ID   HIS22_RHOPA             Reviewed;         131 AA.
AC   P60539;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase 2;
DE            Short=PRA-PH 2;
DE            EC=3.6.1.31;
GN   Name=hisE2; OrderedLocusNames=RPA4705;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572608; CAE30145.1; -; Genomic_DNA.
DR   RefSeq; WP_011160237.1; NC_005296.1.
DR   AlphaFoldDB; P60539; -.
DR   SMR; P60539; -.
DR   STRING; 258594.RPA4705; -.
DR   PRIDE; P60539; -.
DR   EnsemblBacteria; CAE30145; CAE30145; RPA4705.
DR   GeneID; 66895862; -.
DR   KEGG; rpa:RPA4705; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_3_5; -.
DR   OMA; YECADLW; -.
DR   PhylomeDB; P60539; -.
DR   BioCyc; RPAL258594:TX73_RS24055-MON; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001426; 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..131
FT                   /note="Phosphoribosyl-ATP pyrophosphatase 2"
FT                   /id="PRO_0000136385"
FT   REGION          105..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  14605 MW;  52675BFD6E3DBE1C CRC64;
     MADSLDRLYQ AVLAARDLDP ATSRTARLFQ RGSGKMAKKL AEEAIEVVID AVNGNREAVI
     RESADLLYNL TVLWASAGVR PEDVWAEMRR RENLLGIAEK LPKSRIGKPA APHATRRPVI
     PQEARAVRKH R