Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Binding sitei117Substrate1
    Metal bindingi137Iron; via tele nitrogen1 Publication1
    Metal bindingi139Iron1 Publication1
    Binding sitei153Alpha-ketoglutarate1 Publication1
    Binding sitei188Substrate1
    Metal bindingi226Iron; via tele nitrogen1 Publication1
    Binding sitei228Alpha-ketoglutarate1 Publication1
    Binding sitei240Alpha-ketoglutarate1 Publication1

    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.
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi117R → Q: Abolishes 1-deoxypentalenic acid 11-beta-hydroxylase activity. 1 Publication1
    Mutagenesisi188R → Q: Strong reduction of 1-deoxypentalenic acid 11-beta-hydroxylase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004220001 – 2851-deoxypentalenic acid 11-beta-hydroxylaseAdd BLAST285

    Interactioni

    Protein-protein interaction databases

    STRINGi227882.SAV_2991.

    Structurei

    Secondary structure

    1285
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi12 – 14Combined sources3
    Helixi18 – 28Combined sources11
    Beta strandi29 – 33Combined sources5
    Helixi39 – 56Combined sources18
    Turni65 – 67Combined sources3
    Helixi78 – 84Combined sources7
    Helixi87 – 91Combined sources5
    Helixi94 – 104Combined sources11
    Beta strandi108 – 119Combined sources12
    Helixi139 – 142Combined sources4
    Beta strandi150 – 157Combined sources8
    Turni161 – 163Combined sources3
    Beta strandi165 – 169Combined sources5
    Turni170 – 173Combined sources4
    Beta strandi181 – 188Combined sources8
    Beta strandi191 – 195Combined sources5
    Helixi198 – 200Combined sources3
    Beta strandi217 – 221Combined sources5
    Beta strandi226 – 229Combined sources4
    Beta strandi240 – 249Combined sources10
    Helixi256 – 259Combined sources4
    Helixi262 – 265Combined sources4
    Helixi273 – 275Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ82IZ1.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni137 – 139Alpha-ketoglutarate binding3

    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; SAVERM_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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2RDNX-ray1.35A1-285[»]
    2RDQX-ray1.31A1-285[»]
    2RDRX-ray1.70A1-285[»]
    2RDSX-ray1.65A1-285[»]
    ProteinModelPortaliQ82IZ1.
    SMRiQ82IZ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi227882.SAV_2991.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAC70702; BAC70702; SAVERM_2991.
    KEGGisma:SAV_2991.
    PATRICi23719577. VBIStrAve112782_3197.

    Phylogenomic databases

    HOGENOMiHOG000217063.
    KOiK18056.
    OMAiMCHKSIP.
    OrthoDBiPOG091H09D2.

    Enzyme and pathway databases

    UniPathwayiUPA01021.
    BioCyciMetaCyc:MONOMER-16835.
    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: November 2, 2016
    This is version 68 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.