A0A397HQN2 · ANKD_ASPTH
- ProteinCystathionine gamma-synthase-like protein ankD
- GeneankD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids563 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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).
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
- cyclo(L-arginyl-(Z)-dehydro-3,4-dihydroxytyrosyl) + O-acetyl-L-homoserine = acetate + cyclo(L-arginyl-(Z)-dehydro-4-O-homoseryl-tyrosyl) + H+This reaction proceeds in the forward direction.
Cofactor
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | transferase activity | |
Biological Process | transsulfuration |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCystathionine gamma-synthase-like protein ankD
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionA0A397HQN2
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460657 | 1-563 | Cystathionine gamma-synthase-like protein ankD | |||
Sequence: MGELGPASAQHGSDSISFSGSYTQPLGAPQPPNEPHAISVSLPTWEAVTAVMAGADWAICQLQTSYPRFDIHKCVRELHDAVLARFKHPAHTVCRAFPSPEAAERFVSRLQREDPILSVHTARFHLPHDAVPELAKWAAFSVVLFNESLEEVAFEFWEWFGDGISSRHAEFCLTQFSFLNTGSDQPEYQTVGQDSHDLSAMNLPEWIDSSTKDKMDIKSRLASSATSADPALKPMGNDDVLLYATGMAAISAIARALARTSDDSGAVVYGWPYSGTPHCVQGCGFKRYTMYGHGSKADLDSLETLLVSETRFTVLFCEITSNPQLSTPDLHRIRDLADRFGFIVVCDDTLGTSVNVDILPYVDVIITSLTKIFSGAGNVMGGSLMINPNSGHYSTLRALLTTTYEDLYFPLDAKTIARNSSDFAARVHKCNKSALQIANLLNSHASVESVNYPTMVPTAPLYERYRRPDGGYGFLLSVIFREPESAVLFYDKLDVWKGPTVGTNFSISIPYSALAHAKEQDWAASHGVPKHIVRLSVGLEDYGDLSERVNRALREVELREKMG |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MGELGPASAQHGSDSISFSGSYTQPLGAPQPPNEPHA | ||||||
Compositional bias | 10-27 | Polar residues | ||||
Sequence: QHGSDSISFSGSYTQPLG |
Sequence similarities
Belongs to the trans-sulfuration enzymes family. MET7 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length563
- Mass (Da)61,954
- Last updated2018-12-05 v1
- Checksum90ABB5EDE91B543C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 10-27 | Polar residues | ||||
Sequence: QHGSDSISFSGSYTQPLG |
Keywords
- Technical term