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O52402 (ALF_EDWI9) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:NT01EI_3367
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

Protein attributes

Sequence length358 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
Gene Ontology (GO)
   Biological_processglycolytic process

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 – 358358Fructose-bisphosphate aldolase
PRO_0000178715

Regions

Region265 – 2673Dihydroxyacetone phosphate binding By similarity
Region286 – 2894Dihydroxyacetone 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 site621Glyceraldehyde 3-phosphate By similarity
Binding site2271Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict201K → E in AAB92572. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O52402 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 0EAADF89554D8049

FASTA35839,155
        10         20         30         40         50         60 
MSKIFDFVKP GVIFGDDVQK VFQVAKENKF ALPAVNCVGT DSINAVMEAA AKVRAPIIVQ 

        70         80         90        100        110        120 
FSNGGAAFIA GKGLKLEGQQ GAILGAIAGA HHVHQMAEYY GVPVILHTDH CAKKLLPWLD 

       130        140        150        160        170        180 
GLLDAGEKHF AATGKPLFSS HMIDLSEESL EENIEICSQY LARMSKIGMT LELELGCTGG 

       190        200        210        220        230        240 
EEDGVDNSHL DNSALYTQPE DVDYAFTKLS AISPRFTIAA SFGNVHGVYK PGNVQLTPVI 

       250        260        270        280        290        300 
LKNSQEYVSK KHNLPHNSLN FVFHGGSGST AAEIKEAVSY GVVKMNIDTD TQWATWEGVL 

       310        320        330        340        350 
KYYKKNEGYL QGQLGNPEGD DKPNKKYYDP RVWLRAAQTG MIERLEQAFK ELNCIDVL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of Edwardsiella ictaluri proteins expressed and recognized by the channel catfish Ictalurus punctatus immune response during infection."
Moore M.M., Fernandez D.L., Thune R.L.
Dis. Aquat. Organ. 52:93-107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 93-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF037440 Genomic DNA. Translation: AAB92572.1.
CP001600 Genomic DNA. Translation: ACR70504.1.
RefSeqYP_002934739.1. NC_012779.2.

3D structure databases

ProteinModelPortalO52402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634503.NT01EI_3367.

Proteomic databases

PRIDEO52402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR70504; ACR70504; NT01EI_3367.
GeneID7959666.
KEGGeic:NT01EI_3367.
PATRIC21839466. VBIEdwIct114273_2993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAHNSLDFV.
OrthoDBEOG69GZPB.

Enzyme and pathway databases

BioCycEICT634503:GCMY-3338-MONOMER.
SABIO-RKO52402.
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_EDWI9
AccessionPrimary (citable) accession number: O52402
Secondary accession number(s): C5BAU5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 76 of the entry and version 2 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