ID   XTH1_ARATH              Reviewed;         295 AA.
AC   Q9SV61;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 3.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Putative xyloglucan endotransglucosylase/hydrolase protein 1;
DE            Short=At-XTH1;
DE            Short=XTH-1;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH1; OrderedLocusNames=At4g13080; ORFNames=F25G13.170;
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   NOMENCLATURE.
RX   PubMed=12514239; DOI=10.1093/pcp/pcf171;
RA   Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
RT   "The XTH family of enzymes involved in xyloglucan endotransglucosylation
RT   and endohydrolysis: current perspectives and a new unifying nomenclature.";
RL   Plant Cell Physiol. 43:1421-1435(2002).
CC   -!- FUNCTION: May catalyze xyloglucan endohydrolysis (XEH) and/or
CC       endotransglycosylation (XET). Cleaves and religates xyloglucan
CC       polymers, an essential constituent of the primary cell wall, and
CC       thereby participates in cell wall construction of growing tissues (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC         transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC         terminal glucose residue of an acceptor, which can be a xyloglucan or
CC         an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC       extracellular space, apoplast {ECO:0000305}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL079349; CAB45507.1; -; Genomic_DNA.
DR   EMBL; AL161535; CAB78350.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83228.2; -; Genomic_DNA.
DR   PIR; T10210; T10210.
DR   RefSeq; NP_193044.3; NM_117377.3.
DR   AlphaFoldDB; Q9SV61; -.
DR   SMR; Q9SV61; -.
DR   STRING; 3702.Q9SV61; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q9SV61; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT4G13080-1; -.
DR   ProteomicsDB; 242796; -.
DR   EnsemblPlants; AT4G13080.1; AT4G13080.1; AT4G13080.
DR   GeneID; 826922; -.
DR   Gramene; AT4G13080.1; AT4G13080.1; AT4G13080.
DR   KEGG; ath:AT4G13080; -.
DR   Araport; AT4G13080; -.
DR   TAIR; AT4G13080; XTH1.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_048041_2_1_1; -.
DR   InParanoid; Q9SV61; -.
DR   OMA; FPAKPMR; -.
DR   OrthoDB; 337487at2759; -.
DR   BioCyc; ARA:AT4G13080-MONOMER; -.
DR   PRO; PR:Q9SV61; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SV61; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR   GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR   CDD; cd02176; GH16_XET; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF190; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 2-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   Genevisible; Q9SV61; AT.
PE   3: Inferred from homology;
KW   Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW   Transferase.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..295
FT                   /note="Putative xyloglucan endotransglucosylase/hydrolase
FT                   protein 1"
FT                   /id="PRO_0000011801"
FT   DOMAIN          27..225
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         117
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         129..131
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         139..141
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         204..205
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         209
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         283
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            115
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        233..242
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        278..291
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ   SEQUENCE   295 AA;  33621 MW;  5B2E17F7ECD1D19B CRC64;
     MNKMEYLSIF GFVSVLYLII RVDARAYEVN GIDQSKVGFD DNYVVTWGQN NVLKLNQGKE
     VQLSLDHSSG SGFESKNHYE SGFFQIRIKV PPKDTSGVVT AFYLTSKGNT HDEVDFEFLG
     NKEGKLAVQT NVFTNGKGNR EQKLALWFDP SKDFHTYAIL WNPYQIVLYV DNIPVRVFKN
     TTSQGMNYPS KPMQVVVSLW NGENWATDGG KSKINWSLAP FKANFQGFNN SGCFTNAEKN
     ACGSSAYWWN TGSYSKLSDS EQKAYTNVRQ KYMNYDYCSD KVRFHVPPSE CKWNN
//