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Q8X6R8 (FUCA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 72. 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:
L-fuculose phosphate aldolase

EC=4.1.2.17
Alternative name(s):
L-fuculose-1-phosphate aldolase
Gene names
Name:fucA
Ordered Locus Names:Z4117, ECs3660
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde By similarity. HAMAP-Rule MF_00987

Catalytic activity

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. HAMAP-Rule MF_00987

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00987

Pathway

Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. HAMAP-Rule MF_00987

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00987

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fucose metabolism
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfucose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionL-fuculose-phosphate 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 – 215215L-fuculose phosphate aldolase HAMAP-Rule MF_00987
PRO_0000162926

Sites

Active site731Proton acceptor By similarity
Active site1131Proton donor By similarity
Metal binding731Zinc By similarity
Metal binding921Zinc By similarity
Metal binding941Zinc By similarity
Metal binding1551Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X6R8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 072E4EC5A94E76D1

FASTA21523,785
        10         20         30         40         50         60 
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG 

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

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

       190        200        210 
YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57914.1.
BA000007 Genomic DNA. Translation: BAB37083.1.
PIRD91086.
F85931.
RefSeqNP_289355.1. NC_002655.2.
NP_311687.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X6R8.
SMRQ8X6R8. Positions 1-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57914; AAG57914; Z4117.
BAB37083; BAB37083; BAB37083.
GeneID916460.
958302.
KEGGece:Z4117.
ecs:ECs3660.
PATRIC18356799. VBIEscCol44059_3582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0235.
HOGENOMHOG000218184.
KOK01628.
OMAQITCRAG.
OrthoDBEOG6HQSSQ.
ProtClustDBPRK08087.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3624-MONOMER.
ECOO157:FUCA-MONOMER.
UniPathwayUPA00563; UER00626.

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...

Entry information

Entry nameFUCA_ECO57
AccessionPrimary (citable) accession number: Q8X6R8
Secondary accession number(s): Q7AB69
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2002
Last modified: March 19, 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

PATHWAY comments

Index of metabolic and biosynthesis pathways