ID A0A067EYQ1_CITSI Unreviewed; 296 AA.
AC A0A067EYQ1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN ORFNames=CISIN_1g022492mg {ECO:0000313|EMBL:KDO60259.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO60259.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO60259.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK784933; KDO60259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067EYQ1; -.
DR STRING; 2711.A0A067EYQ1; -.
DR PaxDb; 2711-XP_006488017-1; -.
DR eggNOG; ENOG502QQC7; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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:SF146; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 31; 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:UP000027120};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361120};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT CHAIN 24..296
FT /note="Xyloglucan endotransglucosylase/hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT /id="PRO_5005103312"
FT DOMAIN 21..233
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
SQ SEQUENCE 296 AA; 33358 MW; 96AAE77CC2D9AB1D CRC64;
MASILYLLLP LLILMTISSV SNGQGPPSPG YYPSSRINSI GFDQAFRNLW GPQHQRVDQG
TLTVWLDSSS GSGFKSLHSY RSGYFGASIK LQPGYTAGVI TSLYLSNNQD HPGNHDEVDI
EFLGTIPGKP YTLQTNVYIR GSGDGRLIGR ELRFHLWFDP TQDFHHYAVL WSPSELIFFV
DDVPIRRYPR KSDATFPLRP MYLYGSIWDA SSWATEEGRY KADYKYQPFV GQYRNFKIAG
CTADGPSGCH PPPASPSGSG VLSQQQVAAM QWVQRNYLVY NYCYDPKRDH TEIPEC
//
