Q94K71 · CBBY_ARATH

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).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.033 mMxylulose-1,5-bisphosphate
3.06 mMribulose-1,5-bisphosphate
6.2 mMfructose-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.

TypeIDPosition(s)Description
Active site82Nucleophile
Binding site82Mg2+ (UniProtKB | ChEBI)
Binding site82substrate
Active site84Proton donor
Binding site84Mg2+ (UniProtKB | ChEBI)
Binding site91substrate
Binding site125-129substrate
Binding site158-161substrate
Binding site198-204substrate
Binding site258Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentchloroplast envelope
Cellular Componentchloroplast stroma
Cellular Componentcytosol
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CBBY-like protein
  • EC number
  • Short names
    AtCbby

Gene names

    • Name
      CBBY
    • ORF names
      T29H11.60
    • Ordered locus names
      At3g48420

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q94K71
  • Secondary accessions
    • Q67ZZ0
    • Q8LCE8
    • Q9STM2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis84Loss of catalytic activity.
Mutagenesis9140% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Mutagenesis9540% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Mutagenesis11740% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Mutagenesis12997% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Mutagenesis16140% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-65Chloroplast
ChainPRO_000042432166-319CBBY-like protein

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    319
  • Mass (Da)
    34,246
  • Last updated
    2001-12-01 v1
  • Checksum
    DEBCA30D027CFCD6
MATVKISLSLASLSPSSSSSSIQSKLSPSFIPNAAPAKAVKLRFNGKSLRAKPMVYRSSRSVGVTCSASSSLTTLPSALLFDCDGVLVDTEKDGHRISFNDTFKERDLNVTWDVDLYGELLKIGGGKERMTAYFNKVGWPEKAPKDEAERKEFIAGLHKQKTELFMVLIEKKLLPLRPGVAKLVDQALTNGVKVAVCSTSNEKAVSAIVSCLLGPERAEKIKIFAGDVVPKKKPDPAIYNLAAETLGVDPSKCVVVEDSAIGLAAAKAAGMTCIVTKSGYTADEDFENADAVFDCIGDPPEERFDLAFCGSLLRKQFVS

Sequence caution

The sequence CAB41156.1 differs from that shown. Reason: Erroneous gene model prediction The predicted gene has been split into 2 genes: At3g48420 and At3g48425.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict106in Ref. 5; BAD43740
Sequence conflict314in Ref. 6; AAM63700

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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