L-fucose isomerase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P69922 (FUCI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	b2802, JW2773

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Protein existence	Evidence 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-fucose = L-fuculose. HAMAP-Rule MF_01254
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: K_M=17 mM for L-fucose K_M=35 mM for D-arabinose K_M=1.4 mM for L-fuculose K_M=11 mM for D-ribulose

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	D-arabinose catabolic process Inferred from mutant phenotype PubMed 4928018. Source: EcoCyc L-fucose catabolic process Inferred from mutant phenotype PubMed 4928018. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	L-fucose isomerase activity Inferred from direct assay PubMed 4632320. Source: EcoCyc arabinose isomerase activity Inferred from direct assay PubMed 4632320. Source: EcoCyc manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
yebT	P76272	1	EBI-908978,EBI-556588

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 591

591

L-fucose isomerase HAMAP-Rule MF_01254

PRO_0000204145

Sites

Active site

337

Proton acceptor Ref.6

Active site

361

Proton acceptor Ref.6

Metal binding

337

Manganese

Metal binding

361

Manganese

Metal binding

528

Manganese

Experimental info

Sequence conflict

K → P AA sequence Ref.4

Secondary structure

591

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P69922 [UniParc].

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

FASTA

591

64,977

        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' referencesShow '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 277:1453-1474(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, 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.

PIR

ISECFI. JS0185.

RefSeq

NP_417282.1. NC_000913.2.
YP_491010.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FUI	X-ray	2.50	A/B/C/D/E/F	1-591	[»]

ProteinModelPortal

P69922.

SMR

P69922. Positions 1-591.

ModBase

Search...

Protein-protein interaction databases

IntAct

P69922. 2 interactions.

STRING

511145.b2802.

Proteomic databases

PaxDb

P69922.

PRIDE

P69922.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75844; AAC75844; b2802.
BAE76874; BAE76874; BAE76874.

GeneID

12930472.
946195.

KEGG

ecj:Y75_p2739.
eco:b2802.

PATRIC

32121020. VBIEscCol129921_2902.

Organism-specific databases

EchoBASE

EB0345.

EcoGene

EG10349. fucI.

Phylogenomic databases

eggNOG

COG2407.

HOGENOM

HOG000249674.

K01818.

OMA

KIGIRPT.

ProtClustDB

PRK10991.

Enzyme and pathway databases

BioCyc

EcoCyc:FUCISOM-MONOMER.
ECOL316407:JW2773-MONOMER.
MetaCyc:FUCISOM-MONOMER.

UniPathway

UPA00563; UER00624.

Gene expression databases

Genevestigator

P69922.

Family and domain databases

Gene3D

3.20.14.10. 1 hit.
3.40.275.10. 1 hit.
3.40.50.1070. 1 hit.

HAMAP

MF_01254. Fucose_iso.

InterPro

IPR004216. 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]

Pfam

PF02952. Fucose_iso_C. 1 hit.
PF07881. Fucose_iso_N1. 1 hit.
PF07882. Fucose_iso_N2. 1 hit.
[Graphical view]

SUPFAM

SSF50443. Fuc_isomerase_C. 1 hit.
SSF53743. Fuc_isomerase_N. 1 hit.

TIGRFAMs

TIGR01089. fucI. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P69922.

Entry information

Entry name

FUCI_ECOLI

Accession

Primary (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 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents