XTHA_PHAAN
ID XTHA_PHAAN Reviewed; 292 AA.
AC Q41638;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein A;
DE EC=2.4.1.207;
DE AltName: Full=VaXTH1;
DE Flags: Precursor;
GN Name=XTHA; Synonyms=EXT, XTH1;
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-50.
RC STRAIN=cv. Takara Wase;
RX PubMed=8244968; DOI=10.1016/s0021-9258(19)74400-7;
RA Okazawa K., Sato Y., Nakagawa T., Asada K., Kato I., Tomita E.,
RA Nishitani K.;
RT "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a
RT novel class of glycosyltransferase that mediates molecular grafting between
RT matrix polysaccharides in plant cell walls.";
RL J. Biol. Chem. 268:25364-25368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Takara Wase;
RX PubMed=12552143; DOI=10.1093/pcp/pcg002;
RA Nakamura T., Yokoyama R., Tomita E., Nishitani K.;
RT "Two azuki bean XTH genes, VaXTH1 and VaXTH2, with similar tissue-specific
RT expression profiles, are differently regulated by auxin.";
RL Plant Cell Physiol. 44:16-24(2003).
RN [3]
RP IDENTIFICATION, AND ENZYME ACTIVITY.
RC STRAIN=cv. Takara Wase;
RX PubMed=1400418; DOI=10.1016/s0021-9258(19)36797-3;
RA Nishitani K., Tominaga R.;
RT "Endo-xyloglucan transferase, a novel class of glycosyltransferase that
RT catalyzes transfer of a segment of xyloglucan molecule to another
RT xyloglucan molecule.";
RL J. Biol. Chem. 267:21058-21064(1992).
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.
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 Evidence={ECO:0000269|PubMed:1400418};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the phloem fibers of
CC growing internodes. Expressed in xylem cells in the basal part of the
CC internode. In the internode, it is expressed closer to the top of the
CC internode compared to XTHB. {ECO:0000269|PubMed:12552143}.
CC -!- INDUCTION: Up-regulated by indole-3-acetic acid (IAA) and fusicoccin.
CC Effect of IAA is however nullified in 0.25 M mannitol, which prevents
CC cell expansion without affecting auxin action per se.
CC {ECO:0000269|PubMed:12552143}.
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; D16458; BAA03925.1; -; mRNA.
DR EMBL; AB086395; BAC03237.1; -; Genomic_DNA.
DR PIR; A49539; A49539.
DR RefSeq; NP_001316764.1; NM_001329835.1.
DR AlphaFoldDB; Q41638; -.
DR SMR; Q41638; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 108344638; -.
DR KEGG; var:108344638; -.
DR OrthoDB; 1209387at2759; -.
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 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; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Secreted; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8244968"
FT CHAIN 21..292
FT /note="Xyloglucan endotransglucosylase/hydrolase protein A"
FT /id="PRO_0000011837"
FT DOMAIN 21..219
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 109
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 122..124
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 132..134
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 198..199
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 203
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 278
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 107
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 227..236
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 273..286
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 292 AA; 33882 MW; AFA721A5C3B440AA CRC64;
MGSSLWTCLI LLSLASASFA ANPRTPIDVP FGRNYVPTWA FDHIKYLNGG SEIQLHLDKY
TGTGFQSKGS YLFGHFSMYI KLVPGDSAGT VTAFYLSSTN AEHDEIDFEF LGNRTGQPYI
LQTNVFTGGK GDREQRIYLW FDPTTQYHRY SVLWNMYQIV FYVDDYPIRV FKNSNDLGVK
FPFNQPMKIY NSLWNADDWA TRGGLEKTDW SKAPFIASYK GFHIDGCEAS VNAKFCDTQG
KRWWDQPEFR DLDAAQWQKL AWVRNKYTIY NYCTDRKRYS QVPPECTRDR DI
