ID A0A0D2RK89_GOSRA Unreviewed; 249 AA.
AC A0A0D2RK89;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN ORFNames=B456_008G223600 {ECO:0000313|EMBL:KJB51588.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB51588.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB51588.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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 {ECO:0000256|RuleBase:RU361120}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space,
CC apoplast {ECO:0000256|RuleBase:RU361120}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000256|RuleBase:RU361120}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|RuleBase:RU361120}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001747; KJB51588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2RK89; -.
DR EnsemblPlants; KJB51588; KJB51588; B456_008G223600.
DR Gramene; KJB51588; KJB51588; B456_008G223600.
DR Proteomes; UP000032304; Chromosome 8.
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: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 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.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361120};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU361120};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|RuleBase:RU361120};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361120};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT DOMAIN 1..131
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 220..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
SQ SEQUENCE 249 AA; 29404 MW; BBE275CCF4E94FE4 CRC64;
MMQASNGDVF EKNHDELDIE FLGNVEGKPW RFQTNLYGNG STSRGREERY RLWFDPSKEF
HRYSILWTAK NIIFYVDEVP IREVVRSDEM GGDYPTKPMS IYATIWDASS WATNGGKIKV
NYDYAPFTAD FKELVLEGCP MDPIQEYPDF TTCKEKDAWL ETRNFAVLTP KRRSAMRKFR
QHYMYYSCCY DVWRYPVKLP DCVIDPIEKA RFNETGRLRF SGSHKKQAKI AKARRKKKQR
AASKERTEM
//
