Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AB88 (FUCA_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 59. 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:SF2814, S3009
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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_0000162929

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
P0AB88 [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

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN44302.1.
AE014073 Genomic DNA. Translation: AAP18127.1.
RefSeqNP_708595.1. NC_004337.2.
NP_838317.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AB88.
SMRP0AB88. Positions 1-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF2814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN44302; AAN44302; SF2814.
AAP18127; AAP18127; S3009.
GeneID1025774.
1079274.
KEGGsfl:SF2814.
sfx:S3009.
PATRIC18707695. VBIShiFle31049_3302.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_SHIFL
AccessionPrimary (citable) accession number: P0AB88
Secondary accession number(s): P11550
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 19, 2014
This is version 59 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