ID   HIS2_STAAW              Reviewed;         210 AA.
AC   Q8NUI4;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, 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=MW2591;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(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; BA000033; BAB96456.1; -; Genomic_DNA.
DR   RefSeq; NP_647408.1; -.
DR   GeneID; 1004727; -.
DR   GenomeReviews; BA000033_GR; MW2591.
DR   KEGG; sam:MW2591; -.
DR   HOGENOM; Q8NUI4; -.
DR   OMA; Q8NUI4; VHYWSRS.
DR   BioCyc; SAUR196620:MW2591-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    210       Histidine biosynthesis bifunctional
FT                                protein hisIE.
FT                                /FTId=PRO_0000136435.
FT   REGION        1    106       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      107    210       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   210 AA;  23973 MW;  EB5AA9395B1DB6D7 CRC64;
     MTNYKIDFSK GLVPAILQDN QTKQVLMLGY MNQEAFDKTI EDGVVCFYSR SKQRLWTKGE
     TSGHTQRVKD IHVDCDNDTI LIDVIPNGPT CHTGSQSCFN TEVPFSVQTL AQTVQDSAQS
     NNEKSYTKYL LTEGIEKITK KYGEEAFEVV IEAIKGDKKA FVSEVADELY HLFVLMHALG
     VDFSEIEAEL ARRHHKRNNF KGERQNIEQW
//