ID HIS2_ECOLI Reviewed; 203 AA. AC P06989; P78079; Q47596; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 3. DT 24-NOV-2009, entry version 91. DE RecName: Full=Histidine biosynthesis bifunctional protein hisIE; DE Includes: DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase; DE Short=PRA-CH; DE EC=3.5.4.19; DE Includes: DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=b2026, JW2008; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=89094829; PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5; RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.; RT "Structure and function of the Salmonella typhimurium and Escherichia RT coli K-12 histidine operons."; RL J. Mol. Biol. 203:585-606(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86310273; PubMed=3018428; DOI=10.1007/BF00422061; RA Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.; RT "Nucleotide sequence of the Escherichia coli hisD gene and of the RT Escherichia coli and Salmonella typhimurium hisIE region."; RL Mol. Gen. Genet. 203:382-388(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RC STRAIN=K12; RX MEDLINE=94260549; PubMed=8201624; DOI=10.1006/jmbi.1994.1384; RA Jovanovic G., Kostic T., Jankovic M., Savic D.J.; RT "Nucleotide sequence of the Escherichia coli K12 histidine operon RT revisited."; RL J. Mol. Biol. 239:433-435(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=O9:K31-:H- / F719; RX MEDLINE=95238291; PubMed=7536735; RA Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T., RA Kato N., Jann K.; RT "Expression of the O9 polysaccharide of Escherichia coli: sequencing RT of the E. coli O9 rfb gene cluster, characterization of mannosyl RT transferases, and evidence for an ATP-binding cassette transport RT system."; RL J. Bacteriol. 177:2178-2187(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). 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 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; X13462; CAA31818.1; -; Genomic_DNA. DR EMBL; X03974; CAA27613.1; -; Genomic_DNA. DR EMBL; U02072; AAA19744.1; -; Unassigned_DNA. DR EMBL; D43637; BAA07753.1; -; Genomic_DNA. DR EMBL; U00096; AAC75087.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15858.1; -; Genomic_DNA. DR PIR; JS0135; YNECHI. DR RefSeq; AP_002627.1; -. DR RefSeq; NP_416530.1; -. DR DIP; DIP:9907N; -. DR STRING; P06989; -. DR GeneID; 946515; -. DR GenomeReviews; AP009048_GR; JW2008. DR GenomeReviews; U00096_GR; b2026. DR KEGG; ecj:JW2008; -. DR KEGG; eco:b2026; -. DR EchoBASE; EB0446; -. DR EcoGene; EG10451; hisI. DR HOGENOM; P06989; -. DR OMA; VHYWSRS; -. DR BioCyc; EcoCyc:HISTCYCLOPRATPPHOS; -. DR BioCyc; ECOL168927:B2026-MON; -. DR BioCyc; MetaCyc:HISTCYCLOPRATPPHOS; -. DR Genevestigator; P06989; -. 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:HAMAP. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01019; -; 1. DR InterPro; IPR002496; PRA_CycHdrlase. DR InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase. DR Pfam; PF01502; PRA-CH; 1. DR Pfam; PF01503; PRA-PH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Multifunctional enzyme; KW Nucleotide-binding. FT CHAIN 1 203 Histidine biosynthesis bifunctional FT protein hisIE. FT /FTId=PRO_0000136411. FT REGION 1 114 Phosphoribosyl-AMP cyclohydrolase. FT REGION 115 203 Phosphoribosyl-ATP pyrophosphohydrolase. FT VARIANT 5 5 Q -> L (in strain: F719). FT VARIANT 46 46 L -> I (in strain: F719). FT VARIANT 164 164 H -> N (in strain: F719). FT VARIANT 192 193 TT -> GE (in strain: F719). FT VARIANT 196 196 E -> D (in strain: F719). FT VARIANT 199 200 RK -> KN (in strain: F719). FT VARIANT 203 203 Missing (in strain: F719). FT CONFLICT 68 68 S -> P (in Ref. 1; CAA31818). FT CONFLICT 193 193 T -> P (in Ref. 1 and 2). SQ SEQUENCE 203 AA; 22756 MW; 34019009D82E0122 CRC64; MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTLESGK VTFFSRTKQR LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL LVLLQDQGLD LTTVIENLRK RHQ //