ID   PELC_ASPNG              Reviewed;         378 AA.
AC   Q5MBK3;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Probable pectin lyase C;
DE            Short=PLC;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelC;
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   Kusters-van Someren M.A., Visser J.;
RT   "Structure of a fourth Aspergillus niger pectin lyase gene, pelC, and a
RT   sequence comparison with other pectin and pectate lyases.";
RL   Submitted (NOV-2004) 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; AY839647; AAW03313.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5MBK3; -.
DR   SMR; Q5MBK3; -.
DR   STRING; 5061.CADANGAP00008580; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   VEuPathDB; FungiDB:An11g04030; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1154296; -.
DR   VEuPathDB; FungiDB:ATCC64974_90160; -.
DR   VEuPathDB; FungiDB:M747DRAFT_314510; -.
DR   eggNOG; ENOG502SIPU; Eukaryota.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..378
FT                   /note="Probable pectin lyase C"
FT                   /id="PRO_0000394349"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..220
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..324
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  39822 MW;  D8F2C23A27A6E30A CRC64;
     MKVPFLQLLC LNAALASANV VQGAAQGFAA GVTGGGDITP SYPKTNEELV SLLESDEPQV
     VVLTKTFDFI GTEGTTTEDG CAPWGTGKSC QLAINSNGWC GKNPVVTITY DNAAKNGIHI
     KSNKTLVGEG DKGVLSGKGL YFEGGVSNII VQNIKITNLN PGFVWGGDAF TFFGADLIWI
     DHCETSLTGR QHYVTGFHPN TRMTWSNNFL NGVTTHSAGC DDHHYWTMEL VGPGDEITFQ
     NNYVYHTTGR GPALSGTTLF HAVNSVWSSI PGHAIEGGDK GRGLFEGCFF EDVVEIAPAK
     PENQLFSASE ANAASCKSAL GRACQANGYS KSGAFGSSET GFFKDFAGLT IAPAGSATDA
     LAYVPKNCGI GRLESCDA