ID   PELC_ASPNC              Reviewed;         373 AA.
AC   A2QW65;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Probable pectin lyase C;
DE            Short=PLC;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelC; ORFNames=An11g04030;
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. 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; AM270232; CAK48388.1; -; Genomic_DNA.
DR   RefSeq; XP_001394398.1; XM_001394361.1.
DR   AlphaFoldDB; A2QW65; -.
DR   SMR; A2QW65; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; A2QW65; -.
DR   EnsemblFungi; CAK48388; CAK48388; An11g04030.
DR   GeneID; 4984634; -.
DR   KEGG; ang:ANI_1_554094; -.
DR   VEuPathDB; FungiDB:An11g04030; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 7R.
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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..373
FT                   /note="Probable pectin lyase C"
FT                   /id="PRO_5000220580"
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   373 AA;  39359 MW;  A6AF9B110458D2F1 CRC64;
     MKVPFLQLLC LNAALASANV VKGAAQGFAA GVTGGGDITP SYPKTNEELV SLLESDEPQV
     VVLTKTFEFI GTEGTTTENG CAPWGTGKSC QLAINSNGWC GKNPVVTITY DNAAKNGIHI
     KSNKTLVGEG DKGVLSGKGL YFEGGVSNII VQNIKITNLN PGFVWGGDAF TFFGADLIWI
     DHCETSLTGR QHYVTGFHPN TRMTWSNNFL NGVTTHSAGC DDHHYWTMEL VGPGDQITFQ
     NNYVYHTTGR GPALSGTTLF HAVNSVWSSI PGHAIEGGDK GRGLFEGCFF EDVVEIAPAK
     PENQLFSASE ANAASCKSAL GRACQANSYS KSGAFGSSET GFFKDFAGLT IAPAGSATDA
     LAYVPKNCGI GRL