ID   FUCO2_ARATH             Reviewed;         843 AA.
AC   Q8L7W8; Q9SYZ1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Alpha-L-fucosidase 2;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-1,2-fucosidase 2;
DE   AltName: Full=Alpha-L-fucosidase 95A;
DE            Short=AtFuc95A;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase 2;
DE   AltName: Full=Protein ALTERED XYLOGLUCAN 8;
DE   Flags: Precursor;
GN   Name=FUC95A; Synonyms=AXY8; OrderedLocusNames=At4g34260;
GN   ORFNames=F10M10.30;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15262925; DOI=10.1128/jb.186.15.4885-4893.2004;
RA   Katayama T., Sakuma A., Kimura T., Makimura Y., Hiratake J., Sakata K.,
RA   Yamanoi T., Kumagai H., Yamamoto K.;
RT   "Molecular cloning and characterization of Bifidobacterium bifidum 1,2-
RT   alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside
RT   hydrolase family 95).";
RL   J. Bacteriol. 186:4885-4893(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18495185; DOI=10.1016/j.phytochem.2008.03.024;
RA   Leonard R., Pabst M., Bondili J.S., Chambat G., Veit C., Strasser R.,
RA   Altmann F.;
RT   "Identification of an Arabidopsis gene encoding a GH95 alpha1,2-fucosidase
RT   active on xyloglucan oligo- and polysaccharides.";
RL   Phytochemistry 69:1983-1988(2008).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-511 AND PRO-562, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=22080600; DOI=10.1105/tpc.111.089193;
RA   Gunl M., Neumetzler L., Kraemer F., de Souza A., Schultink A., Pena M.,
RA   York W.S., Pauly M.;
RT   "AXY8 encodes an alpha-fucosidase, underscoring the importance of
RT   apoplastic metabolism on the fine structure of Arabidopsis cell wall
RT   polysaccharides.";
RL   Plant Cell 23:4025-4040(2011).
CC   -!- FUNCTION: Hydrolyzes alpha-1,2-linked fucose. Also active on
CC       fucosylated xyloglucan oligosaccharides. No activity with 3-
CC       fucosyllactose, p-nitrophenyl-alpha-I-fucopyranoside, lacto-N-
CC       fucopentaose II, lacto-N-fucopentaose III or alpha 1,6-fucosylated
CC       chitopentaose. Involved in apoplastic xyloglucan metabolism.
CC       {ECO:0000269|PubMed:18495185, ECO:0000269|PubMed:22080600}.
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:18495185};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.65 mM for 2-fucosyllactose {ECO:0000269|PubMed:18495185};
CC         KM=1.5 mM for polymeric xyloglucan {ECO:0000269|PubMed:18495185};
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:18495185};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:22080600}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in vascular tissues,
CC       leaf trichomes, root elongation zone and emerging lateral roots.
CC       {ECO:0000269|PubMed:22080600}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Higher abundance of
CC       fucosylated oligosaccharides and presence of unusual oligosaccharides.
CC       {ECO:0000269|PubMed:22080600}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 95 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36703.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80143.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035521; CAB36703.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161585; CAB80143.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86349.1; -; Genomic_DNA.
DR   EMBL; AY125494; AAM78086.1; -; mRNA.
DR   EMBL; BT002722; AAO11638.1; -; mRNA.
DR   PIR; T04772; T04772.
DR   RefSeq; NP_195152.2; NM_119590.4.
DR   AlphaFoldDB; Q8L7W8; -.
DR   SMR; Q8L7W8; -.
DR   STRING; 3702.Q8L7W8; -.
DR   CAZy; GH95; Glycoside Hydrolase Family 95.
DR   GlyCosmos; Q8L7W8; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT4G34260-1; -.
DR   ProteomicsDB; 230554; -.
DR   EnsemblPlants; AT4G34260.1; AT4G34260.1; AT4G34260.
DR   GeneID; 829575; -.
DR   Gramene; AT4G34260.1; AT4G34260.1; AT4G34260.
DR   KEGG; ath:AT4G34260; -.
DR   Araport; AT4G34260; -.
DR   TAIR; AT4G34260; FUC95A.
DR   eggNOG; ENOG502QQ9E; Eukaryota.
DR   HOGENOM; CLU_004617_2_2_1; -.
DR   InParanoid; Q8L7W8; -.
DR   OMA; KVWRGAC; -.
DR   OrthoDB; 1387368at2759; -.
DR   PhylomeDB; Q8L7W8; -.
DR   BioCyc; ARA:AT4G34260-MONOMER; -.
DR   PRO; PR:Q8L7W8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8L7W8; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0047513; F:1,2-alpha-L-fucosidase activity; IDA:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR049053; AFCA-like_C.
DR   InterPro; IPR016518; Alpha-L-fucosidase.
DR   InterPro; IPR027414; GH95_N_dom.
DR   PANTHER; PTHR31084; ALPHA-L-FUCOSIDASE 2; 1.
DR   PANTHER; PTHR31084:SF0; ALPHA-L-FUCOSIDASE 2; 1.
DR   Pfam; PF14498; Glyco_hyd_65N_2; 1.
DR   Pfam; PF21307; Glyco_hydro_95_C; 1.
DR   PIRSF; PIRSF007663; UCP007663; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q8L7W8; AT.
PE   1: Evidence at protein level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..843
FT                   /note="Alpha-L-fucosidase 2"
FT                   /id="PRO_0000289877"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         511
FT                   /note="C->Y: In axy8-4; Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:22080600"
FT   MUTAGEN         562
FT                   /note="P->L: In axy8-3; Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:22080600"
SQ   SEQUENCE   843 AA;  93725 MW;  2EF1315DF98A1365 CRC64;
     MAEKSSFFVH FSCLLLLLTI IITCGEGVRN PVRPRSSERR ALMDGQDLSR PLKLTFGGPS
     RNWTDAIPIG NGRLGATIWG GVSSEILNIN EDTIWTGVPA DYTNQKAPEA LAEVRRLVDE
     RNYAEATSEA VKLSGQPSDV YQIVGDLNLE FDSSHRKYTQ ASYRRELDLE TAVAKVSYSV
     GAVDFSREFF ASNPDQVIIA KIYASKPGSL SFKVSFDSEL HHHSETNPKA NQILMRGSCR
     PKRLPVNLKK SINATNIPYD DHKGLQFASI LEVRVSNGGS VSSLGGKKLS VEKADWAVLL
     LAASSNFDGP FTMPVDSKID PAKECVNRIS SVQKYSYSDL YARHLGDYQK LFNRVSLHLS
     GSSTNETVQQ ATSTAERVRS FKTDQDPSLV ELLFQYGRYL LISSSRPGTQ VANLQGIWNR
     DIQPPWDGAP HLNINLQMNY WHSLPGNIRE CQEPLFDYMS ALAINGRKTA QVNYGASGWV
     AHQVSDIWAK TSPDRGEAVW ALWPMGGAWL CTHAWEHYTY TMDKEFLKKK GYPLLEGCTS
     FLLDWLIKGK DGFLQTNPST SPEHMFTAPI GKPASVSYSS TMDIAIIKEV FADIVSASEI
     LGKTNDTLIG KVIAAQAKLP PTRISKDGSI REWAEDFEDP EVHHRHVSHL FGLFPGHTIT
     VEKSPELAKA VEATLKKRGE EGPGWSTTWK AALWARLHNS EHAYRMVTHI FDLVDPLNER
     NYEGGLYSNM FTAHPPFQID ANFGFAAAVA EMLVQSTTKD LYLLPALPAD KWPNGIVNGL
     RARGGVTVSI KWMEGNLVEF GLWSEQIVST RIVYRGISAA AELLPGKVFT FDKDLRCIRT
     DKL
//