ID   XTH25_ARATH             Reviewed;         284 AA.
AC   Q38907; Q9SEB0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 25;
DE            Short=At-XTH25;
DE            Short=XTH-25;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH25; Synonyms=EXGT-A5, XTR3; OrderedLocusNames=At5g57550;
GN   ORFNames=MUA2.12;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10557219; DOI=10.1104/pp.121.3.715;
RA   Akamatsu T., Hanzawa Y., Ohtake Y., Takahashi T., Nishitani K., Komeda Y.;
RT   "Expression of endoxyloglucan transferase genes in acaulis mutants of
RT   Arabidopsis.";
RL   Plant Physiol. 121:715-721(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-284, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=8696366; DOI=10.1046/j.1365-313x.1996.9060879.x;
RA   Xu W., Campbell P., Vargheese A.K., Braam J.;
RT   "The Arabidopsis XET-related gene family: environmental and hormonal
RT   regulation of expression.";
RL   Plant J. 9:879-889(1996).
RN   [6]
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: Catalyzes 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   -!- TISSUE SPECIFICITY: Expressed in siliques. Not detected in other tested
CC       tissues. {ECO:0000269|PubMed:10557219}.
CC   -!- INDUCTION: By auxin. Not induced following darkness.
CC       {ECO:0000269|PubMed:8696366}.
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 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF163823; AAD45127.1; -; Genomic_DNA.
DR   EMBL; AB011482; BAB08790.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96914.1; -; Genomic_DNA.
DR   EMBL; AY125495; AAM78087.1; -; mRNA.
DR   EMBL; AY143939; AAN28878.1; -; mRNA.
DR   EMBL; U43485; AAB18364.1; -; mRNA.
DR   PIR; S71222; S71222.
DR   RefSeq; NP_568859.2; NM_125136.4.
DR   AlphaFoldDB; Q38907; -.
DR   SMR; Q38907; -.
DR   STRING; 3702.Q38907; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q38907; 1 site, No reported glycans.
DR   PaxDb; 3702-AT5G57550-1; -.
DR   ProteomicsDB; 242527; -.
DR   EnsemblPlants; AT5G57550.1; AT5G57550.1; AT5G57550.
DR   GeneID; 835859; -.
DR   Gramene; AT5G57550.1; AT5G57550.1; AT5G57550.
DR   KEGG; ath:AT5G57550; -.
DR   Araport; AT5G57550; -.
DR   TAIR; AT5G57550; XTH25.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   InParanoid; Q38907; -.
DR   OMA; GVPKECN; -.
DR   OrthoDB; 337487at2759; -.
DR   PhylomeDB; Q38907; -.
DR   BioCyc; ARA:AT5G57550-MONOMER; -.
DR   PRO; PR:Q38907; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q38907; 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; ISS:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009832; P:plant-type cell wall biogenesis; ISS:TAIR.
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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF303; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 25-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   Genevisible; Q38907; AT.
PE   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW   Transferase.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..284
FT                   /note="Probable xyloglucan endotransglucosylase/hydrolase
FT                   protein 25"
FT                   /id="PRO_0000011825"
FT   DOMAIN          28..218
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        108
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   BINDING         108
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         121..123
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         131..133
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         197..198
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         202
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         273
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            106
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..235
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        268..282
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ   SEQUENCE   284 AA;  32573 MW;  9ADC65F0B0213F76 CRC64;
     MDRSTFILSL LFTLTVSTTT LFSPVFAGTF DTEFDITWGD GRGKVLNNGE LLTLSLDRAS
     GSGFQTKKEY LFGKIDMQLK LVPGNSAGTV TAYYLKSKGD TWDEIDFEFL GNLTGDPYTM
     HTNVYTQGKG DREQQFHLWF DPTADFHTYS VLWNPHHIVF MVDDIPVREF KNLQHMGIQY
     PKLQPMRLYS SLWNADQWAT RGGLVKTDWS KAPFTASYRN FRADACVSSG GRSSCPAGSP
     RWFSQRLDLT AEDKMRVVQR KYMIYNYCTD TKRFPQGFPK ECRH
//