ID   HIS2_MYCTU              Reviewed;          93 AA.
AC   P9WMM9; L0TBF1; O33257; P0A5B1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=Rv2122c; ORFNames=MTCY261.18;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(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   -!- 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; AL123456; CCP44897.1; -; Genomic_DNA.
DR   PIR; E70513; E70513.
DR   RefSeq; WP_003899180.1; NZ_NVQJ01000058.1.
DR   RefSeq; YP_177860.1; NC_000962.3.
DR   PDB; 1Y6X; X-ray; 1.25 A; A=1-93.
DR   PDB; 3C90; X-ray; 1.79 A; A/B/C/X=2-93.
DR   PDBsum; 1Y6X; -.
DR   PDBsum; 3C90; -.
DR   AlphaFoldDB; P9WMM9; -.
DR   SMR; P9WMM9; -.
DR   STRING; 83332.Rv2122c; -.
DR   PaxDb; P9WMM9; -.
DR   DNASU; 888671; -.
DR   GeneID; 45426097; -.
DR   GeneID; 888671; -.
DR   KEGG; mtu:Rv2122c; -.
DR   TubercuList; Rv2122c; -.
DR   eggNOG; COG0140; Bacteria.
DR   OMA; WMAAEYQ; -.
DR   PhylomeDB; P9WMM9; -.
DR   BRENDA; 3.6.1.31; 3445.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0075139; P:response to host iron concentration; IMP:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..93
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136371"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:1Y6X"
FT   HELIX           29..35
FT                   /evidence="ECO:0007829|PDB:1Y6X"
FT   HELIX           38..58
FT                   /evidence="ECO:0007829|PDB:1Y6X"
FT   HELIX           61..82
FT                   /evidence="ECO:0007829|PDB:1Y6X"
FT   HELIX           86..90
FT                   /evidence="ECO:0007829|PDB:1Y6X"
SQ   SEQUENCE   93 AA;  10275 MW;  E4CA193791812D1D CRC64;
     MQQSLAVKTF EDLFAELGDR ARTRPADSTT VAALDGGVHA LGKKLLEEAG EVWLAAEHES
     NDALAEEISQ LLYWTQVLMI SRGLSLDDVY RKL