ID   HIS2_AZOBR              Reviewed;         111 AA.
AC   P26722;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sp6;
RX   PubMed=2664449; DOI=10.1007/bf00334360;
RA   Fani R., Bazzicalupo M., Damiani G., Bianchi A., Schipani C.,
RA   Sgaramella V., Polsinelli M.;
RT   "Cloning of histidine genes of Azospirillum brasilense: organization of the
RT   ABFH gene cluster and nucleotide sequence of the hisB gene.";
RL   Mol. Gen. Genet. 216:224-229(1989).
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; X61207; CAA43520.1; -; Genomic_DNA.
DR   PIR; S16803; S16803.
DR   RefSeq; WP_035670299.1; NZ_WFKD01000020.1.
DR   AlphaFoldDB; P26722; -.
DR   SMR; P26722; -.
DR   GeneID; 56449787; -.
DR   OrthoDB; 2022633at2; -.
DR   UniPathway; UPA00031; UER00007.
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..111
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136341"
SQ   SEQUENCE   111 AA;  11946 MW;  EA8BDE3A36864500 CRC64;
     MAEDKISAAV LDRLYATVQA RKGADPETSY TAKLFHRGTA KIAQKVGEEA VETVIEAVRG
     DKAAMASESA DLLYHLMVLW ADAGLEPAAV WEKLAQREGT SGIAEKNARK S