ID G4TU87_SERID Unreviewed; 593 AA.
AC G4TU87;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=PIIN_08850 {ECO:0000313|EMBL:CCA74880.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA74880.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA74880.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA74880.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA74880.1}.
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DR EMBL; CAFZ01000367; CCA74880.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TU87; -.
DR STRING; 1109443.G4TU87; -.
DR eggNOG; ENOG502QTKY; Eukaryota.
DR HOGENOM; CLU_037882_1_1_1; -.
DR InParanoid; G4TU87; -.
DR OMA; FKIGDWD; -.
DR OrthoDB; 66666at2759; -.
DR Proteomes; UP000007148; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10317; RGL4_C; 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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; IPR016590; Rhamnogalacturonase_B.
DR InterPro; IPR015364; RhgB_N.
DR PANTHER; PTHR36574; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..593
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469434"
FT DOMAIN 557..592
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 529..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 62723 MW; 3FB3D1A6FC791923 CRC64;
MRLALLLSVC AVRTAYAAFG YSSSGSTITV DAGSSNSLIF KVNSNTCDIT SLVYRGAEYQ
YQSTYSHIGS GLGSASVSAT QSGSYIKVTC VTSTLTHYYV VKSGDSTIYM ATYITAEPSI
GELRYIARLN RSLLPNGIQG SYTDLTSSTV EGSDVFRASD GKTYSKFYSS VRHIDDQVHS
VSGNDVVISM VIPNPTSYES SSGGPFHRDI NSDRGAAYHA LYFYMNSGHA QTESYRMGLH
GPYAMVFSRS GLPSKSLDVS FFGSLGIQGW VGASGRGTVS GSVSGVSSSY QRVVHWYNNN
AQYWAYASSS GSFTSPPMKA GTYTMKLYRD EFEVASQTVS VGAGASVTSN IASQEAAISP
LWSIGELDGQ PDGFQNADLQ QHMHPSDVRM STWNAKTYIV GSTALSGFPM AQIKDYNNPT
TIKFTLTSAQ TGAATLRIAT SLSYAGGRPQ ATVNGWVGPV PGAPTDLNSR GFTRGTYRGF
NIMYTVNIPA GTLKAGENTI LINVISGSTS TGFLSPSFVY DSVQLITSGS SSGTSSTSTT
RASSSSSTRP TSTTASGGAP LYGQCGGANW TGPMTCASGT CTYSNEWYSQ CLP
//
