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HISN_MYCTU
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   03-AUG-2022, entry version 132.
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; 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 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.m111.011627;
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   -!- 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; P95189; -.
DR   PRIDE; P95189; -.
DR   DNASU; 888827; -.
DR   GeneID; 888827; -.
DR   KEGG; mtu:Rv3137; -.
DR   TubercuList; Rv3137; -.
DR   eggNOG; COG0483; Bacteria.
DR   InParanoid; P95189; -.
DR   OMA; WRTRAYG; -.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0010125; P:mycothiol biosynthetic process; TAS:Reactome.
DR   InterPro; IPR011809; His_9_proposed.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR02067; his_9_HisN; 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
 
 
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