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Protein

Fructose-bisphosphate aldolase, cytoplasmic isozyme

Gene

At4g26520

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
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), ATP-dependent 6-phosphofructokinase 7 (PFK7), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP-BETA2)
  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), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (At2g21330), Fructose-bisphosphate aldolase (At3g52930), 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Substrate
Binding sitei142 – 1421Substrate
Active sitei183 – 1831Proton acceptorBy similarity
Active sitei225 – 2251Schiff-base intermediate with dihydroxyacetone-P
Sitei358 – 3581Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: TAIR

GO - Biological processi

  • glycolytic process Source: UniProtKB-UniPathway
  • response to hypoxia Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciARA:AT4G26520-MONOMER.
ReactomeiREACT_285761. Fructose catabolism.
REACT_293115. Glycolysis.
REACT_298151. Gluconeogenesis.
REACT_342811. Platelet degranulation.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, cytoplasmic isozyme (EC:4.1.2.13)
Gene namesi
Ordered Locus Names:At4g26520
ORF Names:M3E9.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G26520.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Fructose-bisphosphate aldolase, cytoplasmic isozymePRO_0000216919Add
BLAST

Proteomic databases

PaxDbiP22197.
PRIDEiP22197.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G26520.1.

Structurei

3D structure databases

ProteinModelPortaliP22197.
SMRiP22197. Positions 11-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
InParanoidiP22197.
KOiK01623.
OMAiFKIGATE.
PhylomeDBiP22197.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAFVSKYED ELIKTAKYIA TPGRGILAAD ESTETIGKRF AGINVENTES
60 70 80 90 100
NRQAYRELLF TSPGSYPCLS GVILFEETLY QKTSDGKPFV DLLMENGVIP
110 120 130 140 150
GIKVDKGLVD LAGTNGETTT QGLDSLGARC QQYYEAGARF AKWRAFFKIG
160 170 180 190 200
ATEPSVLSIQ EDARVLARYA IICQENGLVP IVEPEVLTGG SHDIKKCAAV
210 220 230 240 250
TETVLAAVFK ALNYHHVLLE GTLLKPNMVT PGSDSPKVAP ELIAEYTVTA
260 270 280 290 300
LRRTVPPAIP GIVFLSGIQR EEQATLNLNA MNKLDVLKPW TLTFSFGGAL
310 320 330 340 350
QQSAIKAWAG KPENVAKAQA KFLTRCKANK DATLGKYTGW ASGDSAAFEN

LVVIGYRY
Length:358
Mass (Da):38,810
Last modified:September 27, 2005 - v2
Checksum:i3588E066D488C9CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381A → G in CAA37226 (PubMed:2103470).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53058 Genomic DNA. Translation: CAA37226.1.
AL022223 Genomic DNA. Translation: CAA18218.1.
AL161565 Genomic DNA. Translation: CAB79507.1.
CP002687 Genomic DNA. Translation: AEE85213.1.
BT001927 mRNA. Translation: AAN71926.1.
PIRiD85307.
S11958. ADMU.
RefSeqiNP_194382.1. NM_118785.3.
UniGeneiAt.32173.

Genome annotation databases

EnsemblPlantsiAT4G26520.1; AT4G26520.1; AT4G26520.
GeneIDi828758.
KEGGiath:AT4G26520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53058 Genomic DNA. Translation: CAA37226.1.
AL022223 Genomic DNA. Translation: CAA18218.1.
AL161565 Genomic DNA. Translation: CAB79507.1.
CP002687 Genomic DNA. Translation: AEE85213.1.
BT001927 mRNA. Translation: AAN71926.1.
PIRiD85307.
S11958. ADMU.
RefSeqiNP_194382.1. NM_118785.3.
UniGeneiAt.32173.

3D structure databases

ProteinModelPortaliP22197.
SMRiP22197. Positions 11-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G26520.1.

Proteomic databases

PaxDbiP22197.
PRIDEiP22197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G26520.1; AT4G26520.1; AT4G26520.
GeneIDi828758.
KEGGiath:AT4G26520.

Organism-specific databases

TAIRiAT4G26520.

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
InParanoidiP22197.
KOiK01623.
OMAiFKIGATE.
PhylomeDBiP22197.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciARA:AT4G26520-MONOMER.
ReactomeiREACT_285761. Fructose catabolism.
REACT_293115. Glycolysis.
REACT_298151. Gluconeogenesis.
REACT_342811. Platelet degranulation.

Miscellaneous databases

PROiP22197.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the Arabidopsis aldolase gene."
    Chopra S., Dolferus R., Jacobs M.
    Plant Mol. Biol. 15:517-520(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiALF_ARATH
AccessioniPrimary (citable) accession number: P22197
Secondary accession number(s): O65582, Q53YH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 27, 2005
Last modified: June 24, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.