O09345 · P3H2_STRSQ

  • Protein
    L-proline cis-3-hydroxylase 2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

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

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion.

Activity regulation

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.43 mML-proline
0.047 mM2-oxoglutarate
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.

pH Dependence

Optimum pH is 6.0. Is stable from pH 5.5 to 9.0.

Temperature Dependence

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site107Fe cation (UniProtKB | ChEBI)
Binding site109Fe cation (UniProtKB | ChEBI)
Binding site158Fe cation (UniProtKB | ChEBI)
Binding site1682-oxoglutarate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionproline 3-hydroxylase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-proline cis-3-hydroxylase 2
  • EC number
  • Short names
    P3H 2
  • Alternative names
    • Proline 3-hydroxylase 2
    • Proline 3-hydroxylase type II

Organism names

  • Taxonomic identifier
  • Strain
    • TH1 / FERM BP-4399
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    O09345

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003934271-290L-proline cis-3-hydroxylase 2

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    290
  • Mass (Da)
    33,574
  • Last updated
    1997-07-01 v1
  • Checksum
    C571E1DAB598AE1A
MRSHILGKIELDQTRLAPDLAYLAAVPTVEEEYDEFSNGFWKHVPLWNASGDSEDRLYRDLKDAAAQPTAHVEHVPYLKEIVTTVFDGTHLQMARSRNLKNAIVIPHRDFVELDREVDRYFRTFMVLEDSPLAFHSNEDTVIHMRPGEIWFLDAATVHSAVNFSEISRQSLCVDFAFDGPFDEKEIFADATLYAPGSTPDLPERRPFTAEHRRRILSLGQVIERENFRDILFLLSKVHYKYDVHPSETYDWLIEISKQAGDEKMVVKAEQIRDFAVEARALSERFSLTSW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF003371
EMBL· GenBank· DDBJ
AAB60894.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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