ID   PELD_ASPNC              Reviewed;         373 AA.
AC   A2RBL2;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Probable pectin lyase D;
DE            Short=PLD;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelD; ORFNames=An19g00270;
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; AM270415; CAK47350.1; -; Genomic_DNA.
DR   RefSeq; XP_001402523.3; XM_001402486.3.
DR   AlphaFoldDB; A2RBL2; -.
DR   SMR; A2RBL2; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; A2RBL2; -.
DR   EnsemblFungi; CAK47350; CAK47350; An19g00270.
DR   GeneID; 4990385; -.
DR   KEGG; ang:ANI_1_30184; -.
DR   VEuPathDB; FungiDB:An19g00270; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 4ER.
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; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..373
FT                   /note="Probable pectin lyase D"
FT                   /id="PRO_5000221367"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        321..329
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  39024 MW;  5DFFE667E8A46D3F CRC64;
     MKYAAALTAV AALAARAAAV GVSGTPVGFA SSATGGGDAT PVYPTTTDEL VSYLGDDEAR
     VIVLSKTFDF TDTEGTTTTT GCAPWGTASG CQLAINKDDW CTNYEPDAPT TTVTYNTAGE
     LGITVNSNKS LIGEGTSGVI KGRGLRMVSG VSNIIIQNIA VTDINPEYVW GGDAITLDEA
     DLVWIDHVTT ARIGRQHYVL GTDADSRVSI TNNYINGESD YSATCDGHHY WNVYLDGSSD
     KVTFSGNYLY KTSGRAPKVQ DNTYLHIYNN YWENNSGHAF EIGSGGYVLA EGNYFSNVDT
     VLETDTFEGA LFSSDSASST CESYIGRSCV ANVNGGDLTG TSTTVLSNLS GDTLPSADAA
     STSPASNAGQ GNL