ID A0A0A0LGY0_CUCSA Unreviewed; 642 AA.
AC A0A0A0LGY0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=Csa_3G892750 {ECO:0000313|EMBL:KGN60274.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN60274.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN60274.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000256|ARBA:ARBA00001324};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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; CM002924; KGN60274.1; -; Genomic_DNA.
DR RefSeq; XP_004136251.1; XM_004136203.2.
DR AlphaFoldDB; A0A0A0LGY0; -.
DR STRING; 3659.A0A0A0LGY0; -.
DR EnsemblPlants; KGN60274; KGN60274; Csa_3G892750.
DR GeneID; 101204193; -.
DR Gramene; KGN60274; KGN60274; Csa_3G892750.
DR KEGG; csv:101204193; -.
DR eggNOG; ENOG502QQ8E; Eukaryota.
DR OMA; LEEPCLA; -.
DR OrthoDB; 1215403at2759; -.
DR Proteomes; UP000029981; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR CDD; cd10317; RGL4_C; 1.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR InterPro; IPR010325; Rhamnogal_lyase.
DR PANTHER; PTHR32018:SF16; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF06045; Rhamnogal_lyase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 355..425
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 440..629
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 642 AA; 73432 MW; 4FB0C2EE04DB15C5 CRC64;
MANEILQLDI QDHHVVMDNG ILQVTLSKPD GNVTGIKYNS IDNVLEVDDK EAHRGYWDLV
WNSGTPGTTG TFDEMRGREF EVMVQNEEQI ELSFKRNYSF KDKAVPLNID KRFIMLRNSS
GFYSYAIYEH MREWPPFNLP QTRIVFKLRK DKFHYMAIAD DRQRFMPLPE DRLRHRGKPL
DFPEAVLLVN PKEPEFKGEV DDKYQYSCEN KDLKVHGWIS MDPPVGFWQI TPSSEFRSGG
PLKQNLTSHV GPYALAMFLS AHYSGEDLVL KVSPDEPWKK VFGPVFFYLN SVSDGGDPLS
LWEDAKTQMS KEVQSWPYSF PASEDFPPPN QRGRLTGKLF VLDRYVNEEK MPATDAYVGL
AAPGDVGSWQ TEKKGYQFWT KTDADGSFSI EHVRIGDYNL YAWVPGFIGD YRYDVLINVS
SGSDMDVGDL VYEPPRNGPT LWEIGIPDRS AAEFYIPDPD PKYINKLYIN HPDRFRQYGL
WEKYAELHPD ADLVYSVGVS DYTKDWFFAH VNRKRNDGSH LATTWEIKFR LDNIIDKGVS
YTLRVALATA NVAELQIQVN NPEAKPSLFT TGVIGHDNAI ARHGIHGLYR LYSVDILGSL
LVEGENTIFL SQIINNSSFN GIMYDYIRLE GPPSDLIPLN NS
//
