ID   HIS2_SYNY3              Reviewed;         215 AA.
AC   P74755;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   16-JUN-2009, entry version 55.
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=slr0608;
OS   Synechocystis sp. (strain PCC 6803).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18875.1; ALT_INIT; Genomic_DNA.
DR   PIR; S76963; S76963.
DR   RefSeq; NP_443063.1; -.
DR   GeneID; 951868; -.
DR   GenomeReviews; BA000022_GR; slr0608.
DR   KEGG; syn:slr0608; -.
DR   NMPDR; fig|1148.1.peg.3164; -.
DR   HOGENOM; P74755; -.
DR   BioCyc; SSP1148:SLR0608-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    215       Histidine biosynthesis bifunctional
FT                                protein hisIE.
FT                                /FTId=PRO_0000136440.
FT   REGION        1    126       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      127    215       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   215 AA;  23945 MW;  D8720E7D4BB80B60 CRC64;
     MSHSDLPLAN AVPLDKIRYN DQGLVPAIAQ DYLDGTVLML AWMNEAALAK TLATGQVWYW
     SRSRQELWHK GATSGHFQKL LGIRYDCDSD ALLLTIEQKG DIACHTGERS CFHQLDGHKS
     PPPADMLTEL ARVIGDRRDH PTPESYTCKL LAGGDNKILK KIGEESAEVV MACKDDDPEA
     IAGEVADLFY HTLVALAHHN VDLRAVYRKL GDRRR
//