P24197 · YGID_ECOLI

Function

function

In vitro, opens the cyclic ring of dihydroxy-phenylalanine (DOPA) between carbons 4 and 5, thus producing an unstable seco-DOPA that rearranges nonenzymatically to betalamic acid. The physiological substrate is unknown.

Miscellaneous

Betalamic acid is the structural unit of the betalains, natural nitrogen-containing water-soluble pigments with high colorant and bioactive properties, characteristic of plants of the order Caryophyllales.

Caution

It is uncertain whether Met-1 or Met-10 is the initiator.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
7.9 mML-DOPA
kcat is 0.17 min-1 with L-DOPA.

pH Dependence

Optimum pH is 8.0.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site22Zn2+ (UniProtKB | ChEBI)
Binding site57Zn2+ (UniProtKB | ChEBI)
Binding site177Zn2+ (UniProtKB | ChEBI)
Binding site234Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionDOPA dioxygenase activity
Molecular Functionferrous iron binding
Molecular Functionstizolobate synthase activity
Molecular Functionzinc ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4,5-DOPA dioxygenase extradiol
  • EC number

Gene names

    • Name
      ygiD
    • Ordered locus names
      b3039, JW3007

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P24197
  • Secondary accessions
    • Q2M9G1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001694051-2714,5-DOPA dioxygenase extradiol

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    271
  • Mass (Da)
    29,903
  • Last updated
    2016-11-02 v4
  • Checksum
    A74E9035BAF6EB0F
MTPLVKDIIMSSTRMPALFLGHGSPMNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSPALAQRLVELLAPIPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWHGDSSPYPWATSFNEYVKANLTWQGPVEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPITIPVEGIEMGSLSMLSVQIG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict243-270in Ref. 1; AAA71877

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M77129
EMBL· GenBank· DDBJ
AAA71877.1
EMBL· GenBank· DDBJ
Genomic DNA
U28377
EMBL· GenBank· DDBJ
AAA69207.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76075.3
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77095.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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