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P69922

- FUCI_ECOLI

UniProt

P69922 - FUCI_ECOLI

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Protein

L-fucose isomerase

Gene

fucI

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Manganese.

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: Chromosome, UP000000625: 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 – 147
Turni19 – 213
Helixi22 – 4423
Beta strandi55 – 573
Helixi65 – 7612
Turni77 – 793
Beta strandi80 – 8910
Helixi93 – 964
Beta strandi101 – 1033
Beta strandi105 – 1095
Beta strandi113 – 1153
Helixi117 – 13014
Beta strandi136 – 1383
Helixi153 – 17220
Beta strandi176 – 1827
Helixi188 – 1903
Helixi194 – 2018
Beta strandi204 – 2085
Helixi211 – 2188
Helixi224 – 23714
Helixi247 – 2493
Helixi253 – 27523
Helixi279 – 2824
Helixi286 – 2894
Beta strandi294 – 2996
Turni302 – 3087
Helixi313 – 3208
Beta strandi321 – 3244
Beta strandi334 – 3363
Helixi340 – 35314
Beta strandi358 – 3669
Helixi368 – 3758
Helixi381 – 3855
Beta strandi387 – 3904
Helixi398 – 4014
Helixi416 – 4183
Helixi421 – 4299
Beta strandi432 – 4354
Turni438 – 4403
Beta strandi446 – 4494
Beta strandi457 – 46610
Turni467 – 4693
Beta strandi470 – 48011
Helixi485 – 49410
Beta strandi501 – 5066
Helixi512 – 5143
Helixi517 – 5226
Beta strandi525 – 53410
Helixi537 – 54711
Beta strandi551 – 5533
Helixi558 – 5603
Helixi566 – 5694
Helixi574 – 58512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiKEGQDYR.
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 [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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JS0185. ISECFI.
RefSeqi NP_417282.1. NC_000913.3.
YP_491010.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FUI X-ray 2.50 A/B/C/D/E/F 1-591 [» ]
ProteinModelPortali P69922.
SMRi P69922. Positions 1-591.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P69922. 2 interactions.
STRINGi 511145.b2802.

Proteomic databases

PaxDbi P69922.
PRIDEi P69922.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75844 ; AAC75844 ; b2802 .
BAE76874 ; BAE76874 ; BAE76874 .
GeneIDi 12930472.
946195.
KEGGi ecj:Y75_p2739.
eco:b2802.
PATRICi 32121020. VBIEscCol129921_2902.

Organism-specific databases

EchoBASEi EB0345.
EcoGenei EG10349. fucI.

Phylogenomic databases

eggNOGi COG2407.
HOGENOMi HOG000249674.
InParanoidi P69922.
KOi K01818.
OMAi KEGQDYR.
OrthoDBi EOG6FJNCF.
PhylomeDBi P69922.

Enzyme and pathway databases

UniPathwayi UPA00563 ; UER00624 .
BioCyci EcoCyc:FUCISOM-MONOMER.
ECOL316407:JW2773-MONOMER.
MetaCyc:FUCISOM-MONOMER.

Miscellaneous databases

EvolutionaryTracei P69922.
PROi P69922.

Gene expression databases

Genevestigatori P69922.

Family and domain databases

Gene3Di 3.20.14.10. 1 hit.
3.40.275.10. 1 hit.
3.40.50.1070. 1 hit.
HAMAPi MF_01254. Fucose_iso.
InterProi 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 ]
Pfami PF02952. Fucose_iso_C. 1 hit.
PF07881. Fucose_iso_N1. 1 hit.
PF07882. Fucose_iso_N2. 1 hit.
[Graphical view ]
SUPFAMi SSF50443. SSF50443. 1 hit.
SSF53743. SSF53743. 1 hit.
TIGRFAMsi TIGR01089. fucI. 1 hit.
ProtoNeti Search...

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(1989) [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(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.

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: October 29, 2014
This is version 87 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