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Q8J0N6 (ALF2_PARBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 50. 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 2

Short name=FBP aldolase 2
Short name=FBPA 2
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase 2
Gene names
Name:FBA2
OrganismParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifier502779 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Induction

Only detected in the mycelia phase, but not in yeast cells. Ref.1

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Caution

The DNA coding for this protein is not found in the complete genome of strain ATCC MYA-826 / Pb01.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
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

Initiator methionine11Removed By similarity
Chain2 – 363362Fructose-bisphosphate aldolase 2
PRO_0000178760

Regions

Region265 – 2673Dihydroxyacetone phosphate binding By similarity

Sites

Active site1091Proton donor By similarity
Metal binding1101Zinc 1; catalytic By similarity
Metal binding1441Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2261Zinc 1; catalytic By similarity
Metal binding2641Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2271Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8J0N6 [UniParc].

Last modified October 1, 2003. Version 2.
Checksum: 929C731386F46D76

FASTA36339,770
        10         20         30         40         50         60 
MGVKDLLSRK TGVIVGDDVL RLFQHAQENV FAIPAIMVTS SSTGSALEAA RDKSPIVLQT 

        70         80         90        100        110        120 
SNGAAYFAGK GKGVSNDGQS VAGSIAIAAA HYIRSQAPAY GIPVVLHTDH CAKKLLPWLD 

       130        140        150        160        170        180 
GMLDADECYS KLHNEPLFSS HMIDLSEESV EWNIETTAKY LKRAAPMKQW LEMEIGITGG 

       190        200        210        220        230        240 
EEDGVNNESV DNNSLYTQPE DIYTIYKTLS AISPYFSIAA GFGNVHGVYR GDIALRPLLR 

       250        260        270        280        290        300 
HLHNAKYDEQ LKCLQDPLGF FVFHGGSGSS HQPATSITSE FAAKGRVDLE KVAYLPGTSS 

       310        320        330        340        350        360 
LVIAPKDYLM SPYGIPVVLH TDHCKYFDPR VQIREGLKHM SARVQEAKDD FNDSNQAKKL 


LPW 

« Hide

References

[1]"Paracoccidioides brasiliensis presents two different cDNAs encoding homologues of the fructose 1,6-biphosphate aldolase: protein isolation, cloning of the cDNAs and genes, structural, phylogenetic, and expression analysis."
Carneiro L.C., de Faria F.P., Felipe M.S.S., Pereira M., de Almeida Soares C.M.
Fungal Genet. Biol. 42:51-60(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION.
Strain: ATCC MYA-826 / Pb01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY172327 mRNA. Translation: AAN85569.2.
AY581212 Genomic DNA. Translation: AAS99115.2.

3D structure databases

ProteinModelPortalQ8J0N6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 2 hits.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF2_PARBA
AccessionPrimary (citable) accession number: Q8J0N6
Secondary accession number(s): Q6PT81
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2003
Last modified: January 22, 2014
This is version 50 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