ID   HIS2_MYCLE              Reviewed;          93 AA.
AC   Q49786;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=ML1309; ORFNames=B2126_C2_204, MLCB2533.06;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA22920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00017; AAA17196.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL035310; CAA22920.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583921; CAC31690.1; -; Genomic_DNA.
DR   PIR; G87072; G87072.
DR   PIR; S72856; S72856.
DR   RefSeq; NP_301941.1; NC_002677.1.
DR   RefSeq; WP_010908262.1; NC_002677.1.
DR   AlphaFoldDB; Q49786; -.
DR   SMR; Q49786; -.
DR   STRING; 272631.ML1309; -.
DR   EnsemblBacteria; CAC31690; CAC31690; CAC31690.
DR   KEGG; mle:ML1309; -.
DR   PATRIC; fig|272631.5.peg.2415; -.
DR   Leproma; ML1309; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_2_0_11; -.
DR   OMA; WMAAEYQ; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000000806; 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   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..93
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136369"
SQ   SEQUENCE   93 AA;  10415 MW;  947F1CE449CDD3AE CRC64;
     MKQSLAVKTF EDLFAELSER ARTRPTDSAT VASLDGGIHA LGKKILEEAG EVWLAAEHEP
     KEVLAEEISQ LLYWTQVLMI SRGLSLDDVY RKL