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Protein

L-proline cis-3-hydroxylase 2

Gene
N/A
Organism
Streptomyces sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).1 Publication

Catalytic activityi

L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2.1 Publication

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion.1 Publication

Enzyme regulationi

Inhibited by metal ions such as Co2+, Zn2+, Ni2+ or Cu2+. Is also inhibited by EDTA in vitro.1 Publication

Kineticsi

Comparison of both proline 3-hydroxylase isozymes shows that type II enzyme has 1.8-fold higher activity than type I upon L-proline, and 24-fold higher activity upon L-2-azetidinecarboxylic acid.

  1. KM=0.43 mM for L-proline1 Publication
  2. KM=0.047 mM for 2-oxoglutarate1 Publication

    pH dependencei

    Optimum pH is 6.0. Is stable from pH 5.5 to 9.0.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius. Is stable below 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi107 – 1071Iron
    Metal bindingi109 – 1091Iron
    Metal bindingi158 – 1581Iron
    Binding sitei168 – 16812-oxoglutarateSequence analysis

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-proline cis-3-hydroxylase 2 (EC:1.14.11.28)
    Short name:
    P3H 2
    Alternative name(s):
    Proline 3-hydroxylase 2
    Proline 3-hydroxylase type II
    OrganismiStreptomyces sp.
    Taxonomic identifieri1931 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 290290L-proline cis-3-hydroxylase 2PRO_0000393427Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85Combined sources
    Helixi13 – 2513Combined sources
    Beta strandi39 – 479Combined sources
    Turni70 – 734Combined sources
    Helixi77 – 859Combined sources
    Beta strandi88 – 10720Combined sources
    Beta strandi123 – 1264Combined sources
    Beta strandi133 – 1375Combined sources
    Beta strandi140 – 1423Combined sources
    Beta strandi148 – 1514Combined sources
    Beta strandi158 – 1669Combined sources
    Beta strandi170 – 1767Combined sources
    Helixi183 – 1864Combined sources
    Beta strandi187 – 1893Combined sources
    Helixi190 – 1923Combined sources
    Helixi209 – 2168Combined sources
    Helixi217 – 2204Combined sources
    Turni224 – 2263Combined sources
    Helixi227 – 24014Combined sources
    Beta strandi241 – 2433Combined sources
    Helixi247 – 25812Combined sources
    Helixi262 – 27615Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5RX-ray2.30A/B1-290[»]
    1E5SX-ray2.40A/B1-290[»]
    ProteinModelPortaliO09345.
    SMRiO09345. Positions 1-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO09345.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.1720.10. 1 hit.
    2.60.120.330. 1 hit.
    InterProiIPR007803. Asp/Arg/Pro-Hydrxlase.
    IPR027443. IPNS-like.
    IPR008035. Pro_3_hydrox_C.
    [Graphical view]
    PfamiPF05118. Asp_Arg_Hydrox. 1 hit.
    PF05373. Pro_3_hydrox_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O09345-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRSHILGKIE LDQTRLAPDL AYLAAVPTVE EEYDEFSNGF WKHVPLWNAS
    60 70 80 90 100
    GDSEDRLYRD LKDAAAQPTA HVEHVPYLKE IVTTVFDGTH LQMARSRNLK
    110 120 130 140 150
    NAIVIPHRDF VELDREVDRY FRTFMVLEDS PLAFHSNEDT VIHMRPGEIW
    160 170 180 190 200
    FLDAATVHSA VNFSEISRQS LCVDFAFDGP FDEKEIFADA TLYAPGSTPD
    210 220 230 240 250
    LPERRPFTAE HRRRILSLGQ VIERENFRDI LFLLSKVHYK YDVHPSETYD
    260 270 280 290
    WLIEISKQAG DEKMVVKAEQ IRDFAVEARA LSERFSLTSW
    Length:290
    Mass (Da):33,574
    Last modified:July 1, 1997 - v1
    Checksum:iC571E1DAB598AE1A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF003371 Genomic DNA. Translation: AAB60894.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF003371 Genomic DNA. Translation: AAB60894.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5RX-ray2.30A/B1-290[»]
    1E5SX-ray2.40A/B1-290[»]
    ProteinModelPortaliO09345.
    SMRiO09345. Positions 1-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiO09345.

    Family and domain databases

    Gene3Di1.10.1720.10. 1 hit.
    2.60.120.330. 1 hit.
    InterProiIPR007803. Asp/Arg/Pro-Hydrxlase.
    IPR027443. IPNS-like.
    IPR008035. Pro_3_hydrox_C.
    [Graphical view]
    PfamiPF05118. Asp_Arg_Hydrox. 1 hit.
    PF05373. Pro_3_hydrox_C. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiP3H2_STRSQ
    AccessioniPrimary (citable) accession number: O09345
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: July 1, 1997
    Last modified: December 9, 2015
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.