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Q9I5Y1 (ALF_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:fba
Synonyms:fda
Ordered Locus Names:PA0555
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length354 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.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference 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 – 354354Fructose-bisphosphate aldolase
PRO_0000178725

Regions

Region233 – 2353Dihydroxyacetone phosphate binding By similarity
Region275 – 2784Dihydroxyacetone phosphate binding By similarity

Sites

Active site831Proton donor By similarity
Metal binding841Zinc 1; catalytic By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1421Zinc 2 By similarity
Metal binding1981Zinc 1; catalytic By similarity
Metal binding2321Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1991Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I5Y1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 08864F52A39FC9C7

FASTA35438,574
        10         20         30         40         50         60 
MALISMRQML DHAAEFGYGV PAFNVNNLEQ MRAIMEAADK TDSPVIVQAS AGARKYAGAP 

        70         80         90        100        110        120 
FLRHLILAAI EEFPHIPVVM HQDHGTSPDV CQRSIQLGFS SVMMDGSLRE DGKTPADYDY 

       130        140        150        160        170        180 
NVRVTQQTVA FAHACGVSVE GELGCLGSLE TGMAGEEDGV GAEGVLDHSQ LLTDPEEAAD 

       190        200        210        220        230        240 
FVKKTKVDAL AIAIGTSHGA YKFTKPPTGD TLSIQRIKEI HARIPDTHLV MHGSSSVPQD 

       250        260        270        280        290        300 
WLAIINEYGG EIKETYGVPV EEIVEGIKYG VRKVNIDTDL RLASTGAIRR FLAQNPSEFD 

       310        320        330        340        350 
PRKYFSKTVE AMRDICIARY EAFGTAGNAS KIKPISLEGM FQRYARGELD PKVN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG03944.1.
PIRC83575.
RefSeqNP_249246.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I5Y1.
SMRQ9I5Y1. Positions 3-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880792.
KEGGpae:PA0555.
PATRIC19835372. VBIPseAer58763_0587.

Organism-specific databases

PseudoCAPPA0555.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227792.
KOK01624.
OMAELCKDCI.
OrthoDBEOG6HXJ7B.
ProtClustDBPRK09196.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_PSEAE
AccessionPrimary (citable) accession number: Q9I5Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways