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P0AB71 (ALF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase class 2

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II
Gene names
Name:fbaA
Synonyms:fba, fda
Ordered Locus Names:b2925, JW2892
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length359 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. Ref.8

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.8

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Biophysicochemical properties

Kinetic parameters:

The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate.

KM=0.17 mM for fructose-1,6-bisphosphate Ref.8

KM=0.35 mM for tagatose-1,6-bisphosphate

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from mutant phenotype PubMed 16562136. Source: EcoliWiki

zinc ion binding

Inferred from direct assay PubMed 11985624Ref.7. Source: EcoliWiki

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dnaKP0A6Y82EBI-370916,EBI-542092

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.5 Ref.6
Chain2 – 359358Fructose-bisphosphate aldolase class 2
PRO_0000178713

Regions

Region266 – 2683Dihydroxyacetone phosphate binding
Region287 – 2904Dihydroxyacetone phosphate binding

Sites

Active site1101Proton donor Ref.14
Metal binding1111Zinc 1; catalytic
Metal binding1451Zinc 2
Metal binding1751Zinc 2
Metal binding2271Zinc 1; catalytic
Metal binding2651Zinc 1; catalytic
Binding site621Glyceraldehyde 3-phosphate Probable
Binding site2281Dihydroxyacetone phosphate; via amide nitrogen

Amino acid modifications

Modified residue91N6-acetyllysine; alternate Ref.9
Modified residue91N6-malonyllysine; alternate Ref.10
Modified residue91N6-succinyllysine; alternate Ref.11
Modified residue721N6-succinyllysine Ref.11
Modified residue1151N6-succinyllysine Ref.11
Modified residue2311N6-succinyllysine Ref.11
Modified residue2511N6-succinyllysine Ref.11
Modified residue3191N6-succinyllysine Ref.11
Modified residue3261N6-succinyllysine Ref.11
Modified residue3481N6-succinyllysine Ref.11

Experimental info

Mutagenesis361N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. Ref.8
Mutagenesis601Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. Ref.8
Mutagenesis621S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. Ref.8
Mutagenesis621S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. Ref.8
Mutagenesis1081H → A: Loss of activity. Ref.7
Mutagenesis1111H → A: Loss of activity. Ref.7
Mutagenesis1121C → A: Partial loss of activity. Ref.7
Mutagenesis3261K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. Ref.8

Secondary structure

..................................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB71 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7A076D9EA62FBEC4

FASTA35939,147
        10         20         30         40         50         60 
MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ 

        70         80         90        100        110        120 
FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI 

       130        140        150        160        170        180 
DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG 

       190        200        210        220        230        240 
GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT 

       250        260        270        280        290        300 
ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV 

       310        320        330        340        350 
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL 

« Hide

References

« Hide 'large scale' references
[1]"Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
Alefounder P.R., Perham R.N.
Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / CS520.
[2]"Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli."
Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.
Biochem. J. 257:529-534(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[6]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli."
Berry A., Marshall K.E.
FEBS Lett. 318:11-16(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
[8]"Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases."
Zgiby S.M., Thomson G.J., Qamar S., Berry A.
Eur. J. Biochem. 267:1858-1868(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, REACTION MECHANISM, MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326.
Strain: K12 / MG1655 / ATCC 47076.
[9]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[10]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-9.
Strain: K12.
[11]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326 AND LYS-348.
Strain: K12.
[12]"Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase."
Blom N.S., Tetreault S., Coulombe R., Sygusch J.
Nat. Struct. Biol. 3:856-862(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
[13]"The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold."
Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H., Qamar S., Plater A., Berry A., Hunter W.N.
Structure 4:1303-1315(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
[14]"The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity."
Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.
J. Mol. Biol. 287:383-394(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG, ACTIVE SITE.
[15]"The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase."
Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N.
Acta Crystallogr. D 59:611-614(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, METAL BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14436 Genomic DNA. Translation: CAA32605.1.
U28377 Genomic DNA. Translation: AAA69092.1.
U00096 Genomic DNA. Translation: AAC75962.1.
AP009048 Genomic DNA. Translation: BAE76989.1.
PIRADEC2A. S02177.
RefSeqNP_417400.1. NC_000913.3.
YP_491125.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B57X-ray2.00A/B2-359[»]
1DOSX-ray1.67A/B2-359[»]
1GYNX-ray2.00A2-359[»]
1ZENX-ray2.50A2-359[»]
ProteinModelPortalP0AB71.
SMRP0AB71. Positions 2-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid851736. 1 interaction.
DIPDIP-31872N.
IntActP0AB71. 7 interactions.
STRING511145.b2925.

Chemistry

BindingDBP0AB71.
ChEMBLCHEMBL4912.

2D gel databases

SWISS-2DPAGEP0AB71.

Proteomic databases

PaxDbP0AB71.
PRIDEP0AB71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75962; AAC75962; b2925.
BAE76989; BAE76989; BAE76989.
GeneID12933075.
947415.
KEGGecj:Y75_p2856.
eco:b2925.
PATRIC32121264. VBIEscCol129921_3020.

Organism-specific databases

EchoBASEEB0278.
EcoGeneEG10282. fbaA.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAKKAYDPR.
OrthoDBEOG69GZPB.
PhylomeDBP0AB71.
ProtClustDBPRK09197.

Enzyme and pathway databases

BioCycEcoCyc:FRUCTBISALD-CLASSII-MONOMER.
ECOL316407:JW2892-MONOMER.
MetaCyc:FRUCTBISALD-CLASSII-MONOMER.
SABIO-RKP0AB71.
UniPathwayUPA00109; UER00183.

Gene expression databases

GenevestigatorP0AB71.

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...

Other

EvolutionaryTraceP0AB71.
PROP0AB71.

Entry information

Entry nameALF_ECOLI
AccessionPrimary (citable) accession number: P0AB71
Secondary accession number(s): P11604, Q2M9R7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene