ID PUR9_XANCP STANDARD; PRT; 527 AA. AC Q8PD47; DT 15-SEP-2003 (Rel. 42, Created) DT 15-SEP-2003 (Rel. 42, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Bifunctional purine biosynthesis protein purH [Includes: DE Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) DE (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (Inosinicase) DE (IMP synthetase) (ATIC)]. GN PURH OR XCC0498. OS Xanthomonas campestris (pv. campestris). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=340; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33913 / NCPPB 528; RX MEDLINE=22022145; PubMed=12024217; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., RA Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., RA Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., RA Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., RA Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5- CC phosphoribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: De novo purine biosynthesis; ninth step. CC -!- PATHWAY: De novo purine biosynthesis; tenth step. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region (By similarity). CC -!- SIMILARITY: Belongs to the purH family. 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; AE012147; AAM39814.1; -. DR HAMAP; MF_00139; -; 1. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR004362; MGS_like. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR ProDom; PD004666; AICARFT_IMPCHas; 1. DR TIGRFAMs; TIGR00355; purH; 1. KW Purine biosynthesis; Transferase; Hydrolase; Multifunctional enzyme; KW Complete proteome. SQ SEQUENCE 527 AA; 55656 MW; AB8D097E73B3E51E CRC64; MASDFLPVRR ALLSVSDKTG LIDLARALVA RNVELLSTGG TAKAIRDAGL PVKDVAELTG FPEMMDGRVK TLHPLVHGGL LGRAGVDEAV MAEHGIAPID LLVLNLYPFE SVTAKADCTL ADAVENIDIG GPAMLRSAAK NFARVAVATD PAQYADLLAE LEANNGQLSA AQRFALSVAA FNRVAQYDAA ISNYLSAVAD SAESVPTRSP FPAQINSNFI KVMDLRYGEN PHQSGAFYRD LYPVPGTLAT FQQLQGKELS YNNLADADAA WECVRQFDAP ACVIVKHANP CGVAVGVACG DAYELAYATD PTSAFGGILA FNRTLDAATA KAILDRQFVE VLIAPDYEPG ALDYATKKAN VRVLKIPHGA GLNNYDTKRI GSGLLMQSAD NRGMSLGELS VVTKRAPSDA ELADLLFAWR VAKYVKSNAI VYAKDSRTIG VGAGQMSRVV SAKIAALKAE EAKLTVAGSV MASDAFFPFR DGIDAAAAAG IQAVIQPGGS MRDGEVIAAA DEHGLAMVFT GVRHFRH //