Q9SUC6 · BBE22_ARATH
- ProteinBerberine bridge enzyme-like 22
- GeneFAD-OXR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids530 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Cofactor
Note: Binds 1 FAD per subunit in a bicovalent manner.
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 | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | cellular response to hypoxia | |
Biological Process | positive regulation of hydrogen peroxide biosynthetic process | |
Biological Process | response to jasmonic acid |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBerberine bridge enzyme-like 22
- EC number
- Short namesAtBBE-like 22
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SUC6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MRELFMYLFLLFLVLCVKSVYS | ||||||
Chain | PRO_5008180478 | 23-530 | Berberine bridge enzyme-like 22 | |||
Sequence: TPTREQFQNCLSTKQFNSTLKNPINLTTHTLDSRVHTDFSESSSPNSSFLNLNFTSLKPILIVKPKSESEIKQSILCSRKLGVQVRTMSGGHDYEGLSYLSLSPFIIVDLVNLRSISINLTDETAWIQSGATLGEVYYKIAKTSKIHAFAAGICPSVGVGGHISGGGFGTIMRKYGLASDNVVDARLMDVNGKTLDRKTMGEDLFWALRGGGAASFGVVLSWKVKLARVPEKVTCFISQHPMGPSMNKLVHRWQSIGSELDEDLFIRVIIDNSLEGNQRKVKSTFQTLFLGGIDRLIPLMNQKFPELGLRSQDCSEMSWIESIMFFNWRSGQPLEILLNRDLRFEDQYFKAKSDYVQKPVPENVFEEVTKRFLEQDTPLMIFEPLGGKISKISETESPYPHRRGNLYNIQYMVKWKVNEVEEMNKHVRWMRSLHDYMTPYVSKSPRGAYLNYRDLDLGSTKGINTSFEDARKWGETYFKGNFKRLGLVKGKIDPTNFFRNEQSIPPLF | ||||||
Disulfide bond | 32↔99 | |||||
Sequence: CLSTKQFNSTLKNPINLTTHTLDSRVHTDFSESSSPNSSFLNLNFTSLKPILIVKPKSESEIKQSILC | ||||||
Glycosylation | 39 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 47 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 68 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Cross-link | 114↔176 | 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys) | ||||
Sequence: HDYEGLSYLSLSPFIIVDLVNLRSISINLTDETAWIQSGATLGEVYYKIAKTSKIHAFAAGIC | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 486 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Accumulates in cell walls of etiolated hypocotyls.
Induction
By jasmonic acid (e.g. 12-oxo-phytodienoic acid OPDA).
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 77-251 | FAD-binding PCMH-type | ||||
Sequence: TSLKPILIVKPKSESEIKQSILCSRKLGVQVRTMSGGHDYEGLSYLSLSPFIIVDLVNLRSISINLTDETAWIQSGATLGEVYYKIAKTSKIHAFAAGICPSVGVGGHISGGGFGTIMRKYGLASDNVVDARLMDVNGKTLDRKTMGEDLFWALRGGGAASFGVVLSWKVKLARV |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length530
- Mass (Da)60,410
- Last updated2000-05-01 v1
- ChecksumC77A19F802755D54
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 126 | in Ref. 3; AAK56258/AAM91446 | ||||
Sequence: P → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL080282 EMBL· GenBank· DDBJ | CAB45881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161553 EMBL· GenBank· DDBJ | CAB79086.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE84369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF367269 EMBL· GenBank· DDBJ | AAK56258.1 EMBL· GenBank· DDBJ | mRNA | ||
AY133616 EMBL· GenBank· DDBJ | AAM91446.1 EMBL· GenBank· DDBJ | mRNA | ||
AK221267 EMBL· GenBank· DDBJ | BAD93938.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |