FUCO3_ARATH
ID FUCO3_ARATH Reviewed; 372 AA.
AC Q9FXE5; Q681W5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alpha-L-fucosidase 3;
DE EC=3.2.1.51 {ECO:0000269|PubMed:11788770};
DE AltName: Full=Alpha-1,2-fucosidase;
DE Short=AtFXG1;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 3;
DE Flags: Precursor;
GN Name=FXG1; OrderedLocusNames=At1g67830; ORFNames=F12A21.4;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 9-372.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16267099; DOI=10.1093/pcp/pci223;
RA Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:55-63(2006).
CC -!- FUNCTION: Hydrolyzes alpha-1,2-linked fucose. Also active on
CC fucosylated xyloglucan oligosaccharides. {ECO:0000269|PubMed:11788770}.
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:11788770};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:11788770, ECO:0000269|PubMed:16267099}.
CC -!- TISSUE SPECIFICITY: High expression in younger leaves and in the apical
CC region of the inflorescence stem. {ECO:0000269|PubMed:16267099}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: The functional assignment is controversial. {ECO:0000305}.
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DR EMBL; AC008113; AAG28886.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34703.1; -; Genomic_DNA.
DR EMBL; AK175502; BAD43265.1; -; mRNA.
DR RefSeq; NP_176949.1; NM_105451.4.
DR AlphaFoldDB; Q9FXE5; -.
DR SMR; Q9FXE5; -.
DR STRING; 3702.AT1G67830.1; -.
DR PaxDb; Q9FXE5; -.
DR PRIDE; Q9FXE5; -.
DR ProteomicsDB; 230047; -.
DR EnsemblPlants; AT1G67830.1; AT1G67830.1; AT1G67830.
DR GeneID; 843109; -.
DR Gramene; AT1G67830.1; AT1G67830.1; AT1G67830.
DR KEGG; ath:AT1G67830; -.
DR Araport; AT1G67830; -.
DR TAIR; locus:2008535; AT1G67830.
DR eggNOG; ENOG502QQGV; Eukaryota.
DR HOGENOM; CLU_015101_2_0_1; -.
DR InParanoid; Q9FXE5; -.
DR OMA; QAANKWI; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9FXE5; -.
DR BioCyc; ARA:AT1G67830-MON; -.
DR BioCyc; MetaCyc:AT1G67830-MON; -.
DR PRO; PR:Q9FXE5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXE5; baseline and differential.
DR Genevisible; Q9FXE5; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR Pfam; PF00657; Lipase_GDSL; 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..372
FT /note="Alpha-L-fucosidase 3"
FT /id="PRO_0000225694"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /evidence="ECO:0000250"
FT ACT_SITE 348
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 11
FT /note="L -> R (in Ref. 3; BAD43265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40462 MW; D88CA3FEE74A8155 CRC64;
MNPILSSLFA LSLLSSLSPS THAHQCHFPA IFNFGDSNSD TGGLSAAFGQ AGPPHGSSFF
GSPAGRYCDG RLVIDFIAES LGLPYLSAFL DSVGSNFSHG ANFATAGSPI RALNSTLRQS
GFSPFSLDVQ FVQFYNFHNR SQTVRSRGGV YKTMLPESDS FSKALYTFDI GQNDLTAGYF
ANKTVEQVET EVPEIISQFM NAIKNIYGQG GRYFWIHNTG PIGCLAYVIE RFPNKASDFD
SHGCVSPLNH LAQQFNHALK QAVIELRSSL SEAAITYVDV YSLKHELFVH AQGHGFKGSL
VSCCGHGGKY NYNKGIGCGM KKIVKGKEVY IGKPCDEPDK AVVWDGVHFT QAANKFIFDK
IAPGLSKACK RQ
