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   24-JAN-2024, entry version 121.
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.Q9FXE5; -.
DR   GlyCosmos; Q9FXE5; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT1G67830-1; -.
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; AT1G67830; FXG1.
DR   eggNOG; ENOG502QQGV; Eukaryota.
DR   HOGENOM; CLU_015101_2_0_1; -.
DR   InParanoid; Q9FXE5; -.
DR   OMA; RMACHRQ; -.
DR   OrthoDB; 1201565at2759; -.
DR   PhylomeDB; Q9FXE5; -.
DR   BioCyc; ARA:AT1G67830-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G67830-MONOMER; -.
DR   PRO; PR:Q9FXE5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FXE5; baseline and differential.
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; SGNH hydrolase; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   PANTHER; PTHR22835:SF588; ALPHA-L-FUCOSIDASE 3; 1.
DR   PANTHER; PTHR22835; ZINC FINGER FYVE DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   Genevisible; Q9FXE5; 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..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
//