ID   HIS3_ACIC1              Reviewed;         142 AA.
AC   A0LTT2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI; OrderedLocusNames=Acel_1070;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA   Leu D., Pujic P., Richardson P.;
RT   "Complete sequence of Acidothermus cellulolyticus 11B.";
RL   Submitted (OCT-2006) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000481; ABK52842.1; -; Genomic_DNA.
DR   RefSeq; YP_872828.1; -.
DR   GeneID; 4485318; -.
DR   GenomeReviews; CP000481_GR; Acel_1070.
DR   KEGG; ace:Acel_1070; -.
DR   OMA; A0LTT2; MMAWMDD.
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    142       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_1000063385.
SQ   SEQUENCE   142 AA;  15380 MW;  37DF237FA4937A7E CRC64;
     MTRRPSNLDP AIAARLKRDE HGLFPAVAQQ YDTGEVLMVG WMDDEALHRT LTTGRCTYWS
     RSRQEYWVKG ETSGHQQWVK SVALDCDGDT VLVKVDQIGA ACHTGDRTCF DAGQLPAVVG
     EPPTPVGAGE RQPASGTADA AP
//