ID HIS2_XANAC STANDARD; PRT; 206 AA. AC Q8PLG5; DT 29-MAR-2004 (Rel. 43, Created) DT 29-MAR-2004 (Rel. 43, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Histidine biosynthesis bifunctional protein hisIE [Includes: DE Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) (PRA-CH); DE Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) (PRA-PH)]. GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=XAC1835; OS Xanthomonas axonopodis (pv. citri). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=92829; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306 / ATCC 13902 / XV 101; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; 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., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., 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: 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5- CC phosphoribosyl)-AMP + diphosphate. CC -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5- CC phosphoribosyl)-5-((5- CC phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from PRPP: step 2. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from PRPP: step 3. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH CC 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; AE011816; AAM36697.1; -; Genomic_DNA. DR HAMAP; MF_01019; -; 1. DR InterPro; IPR008179; PRA-PH. DR InterPro; IPR002496; PRA_cyclohydro. DR InterPro; IPR008178; Pra_PH/CH. DR Pfam; PF01502; PRA-CH; 1. DR Pfam; PF01503; PRA-PH; 1. DR ProDom; PD002610; PRA_cyclohydro; 1. DR ProDom; PD002611; Pra_PH/CH; 1. KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Hydrolase; Multifunctional enzyme. FT REGION 1 117 Phosphoribosyl-AMP cyclohydrolase. FT REGION 118 206 Phosphoribosyl-ATP pyrophosphohydrolase. SQ SEQUENCE 206 AA; 22262 MW; 1B04984CEEFBD377 CRC64; MGSNEVATGD PLATLDWNKG EGLLPVIVQD ADNLRVLMLG YMNAQALAVT QQRGEVTFFS RSKQRLWTKG ESSGNVLRVV SIQTDCDADT LLVQARPHGP TCHLGRTSCF PSAPGQFLGS LDALVAERER ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQDDD ALLGESADLL YHLIVLLRAR GLGLGDAAAL LESRHQ //