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Protein

Fructose-bisphosphate aldolase, cytoplasmic isozyme 1

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521SubstrateBy similarity
Binding sitei142 – 1421SubstrateBy similarity
Active sitei183 – 1831Proton acceptorBy similarity
Active sitei225 – 2251Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei357 – 3571Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

SABIO-RKP46256.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, cytoplasmic isozyme 1 (EC:4.1.2.13)
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Fructose-bisphosphate aldolase, cytoplasmic isozyme 1PRO_0000216923Add
BLAST

Proteomic databases

PRIDEiP46256.

Structurei

3D structure databases

ProteinModelPortaliP46256.
SMRiP46256. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

P46256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAFVGKYAD ELIKNAKYIA TPGKGILAAD ESTGTIGKRL ASINVENIEA
60 70 80 90 100
NRQALRELLF TSPNALQYLS GVILFEETLY QKSSEGKPFV EILQENNVIP
110 120 130 140 150
GIKVDKGVVE LAGTDGETTT QGFDSLGARC QQYYKAGARF AKWRAVLKIG
160 170 180 190 200
PNEPSELSIQ QNAQGLARYA IICQENGLVL FVEPEILTDG SHDIAKCAAV
210 220 230 240 250
TETVLAACYK ALNDQHVLLE GTLLKPNMVT PGSDSPKVSP EVIGEYTVNA
260 270 280 290 300
LRRTVPAAVP GIVFLSGGQS EEQATLNLNA MNKFDVVKPW TLSFSFGRAL
310 320 330 340 350
QQSTLKTWSG KKENVGKAQD VFLARCKANS EATLGKYGGG SGTGLASESL

HVKDYKY
Length:357
Mass (Da):38,446
Last modified:October 31, 1995 - v1
Checksum:iBB30E70BA0401D61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89828 mRNA. Translation: CAA61946.1.
PIRiS58168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89828 mRNA. Translation: CAA61946.1.
PIRiS58168.

3D structure databases

ProteinModelPortaliP46256.
SMRiP46256. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP46256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
SABIO-RKP46256.

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

  1. Pelzer-Reith B., Schnarrenberger C.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.

Entry informationi

Entry nameiALF1_PEA
AccessioniPrimary (citable) accession number: P46256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: January 6, 2015
This is version 68 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

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.