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Protein

Fructose-bisphosphate aldolase, cytoplasmic isozyme

Gene
N/A
Organism
Spinacia oleracea (Spinach)
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.

Pathwayi: glycolysis

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 (SOVF_097210), Glucose-6-phosphate isomerase, cytosolic (PGIC), Glucose-6-phosphate isomerase (GPIP)
  3. ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), ATP-dependent 6-phosphofructokinase (PFK)
  4. Fructose-bisphosphate aldolase (SOVF_190580), Fructose-bisphosphate aldolase, cytoplasmic isozyme, Fructose-bisphosphate aldolase (SOVF_128030), Fructose-bisphosphate aldolase (SOVF_094960), Fructose-bisphosphate aldolase, chloroplastic, Fructose-bisphosphate aldolase (SOVF_205230), Fructose-bisphosphate aldolase (SOVF_146670), Fructose-bisphosphate aldolase (SOVF_158110)
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)DescriptionActionsGraphical viewLength
Binding sitei53SubstrateBy similarity1
Binding sitei142SubstrateBy similarity1
Active sitei183Proton acceptorBy similarity1
Active sitei225Schiff-base intermediate with dihydroxyacetone-PBy similarity1
Sitei357Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity1

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: AgBase
  • protein self-association Source: AgBase

GO - Biological processi

  • fructose 1,6-bisphosphate metabolic process Source: AgBase
  • glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12898.
SABIO-RKP29356.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, cytoplasmic isozyme (EC:4.1.2.13)
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: AgBase
  • protein complex Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002169251 – 357Fructose-bisphosphate aldolase, cytoplasmic isozymeAdd BLAST357

Proteomic databases

PRIDEiP29356.

Interactioni

GO - Molecular functioni

  • protein self-association Source: AgBase

Structurei

3D structure databases

ProteinModelPortaliP29356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

P29356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAYRGKYAD ELIANASYIA TPGKVILAAD ESTGTIGKRF PSINVENVES
60 70 80 90 100
NRRALRELLF TTPGALPYLS GVILFEETLY QKTADGKPFV DAMKDGGVLP
110 120 130 140 150
GIKVDKGTVE LAGTNGETTT QGLDGLAQRC AQYYTAGARF AKWRAVLKIG
160 170 180 190 200
PTEPSPLAIL ENANGLARYG IICQENGLVP IVEPEILVDG THDIDRCAEV
210 220 230 240 250
SERVLAACYK ALNDHHVLLE GTSLKPNIVT PGSESKKVTP EVIAEYTVRT
260 270 280 290 300
LQRTVPQAVP GVMFLSGGQS EEEATLNLNA MNKLETKKPW TLSFSYGRAL
310 320 330 340 350
QQSTLKAWQG KEENVAKAQE VFLARAKGNS EATLGKYQGG AGGADASESL

HVKDYKY
Length:357
Mass (Da):38,471
Last modified:December 1, 1992 - v1
Checksum:i33150E3D80B1C6DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65742 mRNA. Translation: CAA46649.1.
PIRiS31091. ADSPAC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65742 mRNA. Translation: CAA46649.1.
PIRiS31091. ADSPAC.

3D structure databases

ProteinModelPortaliP29356.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP29356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciMetaCyc:MONOMER-12898.
SABIO-RKP29356.

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...

Entry informationi

Entry nameiALF_SPIOL
AccessioniPrimary (citable) accession number: P29356
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 5, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.