RGLA_ASPFN
ID RGLA_ASPFN Reviewed; 528 AA.
AC B8NCU7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable rhamnogalacturonate lyase A;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglA; ORFNames=AFLA_041820;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963476; EED52480.1; -; Genomic_DNA.
DR RefSeq; XP_002377644.1; XM_002377603.1.
DR AlphaFoldDB; B8NCU7; -.
DR SMR; B8NCU7; -.
DR STRING; 5059.CADAFLAP00005509; -.
DR EnsemblFungi; EED52480; EED52480; AFLA_041820.
DR VEuPathDB; FungiDB:AFLA_041820; -.
DR eggNOG; ENOG502QTKY; Eukaryota.
DR HOGENOM; CLU_037882_1_1_1; -.
DR OMA; DYIKVTC; -.
DR Proteomes; UP000001875; 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; cd10316; RGL4_M; 1.
DR Gene3D; 2.70.98.10; -; 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; PTHR36574; 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; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW 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_0000394366"
FT DISULFID 50..93
FT /evidence="ECO:0000250"
FT DISULFID 184..193
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 56958 MW; 92AB2500E2CAAE20 CRC64;
MLSRTILFST SFLWVRVANA AFGITTSDDS YVIDAGSANS LKFTVSRSSC DITSINYYGS
ELQYSGTGSH IGSGLGSADV SAVEDGDYIK VTCDTDTLTQ YFVVHNGDSV IHMATYTTEE
PSVGELRFIA RLNSELLPNE EPFGDVSTTS GGEAIEGSDV FLVDGETRSK FYSSQRFIDD
QRHCVAGDAH RVCMILNQYE TSSGGPFFRD INSNNGGSYN SLYWYMNSGH VQTEDRRQGL
HGPYSMYFSR SGTPSTDIDT SFFANLDIKG YVAADGRGTV SGTASGADSS FKWVVHWYNA
DAQYWTYTSS DGSFTSPAMK PGDYTMVYYQ GEYKVAETSV SVTAGSSTSK DISGFVETGD
TIFKIGDWDG TPTGFRNAEN QLRMHPSDSR MSSWGPLTYT VGSSELTDFP MAAFKGVNDP
VTIKFTATSA QTGAATLRIG TTLSFAGGRP QATINDYEGS APSAPTNLNS RGVTRGAYRG
LGEVYDVNIP SGTIVEGENT ITISVISGSS GDEFLAPNFI FDCVELFQ