ID   PLYD_ASPFC              Reviewed;         242 AA.
AC   B0YB89;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Probable pectate lyase D;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=plyD; ORFNames=AFUB_091960;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Pectinolytic enzyme 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. Favors pectate, the
CC       anion, over pectin, the methyl ester (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; DS499601; EDP48479.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YB89; -.
DR   SMR; B0YB89; -.
DR   EnsemblFungi; EDP48479; EDP48479; AFUB_091960.
DR   VEuPathDB; FungiDB:AFUB_091960; -.
DR   HOGENOM; CLU_044863_3_0_1; -.
DR   PhylomeDB; B0YB89; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR33407; PTHR33407; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Glycoprotein; Lyase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..242
FT                   /note="Probable pectate lyase D"
FT                   /id="PRO_0000394575"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  25397 MW;  61D7094F2D80D740 CRC64;
     MYQKSLLFSL LASSALAAQF PIPDSKGSVT FDEPYEIAAG ETYDGGYKTY GRGVSCTGQS
     EGGQDDTVFI VQEGGTLKNA IIGSDQIEGV YCLGACTIEN VWWEAVCEDA LSLKGGSGPY
     NIIGGGAQGA DDKVIQHNSG GQVNIDGFTV YDFGKLYRSC GNCDEQYART VTIKNVVANS
     GKTLVGINSN LGDTASIDSS TCATDVKKIC VEYKGNDTGA EPEEISEGPS DACQYSEPLS
     SC