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Reviewed, UniProtKB/Swiss-Prot Q01516 (ALFC1_PEA)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructose-bisphosphate aldolase 1, chloroplastic
    EC=4.1.2.13
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length356 AA.
Sequence statusFragment.
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 processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 6›6Chloroplast Ref.1
Chain7 – 356350Fructose-bisphosphate aldolase 1, chloroplastic
PRO_0000001110

Sites

Active site1831Proton acceptor By similarity
Active site2251Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site531Substrate By similarity
Binding site1431Substrate By similarity
Site3561Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Natural variations

Natural variant351A → W in strain: cv. Little Marvel.

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q01516-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 784A76C196D20941

FASTA35638,657
        10         20         30         40         50         60 
GLTIRAGSYA DELVKTAKTI ASPGRGILAM DESNATCGKR LASIGLENTE VNRQAWRTLL 

        70         80         90        100        110        120 
VTVPTLGEYI SGAILFEETL YQSTTDGRKI VDVLIEQNII PGIKVDKGLV PLAGSNDESW 

       130        140        150        160        170        180 
CQGLDGLASR SAAYYQQGAR FAKWRTVVSI PNGPSALAVK EAAWGLARYA AISQDNGLVP 

       190        200        210        220        230        240 
IVEPEILLDG EHGIDRTFEV AQKVWAEVFY YLAENNVQFE GILLKPSMVT PGAESKDKAS 

       250        260        270        280        290        300 
PTKVAEYTLN LLHRRIPPAV PGIMFLSGGQ SEVEATLNLN AMNKSPNPWH VSFSYARALQ 

       310        320        330        340        350 
NTALKTWGGL PENVKAAQEA LLFRAKSNSL AQLGKYYGDG ESEEAKKELF VKGYSY 

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References

[1]"Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases."
Razdan K., Heinrikson R.L., Zurcher-Neely H., Morris P.W., Anderson L.E.
Arch. Biochem. Biophys. 298:192-197(1992) [PubMed: 1524427] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 7-38.
Strain: cv. Little Marvel and cv. Sparkle.
Tissue: Leaf.

Cross-references

Sequence databases

M97476 Genomic DNA. Translation: AAA33642.1.
PIRS29047.

3D structure databases

HSSPHSSP built from PDB template 1A5C based on UniProtKB P14223.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.2.13. 287.

Family and domain databases

InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11627. Aldolase_I. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
ProDomPD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALFC1_PEA
AccessionPrimary (citable) accession number: Q01516
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents