ID A0A1D6KMX1_MAIZE Unreviewed; 638 AA.
AC A0A1D6KMX1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=ZEAMMB73_Zm00001d031993 {ECO:0000313|EMBL:ONM04178.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM04178.1};
RN [1] {ECO:0000313|EMBL:ONM04178.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM04178.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM007647; ONM04178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6KMX1; -.
DR IntAct; A0A1D6KMX1; 17.
DR STRING; 4577.A0A1D6KMX1; -.
DR PaxDb; 4577-GRMZM2G154124_P01; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR InParanoid; A0A1D6KMX1; -.
DR OMA; PQFYLFN; -.
DR ExpressionAtlas; A0A1D6KMX1; baseline and differential.
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:SF1; 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|EMBL:ONM04178.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 357..428
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 443..632
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 638 AA; 72962 MW; D9A65D9A9851B211 CRC64;
MGDTLIRPSG RKPHAQVEIK NGIFDLTLSN PDGIVTGVRY NGVDNLMEIL NKEDNRGYWD
LVWNPPGQKT GIFDVIKGTE FRIVYQDENQ AEVSFTRNWD PSLEGKAVPL NIDKRFIVLR
GSSGFYTYGI YEHKEGWPDF GLGETRVAFK LRKDMFHYMA LADDRQRIMP MPDDRLPPRG
QPLAYPEAVL LVDPINPELR GEVDDKYQYS CEDQYNNVHG WMSFDPPIGF WQITPSDEFR
TGGPLKQNLT SHVGPTMLAM FLSAHYAGDD LSPKFTNGEY WKKVHGPVFM YLNSSWDASD
PTMLWEDAKV QMMIEKGNWP YCFALSEDFQ KTEQRGCVSG RLLVRDRYID DQDLYASGAY
VGLALPGEAG SWQRECKGYQ FWCRADVDGS FYIRNIVTGN YNLYAWVPGF LGDYKLDATV
TIASGDDIYL GDLVYEPPRD GPTMWEIGVP DRSAAEFYVP DPNPNYVNRL YVNHPADRFR
QYGLWERYAE LYPDSDLVYT VGQSDYSTDW FYAQVNRKID DNTYQPTTWQ IKFDLDSVSP
SSTYKFRVAL ASSALAELQI SFNDQDRAVP HFATGLIGRD NAIARHGIHG LYWLFNIDVA
SAWLVQGVNT IYLKQPRSQS PFQGLMYDYL RLEGPCGC
//