ID A0A3R7JF49_9EURO Unreviewed; 528 AA.
AC A0A3R7JF49;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=Rhamnogalacturonate lyase {ECO:0000256|PIRNR:PIRNR011794};
DE EC=4.2.2.23 {ECO:0000256|PIRNR:PIRNR011794};
GN ORFNames=CFD26_104473 {ECO:0000313|EMBL:RLL96452.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL96452.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL96452.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL96452.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL96452.1}.
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DR EMBL; NIDN02000110; RLL96452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7JF49; -.
DR STRING; 1245748.A0A3R7JF49; -.
DR Proteomes; UP000215289; 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 Reference proteome {ECO:0000313|Proteomes:UP000215289};
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_5018384194"
FT DOMAIN 22..270
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 276..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; 56461 MW; 0CFE340B6CBC0F46 CRC64;
MLLKAALFLS LPFWARVANA AFGITTSSSS YVIDANSPNP LTFTVSRSSC DITSINFYGS
ELQYQSTGSH IGSGLGSATV SATQDGDYIK VTCVTNTLTQ YFVVHNGDPI IHMATYITAE
PSIGELRFIA RLNNALLPNE EPFGDVSNTA GGTAIEGSDV FLVNGQTRSK FYSSQRFIDD
QRHCVSGSAH RVCMILNQYE SSSGGPFHRD INSNNGGSYN ALYWYMNSGH VQTESYRMGL
HGPYSMYFSR SGTPSTNIDT SFFANLGIQG YVPASGRGTV TGKASGADSQ FKWVVHWYND
AAQYWTYTAS DGSFTSPAMK PGTYTMVYYQ GEYKVASTSV SVSAGSTTTK NISGSVQTGS
TIFKIGQWDG QPTGFRNAAN QLRMHPSDSR MANWGPLTYT VGSSSLSDFP MAIFKSVNNP
VTISFTASSS QTGAATLRIG TTLSFAGGRP QAKVNSWTGP IPSAPTNLNS RGVTRGAYRG
LGEVYDVSIP AGTIVAGTNT ITISVVSGSS GDAFLSPNFI FDCVELFQ
//
