ID   PELA_ASPNC              Reviewed;         379 AA.
AC   A2R3I1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable pectin lyase A;
DE            Short=PLA;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA; ORFNames=An14g04370;
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; AM270321; CAK48529.1; -; Genomic_DNA.
DR   RefSeq; XP_001401061.1; XM_001401024.2.
DR   AlphaFoldDB; A2R3I1; -.
DR   SMR; A2R3I1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; A2R3I1; -.
DR   EnsemblFungi; CAK48529; CAK48529; An14g04370.
DR   GeneID; 4987294; -.
DR   KEGG; ang:ANI_1_624124; -.
DR   VEuPathDB; FungiDB:An14g04370; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 1R.
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; IDA:AspGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:AspGD.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..379
FT                   /note="Probable pectin lyase A"
FT                   /id="PRO_5000220959"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  39784 MW;  F0CE263CFC7577BB CRC64;
     MKYSTIFSAA AAVFAGSAAA VGVSGSAEGF AEGVTGGGDA TPVYPDTIDE LVSYLGDDEA
     RVIVLTKTFD FTDSEGTTTG TGCAPWGTAS ACQVAIDQDD WCENYEPDAP SISVEYYNAG
     VLGITVTSNK SLIGEGSSGA IKGKGLRIVS GAENIIIQNI AVTDINPKYV WGGDAITLDD
     CDLVWIDHVT TARIGRQHYV LGTSADNRVS LTNNYIDGVS DYSATCDGYH YWGIYLDGDA
     DLVTMKGNYI YHTSGRSPKV QDNTLLHCVN NYFYDISGHA FEIGEGGYVL AEGNVFQNVD
     TVLETYEGAA FTVPSTTAGE VCSTYLGRDC VINGFGSSGT FSEDSTSFLS DFEGKNIASA
     SAYTSVASSV VANAGQGNL