ID   HIS3_BORA1              Reviewed;         134 AA.
AC   Q2KTT0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI; OrderedLocusNames=BAV3320;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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 3/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PRA-CH family.
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DR   EMBL; AM167904; CAJ50930.1; -; Genomic_DNA.
DR   RefSeq; YP_787815.1; -.
DR   GeneID; 6267176; -.
DR   GenomeReviews; AM167904_GR; BAV3320.
DR   KEGG; bav:BAV3320; -.
DR   NMPDR; fig|521.1.peg.1945; -.
DR   HOGENOM; Q2KTT0; -.
DR   OMA; Q2KTT0; LWLKGES.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01021; -; 1.
DR   InterPro; IPR002496; PRA_CycHdrlase.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_cyclohydro; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase.
FT   CHAIN         1    134       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_1000063390.
SQ   SEQUENCE   134 AA;  15013 MW;  4D5DACC40E478E89 CRC64;
     MSTEPDWMAD VVFDADGLIP AIAQDAENGQ ILMVAWMNRE SLAETAATGR AVYWSRSRKK
     LWRKGEESGH AQQVHELRLD CDGDVILLKV HQNGGIACHT GRASCFYRRL DGTSQRAAWV
     TVDPVLKDPE LIYK
//