ID   RGLA_ASPNC              Reviewed;         531 AA.
AC   A2R2L1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable rhamnogalacturonate lyase A;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglA; ORFNames=An14g01130;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK46452.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM270312; CAK46452.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2R2L1; -.
DR   SMR; A2R2L1; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   PaxDb; A2R2L1; -.
DR   EnsemblFungi; CAK46452; CAK46452; An14g01130.
DR   Proteomes; UP000006706; Chromosome 1R.
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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..531
FT                   /note="Probable rhamnogalacturonate lyase A"
FT                   /id="PRO_5000220898"
FT   DISULFID        50..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..193
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  57138 MW;  B9FAC68AAE5D74CF CRC64;
     MLSKTSLLSL LSLAAGVVNA DFGITTNDDS YVINANSPNS LVFTVDRGSC DITSIVHYGT
     ELQYSGKGSH IGSGLGTATV SATKSGDYIK VTCETDTLTQ YMVVHDGDPI IHMATYITEE
     PSIGELRFIA RLNSDVLPNE EPFGDVSNTA DGEAIEGSDV FLVDGETRSK FYSSQRFIDD
     QRHCIAGDEH RVCMILNQYE TSSGGPFHRD INSNNGGDYN SLYWYMNSGH VQLESYRMGL
     HGPYSMYFSR SGTPSTDIDT SFFADLDIEG YVAESGRGTV SGTASGADSS FDWVVHWYND
     DAQYWTYTSS SGSFTSPAMK PGTYTMVYYQ GEYVVATSEV TVSAGSSTSK DISGSVETGT
     TIFKIGDWDG QPTGFRNAEN QLRMHPSDSR MSDWGPLTYT VGSSSLTDFP MAIFKSVNSP
     VTIKFTATSD QTGAATLRIG TTLSFAGGRP QATINDYEGS APSAPTNLDS RGVTRGAYRG
     YGDVYDVSVP EGTIVEGENT ITISVISGSS GDDFLSPNFL DAVFIIALVD N