ID   RGLA_ASPNG              Reviewed;         499 AA.
AC   Q8NJK5;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Rhamnogalacturonate lyase A;
DE            EC=4.2.2.23;
DE   Flags: Precursor; Fragment;
GN   Name=rglA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=12387863; DOI=10.1016/s0014-5793(02)03391-4;
RA   de Vries R.P., Jansen J., Aguilar G., Paenicova L., Joosten J.A.E.,
RA   Wulfert F., Visser J.;
RT   "Expression profiling of pectinolytic genes from Aspergillus niger.";
RL   FEBS Lett. 530:41-47(2002).
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; AJ489944; CAD36194.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJK5; -.
DR   SMR; Q8NJK5; -.
DR   STRING; 5061.CADANGAP00010833; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   VEuPathDB; FungiDB:An14g01130; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1115401; -.
DR   VEuPathDB; FungiDB:ATCC64974_1090; -.
DR   VEuPathDB; FungiDB:M747DRAFT_271668; -.
DR   eggNOG; ENOG502QTKY; Eukaryota.
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..499
FT                   /note="Rhamnogalacturonate lyase A"
FT                   /id="PRO_0000394368"
FT   DISULFID        49..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..192
FT                   /evidence="ECO:0000250"
FT   NON_TER         499
SQ   SEQUENCE   499 AA;  53915 MW;  0CBD6E4A4EFB0D1E CRC64;
     MLSKTSLLSL LSLAAGVVNA DFGITTSDSY VINANSPNSL VFTVDRGSCD ITSIVHYGTE
     LQYSGKGSHI GSGLGTATVS ATKSGDYIKV TCETDTLTQY MGVHDGDRII HMATYITEEP
     SIGELRFIAR LNSDVLPNEE PFGDVSNTAD GEPIEGSDVF LVDGETRSKF YSSQRFIDDQ
     RHCIAGDEHR VCMILNQYET SSGGPFHRDI NSNNGGDYNS LYWYMNSGHV QLESYRMGLH
     GPYSMYFSRS GTPSTDIDTS FFADLDIEGY VAESGRGTVS GTASGADSSF DWVVHWYNDD
     AQYWTYTSSS GSFTSPAMKP GTYTMVYYQG EYVVATSEVT VSAGSSTSKD ISGSVETGTT
     IFKIGDWDGQ PTGFRNAENQ LRMHPSDSRM SDWGPLTYTV GSSSLTDFPM AIFKSVNSPV
     TIKFTATSDQ TGAATLRIRT TLSFAGGRPQ ATINDYEGSA PSAPTNLDSR GVTRGAYRGY
     GDVYDVSVPE GTIVEGENT