ID   HIS2_PSEAE              Reviewed;         111 AA.
AC   Q9HUB6;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=PA5067;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG08452.1; -; Genomic_DNA.
DR   PIR; F83011; F83011.
DR   RefSeq; NP_253754.1; NC_002516.2.
DR   RefSeq; WP_003103458.1; NZ_QZGE01000002.1.
DR   AlphaFoldDB; Q9HUB6; -.
DR   SMR; Q9HUB6; -.
DR   STRING; 287.DR97_2422; -.
DR   PaxDb; Q9HUB6; -.
DR   PRIDE; Q9HUB6; -.
DR   DNASU; 878486; -.
DR   EnsemblBacteria; AAG08452; AAG08452; PA5067.
DR   GeneID; 878486; -.
DR   KEGG; pae:PA5067; -.
DR   PATRIC; fig|208964.12.peg.5311; -.
DR   PseudoCAP; PA5067; -.
DR   HOGENOM; CLU_123337_1_2_6; -.
DR   InParanoid; Q9HUB6; -.
DR   OMA; FTHEKGE; -.
DR   PhylomeDB; Q9HUB6; -.
DR   BioCyc; PAER208964:G1FZ6-5183-MON; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002438; 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..111
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136376"
SQ   SEQUENCE   111 AA;  12039 MW;  76AD64BE572048D3 CRC64;
     MSDTLTRLAA VLEERKNAAP DSSYVASLYH KGLNKILEKV GEESVETIIA AKDAAASGDC
     QDLIYETADL WFHSLVMLSA LGQHPQAVLD ELERRFGLSG HAEKAARQPS A