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Protein

Fructose-bisphosphate aldolase

Gene

F8J2_100

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.UniRule annotationSAAS annotation

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.SAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (PGI1 (At4g24620)), Glucose-6-phosphate isomerase 1, chloroplastic (PGI1), Glucose-6-phosphate isomerase (PGIC), Glucose-6-phosphate isomerase, cytosolic (PGIC)
  3. ATP-dependent 6-phosphofructokinase 1 (PFK1), ATP-dependent 6-phosphofructokinase 5, chloroplastic (PFK5), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 1 (PFP-ALPHA1), ATP-dependent 6-phosphofructokinase 6 (PFK6), ATP-dependent 6-phosphofructokinase 3 (PFK3), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2 (PFP-ALPHA2), ATP-dependent 6-phosphofructokinase 4, chloroplastic (PFK4), ATP-dependent 6-phosphofructokinase 2 (PFK2), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 (PFP-BETA1), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP-BETA2), ATP-dependent 6-phosphofructokinase 7 (PFK7)
  4. Fructose-bisphosphate aldolase (M3E9.40), Fructose-bisphosphate aldolase (F17C15_110), Fructose-bisphosphate aldolase (At2g36460), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (FBA2), Probable fructose-bisphosphate aldolase 1, chloroplastic (FBA1), Fructose-bisphosphate aldolase (F8J2_100), Fructose-bisphosphate aldolase (F17C15.11), Fructose-bisphosphate aldolase, cytoplasmic isozyme (At4g26520), Probable fructose-bisphosphate aldolase 3, chloroplastic (FBA3), Fructose-bisphosphate aldolase (At2g36460), Probable fructose-bisphosphate aldolase 2, chloroplastic (FBA2), Fructose-bisphosphate aldolase (At5g03690), Fructose-bisphosphate aldolase (At2g21330), Fructose-bisphosphate aldolase (At5g03690)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  • glycolytic process Source: UniProtKB-UniPathway
  • response to cadmium ion Source: TAIR
  • response to karrikin Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciARA:AT3G52930-MONOMER.
ReactomeiR-ATH-114608. Platelet degranulation.
R-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.
R-ATH-70350. Fructose catabolism.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolaseUniRule annotationSAAS annotation (EC:4.1.2.13UniRule annotationSAAS annotation)
Gene namesi
Name:F8J2_100Imported
Ordered Locus Names:At3g52930Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52930.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • mitochondrial envelope Source: TAIR
  • mitochondrion Source: TAIR
  • nucleolus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuolar membrane Source: TAIR
Complete GO annotation...

PTM / Processingi

Proteomic databases

ProMEXiQ9LF98.

Interactioni

Protein-protein interaction databases

IntActiQ9LF98. 4 interactions.
MINTiMINT-8060856.
STRINGi3702.AT3G52930.1.

Structurei

3D structure databases

SMRiQ9LF98. Positions 5-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I fructose-bisphosphate aldolase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
HOGENOMiHOG000220876.
KOiK01623.
OMAiANCQAAQ.
PhylomeDBiQ9LF98.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LF98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAFTSKFAD ELIANAAYIG TPGKGILAAD ESTGTIGKRL ASINVENVET
60 70 80 90 100
NRRNLRELLF TAPGALPCLS GVILFEETLY QKSSDGKLFV DILKEGGVLP
110 120 130 140 150
GIKVDKGTVE LAGTDGETTT QGLDGLGDRC KKYYEAGARF AKWRAVLKIG
160 170 180 190 200
ENEPSEHSIH ENAYGLARYA VICQENGLVP IVEPEILVDG SHDIQKCAAV
210 220 230 240 250
TERVLAACYK ALSDHHVLLE GTLLKPNMVT PGSDSPKVSP EVIAEHTVRA
260 270 280 290 300
LQRTVPAAVP AIVFLSGGQS EEEATRNLNA MNQLKTKKPW SLSFSFGRAL
310 320 330 340 350
QQSTLKTWAG KEENVKAAQE ALYVRCKANS EATLGTYKGD AKLGDGAAES

LHVKDYKY
Length:358
Mass (Da):38,540
Last modified:October 1, 2000 - v1
Checksum:i0E25995B2EE0A319
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY052709 mRNA. Translation: AAK96613.1.
AY057656 mRNA. Translation: AAL15287.1.
AY063718 mRNA. Translation: AAL36068.1.
AY087346 mRNA. Translation: AAM64896.1.
CP002686 Genomic DNA. Translation: AEE79012.1.
AK317380 mRNA. Translation: BAH20051.1.
AL132969 Genomic DNA. Translation: CAB86897.1.
PIRiT47550.
RefSeqiNP_190861.1. NM_115153.3.
UniGeneiAt.25299.
At.75318.

Genome annotation databases

EnsemblPlantsiAT3G52930.1; AT3G52930.1; AT3G52930.
GeneIDi824459.
GrameneiAT3G52930.1; AT3G52930.1; AT3G52930.
KEGGiath:AT3G52930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY052709 mRNA. Translation: AAK96613.1.
AY057656 mRNA. Translation: AAL15287.1.
AY063718 mRNA. Translation: AAL36068.1.
AY087346 mRNA. Translation: AAM64896.1.
CP002686 Genomic DNA. Translation: AEE79012.1.
AK317380 mRNA. Translation: BAH20051.1.
AL132969 Genomic DNA. Translation: CAB86897.1.
PIRiT47550.
RefSeqiNP_190861.1. NM_115153.3.
UniGeneiAt.25299.
At.75318.

3D structure databases

SMRiQ9LF98. Positions 5-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9LF98. 4 interactions.
MINTiMINT-8060856.
STRINGi3702.AT3G52930.1.

Proteomic databases

ProMEXiQ9LF98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52930.1; AT3G52930.1; AT3G52930.
GeneIDi824459.
GrameneiAT3G52930.1; AT3G52930.1; AT3G52930.
KEGGiath:AT3G52930.

Organism-specific databases

TAIRiAT3G52930.

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
HOGENOMiHOG000220876.
KOiK01623.
OMAiANCQAAQ.
PhylomeDBiQ9LF98.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciARA:AT3G52930-MONOMER.
ReactomeiR-ATH-114608. Platelet degranulation.
R-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.
R-ATH-70350. Fructose catabolism.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    European Union Chromosome 3 Arabidopsis Sequencing Consortium, Institute for Genomic Research, Kazusa DNA Research Institute
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. ColumbiaImported.
  3. EU Arabidopsis sequencing project
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
  5. Cited for: NUCLEOTIDE SEQUENCE.
  6. Cited for: NUCLEOTIDE SEQUENCE.
  7. "Full-length messenger RNA sequences greatly improve genome annotation."
    Haas B.J., Volfovsky N., Town C.D., Troukhan M., Alexandrov N., Feldmann K.A., Flavell R.B., White O., Salzberg S.L.
    Genome Biol. 3:RESEARCH0029-RESEARCH0029(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  8. Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  9. "Features of Arabidopsis genes and genome discovered using full-length cDNAs."
    Alexandrov N.A., Troukhan M.E., Brover V.V., Flavell R.B., Feldmann K.A.
    Plant Mol. Biol. 60:71-87(2006)
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 0:0-0(2009)
    Cited for: NUCLEOTIDE SEQUENCE.
  11. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. TAIR
    Swarbreck D., Lamesch P., Wilks C., Huala E.
    Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  13. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. ColumbiaImported.
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiQ9LF98_ARATH
AccessioniPrimary (citable) accession number: Q9LF98
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.