ID   HIS2_PYRAE              Reviewed;          94 AA.
AC   Q8ZY18;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=PAE0986;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}.
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DR   EMBL; AE009441; AAL63178.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZY18; -.
DR   SMR; Q8ZY18; -.
DR   STRING; 178306.PAE0986; -.
DR   EnsemblBacteria; AAL63178; AAL63178; PAE0986.
DR   KEGG; pai:PAE0986; -.
DR   PATRIC; fig|178306.9.peg.733; -.
DR   eggNOG; arCOG02677; Archaea.
DR   HOGENOM; CLU_123337_0_0_2; -.
DR   OMA; FTHEKGE; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002439; 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   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; Reference proteome.
FT   CHAIN           1..94
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136396"
SQ   SEQUENCE   94 AA;  10471 MW;  6D77D4CA62117F29 CRC64;
     MSCQIFEKLE AVIRQRIAEG NPQSYTYRLY SSGVSTIARK VGEEAVEVAV AALAEGRERV
     VEESADLLYH LLVLLNSLGL SLGDVCKELE RRMK