ID HISN_MYCTU Reviewed; 260 AA.
AC P95189; L0TBY2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Histidinol-phosphatase;
DE Short=HolPase;
DE EC=3.1.3.15;
DE AltName: Full=Histidinol-phosphate phosphatase;
GN Name=hisN; Synonyms=impC; OrderedLocusNames=Rv3137;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP DISRUPTION PHENOTYPE, ESSENTIAL GENE, INDUCTION, AND MUTAGENESIS OF ASP-86.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20167072; DOI=10.1186/1471-2180-10-50;
RA Movahedzadeh F., Wheeler P.R., Dinadayala P., Av-Gay Y., Parish T.,
RA Daffe M., Stoker N.G.;
RT "Inositol monophosphate phosphatase genes of Mycobacterium tuberculosis.";
RL BMC Microbiol. 10:50-50(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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 -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC histidinol, the direct precursor of histidine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC -!- INDUCTION: When comparing gene expression levels of the four IMPase
CC family genes in exponential cultures of M.tuberculosis, the level of
CC cysQ is the highest, almost equal to sigA; impA and impC are expressed
CC at approximately 40% of this level, while suhB is lowest, at 12% of the
CC cysQ level. {ECO:0000269|PubMed:20167072}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene appear to be not
CC viable, even in the presence of high levels of exogenous inositol.
CC {ECO:0000269|PubMed:20167072}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45948.1; -; Genomic_DNA.
DR PIR; B70646; B70646.
DR RefSeq; NP_217653.1; NC_000962.3.
DR RefSeq; WP_003917127.1; NZ_NVQJ01000019.1.
DR PDB; 5YHT; X-ray; 2.87 A; A/B=2-260.
DR PDB; 5ZON; X-ray; 1.94 A; A/B/C/D=2-260.
DR PDBsum; 5YHT; -.
DR PDBsum; 5ZON; -.
DR AlphaFoldDB; P95189; -.
DR SMR; P95189; -.
DR STRING; 83332.Rv3137; -.
DR PaxDb; 83332-Rv3137; -.
DR DNASU; 888827; -.
DR GeneID; 888827; -.
DR KEGG; mtu:Rv3137; -.
DR TubercuList; Rv3137; -.
DR eggNOG; COG0483; Bacteria.
DR InParanoid; P95189; -.
DR OrthoDB; 9772456at2; -.
DR PhylomeDB; P95189; -.
DR BRENDA; 3.1.3.15; 3445.
DR Reactome; R-MTU-879299; Mycothiol biosynthesis.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004401; F:histidinol-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010125; P:mycothiol biosynthetic process; TAS:Reactome.
DR CDD; cd01641; Bacterial_IMPase_like_1; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR011809; His_9_proposed.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR02067; his_9_HisN; 1.
DR PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..260
FT /note="Histidinol-phosphatase"
FT /id="PRO_0000404323"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 86
FT /note="D->N: Causes a probable loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20167072"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 38..58
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:5ZON"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 75..86
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5ZON"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5ZON"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5YHT"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5ZON"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5ZON"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:5ZON"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:5ZON"
SQ SEQUENCE 260 AA; 27693 MW; CBCD2C2AA3E01518 CRC64;
MSHDDLMLAL ALADRADELT RVRFGALDLR IDTKPDLTPV TDADRAVESD VRQTLGRDRP
GDGVLGEEFG GSTTFTGRQW IVDPIDGTKN FVRGVPVWAS LIALLEDGVP SVGVVSAPAL
QRRWWAARGR GAFASVDGAR PHRLSVSSVA ELHSASLSFS SLSGWARPGL RERFIGLTDT
VWRVRAYGDF LSYCLVAEGA VDIAAEPQVS VWDLAALDIV VREAGGRLTS LDGVAGPHGG
SAVATNGLLH DEVLTRLNAG
//
