FUCO1_ARATH
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 03-AUG-2022, entry version 119.
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.AT2G28100.1; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR iPTMnet; Q8GW72; -.
DR PaxDb; Q8GW72; -.
DR PRIDE; Q8GW72; -.
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; locus:2046173; AT2G28100.
DR eggNOG; KOG3340; Eukaryota.
DR HOGENOM; CLU_002934_7_1_1; -.
DR InParanoid; Q8GW72; -.
DR OMA; DGWYGGA; -.
DR OrthoDB; 929780at2759; -.
DR BioCyc; ARA:AT2G28100-MON; -.
DR BioCyc; MetaCyc:AT2G28100-MON; -.
DR PRO; PR:Q8GW72; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GW72; baseline and differential.
DR Genevisible; Q8GW72; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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:0006004; P:fucose metabolic process; IBA:GO_Central.
DR GO; GO:0006516; P:glycoprotein catabolic process; TAS:TAIR.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; PTHR10030; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
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
