FUCO2_ARATH
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 03-AUG-2022, entry version 120.
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.AT4G34260.1; -.
DR CAZy; GH95; Glycoside Hydrolase Family 95.
DR PaxDb; Q8L7W8; -.
DR PRIDE; Q8L7W8; -.
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; locus:2116154; AT4G34260.
DR eggNOG; ENOG502QQ9E; Eukaryota.
DR HOGENOM; CLU_004617_2_2_1; -.
DR InParanoid; Q8L7W8; -.
DR OMA; KVWRGAC; -.
DR OrthoDB; 614028at2759; -.
DR PhylomeDB; Q8L7W8; -.
DR BioCyc; ARA:AT4G34260-MON; -.
DR PRO; PR:Q8L7W8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7W8; baseline and differential.
DR Genevisible; Q8L7W8; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0047513; F:1,2-alpha-L-fucosidase activity; IDA:TAIR.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IBA:GO_Central.
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; IPR016518; Alpha-L-fucosidase.
DR InterPro; IPR027414; GH95_N_dom.
DR Pfam; PF14498; Glyco_hyd_65N_2; 1.
DR PIRSF; PIRSF007663; UCP007663; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
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
