ID   HIS2_PARL1              Reviewed;         109 AA.
AC   A7HSG7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020};
DE            Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020};
DE            EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020};
GN   Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020}; OrderedLocusNames=Plav_1230;
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Parvibaculaceae; Parvibaculum.
OX   NCBI_TaxID=402881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA   Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT   1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01020};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_01020}.
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DR   EMBL; CP000774; ABS62850.1; -; Genomic_DNA.
DR   RefSeq; WP_012110118.1; NC_009719.1.
DR   AlphaFoldDB; A7HSG7; -.
DR   SMR; A7HSG7; -.
DR   STRING; 402881.Plav_1230; -.
DR   EnsemblBacteria; ABS62850; ABS62850; Plav_1230.
DR   KEGG; pla:Plav_1230; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_2_5; -.
DR   OMA; FTHEKGE; -.
DR   OrthoDB; 2022633at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000006377; 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..109
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000319657"
SQ   SEQUENCE   109 AA;  11324 MW;  672A22B94D104A93 CRC64;
     MAADASQLDR LFEVIAARKG ADAGSSYTAK LLAKGVPACA QKLGEEAVET VIAAVSGDGG
     GVVSESADLL YHWLVLMAAS NTDPADVYAE LERREGRSGL TEKAARGER