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P69922 (FUCI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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-fucose isomerase

Short name=FucIase
EC=5.3.1.25
Alternative name(s):
6-deoxy-L-galactose isomerase
D-arabinose isomerase
EC=5.3.1.3
Gene names
Name:fucI
Ordered Locus Names:b2802, JW2773
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts the aldose L-fucose into the corresponding ketose L-fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively. HAMAP-Rule MF_01254

Catalytic activity

L-fucopyranose = L-fuculose. Ref.6

D-arabinose = D-ribulose. Ref.6

Cofactor

Manganese.

Pathway

Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 1/3. HAMAP-Rule MF_01254

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP-Rule MF_01254.

Induction

By L-fucose. HAMAP-Rule MF_01254

Sequence similarities

Belongs to the L-fucose isomerase family.

Biophysicochemical properties

Kinetic parameters:

KM=17 mM for L-fucose

KM=35 mM for D-arabinose

KM=1.4 mM for L-fuculose

KM=11 mM for D-ribulose

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-908978,EBI-908978

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591L-fucose isomerase HAMAP-Rule MF_01254
PRO_0000204145

Sites

Active site3371Proton acceptor Ref.6
Active site3611Proton acceptor Ref.6
Metal binding3371Manganese
Metal binding3611Manganese
Metal binding5281Manganese

Experimental info

Sequence conflict81K → P AA sequence Ref.4

Secondary structure

..................................................................................................... 591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69922 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E6245DEEDF34EF9B

FASTA59164,977
        10         20         30         40         50         60 
MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG AAVECVISDT 

        70         80         90        100        110        120 
CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD PTRPKAIWGF NGTERPGAVY 

       130        140        150        160        170        180 
LAAALAAHSQ KGIPAFSIYG HDVQDADDTS IPADVEEKLL RFARAGLAVA SMKGKSYLSL 

       190        200        210        220        230        240 
GGVSMGIAGS IVDHNFFESW LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY 

       250        260        270        280        290        300 
GEDENNKQYQ RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ 

       310        320        330        340        350        360 
GQRHWTDQYP NGDTAEAILN SSFDWNGVRE PFVVATENDS LNGVAMLMGH QLTGTAQVFA 

       370        380        390        400        410        420 
DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG SCKQRDSEGN PTMKPHWEIS 

       430        440        450        460        470        480 
QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS 

       490        500        510        520        530        540 
VELPKDVHDI LNKRTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF 

       550        560        570        580        590 
ITLASMLRIP VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R 

« 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]"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.
[3]"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.
[4]"Identification of a novel sugar-H+ symport protein, FucP, for transport of L-fucose into Escherichia coli."
Gunn F.J., Tate C.G., Henderson P.J.F.
Mol. Microbiol. 12:799-809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-9.
[5]"Enzymatic conversion of L-fucose to L-fuculose."
Green M., Cohen S.S.
J. Biol. Chem. 219:557-568(1956) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Structure and mechanism of L-fucose isomerase from Escherichia coli."
Seemann J.E., Schulz G.E.
J. Mol. Biol. 273:256-268(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH L-FUCITOL, ACTIVE SITES, CATALYTIC ACTIVITY, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15025 Genomic DNA. Translation: CAA33127.1.
U29581 Genomic DNA. Translation: AAB40452.1.
U00096 Genomic DNA. Translation: AAC75844.1.
AP009048 Genomic DNA. Translation: BAE76874.1.
PIRISECFI. JS0185.
RefSeqNP_417282.1. NC_000913.3.
YP_491010.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUIX-ray2.50A/B/C/D/E/F1-591[»]
ProteinModelPortalP69922.
SMRP69922. Positions 1-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP69922. 2 interactions.
STRING511145.b2802.

Proteomic databases

PaxDbP69922.
PRIDEP69922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75844; AAC75844; b2802.
BAE76874; BAE76874; BAE76874.
GeneID12930472.
946195.
KEGGecj:Y75_p2739.
eco:b2802.
PATRIC32121020. VBIEscCol129921_2902.

Organism-specific databases

EchoBASEEB0345.
EcoGeneEG10349. fucI.

Phylogenomic databases

eggNOGCOG2407.
HOGENOMHOG000249674.
KOK01818.
OMAKEGQDYR.
OrthoDBEOG6FJNCF.
PhylomeDBP69922.

Enzyme and pathway databases

BioCycEcoCyc:FUCISOM-MONOMER.
ECOL316407:JW2773-MONOMER.
MetaCyc:FUCISOM-MONOMER.
UniPathwayUPA00563; UER00624.

Gene expression databases

GenevestigatorP69922.

Family and domain databases

Gene3D3.20.14.10. 1 hit.
3.40.275.10. 1 hit.
3.40.50.1070. 1 hit.
HAMAPMF_01254. Fucose_iso.
InterProIPR004216. Fuc/Ara_isomerase_C.
IPR015888. Fuc_isomerase_C.
IPR012888. Fucose_iso_N1.
IPR005763. Fucose_isomerase.
IPR009015. Fucose_isomerase_N/cen.
IPR012889. Fucose_isomerase_N2.
[Graphical view]
PfamPF02952. Fucose_iso_C. 1 hit.
PF07881. Fucose_iso_N1. 1 hit.
PF07882. Fucose_iso_N2. 1 hit.
[Graphical view]
SUPFAMSSF50443. SSF50443. 1 hit.
SSF53743. SSF53743. 1 hit.
TIGRFAMsTIGR01089. fucI. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP69922.
PROP69922.

Entry information

Entry nameFUCI_ECOLI
AccessionPrimary (citable) accession number: P69922
Secondary accession number(s): P11552, Q2MA32
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 85 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