Q94K71 · CBBY_ARATH
- ProteinCBBY-like protein
- GeneCBBY
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids319 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Highly selective xylulose-1,5-bisphosphate (XuBP) phosphatase. Shows also activity towards ribulose-1,5-bisphosphate (RuBP) and fructose-1,6-bisphosphate (FBP), but not towards fructose-6-phosphate (F6P) or ribulose-5-phosphate (Ru5P) (PubMed:27246049).
Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself (PubMed:27246049).
Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself (PubMed:27246049).
Catalytic activity
- D-xylulose 1,5-bisphosphate + H2O = D-xylulose 5-phosphate + phosphate
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.033 mM | xylulose-1,5-bisphosphate | |||||
3.06 mM | ribulose-1,5-bisphosphate | |||||
6.2 mM | fructose-1,6-bisphosphate |
kcat is 2.45 sec-1 with xylulose-1,5-bisphosphate as substrate. kcat is 0.049 sec-1 with ribulose-1,5-bisphosphate as substrate.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 82 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 82 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 82 | substrate | ||||
Sequence: D | ||||||
Active site | 84 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 84 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 91 | substrate | ||||
Sequence: E | ||||||
Binding site | 125-129 | substrate | ||||
Sequence: GGKER | ||||||
Binding site | 158-161 | substrate | ||||
Sequence: HKQK | ||||||
Binding site | 198-204 | substrate | ||||
Sequence: STSNEKA | ||||||
Binding site | 258 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCBBY-like protein
- EC number
- Short namesAtCbby
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94K71
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 84 | Loss of catalytic activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 91 | 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate. | ||||
Sequence: E → A | ||||||
Mutagenesis | 95 | 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate. | ||||
Sequence: H → A | ||||||
Mutagenesis | 117 | 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 129 | 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate. | ||||
Sequence: R → A | ||||||
Mutagenesis | 161 | 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-65 | Chloroplast | ||||
Sequence: MATVKISLSLASLSPSSSSSSIQSKLSPSFIPNAAPAKAVKLRFNGKSLRAKPMVYRSSRSVGVT | ||||||
Chain | PRO_0000424321 | 66-319 | CBBY-like protein | |||
Sequence: CSASSSLTTLPSALLFDCDGVLVDTEKDGHRISFNDTFKERDLNVTWDVDLYGELLKIGGGKERMTAYFNKVGWPEKAPKDEAERKEFIAGLHKQKTELFMVLIEKKLLPLRPGVAKLVDQALTNGVKVAVCSTSNEKAVSAIVSCLLGPERAEKIKIFAGDVVPKKKPDPAIYNLAAETLGVDPSKCVVVEDSAIGLAAAKAAGMTCIVTKSGYTADEDFENADAVFDCIGDPPEERFDLAFCGSLLRKQFVS |
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length319
- Mass (Da)34,246
- Last updated2001-12-01 v1
- ChecksumDEBCA30D027CFCD6
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 106 | in Ref. 5; BAD43740 | ||||
Sequence: R → G | ||||||
Sequence conflict | 314 | in Ref. 6; AAM63700 | ||||
Sequence: R → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL049659 EMBL· GenBank· DDBJ | CAB41156.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002686 EMBL· GenBank· DDBJ | AEE78414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370250 EMBL· GenBank· DDBJ | AAK44065.1 EMBL· GenBank· DDBJ | mRNA | ||
AY063066 EMBL· GenBank· DDBJ | AAL34240.1 EMBL· GenBank· DDBJ | mRNA | ||
AK118118 EMBL· GenBank· DDBJ | BAC42744.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175866 EMBL· GenBank· DDBJ | BAD43629.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175977 EMBL· GenBank· DDBJ | BAD43740.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176795 EMBL· GenBank· DDBJ | BAD44558.1 EMBL· GenBank· DDBJ | mRNA | ||
AY086642 EMBL· GenBank· DDBJ | AAM63700.1 EMBL· GenBank· DDBJ | mRNA |