ID PUR9_XYLFA Reviewed; 527 AA. AC Q9PC10; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 27-MAR-2024, entry version 110. 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=XF_1975; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). 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 -!- SEQUENCE CAUTION: CC Sequence=AAF84777.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE003849; AAF84777.1; ALT_INIT; Genomic_DNA. DR PIR; E82616; E82616. DR RefSeq; WP_031336542.1; NC_002488.3. DR AlphaFoldDB; Q9PC10; -. DR SMR; Q9PC10; -. DR STRING; 160492.XF_1975; -. DR KEGG; xfa:XF_1975; -. DR PATRIC; fig|160492.11.peg.2103; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000812; 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..527 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192151" FT DOMAIN 1..149 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 527 AA; 56715 MW; CD6E95EA587106A7 CRC64; MASDFLPVHR ALLSVSDKTG LVELARALLA YNIELLSTGG TATIIREAGL PVQDVADLTG FPEMMDGRVK TLHPMVHGGL LGRAGIDDAV MAKHGIAPID LLILNLYPFE QITAKKDCTL ADAVDTIDIG GPAMLRSAAK NFARVAVATS PDQYPDLLAE LQAHHGQLSA EKRFALAVAA FNHVAQYDAA ISNYLSSVSD MHTTLPLRHE FPAQLNNTFV KMTELRYGEN PHQTGAFYRD VHPQPGTLAT FQQLQGKTLS YNNLVDADAA WECVRQFEAP ACVIVKHANP CGVAVGKACS DAYEEAYATD PTSAFGGIIA VNRMLDVATM QSILDRQFVE VLIAPDYDAD ALAYATKKAN VRVLRIPSTG VMNRYDFKRI GSGLLVQSTD SLNIHSDALK VVTQLAPTDA QQRDLLFAWH VAKYVKSNAI VYAKDNRTIG IGAGQMSRVY SARIAGIKAA DAHLAVTGSV MASDAFFPFR DSIDAAAAAG IKAVIQPGGS MRDNEVIAAA DEHGIAMVFT GIRHFRH //