ID   HIS3_AZOCH              Reviewed;         133 AA.
AC   Q43925;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yates M., Souza E.M.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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; U48404; AAA92106.1; -; Genomic_DNA.
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; Cytoplasm; Histidine biosynthesis; Hydrolase.
FT   CHAIN         1    133       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_0000136457.
SQ   SEQUENCE   133 AA;  15416 MW;  CEC538C94BE5EA34 CRC64;
     MKDWLDEIHW NADGLVPAIA QDHKTGRILM MAWMNRESLA LTVRENRAIY WSRSRGKLWR
     KGEESGHLQK VHEVRLDCDA DVIVLQVEQL GGIACHTGRE SCFYRVFEDG AWKVVEPILK
     DPDAIYHAGH RHE
//