ID   HIS2_HALS3              Reviewed;          95 AA.
AC   B0R877;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020};
DE            Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020};
DE            EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020};
GN   Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020}; OrderedLocusNames=OE_4641R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC         ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01020};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_01020}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM774415; CAP14946.1; -; Genomic_DNA.
DR   RefSeq; WP_010903939.1; NC_010364.1.
DR   AlphaFoldDB; B0R877; -.
DR   SMR; B0R877; -.
DR   EnsemblBacteria; CAP14946; CAP14946; OE_4641R.
DR   GeneID; 5953455; -.
DR   GeneID; 62885701; -.
DR   KEGG; hsl:OE_4641R; -.
DR   HOGENOM; CLU_123337_0_0_2; -.
DR   OMA; FTHEKGE; -.
DR   PhylomeDB; B0R877; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   Pfam; PF01503; PRA-PH; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW   Hydrolase; Nucleotide-binding.
FT   CHAIN           1..95
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_1000135310"
SQ   SEQUENCE   95 AA;  10583 MW;  3479DA37D322DE60 CRC64;
     MSDPLRELFD VIEDRKETMP ENSYTASLLA DDEKGENAAL EKVGEEATEF LLAAKDGDTD
     ELAHEGADVV YHMLVVLAQQ DMDVEALLAE LDDRR