ID   HIS2_TERTT              Reviewed;         110 AA.
AC   C6AR38;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=TERTU_3195;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001614; ACS93582.1; -; Genomic_DNA.
DR   RefSeq; WP_015820976.1; NC_012997.1.
DR   AlphaFoldDB; C6AR38; -.
DR   SMR; C6AR38; -.
DR   STRING; 377629.TERTU_3195; -.
DR   EnsemblBacteria; ACS93582; ACS93582; TERTU_3195.
DR   GeneID; 58410580; -.
DR   KEGG; ttu:TERTU_3195; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_2_6; -.
DR   OMA; FTHEKGE; -.
DR   OrthoDB; 2022633at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000009080; 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..110
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_1000213296"
SQ   SEQUENCE   110 AA;  12341 MW;  B2B6C29033476AE7 CRC64;
     MSDVLAELDK VLAQRKNAGD PESSYVAKLH HKGLNKILEK VGEECTETIL AAKDAQHDSD
     TQHLIYETAD LWFHSLVMLS HLGLSAEDVL NELARRFDLS GLEEKARRQS