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Protein

L-fucose isomerase

Gene

fucI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

L-fucopyranose = L-fuculose.1 Publication
D-arabinose = D-ribulose.1 Publication

Cofactori

Kineticsi

  1. KM=17 mM for L-fucose
  2. KM=35 mM for D-arabinose
  3. KM=1.4 mM for L-fuculose
  4. KM=11 mM for D-ribulose

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei337 – 3371Proton acceptor1 Publication
Metal bindingi337 – 3371Manganese
Active sitei361 – 3611Proton acceptor1 Publication
Metal bindingi361 – 3611Manganese
Metal bindingi528 – 5281Manganese

GO - Molecular functioni

  1. arabinose isomerase activity Source: EcoCyc
  2. identical protein binding Source: IntAct
  3. L-fucose isomerase activity Source: EcoCyc
  4. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-arabinose catabolic process Source: EcoCyc
  2. L-fucose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FUCISOM-MONOMER.
ECOL316407:JW2773-MONOMER.
MetaCyc:FUCISOM-MONOMER.
UniPathwayiUPA00563; UER00624.

Names & Taxonomyi

Protein namesi
Recommended name:
L-fucose isomerase (EC:5.3.1.25)
Short name:
FucIase
Alternative name(s):
6-deoxy-L-galactose isomerase
D-arabinose isomerase (EC:5.3.1.3)
Gene namesi
Name:fucI
Ordered Locus Names:b2802, JW2773
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10349. fucI.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591L-fucose isomerasePRO_0000204145Add
BLAST

Proteomic databases

PaxDbiP69922.
PRIDEiP69922.

Expressioni

Inductioni

By L-fucose.

Gene expression databases

GenevestigatoriP69922.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-908978,EBI-908978

Protein-protein interaction databases

IntActiP69922. 2 interactions.
STRINGi511145.b2802.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Turni19 – 213Combined sources
Helixi22 – 4423Combined sources
Beta strandi55 – 573Combined sources
Helixi65 – 7612Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 8910Combined sources
Helixi93 – 964Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi113 – 1153Combined sources
Helixi117 – 13014Combined sources
Beta strandi136 – 1383Combined sources
Helixi153 – 17220Combined sources
Beta strandi176 – 1827Combined sources
Helixi188 – 1903Combined sources
Helixi194 – 2018Combined sources
Beta strandi204 – 2085Combined sources
Helixi211 – 2188Combined sources
Helixi224 – 23714Combined sources
Helixi247 – 2493Combined sources
Helixi253 – 27523Combined sources
Helixi279 – 2824Combined sources
Helixi286 – 2894Combined sources
Beta strandi294 – 2996Combined sources
Turni302 – 3087Combined sources
Helixi313 – 3208Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi334 – 3363Combined sources
Helixi340 – 35314Combined sources
Beta strandi358 – 3669Combined sources
Helixi368 – 3758Combined sources
Helixi381 – 3855Combined sources
Beta strandi387 – 3904Combined sources
Helixi398 – 4014Combined sources
Helixi416 – 4183Combined sources
Helixi421 – 4299Combined sources
Beta strandi432 – 4354Combined sources
Turni438 – 4403Combined sources
Beta strandi446 – 4494Combined sources
Beta strandi457 – 46610Combined sources
Turni467 – 4693Combined sources
Beta strandi470 – 48011Combined sources
Helixi485 – 49410Combined sources
Beta strandi501 – 5066Combined sources
Helixi512 – 5143Combined sources
Helixi517 – 5226Combined sources
Beta strandi525 – 53410Combined sources
Helixi537 – 54711Combined sources
Beta strandi551 – 5533Combined sources
Helixi558 – 5603Combined sources
Helixi566 – 5694Combined sources
Helixi574 – 58512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUIX-ray2.50A/B/C/D/E/F1-591[»]
ProteinModelPortaliP69922.
SMRiP69922. Positions 1-591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69922.

Family & Domainsi

Sequence similaritiesi

Belongs to the L-fucose isomerase family.Curated

Phylogenomic databases

eggNOGiCOG2407.
HOGENOMiHOG000249674.
InParanoidiP69922.
KOiK01818.
OMAiRTDPTWP.
OrthoDBiEOG6FJNCF.
PhylomeDBiP69922.

Family and domain databases

Gene3Di3.20.14.10. 1 hit.
3.40.275.10. 1 hit.
3.40.50.1070. 1 hit.
HAMAPiMF_01254. Fucose_iso.
InterProiIPR004216. 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]
PfamiPF02952. Fucose_iso_C. 1 hit.
PF07881. Fucose_iso_N1. 1 hit.
PF07882. Fucose_iso_N2. 1 hit.
[Graphical view]
SUPFAMiSSF50443. SSF50443. 1 hit.
SSF53743. SSF53743. 1 hit.
TIGRFAMsiTIGR01089. fucI. 1 hit.

Sequencei

Sequence statusi: Complete.

P69922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG
60 70 80 90 100
AAVECVISDT CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD
110 120 130 140 150
PTRPKAIWGF NGTERPGAVY LAAALAAHSQ KGIPAFSIYG HDVQDADDTS
160 170 180 190 200
IPADVEEKLL RFARAGLAVA SMKGKSYLSL GGVSMGIAGS IVDHNFFESW
210 220 230 240 250
LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY GEDENNKQYQ
260 270 280 290 300
RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ
310 320 330 340 350
GQRHWTDQYP NGDTAEAILN SSFDWNGVRE PFVVATENDS LNGVAMLMGH
360 370 380 390 400
QLTGTAQVFA DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG
410 420 430 440 450
SCKQRDSEGN PTMKPHWEIS QQEADACLAA TEWCPAIHEY FRGGGYSSRF
460 470 480 490 500
LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS VELPKDVHDI LNKRTNSTWP
510 520 530 540 550
TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF ITLASMLRIP
560 570 580 590
VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R
Length:591
Mass (Da):64,977
Last modified:January 4, 2005 - v1
Checksum:iE6245DEEDF34EF9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81K → P AA sequence (PubMed:8052131).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15025 Genomic DNA. Translation: CAA33127.1.
U29581 Genomic DNA. Translation: AAB40452.1.
U00096 Genomic DNA. Translation: AAC75844.1.
AP009048 Genomic DNA. Translation: BAE76874.1.
PIRiJS0185. ISECFI.
RefSeqiNP_417282.1. NC_000913.3.
YP_491010.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75844; AAC75844; b2802.
BAE76874; BAE76874; BAE76874.
GeneIDi12930472.
946195.
KEGGiecj:Y75_p2739.
eco:b2802.
PATRICi32121020. VBIEscCol129921_2902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15025 Genomic DNA. Translation: CAA33127.1.
U29581 Genomic DNA. Translation: AAB40452.1.
U00096 Genomic DNA. Translation: AAC75844.1.
AP009048 Genomic DNA. Translation: BAE76874.1.
PIRiJS0185. ISECFI.
RefSeqiNP_417282.1. NC_000913.3.
YP_491010.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUIX-ray2.50A/B/C/D/E/F1-591[»]
ProteinModelPortaliP69922.
SMRiP69922. Positions 1-591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP69922. 2 interactions.
STRINGi511145.b2802.

Proteomic databases

PaxDbiP69922.
PRIDEiP69922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75844; AAC75844; b2802.
BAE76874; BAE76874; BAE76874.
GeneIDi12930472.
946195.
KEGGiecj:Y75_p2739.
eco:b2802.
PATRICi32121020. VBIEscCol129921_2902.

Organism-specific databases

EchoBASEiEB0345.
EcoGeneiEG10349. fucI.

Phylogenomic databases

eggNOGiCOG2407.
HOGENOMiHOG000249674.
InParanoidiP69922.
KOiK01818.
OMAiRTDPTWP.
OrthoDBiEOG6FJNCF.
PhylomeDBiP69922.

Enzyme and pathway databases

UniPathwayiUPA00563; UER00624.
BioCyciEcoCyc:FUCISOM-MONOMER.
ECOL316407:JW2773-MONOMER.
MetaCyc:FUCISOM-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69922.
PROiP69922.

Gene expression databases

GenevestigatoriP69922.

Family and domain databases

Gene3Di3.20.14.10. 1 hit.
3.40.275.10. 1 hit.
3.40.50.1070. 1 hit.
HAMAPiMF_01254. Fucose_iso.
InterProiIPR004216. 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]
PfamiPF02952. Fucose_iso_C. 1 hit.
PF07881. Fucose_iso_N1. 1 hit.
PF07882. Fucose_iso_N2. 1 hit.
[Graphical view]
SUPFAMiSSF50443. SSF50443. 1 hit.
SSF53743. SSF53743. 1 hit.
TIGRFAMsiTIGR01089. fucI. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
    Lu Z., Lin E.C.C.
    Nucleic Acids Res. 17:4883-4884(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. 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(2005) [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(1993) [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(1955) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH L-FUCITOL, ACTIVE SITES, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiFUCI_ECOLI
AccessioniPrimary (citable) accession number: P69922
Secondary accession number(s): P11552, Q2MA32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.