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Protein

Fructose-bisphosphate aldolase

Gene

FBA1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

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 (RAG2)
  3. ATP-dependent 6-phosphofructokinase subunit alpha (PFK1), ATP-dependent 6-phosphofructokinase subunit beta (PFK2)
  4. Fructose-bisphosphate aldolase (FBA1)
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 sitei63 – 631Glyceraldehyde 3-phosphateBy similarity
Active sitei110 – 1101Proton donorBy similarity
Metal bindingi111 – 1111Zinc 1; catalyticBy similarity
Metal bindingi145 – 1451Zinc 2By similarity
Metal bindingi175 – 1751Zinc 2By similarity
Metal bindingi227 – 2271Zinc 1; catalyticBy similarity
Binding sitei228 – 2281Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi266 – 2661Zinc 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:FBA1
Ordered Locus Names:KLLA0E07546g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Chromosome E

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Fructose-bisphosphate aldolasePRO_0000178758Add
BLAST

Proteomic databases

PRIDEiQ9C2U0.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi284590.XP_454290.1.

Structurei

3D structure databases

ProteinModelPortaliQ9C2U0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 2693Dihydroxyacetone phosphate bindingBy similarity
Regioni288 – 2914Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
InParanoidiQ9C2U0.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG7HTHSN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C2U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAQDVLTRK TGVIVGDDVK ALFDYAKEHK FAIPAINVTS SSTVVAALEA
60 70 80 90 100
ARDNKSPIIL QTSNGGAAYF AGKGVSNEGQ NASIRGSIAA AHYIRSIAPA
110 120 130 140 150
YGIPVVLHTD HCAKKLLPWF DGMLKADEEY FAKHGEPLFS SHMLDLSEET
160 170 180 190 200
DEENIGLCVK YFTRMAKIHQ WLEMEIGITG GEEDGVNNEG TSNDKLYTTP
210 220 230 240 250
ETVFSVHEAL SKISPNFSIA SAFGNVHGVY KIAAALKPEL LGTFQDYAAK
260 270 280 290 300
QLNKKAEDKP LYLVFHGGSG SSTKDFHTAI DFGVVKVNLD TDCQFAYLSG
310 320 330 340 350
IRDYVLNKKD YLMTPVGNPT GEDSPNKKYY DPRVWVREGE KTMSKRITQA
360
LEIFRTKGAL E
Length:361
Mass (Da):39,600
Last modified:October 1, 2002 - v2
Checksum:iDCF0BEC26FF953D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272114 Genomic DNA. Translation: CAC29023.2.
CR382125 Genomic DNA. Translation: CAG99377.1.
RefSeqiXP_454290.1. XM_454290.1.

Genome annotation databases

GeneIDi2894094.
KEGGikla:KLLA0E07569g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272114 Genomic DNA. Translation: CAC29023.2.
CR382125 Genomic DNA. Translation: CAG99377.1.
RefSeqiXP_454290.1. XM_454290.1.

3D structure databases

ProteinModelPortaliQ9C2U0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284590.XP_454290.1.

Proteomic databases

PRIDEiQ9C2U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2894094.
KEGGikla:KLLA0E07569g.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
InParanoidiQ9C2U0.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG7HTHSN.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiALF_KLULA
AccessioniPrimary (citable) accession number: Q9C2U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.