XTH34_POPPZ
ID XTH34_POPPZ Reviewed; 294 AA.
AC Q8GZD5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Xyloglucan endotransglucosylase protein 34 {ECO:0000305};
DE Short=XET protein 34 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12595718, ECO:0000269|PubMed:15020748, ECO:0000269|PubMed:15125664, ECO:0000269|PubMed:15804235, ECO:0000269|PubMed:16014999};
DE AltName: Full=PttXET16-34 {ECO:0000303|PubMed:17504814};
DE AltName: Full=PttXET16A {ECO:0000303|PubMed:12468728, ECO:0000303|PubMed:15020748, ECO:0000303|PubMed:15125664, ECO:0000303|PubMed:15804235};
DE AltName: Full=Xyloglucan endotransglucosylase protein 16A {ECO:0000305};
DE Short=XET protein 16A {ECO:0000305};
DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 34 {ECO:0000305};
DE Short=XTH protein 34 {ECO:0000305};
DE Flags: Precursor;
GN Name=XTH16-34 {ECO:0000303|PubMed:17504814};
GN Synonyms=XET16A {ECO:0000303|PubMed:12468728, ECO:0000303|PubMed:12595718,
GN ECO:0000303|PubMed:15020748, ECO:0000303|PubMed:15804235,
GN ECO:0000303|PubMed:16014999, ECO:0000303|PubMed:17504814,
GN ECO:0000312|EMBL:AAN87142.1};
OS Populus tremula x Populus tremuloides (Hybrid aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=47664 {ECO:0000312|EMBL:AAN87142.1};
RN [1] {ECO:0000312|EMBL:AAN87142.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHYLOGENETIC ANALYSIS.
RX PubMed=12468728; DOI=10.1105/tpc.007773;
RA Bourquin V., Nishikubo N., Abe H., Brumer H., Denman S., Eklund M.,
RA Christiernin M., Teeri T.T., Sundberg B., Mellerowicz E.J.;
RT "Xyloglucan endotransglycosylases have a function during the formation of
RT secondary cell walls of vascular tissues.";
RL Plant Cell 14:3073-3088(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND CRYSTALLIZATION.
RX PubMed=12595718; DOI=10.1107/s090744490202348x;
RA Johansson P., Denman S., Brumer H., Kallas A.M., Henriksson H.,
RA Bergfors T., Teeri T.T., Jones T.A.;
RT "Crystallization and preliminary X-ray analysis of a xyloglucan
RT endotransglycosylase from Populus tremula x tremuloides.";
RL Acta Crystallogr. D 59:535-537(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=15125664; DOI=10.1021/ja0316770;
RA Brumer H. III, Zhou Q., Baumann M.J., Carlsson K., Teeri T.T.;
RT "Activation of crystalline cellulose surfaces through the chemoenzymatic
RT modification of xyloglucan.";
RL J. Am. Chem. Soc. 126:5715-5721(2004).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16014999; DOI=10.1007/s12010-005-0006-4;
RA Bollok M., Henriksson H., Kallas A., Jahic M., Teeri T.T., Enfors S.O.;
RT "Production of poplar xyloglucan endotransglycosylase using the
RT methylotrophic yeast Pichia pastoris.";
RL Appl. Biochem. Biotechnol. 126:61-77(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION,
RP AND MUTAGENESIS OF ASN-115.
RX PubMed=15804235; DOI=10.1042/bj20041749;
RA Kallas A.M., Piens K., Denman S.E., Henriksson H., Faeldt J., Johansson P.,
RA Brumer H., Teeri T.T.;
RT "Enzymatic properties of native and deglycosylated hybrid aspen (Populus
RT tremulaxtremuloides) xyloglucan endotransglycosylase 16A expressed in
RT Pichia pastoris.";
RL Biochem. J. 390:105-113(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=17504814; DOI=10.1093/pcp/pcm055;
RA Nishikubo N., Awano T., Banasiak A., Bourquin V., Ibatullin F., Funada R.,
RA Brumer H., Teeri T.T., Hayashi T., Sundberg B., Mellerowicz E.J.;
RT "Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of
RT tension wood fibers in poplar--a glimpse into the mechanism of the
RT balancing act of trees.";
RL Plant Cell Physiol. 48:843-855(2007).
RN [7] {ECO:0007744|PDB:1UMZ, ECO:0007744|PDB:1UN1}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-294 AND IN COMPLEX WITH
RP XYLOGLUCAN NONASACCHARIDE, FUNCTION, CATALYTIC ACTIVITY, PTM, ACTIVE SITES,
RP GLYCOSYLATION AT ASN-115, DISULFIDE BONDS, REACTION MECHANISM OF
RP TRANSGLYCOSYLATION, AND 3D-STRUCTURE MODELING OF XYLOGLUCAN DONOR
RP SACCHARIDE.
RX PubMed=15020748; DOI=10.1105/tpc.020065;
RA Johansson P., Brumer H., Baumann M.J., Kallas A.M., Henriksson H.,
RA Denman S.E., Teeri T.T., Jones T.A.;
RT "Crystal structures of a poplar xyloglucan endotransglycosylase reveal
RT details of transglycosylation acceptor binding.";
RL Plant Cell 16:874-886(2004).
CC -!- FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves
CC and religates xyloglucan polymers (PubMed:12595718, PubMed:15020748,
CC PubMed:16014999, PubMed:15804235, PubMed:15125664). Does not catalyze
CC xyloglucan endohydrolysis (XEH) (PubMed:15804235). Involved in early
CC phases of secondary (S) cell wall formation in fibers of the xylem and
CC phloem vascular tissues of wood stems. May play a role in restructuring
CC primary cell walls, possibly creating and reinforcing the connections
CC between the primary and S cell wall layers (PubMed:12468728). Functions
CC in the gelatinous (G) layers of the tension wood fibers that are
CC involved in bending of the wood stems. May play a role in G fiber
CC shrinking by repairing broken xyloglucan cross-links between G and S2
CC cell wall layers via its XET activity to maintain connections between
CC the layers (PubMed:17504814). {ECO:0000269|PubMed:12468728,
CC ECO:0000269|PubMed:12595718, ECO:0000269|PubMed:15020748,
CC ECO:0000269|PubMed:15125664, ECO:0000269|PubMed:15804235,
CC ECO:0000269|PubMed:16014999, ECO:0000269|PubMed:17504814}.
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:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12595718,
CC ECO:0000269|PubMed:15020748, ECO:0000269|PubMed:15125664,
CC ECO:0000269|PubMed:15804235, ECO:0000269|PubMed:16014999};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for reduced xyloglucan-derived nonasaccharide as acceptor
CC substrate (at pH 5.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15804235};
CC Vmax=42.5 nmol/min/mg enzyme with reduced xyloglucan-derived
CC nonasaccharide as acceptor substrate (at pH 5.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:15804235};
CC pH dependence:
CC Optimum pH is approximately 5.5. Loses activity rapidly at pH 4-5.
CC {ECO:0000269|PubMed:15804235};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:15804235};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12468728,
CC ECO:0000269|PubMed:17504814}. Secreted, extracellular space, apoplast
CC {ECO:0000255|RuleBase:RU361120}. Cytoplasm
CC {ECO:0000269|PubMed:12468728}. Note=Localizes to the cytoplasm of
CC cambial cells. Localizes to the cytoplasm of xylem fibers in the early
CC stages of secondary cell wall formation. {ECO:0000269|PubMed:12468728}.
CC -!- TISSUE SPECIFICITY: Expressed in mature gelatinous (G) cell wall layer
CC of the tension wood fibers. Highly expressed in the outer zone of the G
CC layer close to the secondary S2 layer. Not expressed in the mature
CC walls of the ray cells or vessel elements (at protein level)
CC (PubMed:17504814). Highest expression in both the phloem/cambium and
CC differentiating xylem of the mature stem containing primarily secondary
CC cell wall forming cells, in root tips and young roots. Expressed at low
CC levels in apical bud (PubMed:12468728). {ECO:0000269|PubMed:12468728,
CC ECO:0000269|PubMed:17504814}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in cell walls of developing
CC fibers at the early secondary walled stage of both phloem/cambium and
CC xylem vascular tissues. Not expressed at later stages of secondary wall
CC formation. Expressed in the innermost secondary wall layers of the
CC developing phloem fibers. Expressed in the nacreous walls of developing
CC phloem sieve tubes in the secondary phloem, and more weakly in both
CC fusiform and ray initials of the cambium. Expression in expanding xylem
CC cells is weaker than in the cambium, and developing vessel elements
CC have weaker expression than expanding fibers (at protein level)
CC (PubMed:12468728). Expressed in developing gelatinous (G) cell wall
CC layer of the tension wood fibers (at protein level) (PubMed:17504814).
CC Transiently expressed in developing leaves (PubMed:12468728).
CC {ECO:0000269|PubMed:12468728, ECO:0000269|PubMed:17504814}.
CC -!- INDUCTION: Down-regulated in developing tension wood at the primary
CC walled stage. {ECO:0000269|PubMed:17504814}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000255|RuleBase:RU361120}.
CC -!- PTM: N-glycosylated. Contains N-acetylglucosamine and mannose
CC (PubMed:15804235, PubMed:15020748). Glycosylation is not essential for
CC its catalytic activity (PubMed:15804235). {ECO:0000269|PubMed:15020748,
CC ECO:0000269|PubMed:15804235}.
CC -!- BIOTECHNOLOGY: This enzyme is used in a developed method for activation
CC of cellulosic materials for industrial applications. Through its
CC transglycosylase activity, chemically modified xyloglucan
CC oligosaccharides are attached to xyloglucan, which has naturally high
CC affinity for cellulose. Then, the chemically modified xyloglucan is
CC adsorbed onto desired cellulosic surfaces. As a result, efficient
CC attachment of a variety of chemical modifications onto cellulose
CC surfaces is attained while the integrity and strength of the fiber is
CC maintained. {ECO:0000269|PubMed:15125664}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF515607; AAN87142.1; -; mRNA.
DR PDB; 1UMZ; X-ray; 1.80 A; A/B=23-294.
DR PDB; 1UN1; X-ray; 2.10 A; A/B=23-294.
DR PDBsum; 1UMZ; -.
DR PDBsum; 1UN1; -.
DR SMR; Q8GZD5; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR BRENDA; 2.4.1.207; 4980.
DR EvolutionaryTrace; Q8GZD5; -.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IDA: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 3D-structure; Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Cytoplasm; Disulfide bond; Glycoprotein; Glycosidase; Glycosyltransferase;
KW Hydrolase; Secreted; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT CHAIN 23..294
FT /note="Xyloglucan endotransglucosylase protein 34"
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT /id="PRO_5005144460"
FT DOMAIN 23..221
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098,
FT ECO:0000305"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064,
FT ECO:0000305|PubMed:15020748"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064,
FT ECO:0000305|PubMed:15020748"
FT BINDING 111
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT BINDING 124..126
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT BINDING 134..136
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT BINDING 200..201
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT BINDING 205
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT BINDING 280
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ"
FT SITE 109
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:15020748"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-2,
FT ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ,
FT ECO:0007744|PDB:1UN1"
FT DISULFID 229..238
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ, ECO:0007744|PDB:1UN1"
FT DISULFID 275..288
FT /evidence="ECO:0000269|PubMed:15020748,
FT ECO:0007744|PDB:1UMZ, ECO:0007744|PDB:1UN1"
FT MUTAGEN 115
FT /note="N->S: No effect on catalytic activity. No
FT significant differences in reaction kinetics compared to
FT wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:15804235"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1UMZ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:1UMZ"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 217..230
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1UMZ"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:1UMZ"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1UMZ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1UMZ"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:1UMZ"
SQ SEQUENCE 294 AA; 34218 MW; 168017205AF55A4D CRC64;
MAAAYPWTLF LGMLVMVSGT MGAALRKPVD VAFGRNYVPT WAFDHIKYFN GGNEIQLHLD
KYTGTGFQSK GSYLFGHFSM QMKLVPGDSA GTVTAFYLSS QNSEHDEIDF EFLGNRTGQP
YILQTNVFTG GKGDREQRIY LWFDPTKEFH YYSVLWNMYM IVFLVDDVPI RVFKNCKDLG
VKFPFNQPMK IYSSLWNADD WATRGGLEKT DWSKAPFIAS YRSFHIDGCE ASVEAKFCAT
QGARWWDQKE FQDLDAFQYR RLSWVRQKYT IYNYCTDRSR YPSMPPECKR DRDI
