ID A0A1S3U7D9_VIGRR Unreviewed; 636 AA.
AC A0A1S3U7D9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN Name=LOC106762503 {ECO:0000313|RefSeq:XP_022636472.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022636472.1};
RN [1] {ECO:0000313|RefSeq:XP_022636472.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022636472.1};
RG RefSeq;
RL Submitted (NOV-2023) 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_014501948.1; XM_014646462.1.
DR RefSeq; XP_014501949.1; XM_014646463.1.
DR RefSeq; XP_022636472.1; XM_022780751.1.
DR AlphaFoldDB; A0A1S3U7D9; -.
DR Proteomes; UP000087766; Chromosome 5.
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:SF8; 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, ECO:0000313|RefSeq:XP_022636472.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 354..426
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 440..628
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 636 AA; 72409 MW; AB666A5FD33897B3 CRC64;
MSGPGVRLHI QDHHVVMDNG IVQVTLSNPG GIVTGIRYNG VDNLLEVLNK ESNRGYWDLV
WSAPGSKGIF DVIQGTCFKV IVQNEEQVEL SFTRMWDPSL EGKFVPLNID KRFIMLRGSS
GFYSYGIYEH LNGWPDFDLG ETRITFKLRK DKFQYMAMAD NRRRILPYPE DRLPGRCQTL
GFAEAVLLTN PKDPQLQGEV DDKYHYSCAN KDNQVHGWIS FSPPVGFWQI TPSDEFRSGG
PLKQNLTSHV GPTTLAMFLS SHYAGQDLVP KIRGGESWKK VFGPVYIYLN SAPVGDDPLW
LWEDAKIQMM NEVQSWPYHF PASEDFLKSD QRGNVSGRLL VLDKYICTDL ISANGAYVGL
APPGDAGSWQ RECKDYQFWT RADENGFFTI RNVRPGDYNL FAWVPGFVGD YKFVDSMKIT
PGSYTELGEL VYEPPRDGPT LWEIGIPDRS AAEFYAPDPN PQYINRLFIN HPDRFRQYGL
WERYTELYPD ADLVYTVGVS DYTKDWFYAQ APRKKEDNTL EGTTWQIKFE VRSVVKGSTY
KLRVAIASAT LAELQIRVND PNTARPLFTT GLIGRDNSIA RHGIHGIYWF YNVNIPGSLL
IDGTNTIYFT QPRCTSPFQG IMYDYIRLEG PPCEGI
//
