ID   HIS2_SACS2              Reviewed;          94 AA.
AC   O33776;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 3.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=SSO6223;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=9209067; DOI=10.1128/jb.179.13.4429-4432.1997;
RA   Charlebois R.L., Sensen C.W., Doolittle W.F., Brown J.R.;
RT   "Evolutionary analysis of the hisCGABdFDEHI gene cluster from the archaeon
RT   Sulfolobus solfataricus P2.";
RL   J. Bacteriol. 179:4429-4432(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U82227; AAB63024.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40910.1; ALT_INIT; Genomic_DNA.
DR   PIR; G90206; G90206.
DR   RefSeq; WP_009991118.1; NC_002754.1.
DR   AlphaFoldDB; O33776; -.
DR   SMR; O33776; -.
DR   STRING; 273057.SSO6223; -.
DR   EnsemblBacteria; AAK40910; AAK40910; SSO6223.
DR   GeneID; 44129600; -.
DR   KEGG; sso:SSO6223; -.
DR   PATRIC; fig|273057.12.peg.606; -.
DR   eggNOG; arCOG02677; Archaea.
DR   HOGENOM; CLU_123337_1_1_2; -.
DR   InParanoid; O33776; -.
DR   OMA; FTHEKGE; -.
DR   PhylomeDB; O33776; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001974; 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; Reference proteome.
FT   CHAIN           1..94
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136398"
SQ   SEQUENCE   94 AA;  10853 MW;  CBD50DBE2C9382E6 CRC64;
     MSNEIVDELY KIILDRIEKR PTGSYTAEIV NKGKPYVARK VGEESVETIV ASLAENKERF
     ISEVADLIYH LLVLMALEGV TPEDIYRELE RRRK