Q8GXX0 · ERV1_ARATH
- ProteinFAD-linked sulfhydryl oxidase ERV1
- GeneERV1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids191 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation (PubMed:14996837, PubMed:16893552).
Oxidizes thioredoxin in vitro (PubMed:14996837, PubMed:16893552).
Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space, and can act independently of the oxidoreductase MIA40 (PubMed:29117860, PubMed:38001802).
Can oxidize the cytochrome c oxidase assembly protein COX19, a typical substrate of MIA40 (PubMed:38001802).
Oxidizes thioredoxin in vitro (PubMed:14996837, PubMed:16893552).
Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space, and can act independently of the oxidoreductase MIA40 (PubMed:29117860, PubMed:38001802).
Can oxidize the cytochrome c oxidase assembly protein COX19, a typical substrate of MIA40 (PubMed:38001802).
Catalytic activity
- O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'This reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 76 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 81 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 121 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 125 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 148 | FAD (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 151 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 152 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 155 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 160 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 171 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | flavin-dependent sulfhydryl oxidase activity | |
Molecular Function | identical protein binding | |
Molecular Function | thiol oxidase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-linked sulfhydryl oxidase ERV1
- EC number
- Short namesAtErv1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8GXX0
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Embryonic lethality when homozygous.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 177 | Loss the capacity to oxidize thioredoxin; when associated with A-182. | ||||
Sequence: C → A | ||||||
Mutagenesis | 182 | Loss the capacity to oxidize thioredoxin; when associated with A-177. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000401377 | 1-191 | FAD-linked sulfhydryl oxidase ERV1 | |||
Sequence: MGEKPWQPLLQSFEKLSNCVQTHLSNFIGIKNTPPSSQSTIQNPIISLDSSPPIATNSSSLQKLPLKDKSTGPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARWGKLECEQKSCDLHGTSMDF | ||||||
Disulfide bond | 119↔122 | Redox-active | ||||
Sequence: CREC | ||||||
Disulfide bond | 148↔165 | |||||
Sequence: CHVHNTVNRSLGKLVFPC | ||||||
Disulfide bond | 177↔182 | |||||
Sequence: CEQKSC |
Post-translational modification
Contains three disulfide bonds; one catalytic disulfide (Cys-119 to Cys-122), one structural disulfide (Cys-148 to Cys-165), and one shuttle disulfide (Cys-177 to Cys-182).
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 72-172 | ERV/ALR sulfhydryl oxidase | ||||
Sequence: GPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARW | ||||||
Motif | 177-182 | Required for dimerization and substrate specificity | ||||
Sequence: CEQKSC |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length191
- Mass (Da)21,600
- Last updated2003-03-01 v1
- Checksum7CC7FEA44C0D4B38
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8AP23 | A0A1P8AP23_ARATH | ERV1 | 157 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 35-36 | in Ref. 6; AAM63908 | ||||
Sequence: PS → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ551263 EMBL· GenBank· DDBJ | CAD83013.1 EMBL· GenBank· DDBJ | mRNA | ||
AC079674 EMBL· GenBank· DDBJ | AAG51780.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE32487.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117991 EMBL· GenBank· DDBJ | BAC42626.1 EMBL· GenBank· DDBJ | mRNA | ||
BT003718 EMBL· GenBank· DDBJ | AAO39946.1 EMBL· GenBank· DDBJ | mRNA | ||
AY086861 EMBL· GenBank· DDBJ | AAM63908.1 EMBL· GenBank· DDBJ | mRNA |