ID HIS2_XANAC Reviewed; 206 AA. AC Q8PLG5; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 22-APR-2020, entry version 99. DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE {ECO:0000255|HAMAP-Rule:MF_01019}; DE Includes: DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01019}; DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01019}; DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01019}; DE Includes: DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01019}; DE Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01019}; DE EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01019}; GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01019}; GN Synonyms=hisIE {ECO:0000255|HAMAP-Rule:MF_01019}; GN OrderedLocusNames=XAC1835; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX 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., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D- CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01019}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta- CC D-ribosyl)-5-[(5-phospho-beta-D- CC ribosylamino)methylideneamino]imidazole-4-carboxamide; CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, CC ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01019}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC {ECO:0000255|HAMAP-Rule:MF_01019}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC {ECO:0000255|HAMAP-Rule:MF_01019}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01019}. CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. CC {ECO:0000255|HAMAP-Rule:MF_01019}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family. CC {ECO:0000255|HAMAP-Rule:MF_01019}. 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; AE008923; AAM36697.1; -; Genomic_DNA. DR RefSeq; WP_003486226.1; NC_003919.1. DR SMR; Q8PLG5; -. DR STRING; 190486.XAC1835; -. DR EnsemblBacteria; AAM36697; AAM36697; XAC1835. DR KEGG; xac:XAC1835; -. DR eggNOG; ENOG4105K8F; Bacteria. DR eggNOG; COG0139; LUCA. DR eggNOG; COG0140; LUCA. DR HOGENOM; CLU_048577_3_1_6; -. DR KO; K11755; -. DR OMA; ERSCFHQ; -. DR BioCyc; XAXO190486:XAC_RS09330-MONOMER; -. DR UniPathway; UPA00031; UER00007. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000000576; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd11534; NTP-PPase_HisIE_like; 1. DR Gene3D; 3.10.20.400; -; 1. DR HAMAP; MF_01020; HisE; 1. DR HAMAP; MF_01019; HisIE; 1. DR InterPro; IPR023019; His_synth_HisIE. DR InterPro; IPR008179; HisE. DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf. DR Pfam; PF01502; PRA-CH; 1. DR Pfam; PF01503; PRA-PH; 1. DR SUPFAM; SSF141734; SSF141734; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis; KW Hydrolase; Multifunctional enzyme; Nucleotide-binding. FT CHAIN 1..206 FT /note="Histidine biosynthesis bifunctional protein HisIE" FT /id="PRO_0000136450" FT REGION 1..117 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT REGION 118..206 FT /note="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 //