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Q02150

- HIS9_LACLA

UniProt

Q02150 - HIS9_LACLA

Protein

Histidinol-phosphatase

Gene

hisK

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: InterPro
    3. histidinol-phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciLLAC272623:GHSH-1304-MONOMER.
    UniPathwayiUPA00031; UER00013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol-phosphatase (EC:3.1.3.15)
    Short name:
    HolPase
    Gene namesi
    Name:hisK
    Ordered Locus Names:LL1216
    ORF Names:L37351
    OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
    Taxonomic identifieri272623 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    ProteomesiUP000002196: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Histidinol-phosphatasePRO_0000122319Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272623.L37351.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 2910
    Beta strandi33 – 4210
    Helixi54 – 6714
    Turni68 – 714
    Beta strandi73 – 819
    Helixi84 – 863
    Helixi87 – 948
    Beta strandi100 – 1056
    Helixi119 – 1213
    Helixi126 – 14318
    Beta strandi148 – 1503
    Helixi155 – 1584
    Beta strandi159 – 1613
    Helixi170 – 1723
    Helixi173 – 18513
    Beta strandi189 – 1935
    Turni195 – 1984
    Helixi200 – 21516
    Beta strandi220 – 2245
    Beta strandi228 – 2303
    Helixi234 – 24613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GC3X-ray1.32A2-269[»]
    4GK8X-ray1.93A2-269[»]
    4GYFX-ray1.65A2-269[»]
    ProteinModelPortaliQ02150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PHP hydrolase family. HisK subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1387.
    HOGENOMiHOG000244025.
    KOiK04486.
    OMAiLDYPARY.
    OrthoDBiEOG6JMMRV.

    Family and domain databases

    InterProiIPR010140. Histidinol_P_phosphatase_HisJ.
    IPR004013. PHP_C.
    IPR003141. Pol/His_phosphatase_N.
    IPR016195. Pol/histidinol_Pase-like.
    [Graphical view]
    PANTHERiPTHR21039. PTHR21039. 1 hit.
    PfamiPF02811. PHP. 1 hit.
    [Graphical view]
    SMARTiSM00481. POLIIIAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF89550. SSF89550. 1 hit.
    TIGRFAMsiTIGR01856. hisJ_fam. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q02150-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLDYHFHS HFSADSEELP RKHVTEAIAH GLEEICFTEH RDFYFPGMDF    50
    SLNLPEYFQE INRLQAEFKD KIKIKIGLEM GIDLRFKSEI NQFIDSAPFD 100
    FVIASVHEIG DIEVYDGTEF YLQKIKEEAQ REYLLACLDV VQNFENYNSF 150
    GHLDYVARYG PYTDKSIKFA ENREILFEIL RALASKEKAL EINTRLFDDP 200
    KTEQFYSDLL INFKKLGGKF ITLGTDSHIA KRDWLSIHKA RTLIKKAGFH 250
    ELATFSGMKI DKNKKSIKE 269
    Length:269
    Mass (Da):31,473
    Last modified:September 26, 2001 - v2
    Checksum:iCF51601DEDD5B8C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251T → I in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti30 – 301H → Y in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti71 – 733KIK → EIN in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti125 – 1251I → T in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti146 – 1461N → T in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti168 – 1681K → T in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti187 – 1871E → G in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti203 – 2031E → G in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti215 – 2151K → R in AAB81911. (PubMed:1400209)Curated
    Sequence conflicti250 – 2501H → R in AAB81911. (PubMed:1400209)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92974 Genomic DNA. Translation: AAB81911.1.
    AE005176 Genomic DNA. Translation: AAK05314.1.
    PIRiD47754.
    H86776.
    RefSeqiNP_267372.1. NC_002662.1.

    Genome annotation databases

    EnsemblBacteriaiAAK05314; AAK05314; L37351.
    GeneIDi1114864.
    KEGGilla:L37351.
    PATRICi22294810. VBILacLac136773_1313.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92974 Genomic DNA. Translation: AAB81911.1 .
    AE005176 Genomic DNA. Translation: AAK05314.1 .
    PIRi D47754.
    H86776.
    RefSeqi NP_267372.1. NC_002662.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GC3 X-ray 1.32 A 2-269 [» ]
    4GK8 X-ray 1.93 A 2-269 [» ]
    4GYF X-ray 1.65 A 2-269 [» ]
    ProteinModelPortali Q02150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272623.L37351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK05314 ; AAK05314 ; L37351 .
    GeneIDi 1114864.
    KEGGi lla:L37351.
    PATRICi 22294810. VBILacLac136773_1313.

    Phylogenomic databases

    eggNOGi COG1387.
    HOGENOMi HOG000244025.
    KOi K04486.
    OMAi LDYPARY.
    OrthoDBi EOG6JMMRV.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00013 .
    BioCyci LLAC272623:GHSH-1304-MONOMER.

    Family and domain databases

    InterProi IPR010140. Histidinol_P_phosphatase_HisJ.
    IPR004013. PHP_C.
    IPR003141. Pol/His_phosphatase_N.
    IPR016195. Pol/histidinol_Pase-like.
    [Graphical view ]
    PANTHERi PTHR21039. PTHR21039. 1 hit.
    Pfami PF02811. PHP. 1 hit.
    [Graphical view ]
    SMARTi SM00481. POLIIIAc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89550. SSF89550. 1 hit.
    TIGRFAMsi TIGR01856. hisJ_fam. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis."
      Delorme C., Ehrlich S.D., Renault P.
      J. Bacteriol. 174:6571-6579(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCDO 2118.
    2. "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
      Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
      Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: IL1403.

    Entry informationi

    Entry nameiHIS9_LACLA
    AccessioniPrimary (citable) accession number: Q02150
    Secondary accession number(s): Q9CG89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 95 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3