Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9C2U0 (ALF_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. 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
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
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:FBA1
Ordered Locus Names:KLLA0E07546g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces ›

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Fructose-bisphosphate aldolase
PRO_0000178758

Regions

Region267 – 2693Dihydroxyacetone phosphate binding By similarity
Region288 – 2914Dihydroxyacetone phosphate binding By similarity

Sites

Active site1101Proton donor By similarity
Metal binding1111Zinc 1; catalytic By similarity
Metal binding1451Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2271Zinc 1; catalytic By similarity
Metal binding2661Zinc 1; catalytic By similarity
Binding site631Glyceraldehyde 3-phosphate By similarity
Binding site2281Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C2U0 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: DCF0BEC26FF953D5

FASTA36139,600
        10         20         30         40         50         60 
MPAQDVLTRK TGVIVGDDVK ALFDYAKEHK FAIPAINVTS SSTVVAALEA ARDNKSPIIL 

        70         80         90        100        110        120 
QTSNGGAAYF AGKGVSNEGQ NASIRGSIAA AHYIRSIAPA YGIPVVLHTD HCAKKLLPWF 

       130        140        150        160        170        180 
DGMLKADEEY FAKHGEPLFS SHMLDLSEET DEENIGLCVK YFTRMAKIHQ WLEMEIGITG 

       190        200        210        220        230        240 
GEEDGVNNEG TSNDKLYTTP ETVFSVHEAL SKISPNFSIA SAFGNVHGVY KIAAALKPEL 

       250        260        270        280        290        300 
LGTFQDYAAK QLNKKAEDKP LYLVFHGGSG SSTKDFHTAI DFGVVKVNLD TDCQFAYLSG 

       310        320        330        340        350        360 
IRDYVLNKKD YLMTPVGNPT GEDSPNKKYY DPRVWVREGE KTMSKRITQA LEIFRTKGAL 


E

« Hide

References

« Hide 'large scale' references
[1]"Isolation and transcriptional regulation of the Kluyveromyces lactis FBA1 (fructose-1,6-bisphosphate aldolase) gene."
Diaz Prado S.M., Cerdan M.E., Gonzalez Siso M.I.
Can. J. Microbiol. 50:645-652(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ272114 Genomic DNA. Translation: CAC29023.2.
CR382125 Genomic DNA. Translation: CAG99377.1.
RefSeqXP_454290.1. XM_454290.1.

3D structure databases

ProteinModelPortalQ9C2U0.
ModBaseSearch...

Protein-protein interaction databases

STRING28985.Q9C2U0.

Proteomic databases

PRIDEQ9C2U0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2894094.
KEGGkla:KLLA0E07569g.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAREGEKTM.
OrthoDBEOG4J14HR.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_KLULA
AccessionPrimary (citable) accession number: Q9C2U0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2002
Last modified: May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents