ID   PLYF_ASPFC              Reviewed;         234 AA.
AC   B0Y953;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Probable pectate lyase F;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=plyF; ORFNames=AFUB_079680;
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; DS499599; EDP49934.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y953; -.
DR   SMR; B0Y953; -.
DR   EnsemblFungi; EDP49934; EDP49934; AFUB_079680.
DR   VEuPathDB; FungiDB:AFUB_079680; -.
DR   HOGENOM; CLU_044863_3_1_1; -.
DR   PhylomeDB; B0Y953; -.
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; Lyase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..234
FT                   /note="Probable pectate lyase F"
FT                   /id="PRO_0000394587"
SQ   SEQUENCE   234 AA;  24810 MW;  F341151E0E52F40F CRC64;
     MWSSIAAFPV LVPVALACLG YEGGVPTPTA HHSNSAVIEV AAGQVFDAGW AKYDRGSGAC
     KGQSEGDWKD AVFYLHSGAT LKNVIIGANQ AEGVHCDGPC TLQFVWFEDV CEDAITIKND
     KAGQETWIIG GGAYHASDKI VQHNGCGTVN IINFYAEDYG KVYRSCGNCD KQCKRNVYVE
     GTTARNGGEV VGINLNYGDT ATLKNVCADS AHPCVFYDGC AGDCEPKKVG YCSG