ID A0A0D3DVZ4_BRAOL Unreviewed; 675 AA.
AC A0A0D3DVZ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN Name=106309817 {ECO:0000313|EnsemblPlants:Bo8g100950.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g100950.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g100950.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo8g100950.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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}.
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DR RefSeq; XP_013602404.1; XM_013746950.1.
DR RefSeq; XP_013602405.1; XM_013746951.1.
DR AlphaFoldDB; A0A0D3DVZ4; -.
DR STRING; 109376.A0A0D3DVZ4; -.
DR EnsemblPlants; Bo8g100950.1; Bo8g100950.1; Bo8g100950.
DR GeneID; 106309817; -.
DR Gramene; Bo8g100950.1; Bo8g100950.1; Bo8g100950.
DR KEGG; boe:106309817; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_015099_1_0_1; -.
DR OMA; TESWPYD; -.
DR OrthoDB; 1215403at2759; -.
DR Proteomes; UP000032141; Chromosome C8.
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:SF6; 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:UP000032141};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..675
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002260623"
FT DOMAIN 396..467
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 481..669
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 675 AA; 77366 MW; 6CFB263F181BF202 CRC64;
MKLGAPRKKS GWVMLQVLLL HLLVQSVHSQ NSRNKLNITN PGQSIPGLAV QLKRVSNERV
VVDNGIIQVT FSSPQGLITG IKYNGIDNVL DDEIDDRGYW DVAWYEPEKA LEIDKLEGTK
FEIITQNEEQ VEISFTRTWT ISKRGSLVPL NVDKRYIIRT GVSGIYMYGI LERLEDWPDV
DMDQIRIVFK LNPKKFDFMA ISDDRQRSMP SMADRDNAKI LAYREAVLLT NPKNPMFKGE
VDDKYMYSME DKDNNVHGWI SSDPPVGFWM ITPSDEFRLG GPIKQDLTSH AGPITLSMFT
STHYAGKEMR MDYRNGEPWK KVFGPVLAYL NSVSPKDSTL RLWKDAKRQM AEEVRSWPYD
FVNSEDYPLS HQRGTIEGQF YIKDRYVSRL NIYGKFAFVG LAPCGEAGSW QTESKGYQFW
TKADRKGRFI IENVRAGNYS LYAWGYGFIG DYKYEQNITI TPGSQMNVGP IVYEPPRNGP
TLWEIGVPDR TAGEFYIPDP YPTLMNKLYV NPLQDRFRQY GLWDRYADLY PQNDLVYTVG
VSDYKRDWFF AHVTRNAGNN TYDSTTWQII FNLENVNRVG LYTLRIALAS AADSELQVRV
NNPKSDHIFT TGLIGKDNAI ARHGIHGLYR LYSINVAGDL LSVGDNTIYL TQSRSVGPFQ
GVMYDYIRLE SPFTT
//
