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Protein

L-fuculose phosphate aldolase

Gene

fucA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde.1 PublicationUniRule annotation

Catalytic activityi

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.1 PublicationUniRule annotation

Cofactori

Zn2+3 PublicationsUniRule annotationNote: Binds 1 zinc ion per subunit.3 PublicationsUniRule annotation

pH dependencei

Optimum pH is 7.2.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Proton acceptor1 Publication
Metal bindingi73 – 731Zinc3 PublicationsUniRule annotation
Metal bindingi92 – 921Zinc3 PublicationsUniRule annotation
Metal bindingi94 – 941Zinc3 PublicationsUniRule annotation
Active sitei113 – 1131Proton donor1 Publication
Metal bindingi155 – 1551Zinc3 PublicationsUniRule annotation

GO - Molecular functioni

  1. aldehyde-lyase activity Source: EcoCyc
  2. L-fuculose-phosphate aldolase activity Source: EcoCyc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. D-arabinose catabolic process Source: EcoCyc
  2. L-fucose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
SABIO-RKP0AB87.
UniPathwayiUPA00563; UER00626.

Names & Taxonomyi

Protein namesi
Recommended name:
L-fuculose phosphate aldolaseUniRule annotation (EC:4.1.2.17UniRule annotation)
Alternative name(s):
L-fuculose-1-phosphate aldolaseUniRule annotation
Gene namesi
Name:fucAUniRule annotation
Synonyms:fucC, prd
Ordered Locus Names:b2800, JW2771
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10348. fucA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215L-fuculose phosphate aldolasePRO_0000162925Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0AB87.

Interactioni

Subunit structurei

Homotetramer.4 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
yneKP761501EBI-1130362,EBI-1128384

Protein-protein interaction databases

DIPiDIP-9710N.
IntActiP0AB87. 1 interaction.
STRINGi511145.b2800.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917Combined sources
Helixi24 – 263Combined sources
Beta strandi29 – 346Combined sources
Beta strandi37 – 404Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 493Combined sources
Helixi52 – 543Combined sources
Beta strandi56 – 583Combined sources
Helixi74 – 8310Combined sources
Beta strandi89 – 935Combined sources
Helixi96 – 1049Combined sources
Beta strandi110 – 1123Combined sources
Helixi113 – 1186Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 14310Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1638Combined sources
Helixi164 – 18522Combined sources
Helixi196 – 20510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0AB87.
SMRiP0AB87. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB87.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0235.
HOGENOMiHOG000218184.
InParanoidiP0AB87.
KOiK01628.
OMAiIPPFHYM.
OrthoDBiEOG6HQSSQ.
PhylomeDBiP0AB87.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_00987. FucA.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view]
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR01086. fucA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AB87-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL
60 70 80 90 100
TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA
110 120 130 140 150
VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT
160 170 180 190 200
LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA
210
VVLEKFKTYG LRIEE
Length:215
Mass (Da):23,775
Last modified:November 8, 2005 - v1
Checksum:iBA9897E13ABE4A22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB33495. ADECFP.
RefSeqiNP_417280.1. NC_000913.3.
YP_491008.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneIDi12930230.
947282.
KEGGiecj:Y75_p2737.
eco:b2800.
PATRICi32121016. VBIEscCol129921_2900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB33495. ADECFP.
RefSeqiNP_417280.1. NC_000913.3.
YP_491008.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0AB87.
SMRiP0AB87. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9710N.
IntActiP0AB87. 1 interaction.
STRINGi511145.b2800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneIDi12930230.
947282.
KEGGiecj:Y75_p2737.
eco:b2800.
PATRICi32121016. VBIEscCol129921_2900.

Organism-specific databases

EchoBASEiEB0344.
EcoGeneiEG10348. fucA.

Phylogenomic databases

eggNOGiCOG0235.
HOGENOMiHOG000218184.
InParanoidiP0AB87.
KOiK01628.
OMAiIPPFHYM.
OrthoDBiEOG6HQSSQ.
PhylomeDBiP0AB87.

Enzyme and pathway databases

UniPathwayiUPA00563; UER00626.
BioCyciEcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
SABIO-RKP0AB87.

Miscellaneous databases

EvolutionaryTraceiP0AB87.
PROiP0AB87.

Gene expression databases

GenevestigatoriP0AB87.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_00987. FucA.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view]
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR01086. fucA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiFUCA_ECOLI
AccessioniPrimary (citable) accession number: P0AB87
Secondary accession number(s): P11550, Q2MA34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: January 7, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.