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Q9HGY9 (ALF_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. 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

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:fbaA
ORF Names:AO090003000725
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Sequence caution

The sequence BAB12232.1 differs from that shown. Reason: Frameshift at positions 85 and 140.

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: UniProtKB-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 – 362362Fructose-bisphosphate aldolase
PRO_0000178756

Regions

Region269 – 2713Dihydroxyacetone phosphate binding By similarity
Region290 – 2934Dihydroxyacetone phosphate binding By similarity

Sites

Active site1121Proton donor By similarity
Metal binding1131Zinc 1; catalytic By similarity
Metal binding1471Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2291Zinc 1; catalytic By similarity
Metal binding2681Zinc 1; catalytic By similarity
Binding site651Glyceraldehyde 3-phosphate By similarity
Binding site2301Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HGY9 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 636526911421E17E

FASTA36239,721
        10         20         30         40         50         60 
MGVGVLEKLS RKTGVIVGDD VLRLFEHAQQ NNYAIPAVNV TSSSTVVASL EAARDQNCPI 

        70         80         90        100        110        120 
VLQLSQGGAA YFAGKGVSND GQQASIAGGI AAAHYIRSLA PAYGIPVVLH TDHCAKKLLP 

       130        140        150        160        170        180 
WLDGLLDEDE RYFKLHGEPL FSSHMIDLSE EPVDYNIQTT AAYLKRAAPM KQWLEMEIGI 

       190        200        210        220        230        240 
TGGEEDGVNN EDVDNNSLYT QPEDILAIHK ALSPISPYFS IAAGFGNVHG VYKPGNVKLH 

       250        260        270        280        290        300 
PELLKKHQAY VKEKIGSNKD KPVFFVFHGG SGSSKEEYKE AISYGVVKVN VDTDMQFAYM 

       310        320        330        340        350        360 
SGIRDYILKK KDYLMTAVGN PEGEDKPNKK SFDPRVWVRE GEKTMSQRVK VALEDFNTAG 


QL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032272 mRNA. Translation: BAB12232.1. Frameshift.
AP007155 Genomic DNA. Translation: BAE57870.1.
RefSeqXP_001819872.1. XM_001819820.2.

3D structure databases

ProteinModelPortalQ9HGY9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00001323; CADAORAP00001304; CADAORAG00001323.
GeneID5991855.
KEGGaor:AOR_1_1284154.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAKKAYDPR.
OrthoDBEOG7HTHSN.

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_ASPOR
AccessionPrimary (citable) accession number: Q9HGY9
Secondary accession number(s): Q2UKP5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 2, 2006
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways