ID   HIS21_BRADU             Reviewed;         106 AA.
AC   Q89WM3;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase 1;
DE            Short=PRA-PH 1;
DE            EC=3.6.1.31;
GN   Name=hisE1; OrderedLocusNames=blr0655;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC45920.1; -; Genomic_DNA.
DR   RefSeq; NP_767295.1; NC_004463.1.
DR   RefSeq; WP_011083482.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89WM3; -.
DR   SMR; Q89WM3; -.
DR   STRING; 224911.27348904; -.
DR   EnsemblBacteria; BAC45920; BAC45920; BAC45920.
DR   GeneID; 64020517; -.
DR   KEGG; bja:blr0655; -.
DR   PATRIC; fig|224911.44.peg.24; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_1_5; -.
DR   InParanoid; Q89WM3; -.
DR   OMA; FTHEKGE; -.
DR   PhylomeDB; Q89WM3; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002526; 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..106
FT                   /note="Phosphoribosyl-ATP pyrophosphatase 1"
FT                   /id="PRO_0000136350"
SQ   SEQUENCE   106 AA;  11536 MW;  6702D7FBFE9C0A03 CRC64;
     MPRFTIHDLA ETIDARAAAG GEGSYTRKLL DKGAEHCAKK FGEEAVETVI AAVENDRAHL
     IAEGADLLYH FLVLLKARGI KLEEVEAALG KRTSMSGLEE KASRKE