ID A0A317VU79_ASPEC Unreviewed; 528 AA.
AC A0A317VU79;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=Rhamnogalacturonate lyase {ECO:0000256|PIRNR:PIRNR011794};
DE EC=4.2.2.23 {ECO:0000256|PIRNR:PIRNR011794};
GN ORFNames=BO83DRAFT_462025 {ECO:0000313|EMBL:PWY77896.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY77896.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY77896.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY77896.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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 ECO:0000256|PIRNR:PIRNR011794};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR011794}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418, ECO:0000256|PIRNR:PIRNR011794}.
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:PWY77896.1}.
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DR EMBL; MSFU01000007; PWY77896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VU79; -.
DR VEuPathDB; FungiDB:BO83DRAFT_462025; -.
DR OrthoDB; 66666at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 1.
DR PIRSF; PIRSF011794; Rhamnogalacturonase_B; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR011794-1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR011794};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR011794};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR011794}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT CHAIN 21..528
FT /note="Rhamnogalacturonate lyase"
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT /id="PRO_5016196008"
FT DOMAIN 22..270
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 277..349
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 361..526
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
FT DISULFID 50..93
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
FT DISULFID 184..193
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
SQ SEQUENCE 528 AA; 57097 MW; B30BBE78DACEEB43 CRC64;
MLSRTSLLSL LSLAAGVVNA DFGITTNDDS YVINANSPNS LVFTVDRGSC DITSIVHYGT
ELQYSGKGSH IGSGLGTATV SAAKSGDYIK VTCETDTLTQ YMVVHDGDPI IHMATYIMEE
PSIGELRFIA RLNPDELPNE EPFGDVSNTA DGEAIEGSDV FLVDGETRSK FYSSQRFIDD
QRHCIAGDEH RVCMILNQYE TSSGGPFHRD INSNNGGDYN SLYWYMNSGH VQTESYRMGL
HGPYSMYFSR SGTPSTDIET SFFADLDIEG YVAEADRGTV SGTASGADSS FDWVVHWYND
DAQYWTYTSS SGSFTSPAMK PGTYTMVYYQ GEYVVATSEV TVSAGSSTTK NISGSVKTGT
TIFKIGDWDG QPTGFRNAEN QLRMHPSDSR MSDWGPLTYT VGSSSLTDFP MAVFKAVNNP
VTIKFTATSD QTGAATLRIG TTLSFAGGRP QATINDYEGS APSAPTNLNS RGVTRGAYRG
YGEVYDVSVP EGTIVEGENT ITISVISGSS GDEFLSPNFI FDCVELFQ
//
