A0A397HQN2 · ANKD_ASPTH

Function

function

Cystathionine gamma-synthase-like protein; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide (PubMed:36702957).
AnkD catalyzes the attachment of L-homoserine moiety using O-acetyl-L-homoserine as co-substrate (PubMed:36702957).
Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A (PubMed:36702957).

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Secondary metabolite biosynthesis.

GO annotations

AspectTerm
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransferase activity
Biological Processtranssulfuration

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cystathionine gamma-synthase-like protein ankD
  • EC number
  • Alternative names
    • Ank biosynthesis cluster protein D

Gene names

    • Name
      ankD
    • ORF names
      CDV56_108975

Organism names

Accessions

  • Primary accession
    A0A397HQN2

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004606571-563Cystathionine gamma-synthase-like protein ankD

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-37Disordered
Compositional bias10-27Polar residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    563
  • Mass (Da)
    61,954
  • Last updated
    2018-12-05 v1
  • Checksum
    90ABB5EDE91B543C
MGELGPASAQHGSDSISFSGSYTQPLGAPQPPNEPHAISVSLPTWEAVTAVMAGADWAICQLQTSYPRFDIHKCVRELHDAVLARFKHPAHTVCRAFPSPEAAERFVSRLQREDPILSVHTARFHLPHDAVPELAKWAAFSVVLFNESLEEVAFEFWEWFGDGISSRHAEFCLTQFSFLNTGSDQPEYQTVGQDSHDLSAMNLPEWIDSSTKDKMDIKSRLASSATSADPALKPMGNDDVLLYATGMAAISAIARALARTSDDSGAVVYGWPYSGTPHCVQGCGFKRYTMYGHGSKADLDSLETLLVSETRFTVLFCEITSNPQLSTPDLHRIRDLADRFGFIVVCDDTLGTSVNVDILPYVDVIITSLTKIFSGAGNVMGGSLMINPNSGHYSTLRALLTTTYEDLYFPLDAKTIARNSSDFAARVHKCNKSALQIANLLNSHASVESVNYPTMVPTAPLYERYRRPDGGYGFLLSVIFREPESAVLFYDKLDVWKGPTVGTNFSISIPYSALAHAKEQDWAASHGVPKHIVRLSVGLEDYGDLSERVNRALREVELREKMG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-27Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKHU02000029
EMBL· GenBank· DDBJ
RHZ63463.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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