ID RGLA_ASPFC Reviewed; 528 AA.
AC B0YEH9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-MAY-2023, entry version 59.
DE RecName: Full=Probable rhamnogalacturonate lyase A;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglA; ORFNames=AFUB_099240;
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone
CC of pectin (By similarity). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
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DR EMBL; DS499603; EDP47323.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YEH9; -.
DR SMR; B0YEH9; -.
DR GlyCosmos; B0YEH9; 3 sites, No reported glycans.
DR EnsemblFungi; EDP47323; EDP47323; AFUB_099240.
DR VEuPathDB; FungiDB:AFUB_099240; -.
DR HOGENOM; CLU_037882_1_1_1; -.
DR PhylomeDB; B0YEH9; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
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: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; 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; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Lyase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..528
FT /note="Probable rhamnogalacturonate lyase A"
FT /id="PRO_0000394365"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..93
FT /evidence="ECO:0000250"
FT DISULFID 184..193
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 56736 MW; E0B22BB3995084E4 CRC64;
MLSKATLLLF LPSWARVTYA AFGITTTSSS YVIDANSPNP LKFTVNRSNC DITSINFYGA
ELQYQGTGSH IGSGLGSASV SATQSGDYIK VTCSTSTLTH YFVVHNGDPI IHMATYITAE
PSIGELRFIA RLNNELLPNE EPFGEVSNTS GGTAIEGSDV FLVNGQTRSK FYSSERFIDD
HRHCVSGSAH RVCMILNQYE SSSGGPFHRD INTNNGGQYN ALYWYMNSGH VQTEANRMGL
HGPYSMYFSR SGTPGTNIDT SFFANLDIQG YVPDSARGKV SGKASGADST FKWVVHWYND
EAQYWTYTAS DGSFTSPAMK PGTYTMVYYQ GEYKVASTSV SVSAGSTTTK NISGSVTTGK
TIFKIGEWDG QPTGFRNAAN QLRMHPSDSR MSSWGPLTYT VGSSSLSDFP MAIFKSVNSP
VTIKFTASSS QTGAATLRIG TTLSFAGGRP QVTVNSWTGP IPSAPKDLNS RGVTRGAYRG
LGEVYDVAIP AGTIVAGTNT ITISVVSGSS GDAFLSPNFI FDCVELFQ
//
