ID   HIS2_BRUME              Reviewed;         107 AA.
AC   P64351; Q8YE38;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=BMEI2040;
OS   Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094
OS   / 16M).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella;
OC   Brucella melitensis group.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL53221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL53221.1; ALT_INIT; Genomic_DNA.
DR   PIR; AB3507; AB3507.
DR   RefSeq; WP_002965152.1; NC_003317.1.
DR   AlphaFoldDB; P64351; -.
DR   SMR; P64351; -.
DR   GeneID; 93017603; -.
DR   KEGG; bme:BMEI2040; -.
DR   KEGG; bmel:DK63_1453; -.
DR   PATRIC; fig|224914.52.peg.1530; -.
DR   eggNOG; COG0140; Bacteria.
DR   PhylomeDB; P64351; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000000419; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   NCBIfam; TIGR03188; histidine_hisI; 1.
DR   NCBIfam; NF001613; PRK00400.1-5; 1.
DR   PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR42945:SF9; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HISIE; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..107
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136352"
SQ   SEQUENCE   107 AA;  11253 MW;  4335A80E49ACB391 CRC64;
     MSQFTLADLE RIVAERASVT DGTSYTASLV AKGQPKAAQK LGEEAVETVI AAVSGDRAGV
     VSESADLLYH LAVVWNIAGV ALEDVLQELQ RRTAQTGLAE KASRPKG
//