A2AJL3 · FGGY_MOUSE

  • Protein
    FGGY carbohydrate kinase domain-containing protein
  • Gene
    Fggy
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. Postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Can phosphorylate ribitol with low efficiency.

Catalytic activity

Pathway

Carbohydrate metabolism; pentose and glucuronate interconversion.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionD-ribulokinase activity
Biological Processcarbohydrate phosphorylation
Biological Processneuron cellular homeostasis
Biological Processpentose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    FGGY carbohydrate kinase domain-containing protein
  • Alternative names
    • D-ribulokinase FGGY
      (EC:2.7.1.47
      ) . EC:2.7.1.47 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      Fggy

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    A2AJL3
  • Secondary accessions
    • Q8BUF2
    • Q8K0F0
    • Q9D7H0

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003264531-552FGGY carbohydrate kinase domain-containing protein

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

A2AJL3-1

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.

  • Length
    552
  • Mass (Da)
    60,336
  • Last updated
    2007-02-20 v1
  • Checksum
    F9EF93D1D013E1B3
MMSGRDQEPSRYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQKEYSAIMNGS

A2AJL3-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 360-387: CQSIYAYLNSHLDLIKKAQPVGFLTVDL → NLQKHHGIHGDTPGIAKYELEVTSSKAF
    • 388-552: Missing

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A2AJL4A2AJL4_MOUSEFggy464
B1AY71B1AY71_MOUSEFggy79
F6V664F6V664_MOUSEFggy133
F7ANG8F7ANG8_MOUSEFggy64
F6WQK7F6WQK7_MOUSEFggy32
B7ZCH9B7ZCH9_MOUSEFggy175
D6RG41D6RG41_MOUSEFggy110
D6RHR3D6RHR3_MOUSEFggy103
H3BJ80H3BJ80_MOUSEFggy77

Sequence caution

The sequence BAB26167.1 differs from that shown. Reason: Erroneous initiation
The sequence BAC39466.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict280in Ref. 1; BAC39466
Alternative sequenceVSP_032660360-387in isoform 2
Alternative sequenceVSP_032661388-552in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK009249
EMBL· GenBank· DDBJ
BAB26167.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK085534
EMBL· GenBank· DDBJ
BAC39466.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AL772131
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL844609
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL928634
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BX005293
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC031708
EMBL· GenBank· DDBJ
AAH31708.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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