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A9N2J1 (FUCI_SALPB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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-fucose isomerase

EC=5.3.1.25
Alternative name(s):
6-deoxy-L-galactose isomerase
FucIase
Gene names
Name:fucI
Ordered Locus Names:SPAB_03704
OrganismSalmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]
Taxonomic identifier1016998 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts the aldose L-fucose into the corresponding ketose L-fuculose By similarity. HAMAP-Rule MF_01254

Catalytic activity

L-fucopyranose = L-fuculose. HAMAP-Rule MF_01254

Cofactor

Manganese By similarity. HAMAP-Rule MF_01254

Pathway

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

Subunit structure

Homohexamer By similarity. HAMAP-Rule MF_01254

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01254.

Sequence similarities

Belongs to the L-fucose isomerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fucose metabolism
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-fucose catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-fucose isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591L-fucose isomerase HAMAP-Rule MF_01254
PRO_1000085805

Sites

Active site3371Proton acceptor By similarity
Active site3611Proton acceptor By similarity
Metal binding3371Manganese By similarity
Metal binding3611Manganese By similarity
Metal binding5281Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
A9N2J1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0A1C6512CFDB846B

FASTA59164,789
        10         20         30         40         50         60 
MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL ITEKMRHACG AQVECVIADT 

        70         80         90        100        110        120 
CIAGMAESAA CEEKFSSQNV GVTITVTPCW CYGSETIDMD PMRPKAIWGF NGTERPGAVY 

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

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

       250        260        270        280        290        300 
GEDQNASQYK RNEAQNRAVL KESLLMAMCI RDMMQGNKTL ADKGLVEESL GYNAIAAGFQ 

       310        320        330        340        350        360 
GQRHWTDQYP NGDTAEALLN SSFDWNGVRE PFVVATENDS LNGVAMLFGH QLTGTAQIFA 

       370        380        390        400        410        420 
DVRTYWSPEA VERVTGQALS GLAEHGIIHL INSGSAALDG ACKQRDSEGK PTMKPHWEIS 

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

       490        500        510        520        530        540 
VELPKAMHDQ LDARTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF 

       550        560        570        580        590 
ITLAAMLRIP VCMHNVEEAK IYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000886 Genomic DNA. Translation: ABX69042.1.
RefSeqYP_001589875.1. NC_010102.1.

3D structure databases

ProteinModelPortalA9N2J1.
SMRA9N2J1. Positions 1-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272994.SPAB_03704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX69042; ABX69042; SPAB_03704.
PATRIC18534304. VBISalEnt120821_2993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2407.
HOGENOMHOG000249674.
OMAKIGIRPT.
OrthoDBEOG6FJNCF.
ProtClustDBPRK10991.

Enzyme and pathway databases

BioCycSENT28901:GH9O-3695-MONOMER.
UniPathwayUPA00563; UER00624.

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...

Entry information

Entry nameFUCI_SALPB
AccessionPrimary (citable) accession number: A9N2J1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 46 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