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P16096 (ALFC_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase, chloroplastic

EC=4.1.2.13
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandSchiff base
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Chloroplast Ref.2
Chain47 – 394348Fructose-bisphosphate aldolase, chloroplastic
PRO_0000001113

Sites

Active site2231Proton acceptor By similarity
Active site2651Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site931Substrate By similarity
Binding site1831Substrate By similarity
Site3941Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Experimental info

Sequence conflict260 – 2634EGSS → RDP in CAA47293. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16096 [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: 9D8A813E1636B274

FASTA39442,468
        10         20         30         40         50         60 
MASASLLKTS PVLDNPEFLK GQTLRIPSVA GVRFTPSGSS SLTVRASSYA DELVKTAKTV 

        70         80         90        100        110        120 
ASPGRGILAM DESNATCGKR LASIGLENTE ANRQAYRTLL ISAPGLGQYV SGAILFEETL 

       130        140        150        160        170        180 
YQSTTDGKKM VDVLIEQGIV PGIKVDKGWL PLPGSNDESW CQGLDGLACR SAAYYQQGAR 

       190        200        210        220        230        240 
FAKWRTVVSI PNGPSALAVK EAAWGLARYA AITQDNGLDP ILEPEIMLDG EHGIDRTFRV 

       250        260        270        280        290        300 
AQQVWAEVFF NLAENNVLLE GSSLKPSMVG PGALSARKGP PEQVADYPLK LLHRRRGPVV 

       310        320        330        340        350        360 
PGIMVLSGGQ SEVEATLNLN AMNQSPNPWH VSFSYARALQ NTCLKTWVEG QENVKAQDFA 

       370        380        390 
CAKSNSLAQL GKYTGEGESE ERKKDMFVKA TLTY 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66814 mRNA. Translation: CAA47293.1.
PIRADSPAP. S31090.

3D structure databases

ProteinModelPortalP16096.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP16096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12899.
SABIO-RKP16096.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALFC_SPIOL
AccessionPrimary (citable) accession number: P16096
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways