ID   FUCO1_ARATH             Reviewed;         506 AA.
AC   Q8GW72; Q9ZUV2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Alpha-L-fucosidase 1;
DE            EC=3.2.1.51 {ECO:0000269|PubMed:16516937};
DE   AltName: Full=Alpha-1,3/4-fucosidase {ECO:0000303|PubMed:16516937};
DE            Short=AtFUC1 {ECO:0000303|PubMed:11788770};
DE   AltName: Full=Alpha-L-fucoside fucohydrolase;
DE   Flags: Precursor;
GN   Name=FUC1; OrderedLocusNames=At2g28100; ORFNames=F24D13.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   PRELIMINARY FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11788770; DOI=10.1104/pp.128.1.247;
RA   de La Torre F., Sampedro J., Zarra I., Revilla G.;
RT   "AtFXG1, an Arabidopsis gene encoding alpha-L-fucosidase active against
RT   fucosylated xyloglucan oligosaccharides.";
RL   Plant Physiol. 128:247-255(2002).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16516937; DOI=10.1016/j.phytochem.2006.01.021;
RA   Zeleny R., Leonard R., Dorfner G., Dalik T., Kolarich D., Altmann F.;
RT   "Molecular cloning and characterization of a plant alpha1,3/4-fucosidase
RT   based on sequence tags from almond fucosidase I.";
RL   Phytochemistry 67:641-648(2006).
CC   -!- FUNCTION: Hydrolyzes both 3- and 4-linked fucoses in Lewis
CC       determinants. Not active on neither 2-linked fucose nor on fucose in
CC       alpha-1,3-linkage to the innermost GlcNAc.
CC       {ECO:0000269|PubMed:16516937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose;
CC         Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51;
CC         Evidence={ECO:0000269|PubMed:16516937};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12289;
CC         Evidence={ECO:0000305|PubMed:16516937};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=28 uM for lacto-N-fucopentaose II {ECO:0000269|PubMed:16516937};
CC         KM=6.2 uM for 3-fucosyllactose {ECO:0000269|PubMed:16516937};
CC       pH dependence:
CC         Optimum pH is 5. Activity decreases sharply toward pH 7.
CC         {ECO:0000269|PubMed:16516937};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:11788770}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
CC   -!- CAUTION: Was reported by PubMed:11788770 to be an alpha-1,2-fucosidase.
CC       {ECO:0000305|PubMed:11788770}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC98456.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005851; AAC98456.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08079.1; -; Genomic_DNA.
DR   EMBL; AK119039; BAC43615.1; -; mRNA.
DR   PIR; G84680; G84680.
DR   RefSeq; NP_180377.2; NM_128370.3.
DR   AlphaFoldDB; Q8GW72; -.
DR   SMR; Q8GW72; -.
DR   BioGRID; 2705; 1.
DR   IntAct; Q8GW72; 1.
DR   STRING; 3702.Q8GW72; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GlyCosmos; Q8GW72; 6 sites, No reported glycans.
DR   iPTMnet; Q8GW72; -.
DR   PaxDb; 3702-AT2G28100-1; -.
DR   ProteomicsDB; 230046; -.
DR   EnsemblPlants; AT2G28100.1; AT2G28100.1; AT2G28100.
DR   GeneID; 817355; -.
DR   Gramene; AT2G28100.1; AT2G28100.1; AT2G28100.
DR   KEGG; ath:AT2G28100; -.
DR   Araport; AT2G28100; -.
DR   TAIR; AT2G28100; FUC1.
DR   eggNOG; KOG3340; Eukaryota.
DR   HOGENOM; CLU_002934_7_1_1; -.
DR   InParanoid; Q8GW72; -.
DR   OMA; YFFDSWF; -.
DR   OrthoDB; 2955544at2759; -.
DR   BioCyc; ARA:AT2G28100-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G28100-MONOMER; -.
DR   PRO; PR:Q8GW72; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8GW72; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006516; P:glycoprotein catabolic process; TAS:TAIR.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF27; ALPHA-L-FUCOSIDASE 1; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   Genevisible; Q8GW72; AT.
PE   1: Evidence at protein level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..506
FT                   /note="Alpha-L-fucosidase 1"
FT                   /id="PRO_0000225692"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        135
FT                   /note="E -> G (in Ref. 3; BAC43615)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  57186 MW;  5DD0B508E4560CB9 CRC64;
     MNSQITLFFF FFSILSLSQI SNSSSLLKPH PCPILPLPSS QQLQWQLGSM AMFLHFGPNT
     FTDSEWGTGK ANPSIFNPTH LNASQWVQIA KDSGFSRVIL TAKHHDGFCL WPSEYTDYSV
     KSSQWRNGAG DVVAELASAA KEAGIGLGLY LSPWDRHEQC YGKTLEYNEF YLSQMTELLT
     KYGEIKEVWL DGAKGDGEKD MEYFFDTWFS LIHQLQPKAV IFSDAGPDVR WIGDEAGLAG
     STCWSLFNRT NAKIGDTEPS YSQEGDGYGQ DWVPAECDVS IRPGWFWHAS ESPKPAVQLL
     DIYYNSVGRN CLFLLNVPPN SSGLISEQDI KVLEEFSEMK NSIFSNNLAR KAFVNSSSIR
     GDQSSQFGPK NVLEEGLDKY WAPEENQNEW VLYLEFKDLV SFNVLEIREP IHMGQRIASF
     HLETRKTGSG EWERVVSGTT VGNKRLLRFL NVVESRSLKL VVDKARTDPL ISYLGLYMDK
     FSGSSRNTTK ITITRTLKEE QQLHDL
//