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Protein

Fructose-bisphosphate aldolase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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, cytosolic (PGIC), Glucose-6-phosphate isomerase (GPIP)
  3. ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK)
  4. Fructose-bisphosphate aldolase, cytoplasmic isozyme, Fructose-bisphosphate aldolase, chloroplastic
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 sitei93 – 931SubstrateBy similarity
Binding sitei183 – 1831SubstrateBy similarity
Active sitei223 – 2231Proton acceptorBy similarity
Active sitei265 – 2651Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei394 – 3941Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12899.
BRENDAi4.1.2.13. 5812.
SABIO-RKP16096.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Chloroplast1 PublicationAdd
BLAST
Chaini47 – 394348Fructose-bisphosphate aldolase, chloroplasticPRO_0000001113Add
BLAST

Proteomic databases

PRIDEiP16096.

Structurei

3D structure databases

ProteinModelPortaliP16096.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASASLLKTS PVLDNPEFLK GQTLRIPSVA GVRFTPSGSS SLTVRASSYA
60 70 80 90 100
DELVKTAKTV ASPGRGILAM DESNATCGKR LASIGLENTE ANRQAYRTLL
110 120 130 140 150
ISAPGLGQYV SGAILFEETL YQSTTDGKKM VDVLIEQGIV PGIKVDKGWL
160 170 180 190 200
PLPGSNDESW CQGLDGLACR SAAYYQQGAR FAKWRTVVSI PNGPSALAVK
210 220 230 240 250
EAAWGLARYA AITQDNGLDP ILEPEIMLDG EHGIDRTFRV AQQVWAEVFF
260 270 280 290 300
NLAENNVLLE GSSLKPSMVG PGALSARKGP PEQVADYPLK LLHRRRGPVV
310 320 330 340 350
PGIMVLSGGQ SEVEATLNLN AMNQSPNPWH VSFSYARALQ NTCLKTWVEG
360 370 380 390
QENVKAQDFA CAKSNSLAQL GKYTGEGESE ERKKDMFVKA TLTY
Length:394
Mass (Da):42,468
Last modified:November 1, 1995 - v3
Checksum:i9D8A813E1636B274
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2634EGSS → RDP in CAA47293 (PubMed:8425060).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66814 mRNA. Translation: CAA47293.1.
PIRiS31090. ADSPAP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66814 mRNA. Translation: CAA47293.1.
PIRiS31090. ADSPAP.

3D structure databases

ProteinModelPortaliP16096.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP16096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciMetaCyc:MONOMER-12899.
BRENDAi4.1.2.13. 5812.
SABIO-RKP16096.

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. "Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach."
    Pelzer-Reith B., Penger A., Schnarrenberger C.
    Plant Mol. Biol. 21:331-340(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase."
    Lebherz H.G., Leadbetter M.M., Bradshaw R.A.
    J. Biol. Chem. 259:1011-1017(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-64.
  3. Bairoch A.
    Unpublished observations (NOV-1995)
    Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT.

Entry informationi

Entry nameiALFC_SPIOL
AccessioniPrimary (citable) accession number: P16096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.