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Protein

Alpha-L-fucosidase 3

Gene

FXG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes alpha-1,2-linked fucose. Also active on fucosylated xyloglucan oligosaccharides.1 Publication

Catalytic activityi

An alpha-L-fucoside + H2O = L-fucose + an alcohol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371NucleophileBy similarity
Active sitei345 – 3451By similarity
Active sitei348 – 3481By similarity

GO - Molecular functioni

  • alpha-L-fucosidase activity Source: TAIR
  • hydrolase activity, acting on ester bonds Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT1G67830-MONOMER.
MetaCyc:AT1G67830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-fucosidase 3 (EC:3.2.1.51)
Alternative name(s):
Alpha-1,2-fucosidase
Short name:
AtFXG1
Alpha-L-fucoside fucohydrolase 3
Gene namesi
Name:FXG1
Ordered Locus Names:At1g67830
ORF Names:F12A21.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G67830.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: UniProtKB-SubCell
  • plant-type cell wall Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 372349Alpha-L-fucosidase 3PRO_0000225694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9FXE5.
PRIDEiQ9FXE5.

Expressioni

Tissue specificityi

High expression in younger leaves and in the apical region of the inflorescence stem.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G67830.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FXE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG245146.
HOGENOMiHOG000237648.
InParanoidiQ9FXE5.
KOiK01206.
OMAiDCHFPAV.
PhylomeDBiQ9FXE5.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. GDSL.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FXE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPILSSLFA LSLLSSLSPS THAHQCHFPA IFNFGDSNSD TGGLSAAFGQ
60 70 80 90 100
AGPPHGSSFF GSPAGRYCDG RLVIDFIAES LGLPYLSAFL DSVGSNFSHG
110 120 130 140 150
ANFATAGSPI RALNSTLRQS GFSPFSLDVQ FVQFYNFHNR SQTVRSRGGV
160 170 180 190 200
YKTMLPESDS FSKALYTFDI GQNDLTAGYF ANKTVEQVET EVPEIISQFM
210 220 230 240 250
NAIKNIYGQG GRYFWIHNTG PIGCLAYVIE RFPNKASDFD SHGCVSPLNH
260 270 280 290 300
LAQQFNHALK QAVIELRSSL SEAAITYVDV YSLKHELFVH AQGHGFKGSL
310 320 330 340 350
VSCCGHGGKY NYNKGIGCGM KKIVKGKEVY IGKPCDEPDK AVVWDGVHFT
360 370
QAANKFIFDK IAPGLSKACK RQ
Length:372
Mass (Da):40,462
Last modified:March 1, 2001 - v1
Checksum:iD88CA3FEE74A8155
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → R in BAD43265 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008113 Genomic DNA. Translation: AAG28886.1.
CP002684 Genomic DNA. Translation: AEE34703.1.
AK175502 mRNA. Translation: BAD43265.1.
RefSeqiNP_176949.1. NM_105451.3.
UniGeneiAt.23529.
At.35596.

Genome annotation databases

EnsemblPlantsiAT1G67830.1; AT1G67830.1; AT1G67830.
GeneIDi843109.
KEGGiath:AT1G67830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008113 Genomic DNA. Translation: AAG28886.1.
CP002684 Genomic DNA. Translation: AEE34703.1.
AK175502 mRNA. Translation: BAD43265.1.
RefSeqiNP_176949.1. NM_105451.3.
UniGeneiAt.23529.
At.35596.

3D structure databases

ProteinModelPortaliQ9FXE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G67830.1.

Proteomic databases

PaxDbiQ9FXE5.
PRIDEiQ9FXE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G67830.1; AT1G67830.1; AT1G67830.
GeneIDi843109.
KEGGiath:AT1G67830.

Organism-specific databases

TAIRiAT1G67830.

Phylogenomic databases

eggNOGiNOG245146.
HOGENOMiHOG000237648.
InParanoidiQ9FXE5.
KOiK01206.
OMAiDCHFPAV.
PhylomeDBiQ9FXE5.

Enzyme and pathway databases

BioCyciARA:AT1G67830-MONOMER.
MetaCyc:AT1G67830-MONOMER.

Miscellaneous databases

PROiQ9FXE5.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. GDSL.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-372.
    Strain: cv. Columbia.
  4. "AtFXG1, an Arabidopsis gene encoding alpha-L-fucosidase active against fucosylated xyloglucan oligosaccharides."
    de La Torre F., Sampedro J., Zarra I., Revilla G.
    Plant Physiol. 128:247-255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana."
    Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.
    Plant Cell Physiol. 47:55-63(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFUCO3_ARATH
AccessioniPrimary (citable) accession number: Q9FXE5
Secondary accession number(s): Q681W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The functional assignment is controversial.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. 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.