P53780 · METC_ARATH
- ProteinCystathionine beta-lyase, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the penultimate step in the de novo biosynthesis of methionine (PubMed:11402193, PubMed:31002461, PubMed:8541513).
Its role in methionine metabolism may affect plant development in different organs, probably by modifying plant auxin transport (PubMed:31002461).
Its cysteine desulfhydrase activity may be involved in hydrogen sulfur production using L-cysteine as a substrate (PubMed:35472754).
Its role in methionine metabolism may affect plant development in different organs, probably by modifying plant auxin transport (PubMed:31002461).
Its cysteine desulfhydrase activity may be involved in hydrogen sulfur production using L-cysteine as a substrate (PubMed:35472754).
Catalytic activity
- H2O + L,L-cystathionine = L-homocysteine + NH4+ + pyruvateThis reaction proceeds in the forward direction.
Cofactor
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 127 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 129 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 157 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 158 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 275 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 277 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Molecular Function | cysteine-S-conjugate beta-lyase activity | |
Molecular Function | molecular adaptor activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | L-methionine biosynthetic process from L-homoserine via cystathionine | |
Biological Process | methionine metabolic process | |
Biological Process | transsulfuration |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCystathionine beta-lyase, chloroplastic
- EC number
- Short namesCBL
- 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 accessionP53780
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreased abundance of several PIN-FORMED (PIN) proteins, involved in plant auxin transport, and impaired auxin-responsive gene expression.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-55 | Chloroplast | ||||
Sequence: MTSSLSLHSSFVPSFADLSDRGLISKNSPTSVSISKVPTWEKKQISNRNSFKLNC | ||||||
Chain | PRO_0000033454 | 56-464 | Cystathionine beta-lyase, chloroplastic | |||
Sequence: VMEKSVDGQTHSTVNNTTDSLNTMNIKEEASVSTLLVNLDNKFDPFDAMSTPLYQTATFKQPSAIENGPYDYTRSGNPTRDALESLLAKLDKADRAFCFTSGMAALSAVTHLIKNGEEIVAGDDVYGGSDRLLSQVVPRSGVVVKRVNTTKLDEVAAAIGPQTKLVWLESPTNPRQQISDIRKISEMAHAQGALVLVDNSIMSPVLSRPLELGADIVMHSATKFIAGHSDVMAGVLAVKGEKLAKEVYFLQNSEGSGLAPFDCWLCLRGIKTMALRIEKQQENARKIAMYLSSHPRVKKVYYAGLPDHPGHHLHFSQAKGAGSVFSFITGSVALSKHLVETTKYFSIAVSFGSVKSLISMPCFMSHASIPAEVREARGLTEDLVRISAGIEDVDDLISDLDIAFKTFPL | ||||||
Modified residue | 278 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P53780-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length464
- Mass (Da)50,430
- Last updated1996-10-01 v1
- ChecksumDE756848549D2CA6
P53780-2
- Name2
- NoteMay be due to a competing donor splice site.
- Differences from canonical
- 63-78: GQTHSTVNNTTDSLNT → A
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4J244 | F4J244_ARATH | CBL | 378 | ||
A0A1I9LQK6 | A0A1I9LQK6_ARATH | CBL | 408 | ||
A0A1I9LQK7 | A0A1I9LQK7_ARATH | CBL | 386 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008894 | 63-78 | in isoform 2 | |||
Sequence: GQTHSTVNNTTDSLNT → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L40511 EMBL· GenBank· DDBJ | AAA99176.1 EMBL· GenBank· DDBJ | mRNA | ||
AL138655 EMBL· GenBank· DDBJ | CAB72175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE79603.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE79605.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY064018 EMBL· GenBank· DDBJ | AAL36374.1 EMBL· GenBank· DDBJ | mRNA | ||
AY114051 EMBL· GenBank· DDBJ | AAM45099.1 EMBL· GenBank· DDBJ | mRNA |