ID   PELD_ASPNG              Reviewed;         373 AA.
AC   P22864;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Pectin lyase D;
DE            Short=PLD;
DE            EC=4.2.2.10;
DE   AltName: Full=Pectin lyase I;
DE            Short=PLI;
DE   Flags: Precursor;
GN   Name=pelD;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-30 AND
RP   148-167.
RC   STRAIN=N756;
RX   PubMed=2373363; DOI=10.1016/0378-1119(90)90211-9;
RA   Gysler C., Harmsen J.A.M., Kester H.C.M., Visser J., Heim J.;
RT   "Isolation and structure of the pectin lyase D-encoding gene from
RT   Aspergillus niger.";
RL   Gene 89:101-108(1990).
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:0000305}.
CC   -!- PTM: May be O-glycosylated; does not contain N-acetylglucosamine.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; M55657; AAA32701.1; -; Genomic_DNA.
DR   PIR; JH0155; JH0155.
DR   AlphaFoldDB; P22864; -.
DR   SMR; P22864; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   GlyCosmos; P22864; 3 sites, No reported glycans.
DR   VEuPathDB; FungiDB:An19g00270; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1136270; -.
DR   VEuPathDB; FungiDB:ATCC64974_62770; -.
DR   VEuPathDB; FungiDB:M747DRAFT_273902; -.
DR   eggNOG; ENOG502QXM6; Eukaryota.
DR   BioCyc; MetaCyc:MONOMER-20552; -.
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; IEA:UniProtKB-EC.
DR   FunFam; 2.160.20.10:FF:000003; Pectin lyase F; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; PECTATE LYASE 18-RELATED; 1.
DR   PANTHER; PTHR31683:SF16; PECTIN LYASE A-RELATED; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lyase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:2373363"
FT   CHAIN           20..373
FT                   /note="Pectin lyase D"
FT                   /id="PRO_0000024898"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..366
FT                   /note="Low complexity"
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"
FT   CONFLICT        27
FT                   /note="V -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   373 AA;  39038 MW;  B758DCCEFFE2345C CRC64;
     MKYAAALTAI 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
//