ID   HIS2_ECOL6              Reviewed;         203 AA.
AC   Q8FG47;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=c2553;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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 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 (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.
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DR   EMBL; AE014075; AAN81008.1; -; Genomic_DNA.
DR   RefSeq; NP_754441.1; -.
DR   GeneID; 1037829; -.
DR   GenomeReviews; AE014075_GR; c2553.
DR   KEGG; ecc:c2553; -.
DR   HOGENOM; Q8FG47; -.
DR   OMA; Q8FG47; VHYWSRS.
DR   BRENDA; 3.5.4.19; 292881.
DR   BRENDA; 3.6.1.31; 292881.
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_cyclohydro; 1.
DR   ProDom; PD002611; Pra_PH/CH; 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_0000136412.
FT   REGION        1    114       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      115    203       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   203 AA;  22828 MW;  3BBF7F6AE84D646C CRC64;
     MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDRTIESGK VTFFSRTKQR
     LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ
     LLAERKSADP ETSYTAKLYA SGSKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL
     LVLLQDQDLD LTTVIENLRK RHQ
//