009437.1. DR AlphaFoldDB; A4XKZ2; -. DR SMR; A4XKZ2; -. DR STRING; 351627.Csac_1992; -. DR KEGG; csc:Csac_1992; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_9; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000256; 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; Transferase. FT CHAIN 1..513 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_1000018866" FT DOMAIN 1..145 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 513 AA; 58028 MW; D217E2C207CBC537 CRC64; MTKKAIISVY NKDGILEFAK ELKNLGYEII STGGTMKYLK ENRIDVINIS DVTNFPEILD GRVKTLHPNI HAGILAIKDN EEHVKTLNDL NISTIDMVVV NLYPFKETIF RENVAFEDVI ENIDIGGPTM LRAAAKNFKY ITVIIDPADY GLVLKEIKEN GDVSFETRFY LATKVFEYTA YYDSMIFNYF KYIRGDKSFP DYLTVPLETV QKLRYGENPH QQASFYKITL PFIEKSNIAN AEQLHGKDLS YNNILDSDSA IELLKEFDEP TCVAIKHNNP CGVASGDNIF EAYKKVYNSD PVSIFGGIVA FNRKVDRQTA EELKKIFLEI VIAPDFDEDA LSLLSTKKDL RILKLLTLDK TDVYYDVKSV NGGMLVQEKD RKLLNEDYQV VTERRPTEKE IEDLIFAWKV VKHVKSNAIV IAKDKMTLGI GMGQTNRIWA VEHAISRSRF DLNGAVLASD AFFPFSDSVE AAGKAGITAI IQPGGSIRDK ESIDAANKYN IAMIFTGIRH FRH //