ID   PELE_ASPNG              Reviewed;         370 AA.
AC   B3GQR3;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Probable pectin lyase E;
DE            Short=PLE;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelE;
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;
RA   Schaap P.J., van der Aa J., Martens-Uzunova E.;
RT   "Assessment of the pectin degrading enzyme network of Aspergillus niger by
RT   functional genomics.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; EU719193; ACE00421.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3GQR3; -.
DR   SMR; B3GQR3; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   VEuPathDB; FungiDB:An11g04030; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1213151; -.
DR   VEuPathDB; FungiDB:ATCC64974_58860; -.
DR   VEuPathDB; FungiDB:M747DRAFT_314510; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0047490; F:pectin lyase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 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..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..370
FT                   /note="Probable pectin lyase E"
FT                   /id="PRO_0000394355"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..319
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  38815 MW;  DF705285374CB78C CRC64;
     MAFAHHAEAA QSSIVSGSAP GFAAGVTGGG DATPVYPTTI DELKEYLTSS SPQNIVIEGT
     FDFVGSEGTK TYQACNIYDC TPDNGGQAIL NTLGGCGDTS TYDVTIDVAG YQGINVASDK
     TLVGKGTGAV LNGKGLRFVG VSNIIIQNIE ITNLNPKYVW GGDALTFSDT NQIWIDHVTT
     SSLGRQHYSF GQESDNAITI SNSFINGKTD YSATCDGHTY WGLELVGSSD QITFYKNYVY
     YTSGRSPALS GNTLFHAVNS VWADNSGHAI EGTDNGMGLF EGNVFNNVPT IVQSGFVGQL
     FSSESANLSQ CETSLGRDCV TNAYTSSGSF SYDDDGFFVD FENLPIVSAA SASSIASTVP
     SDAGNTLSST