A0A4D6NET5 · A0A4D6NET5_VIGUN
- ProteinPolyphenol oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids559 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Note: Binds 2 copper ions per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 147 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 169 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 178 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 300 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 304 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 334 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | catechol oxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | pigment biosynthetic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Vigna
Accessions
- Primary accessionA0A4D6NET5
Proteomes
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MNTPSKLLPLFLALLLFLIPLTFI | ||||||
Chain | PRO_5020030373 | 25-559 | ||||
Sequence: LNTSTQTYKPFHGLTATTSNHRHKNIDHSFSVSKAISLNITHCFPAELPSNPITDNHCCPSKPSFSNLIDFKDFASPNATLRVRKPFHMLDEQYIAKFEKGIALMKALPQDDPRSFIQQAKVHCAYCNGAYHLEPPFQDTKFDIHVSWFFFPFHRWYMYFFERILGNLIGDPDFALPFWNWDSAEGMQMPSCFTDHNSSLYNQLRHQKHLPPHVVDLNYHLDDSYVPSQQQVSYNLGTMYKQMVLASTTELFMGSPFRLGDNNPHPGMGSVEVAPHNTLHSWIGGADTPHHEDMGTFYTAARDPIFYVHHANMDRMWAIWKTLGEGRRDYSDEDWLDSEFYFYDENADFVRVKVRDCVDTKKLGYVYQDVDLPWLRTPPTSRKSKLLRQRKKDEVLSWKPIKFPLVLDSVTSVIVKRPKKKRSREEREKEEEVLVMEGIEFGSDKYVKFDVHVDDDEERLSNPDETEFVGSFVNVPHGHGHNITTTFKVAISKVLENLEVAEDDDVLVTLVPRVGQGDLILGNIKIEFFPRELKD | ||||||
Disulfide bond | 67↔83 | |||||
Sequence: CFPAELPSNPITDNHCC | ||||||
Disulfide bond | 82↔148 | |||||
Sequence: CCPSKPSFSNLIDFKDFASPNATLRVRKPFHMLDEQYIAKFEKGIALMKALPQDDPRSFIQQAKVHC | ||||||
Cross-link | 151↔169 | 2'-(S-cysteinyl)-histidine (Cys-His) | ||||
Sequence: CNGAYHLEPPFQDTKFDIH |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 169-186 | Tyrosinase copper-binding | ||||
Sequence: HVSWFFFPFHRWYMYFFE | ||||||
Domain | 327-338 | Tyrosinase copper-binding | ||||
Sequence: DPIFYVHHANMD |
Sequence similarities
Belongs to the tyrosinase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length559
- Mass (Da)64,640
- Last updated2019-07-03 v1
- ChecksumC400DE6695D57235