ID   PELF_ASPNG              Reviewed;         476 AA.
AC   Q8NJK6;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Probable pectin lyase F;
DE            Short=PLF;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF;
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;
RX   PubMed=12387863; DOI=10.1016/s0014-5793(02)03391-4;
RA   de Vries R.P., Jansen J., Aguilar G., Paenicova L., Joosten J.A.E.,
RA   Wulfert F., Visser J.;
RT   "Expression profiling of pectinolytic genes from Aspergillus niger.";
RL   FEBS Lett. 530:41-47(2002).
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; AJ489943; CAD34589.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJK6; -.
DR   SMR; Q8NJK6; -.
DR   STRING; 5061.CADANGAP00012161; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   VEuPathDB; FungiDB:An15g07160; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1164044; -.
DR   VEuPathDB; FungiDB:ATCC64974_27210; -.
DR   VEuPathDB; FungiDB:M747DRAFT_313795; -.
DR   eggNOG; ENOG502QXM6; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..476
FT                   /note="Probable pectin lyase F"
FT                   /id="PRO_0000394358"
FT   REGION          412..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..333
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  49455 MW;  A0E1FACEE1D8039A CRC64;
     MTLLRHLLTA TALLGASVQA AQGVTGSPFG FASGTTGGGD ATPAAPSDIS QLKTWLSDST
     PRVILIDKEF NFLGSEGKCT NCECCKPASN TCGSSGQNAV KQNGSDWCGS YPTLTCTYDN
     AGIEGLEVAS NKSIVGVGSS GVLRGKGLRL VNGVSNIIIQ NIHITELNPE FIWGGDAITL
     DGTNNVWIDH VKINLIGRQM FVAGYEASHS VTISNSEFDG ETSWSATCDG HHYWTVLGYG
     HNDKITFANN YIHHTSGRSP KLEFNSFWHA YNNYWYNNTG HAFDVGKNTR ALIEGNVMVQ
     VDTPLLADSN PGAVFAVNTS DVSTCTSTLG RTCVPNTLIS SGTLSGSDSS VISSWPSGES
     DVTVMAASKV ASYVKANAGI GKLGNGSGSS STVGAAATSA VAKRADSDDA PFVPAYSEAG
     PGASAVPTQP SWSWRTVTNG PAPTGAPSDS PSAPQGLGAP VQASNKHHHQ GHGRGY