ID   XTH30_ARATH             Reviewed;         343 AA.
AC   Q38908; Q8LDA9; Q9FVR2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 30;
DE            Short=At-XTH30;
DE            Short=XTH-30;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH30; Synonyms=XTR4; OrderedLocusNames=At1g32170;
GN   ORFNames=F3C3.5;
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].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-343.
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   TISSUE SPECIFICITY.
RX   PubMed=11673616; DOI=10.1093/pcp/pce154;
RA   Yokoyama R., Nishitani K.;
RT   "A comprehensive expression analysis of all members of a gene family
RT   encoding cell-wall enzymes allowed us to predict cis-regulatory regions
RT   involved in cell-wall construction in specific organs of Arabidopsis.";
RL   Plant Cell Physiol. 42:1025-1033(2001).
RN   [7]
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: Predominantly expressed in green siliques.
CC       {ECO:0000269|PubMed:11673616}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast to group 1 and group 2
CC       endotransglucosylase/hydrolase proteins, it may not contain the ligase
CC       activity, and may catalyze endohydrolysis xyloglucan polymers only.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AC084165; AAG23439.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31443.1; -; Genomic_DNA.
DR   EMBL; AY062698; AAL32776.1; -; mRNA.
DR   EMBL; AY086104; AAM67311.1; -; mRNA.
DR   EMBL; U43486; AAB18365.1; -; mRNA.
DR   PIR; B86446; B86446.
DR   PIR; S71223; S71223.
DR   RefSeq; NP_174496.1; NM_102950.4.
DR   AlphaFoldDB; Q38908; -.
DR   SMR; Q38908; -.
DR   STRING; 3702.Q38908; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q38908; 1 site, No reported glycans.
DR   PaxDb; 3702-AT1G32170-1; -.
DR   ProteomicsDB; 242793; -.
DR   EnsemblPlants; AT1G32170.1; AT1G32170.1; AT1G32170.
DR   GeneID; 840109; -.
DR   Gramene; AT1G32170.1; AT1G32170.1; AT1G32170.
DR   KEGG; ath:AT1G32170; -.
DR   Araport; AT1G32170; -.
DR   TAIR; AT1G32170; XTH30.
DR   eggNOG; ENOG502QURN; Eukaryota.
DR   HOGENOM; CLU_048041_1_2_1; -.
DR   InParanoid; Q38908; -.
DR   OMA; NIAGKPW; -.
DR   OrthoDB; 337487at2759; -.
DR   PhylomeDB; Q38908; -.
DR   BioCyc; ARA:AT1G32170-MONOMER; -.
DR   BRENDA; 2.4.1.207; 399.
DR   PRO; PR:Q38908; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q38908; 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; 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:SF288; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 30-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; PS51762; GH16_2; 1.
DR   Genevisible; Q38908; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..343
FT                   /note="Probable xyloglucan endotransglucosylase/hydrolase
FT                   protein 30"
FT                   /id="PRO_0000011830"
FT   DOMAIN          24..224
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          306..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         113
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         126..128
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         136..140
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         203..204
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         208
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         285
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            111
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        280..293
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CONFLICT        202
FT                   /note="S -> F (in Ref. 4; AAM67311)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  39888 MW;  B4DD6A9CE8451CD2 CRC64;
     MSKSSYNHIF ILILCLCLRS SSAFTNLNTL SFEESLSPLF GDANLVRSPD DLSVRLLLDR
     YTGSGFISSN MYQHGFYSSM IKLPADYTAG VVVAFYTSNG DVFEKTHDEL DIEFLGNIKG
     KPWRFQTNLY GNGSTHRGRE ERYRLWFDPS KEFHRYSILW TPHKIIFWVD DVPIREVIRN
     DAMGADYPAK PMALYATIWD ASDWATSGGK YKANYKFAPF VAEFKSFSLD GCSVDPIQEV
     PMDCSDSVDF LESQDYSSIN SHQRAAMRRF RQRFMYYSYC YDTLRYPEPL PECVIVPAEK
     DRFKETGRLK FGGTEARERR RNRRQQRRPE IEIESDPDDR KLL
//