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Protein

Histidinol-phosphatase

Gene

hisN

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.By similarity

Catalytic activityi

L-histidinol phosphate + H2O = L-histidinol + phosphate.

Cofactori

Mg2+By similarity

Pathwayi: L-histidine biosynthesis

This protein is involved in step 8 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE), Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI), Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. Phosphoribosyl isomerase A (priA), Phosphoribosyl isomerase A (priA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Histidinol-phosphatase (hisN)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi67Magnesium 1By similarity1
Binding sitei67SubstrateBy similarity1
Metal bindingi83Magnesium 1By similarity1
Metal bindingi83Magnesium 2By similarity1
Metal bindingi85Magnesium 1; via carbonyl oxygenBy similarity1
Metal bindingi86Magnesium 2By similarity1
Binding sitei185SubstrateBy similarity1
Metal bindingi213Magnesium 2By similarity1
Binding sitei213SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • growth Source: MTBBASE
  • histidine biosynthetic process Source: UniProtKB
  • inositol metabolic process Source: GO_Central
  • inositol phosphate dephosphorylation Source: GO_Central
  • mycothiol biosynthetic process Source: Reactome
  • phosphatidylinositol phosphorylation Source: InterPro
  • signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7402-MONOMER.
ReactomeiR-MTU-879299. Mycothiol biosynthesis.
UniPathwayiUPA00031; UER00013.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphatase (EC:3.1.3.15)
Short name:
HolPase
Alternative name(s):
Histidinol-phosphate phosphatase
Gene namesi
Name:hisN
Synonyms:impC
Ordered Locus Names:Rv3137
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3137.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Strains lacking this gene appear to be not viable, even in the presence of high levels of exogenous inositol.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86D → N: Causes a probable loss of enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004043231 – 260Histidinol-phosphataseAdd BLAST260

Proteomic databases

PaxDbiP95189.

Expressioni

Inductioni

When comparing gene expression levels of the four IMPase family genes in exponential cultures of M.tuberculosis, the level of cysQ is the highest, almost equal to sigA; impA and impC are expressed at approximately 40% of this level, while suhB is lowest, at 12% of the cysQ level.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3137.

Structurei

3D structure databases

ProteinModelPortaliP95189.
SMRiP95189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 88Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiENOG4107TK4. Bacteria.
COG0483. LUCA.
HOGENOMiHOG000282239.
InParanoidiP95189.
KOiK05602.
OMAiTKPDMTP.
PhylomeDBiP95189.

Family and domain databases

InterProiIPR011809. His_9_proposed.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR02067. his_9_HisN. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P95189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHDDLMLAL ALADRADELT RVRFGALDLR IDTKPDLTPV TDADRAVESD
60 70 80 90 100
VRQTLGRDRP GDGVLGEEFG GSTTFTGRQW IVDPIDGTKN FVRGVPVWAS
110 120 130 140 150
LIALLEDGVP SVGVVSAPAL QRRWWAARGR GAFASVDGAR PHRLSVSSVA
160 170 180 190 200
ELHSASLSFS SLSGWARPGL RERFIGLTDT VWRVRAYGDF LSYCLVAEGA
210 220 230 240 250
VDIAAEPQVS VWDLAALDIV VREAGGRLTS LDGVAGPHGG SAVATNGLLH
260
DEVLTRLNAG
Length:260
Mass (Da):27,693
Last modified:July 1, 1997 - v2
Checksum:iCBCD2C2AA3E01518
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45948.1.
PIRiB70646.
RefSeqiNP_217653.1. NC_000962.3.
WP_003917127.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45948; CCP45948; Rv3137.
GeneIDi888827.
KEGGimtu:Rv3137.
PATRICi18155583. VBIMycTub87468_3503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45948.1.
PIRiB70646.
RefSeqiNP_217653.1. NC_000962.3.
WP_003917127.1. NZ_KK339370.1.

3D structure databases

ProteinModelPortaliP95189.
SMRiP95189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3137.

Proteomic databases

PaxDbiP95189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45948; CCP45948; Rv3137.
GeneIDi888827.
KEGGimtu:Rv3137.
PATRICi18155583. VBIMycTub87468_3503.

Organism-specific databases

TubercuListiRv3137.

Phylogenomic databases

eggNOGiENOG4107TK4. Bacteria.
COG0483. LUCA.
HOGENOMiHOG000282239.
InParanoidiP95189.
KOiK05602.
OMAiTKPDMTP.
PhylomeDBiP95189.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00013.
BioCyciMTBH37RV:G185E-7402-MONOMER.
ReactomeiR-MTU-879299. Mycothiol biosynthesis.

Family and domain databases

InterProiIPR011809. His_9_proposed.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
TIGRFAMsiTIGR02067. his_9_HisN. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISN_MYCTU
AccessioniPrimary (citable) accession number: P95189
Secondary accession number(s): L0TBY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.