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Protein
Submitted name:

Alpha-L-fucosidase

Gene

BT_2970

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. alpha-L-fucosidase activity Source: InterPro

GO - Biological processi

  1. fucose metabolic process Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-3033-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha-L-fucosidaseImported
Gene namesi
Ordered Locus Names:BT_2970Imported
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)Imported
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000001414 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi226186.BT_2970.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WVSX-ray2.19A/B/C/D31-473[»]
2WVTX-ray1.80A/B31-473[»]
2WVUX-ray1.95A/B/C/D31-473[»]
2WVVX-ray1.73A/B/C/D35-484[»]
2XIBX-ray2.20A/B/C/D32-484[»]
2XIIX-ray1.80A/B32-484[»]
4J27X-ray1.59A/B35-484[»]
4J28X-ray1.73A/B35-484[»]
4JFSX-ray2.00A/B35-484[»]
4JFTX-ray2.10A/B35-484[»]
4JFUX-ray1.66A/B35-484[»]
4JFVX-ray1.88A/B/C/D35-484[»]
4JFWX-ray2.10A/B/C/D35-484[»]
4JL1X-ray1.68A/B35-484[»]
4JL2X-ray1.70A/B35-484[»]
4PCSX-ray1.77A/B/C/D35-473[»]
4PCTX-ray2.10A/B/C/D35-473[»]
4PEEX-ray1.95A/B/C/D35-480[»]
4WSJX-ray1.64A/B/C/D35-479[»]
4WSKX-ray1.92A/B/C/D35-480[»]
ProteinModelPortaliQ8A3I4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8A3I4.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000108902.
InParanoidiQ8A3I4.
OMAiYESGYER.
OrthoDBiEOG6GXTRQ.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016286. FUC_metazoa-typ.
IPR000933. Glyco_hydro_29.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10030. PTHR10030. 1 hit.
PfamiPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFiPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSiPR00741. GLHYDRLASE29.
SMARTiSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8A3I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNTIIYRMK SRLITLLLLL ITVSSVTFAQ EAKKEIPLKY GATNEGKRQD
60 70 80 90 100
PAMQKFRDNR LGAFIHWGLY AIPGGEWNGK VYGGAAEWLK SWAKVPADEW
110 120 130 140 150
LKLMDQWNPT KFDAKKWAKM AKEMGTKYVK ITTKHHEGFC LWPSKYTKYT
160 170 180 190 200
VANTPYKRDI LGELVKAYND EGIDVHFYFS VMDWSNPDYR YDIKSKEDSI
210 220 230 240 250
AFSRFLEFTD NQLKELATRY PTVKDFWFDG TWDASVKKNG WWTAHAEQML
260 270 280 290 300
KELVPGVAIN SRLRADDKGK RHFDSNGRLM GDYESGYERR LPDPVKDLKV
310 320 330 340 350
TQWDWEACMT IPENQWGYHK DWSLSYVKTP IEVIDRIVHA VSMGGNMVVN
360 370 380 390 400
FGPQADGDFR PEEKAMATAI GKWMNRYGKA VYACDYAGFE KQDWGYYTRG
410 420 430 440 450
KNDEVYMVVF NQPYSERLIV KTPKGITVEK ATLLTTGEDI TVVETTRNEY
460 470 480
NVSVPKKNPG EPYVIQLKVR AAKGTKSIYR DALT
Length:484
Mass (Da):55,914
Last modified:May 31, 2003 - v1
Checksum:i1A6D1745A4554F1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO78076.1.
RefSeqiNP_811882.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO78076; AAO78076; BT_2970.
GeneIDi1075834.
KEGGibth:BT_2970.
PATRICi21060913. VBIBacThe70966_3020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO78076.1.
RefSeqiNP_811882.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WVSX-ray2.19A/B/C/D31-473[»]
2WVTX-ray1.80A/B31-473[»]
2WVUX-ray1.95A/B/C/D31-473[»]
2WVVX-ray1.73A/B/C/D35-484[»]
2XIBX-ray2.20A/B/C/D32-484[»]
2XIIX-ray1.80A/B32-484[»]
4J27X-ray1.59A/B35-484[»]
4J28X-ray1.73A/B35-484[»]
4JFSX-ray2.00A/B35-484[»]
4JFTX-ray2.10A/B35-484[»]
4JFUX-ray1.66A/B35-484[»]
4JFVX-ray1.88A/B/C/D35-484[»]
4JFWX-ray2.10A/B/C/D35-484[»]
4JL1X-ray1.68A/B35-484[»]
4JL2X-ray1.70A/B35-484[»]
4PCSX-ray1.77A/B/C/D35-473[»]
4PCTX-ray2.10A/B/C/D35-473[»]
4PEEX-ray1.95A/B/C/D35-480[»]
4WSJX-ray1.64A/B/C/D35-479[»]
4WSKX-ray1.92A/B/C/D35-480[»]
ProteinModelPortaliQ8A3I4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226186.BT_2970.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO78076; AAO78076; BT_2970.
GeneIDi1075834.
KEGGibth:BT_2970.
PATRICi21060913. VBIBacThe70966_3020.

Phylogenomic databases

HOGENOMiHOG000108902.
InParanoidiQ8A3I4.
OMAiYESGYER.
OrthoDBiEOG6GXTRQ.

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-3033-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8A3I4.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016286. FUC_metazoa-typ.
IPR000933. Glyco_hydro_29.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10030. PTHR10030. 1 hit.
PfamiPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFiPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSiPR00741. GLHYDRLASE29.
SMARTiSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
    Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
    Science 299:2074-2076(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VPI-5482Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482Imported.
  3. "Structural and thermodynamic analyses of alpha-L-fucosidase inhibitors."
    Lammerts van Bueren A., Popat S.D., Lin C.H., Davies G.J.
    ChemBioChem 11:1971-1974(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 32-484.
  4. "Analysis of the reaction coordinate of alpha-L-fucosidases: a combined structural and quantum mechanical approach."
    Lammerts van Bueren A., Ardevol A., Fayers-Kerr J., Luo B., Zhang Y., Sollogoub M., Bleriot Y., Rovira C., Davies G.J.
    J. Am. Chem. Soc. 132:1804-1806(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 35-484.
  5. "Three dimensional structure of a bacterial alpha-l-fucosidase with a 5-membered iminocyclitol inhibitor."
    Wright D.W., Moreno-Vargas A.J., Carmona A.T., Robina I., Davies G.J.
    Bioorg. Med. Chem. 21:4751-4754(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 35-484.
  6. "alpha-L-fucosidase inhibition by pyrrolidine-ferrocene hybrids: rationalization of ligand-binding properties by structural studies."
    Hottin A., Wright D.W., Steenackers A., Delannoy P., Dubar F., Biot C., Davies G.J., Behr J.B.
    Chemistry 19:9526-9533(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 35-484.
  7. "Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one."
    Davies G.J., Wright D.W.
    Submitted (SEP-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 35-479.
  8. "Crystal structure of a bacterial fucosidase."
    Davies G.J.
    Submitted (SEP-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 35-480.
  9. "Exploiting the hydrophobic terrain in fucosidases with aryl-substituted pyrrolidine iminosugars."
    Hottin A., Wright D.W., Davies G.J., Behr J.B.
    ChemBioChem 16:277-283(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 35-473.

Entry informationi

Entry nameiQ8A3I4_BACTN
AccessioniPrimary (citable) accession number: Q8A3I4
Entry historyi
Integrated into UniProtKB/TrEMBL: May 31, 2003
Last sequence update: May 31, 2003
Last modified: March 31, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.