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Protein

1-deoxypentalenic acid 11-beta-hydroxylase

Gene

ptlH

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 1-deoxypentalenic acid to 11-beta-hydroxy-1-deoxypentalenic acid in the biosynthesis of neopentalenolactone antibiotic.2 Publications

Catalytic activityi

1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11-beta-hydroxypentalenate + succinate + CO2.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Fe cation1 Publication
  • L-ascorbateBy similarity

Kineticsi

kcat is 4.2 sec(-1) with 1-deoxypentalenic acid.

  1. KM=0.57 mM for 1-deoxypentalenic acid1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Pathwayi: neopentalenolactone biosynthesis

    This protein is involved in the pathway neopentalenolactone biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway neopentalenolactone biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171Substrate
    Metal bindingi137 – 1371Iron; via tele nitrogen1 Publication
    Metal bindingi139 – 1391Iron1 Publication
    Binding sitei153 – 1531Alpha-ketoglutarate1 Publication
    Binding sitei188 – 1881Substrate
    Metal bindingi226 – 2261Iron; via tele nitrogen1 Publication
    Binding sitei228 – 2281Alpha-ketoglutarate1 Publication
    Binding sitei240 – 2401Alpha-ketoglutarate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • antibiotic biosynthetic process Source: UniProtKB
    • lactone biosynthetic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16835.
    SAVE227882:GJU1-3013-MONOMER.
    BRENDAi1.14.11.35. 5980.
    UniPathwayiUPA01021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-deoxypentalenic acid 11-beta-hydroxylase (EC:1.14.11.35)
    Alternative name(s):
    Neopentalenolactone biosynthesis protein H
    Gene namesi
    Name:ptlH
    Ordered Locus Names:SAV_2991
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
    Proteomesi
    • UP000000428 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi117 – 1171R → Q: Abolishes 1-deoxypentalenic acid 11-beta-hydroxylase activity. 1 Publication
    Mutagenesisi188 – 1881R → Q: Strong reduction of 1-deoxypentalenic acid 11-beta-hydroxylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2852851-deoxypentalenic acid 11-beta-hydroxylasePRO_0000422000Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi227882.SAV_2991.

    Structurei

    Secondary structure

    1
    285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 143Combined sources
    Helixi18 – 2811Combined sources
    Beta strandi29 – 335Combined sources
    Helixi39 – 5618Combined sources
    Turni65 – 673Combined sources
    Helixi78 – 847Combined sources
    Helixi87 – 915Combined sources
    Helixi94 – 10411Combined sources
    Beta strandi108 – 11912Combined sources
    Helixi139 – 1424Combined sources
    Beta strandi150 – 1578Combined sources
    Turni161 – 1633Combined sources
    Beta strandi165 – 1695Combined sources
    Turni170 – 1734Combined sources
    Beta strandi181 – 1888Combined sources
    Beta strandi191 – 1955Combined sources
    Helixi198 – 2003Combined sources
    Beta strandi217 – 2215Combined sources
    Beta strandi226 – 2294Combined sources
    Beta strandi240 – 24910Combined sources
    Helixi256 – 2594Combined sources
    Helixi262 – 2654Combined sources
    Helixi273 – 2753Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RDNX-ray1.35A1-285[»]
    2RDQX-ray1.31A1-285[»]
    2RDRX-ray1.70A1-285[»]
    2RDSX-ray1.65A1-285[»]
    ProteinModelPortaliQ82IZ1.
    SMRiQ82IZ1. Positions 2-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ82IZ1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 1393Alpha-ketoglutarate binding

    Sequence similaritiesi

    Belongs to the PhyH family.Curated

    Phylogenomic databases

    HOGENOMiHOG000217063.
    KOiK18056.
    OMAiMCHKSIP.
    OrthoDBiPOG091H09D2.

    Family and domain databases

    InterProiIPR008775. Phytyl_CoA_dOase.
    [Graphical view]
    PfamiPF05721. PhyH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q82IZ1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTNVTGDYTD CTPLLGDRAA LDSFYEEHGY LFLRNVLDRD LVKTVAEQMR
    60 70 80 90 100
    EGLVALGAAD PHATLEELTI DSFESVDEVA MHDYVKYDAF WNNPSTIKVF
    110 120 130 140 150
    EQVFGEPVFV FLSTTIRYYP SQAGSEEPSF HYLTPFHQDG FYIGPNQDFR
    160 170 180 190 200
    TFWIPLIRTT RESGGVALAD GSHRRGKRDH VLNESFRRFG HPVRGIPPTE
    210 220 230 240 250
    VSEDEHLLHS PMEPGDILLF HAHMCHKSIP NLSKDPRLMR MSMDTRVQPA
    260 270 280
    KSHRGFNAMT PWTESAKDAS KGIMAKITGT PTDVE
    Length:285
    Mass (Da):32,264
    Last modified:July 24, 2007 - v2
    Checksum:i9E48B0F63540D4B3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000030 Genomic DNA. Translation: BAC70702.2.
    RefSeqiWP_037648981.1. NZ_JZJK01000090.1.

    Genome annotation databases

    EnsemblBacteriaiBAC70702; BAC70702; SAV_2991.
    KEGGisma:SAV_2991.
    PATRICi23719577. VBIStrAve112782_3197.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000030 Genomic DNA. Translation: BAC70702.2.
    RefSeqiWP_037648981.1. NZ_JZJK01000090.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RDNX-ray1.35A1-285[»]
    2RDQX-ray1.31A1-285[»]
    2RDRX-ray1.70A1-285[»]
    2RDSX-ray1.65A1-285[»]
    ProteinModelPortaliQ82IZ1.
    SMRiQ82IZ1. Positions 2-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi227882.SAV_2991.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAC70702; BAC70702; SAV_2991.
    KEGGisma:SAV_2991.
    PATRICi23719577. VBIStrAve112782_3197.

    Phylogenomic databases

    HOGENOMiHOG000217063.
    KOiK18056.
    OMAiMCHKSIP.
    OrthoDBiPOG091H09D2.

    Enzyme and pathway databases

    UniPathwayiUPA01021.
    BioCyciMetaCyc:MONOMER-16835.
    SAVE227882:GJU1-3013-MONOMER.
    BRENDAi1.14.11.35. 5980.

    Miscellaneous databases

    EvolutionaryTraceiQ82IZ1.

    Family and domain databases

    InterProiIPR008775. Phytyl_CoA_dOase.
    [Graphical view]
    PfamiPF05721. PhyH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPTLH_STRAW
    AccessioniPrimary (citable) accession number: Q82IZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: July 24, 2007
    Last modified: September 7, 2016
    This is version 66 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    S.avermitilis does not produce pentalenolactone itself in vivo but instead a group of new metabolites that are neopentalenolactone derivatives.1 Publication

    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

    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.