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Q96UH7 (ALF1_PARBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 59. 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 1

Short name=FBP aldolase 1
Short name=FBPA 1
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase 1
Gene names
Name:FBA1
ORF Names:PAAG_01995
OrganismParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis) [Complete proteome]
Taxonomic identifier502779 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Preferentially expressed in yeast cells, the host parasitic phase. Ref.1 Ref.3

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
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 Ref.3
Chain2 – 360359Fructose-bisphosphate aldolase 1
PRO_0000377379

Regions

Region267 – 2693Dihydroxyacetone 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

Experimental info

Sequence conflict2481Y → H in AAL25625. Ref.1
Sequence conflict2481Y → H in AAL34519. Ref.1
Sequence conflict3441S → C in AAL25625. Ref.1
Sequence conflict3441S → C in AAL34519. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96UH7 [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 67475F644C58E162

FASTA36039,632
        10         20         30         40         50         60 
MGVKDILSRK TGVIVGDDVL RLFQHAQEKV FAIPAINVTS SSTVVAALEA ARDKNSPIIL 

        70         80         90        100        110        120 
QVSQGGAAFF AGKGVPNGKQ EASVAGAIAA AHYIRSIAPS YGIPVVLHTD HCAKKLLPWL 

       130        140        150        160        170        180 
DGMLDADECY FKLHNEPLFS SHMIDLSEES VEWNIETTAK YLKRAAPMKQ WLEMEIGITG 

       190        200        210        220        230        240 
GEEDGVNNES VDNNSLYTQP EDIYTIYKTL SAISPYFSIA AGFGNVHGVY KPGNVRLHPE 

       250        260        270        280        290        300 
LLSKHQAYVK EKTGSSKNKP VYLVFHGGSG STKAEFKEAI SYGVVKVNLD TDLQYAYLSG 

       310        320        330        340        350        360 
VRDFVLKKKD YLMSAVGNPE GEDKPNKKYF DPRVWIREGE KTMSARVQEA FDDFNTSNQL 

« Hide

References

« Hide 'large scale' 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], PROTEIN SEQUENCE OF 328-339 AND 343-359, INDUCTION.
[2]"Comparative genomic analysis of human fungal pathogens causing paracoccidioidomycosis."
Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I. expand/collapse author list , Matsuo A.L., Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.
PLoS Genet. 7:E1002345-E1002345(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-826 / Pb01.
[3]"Two-dimensional electrophoresis and characterization of antigens from Paracoccidioides brasiliensis."
da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A., de Almeida Soares C.M.
Microbes Infect. 3:535-542(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-37, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY057387 Genomic DNA. Translation: AAL25625.2.
AY233454 mRNA. Translation: AAL34519.2.
DS572814 Genomic DNA. Translation: EEH39806.1.
RefSeqXP_002796107.1. XM_002796061.1.

3D structure databases

ProteinModelPortalQ96UH7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9099250.
KEGGpbl:PAAG_01995.

Phylogenomic databases

KOK01624.
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 nameALF1_PARBA
AccessionPrimary (citable) accession number: Q96UH7
Secondary accession number(s): C1GU00, Q8X219
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: September 1, 2009
Last modified: January 22, 2014
This is version 59 of the entry and version 3 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