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P0AB87 (FUCA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:
L-fuculose phosphate aldolase

EC=4.1.2.17
Alternative name(s):
L-fuculose-1-phosphate aldolase
Gene names
Name:fucA
Synonyms:fucC, prd
Ordered Locus Names:b2800, JW2771
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde. Ref.6

Catalytic activity

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. Ref.6

Cofactor

Binds 1 zinc ion per subunit. Ref.7 Ref.8 Ref.9

Pathway

Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. Ref.6

Subunit structure

Homotetramer. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the aldolase class II family. AraD/FucA subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.2. Ref.6

Binary interactions

With

Entry

#Exp.

IntAct

Notes

yneKP761501EBI-1130362,EBI-1128384

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215L-fuculose phosphate aldolase HAMAP-Rule MF_00987
PRO_0000162925

Sites

Active site731Proton acceptor Probable
Active site1131Proton donor Probable
Metal binding731Zinc
Metal binding921Zinc
Metal binding941Zinc
Metal binding1551Zinc

Secondary structure

....................................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB87 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: BA9897E13ABE4A22

FASTA21523,775
        10         20         30         40         50         60 
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG 

        70         80         90        100        110        120 
NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRSIPA IHYMIAAAGG 

       130        140        150        160        170        180 
NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL 

       190        200        210 
YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
Lu Z., Lin E.C.C.
Nucleic Acids Res. 17:4883-4884(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol."
Chen Y.M., Lu Z., Lin E.C.C.
J. Bacteriol. 171:6097-6105(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[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]"Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae."
Conway T., Ingram L.O.
J. Bacteriol. 171:3754-3759(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-215.
Strain: K12.
[6]"The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate."
Ghalambor M.A., Heath E.C.
J. Biol. Chem. 237:2427-2433(1962) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
Strain: O111:B4.
[7]"The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli."
Dreyer M.K., Schulz G.E.
J. Mol. Biol. 231:549-553(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS), COFACTOR, SUBUNIT.
[8]"Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure."
Dreyer M.K., Schulz G.E.
J. Mol. Biol. 259:458-466(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC MECHANISM, COFACTOR, SUBUNIT, ACTIVE SITES.
[9]"Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli."
Dreyer M.K., Schulz G.E.
Acta Crystallogr. D 52:1082-1091(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.
[10]"Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis."
Joerger A.C., Gosse C., Fessner W.-D., Schulz G.E.
Biochemistry 39:6033-6041(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ZINC, MUTAGENESIS.
[11]"Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis."
Joerger A.C., Mueller-Dieckmann C., Schulz G.E.
J. Mol. Biol. 303:531-543(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF MUTANTS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31059 Genomic DNA. Translation: AAA23823.1.
X15025 Genomic DNA. Translation: CAA33125.1.
U29581 Genomic DNA. Translation: AAB40450.1.
U00096 Genomic DNA. Translation: AAC75842.1.
AP009048 Genomic DNA. Translation: BAE76872.1.
M27177 Genomic DNA. No translation available.
PIRADECFP. B33495.
RefSeqNP_417280.1. NC_000913.3.
YP_491008.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZUX-ray2.09P1-215[»]
1DZVX-ray1.86P1-215[»]
1DZWX-ray2.17P1-215[»]
1DZXX-ray2.18P1-215[»]
1DZYX-ray2.44P1-213[»]
1DZZX-ray1.92P1-215[»]
1E46X-ray2.55P1-215[»]
1E47X-ray2.15P1-215[»]
1E48X-ray1.97P1-215[»]
1E49X-ray2.53P1-215[»]
1E4AX-ray2.15P1-215[»]
1E4BX-ray1.84P1-215[»]
1E4CX-ray1.66P1-215[»]
1FUAX-ray1.92A1-215[»]
2FUAX-ray2.00A1-215[»]
3FUAX-ray2.67A1-215[»]
4FUAX-ray2.43A1-215[»]
ProteinModelPortalP0AB87.
SMRP0AB87. Positions 1-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9710N.
IntActP0AB87. 1 interaction.
STRING511145.b2800.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneID12930230.
947282.
KEGGecj:Y75_p2737.
eco:b2800.
PATRIC32121016. VBIEscCol129921_2900.

Organism-specific databases

EchoBASEEB0344.
EcoGeneEG10348. fucA.

Phylogenomic databases

eggNOGCOG0235.
HOGENOMHOG000218184.
KOK01628.
OMAIPPFHYM.
OrthoDBEOG6HQSSQ.
PhylomeDBP0AB87.
ProtClustDBPRK08087.

Enzyme and pathway databases

BioCycEcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
SABIO-RKP0AB87.
UniPathwayUPA00563; UER00626.

Gene expression databases

GenevestigatorP0AB87.

Family and domain databases

Gene3D3.40.225.10. 1 hit.
HAMAPMF_00987. FucA.
InterProIPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view]
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. SSF53639. 1 hit.
TIGRFAMsTIGR01086. fucA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AB87.
PROP0AB87.

Entry information

Entry nameFUCA_ECOLI
AccessionPrimary (citable) accession number: P0AB87
Secondary accession number(s): P11550, Q2MA34
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 72 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

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