ID   HIS2_STAES              Reviewed;         211 AA.
AC   Q8CQ91;
DT   06-JUN-2003, 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=SE_0277;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03874.1; -; Genomic_DNA.
DR   RefSeq; NP_763832.1; -.
DR   GeneID; 1058076; -.
DR   GenomeReviews; AE015929_GR; SE_0277.
DR   KEGG; sep:SE0277; -.
DR   HOGENOM; Q8CQ91; -.
DR   OMA; Q8CQ91; VHYWSRS.
DR   BioCyc; SEPI176280:SE_0277-MON; -.
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    211       Histidine biosynthesis bifunctional
FT                                protein hisIE.
FT                                /FTId=PRO_0000136436.
FT   REGION        1    107       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      108    211       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   211 AA;  24334 MW;  444A8063ABF82AF6 CRC64;
     MNKLIDFSKG LVPVILQHAQ TDSVLMLGYM NEEAYQKTLK EKKVTFFSRS KQRLWTKGET
     SGHFQHVESI HLDCDQDAIL IKVMPQGPTC HTGSLSCFNS EIESRFKIQA LAQTIHQSAK
     SNQSNSYTQY LLKEGIEKIS KKFGEEAFEV VIGAIKHNRE EVINETADVM YHLFVLLHSL
     DIPFSEVEQV LAHRHQKRNN FKGERKKVQE W
//