XTHB_PHAAN
ID XTHB_PHAAN Reviewed; 293 AA.
AC Q8LNZ5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein B;
DE EC=2.4.1.207;
DE AltName: Full=VaXTH2;
DE Flags: Precursor;
GN Name=XTHB; Synonyms=XTH2;
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 [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).
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 the phloem fibers of
CC growing internodes. Weakly or not expressed in the xylem. In the
CC internode, it is expressed closer to the bottom of the internode
CC compared to XTHA. {ECO:0000269|PubMed:12552143}.
CC -!- INDUCTION: Up-regulated by indole-3-acetic acid (IAA). Effect of IAA is
CC not affected by mannitol. Not up-regulated by fusicoccin.
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; AB086396; BAC03238.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8LNZ5; -.
DR SMR; Q8LNZ5; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
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 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..293
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein B"
FT /id="PRO_0000011838"
FT DOMAIN 23..220
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 110
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 123..125
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 133..135
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 199..200
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 204
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 279
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..237
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 274..287
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 293 AA; 34096 MW; BD2FA9A049211CD5 CRC64;
MASSLLILCL VLVSLASSAL CAAPRRPVDV PFGRNYIPTW AFDHIKYFNG GSEIQLHLDK
YTGTGFQTKG SYLFGHFSMN IKMVPGDSAG TVTAFCLSSQ NAEHDEIDFE FLGNRTGQPY
ILQTNVFTGG KGDREQRIYL WFDPTKAYHR YSVLWNMYQI VFLVDNIPIR VFKNLKELGV
KFPFNQPMKV YNSLWNADDW ATRGGLEKTD WSKAPFVAEY KGFHVDGCEA SVNSRFCATQ
GKRWWDQTEF RDLDSFQWRR LKWVRQKFTI YNYCTDRTRY PQLPPECRRN RDI
