ID   PLYF_NEOFI              Reviewed;         234 AA.
AC   A1D5E3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable pectate lyase F;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=plyF; ORFNames=NFIA_023470;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027688; EAW23636.1; -; Genomic_DNA.
DR   RefSeq; XP_001265533.1; XM_001265532.1.
DR   AlphaFoldDB; A1D5E3; -.
DR   SMR; A1D5E3; -.
DR   STRING; 36630.CADNFIAP00000787; -.
DR   EnsemblFungi; EAW23636; EAW23636; NFIA_023470.
DR   GeneID; 4590823; -.
DR   KEGG; nfi:NFIA_023470; -.
DR   VEuPathDB; FungiDB:NFIA_023470; -.
DR   eggNOG; ENOG502QSM3; Eukaryota.
DR   HOGENOM; CLU_044863_3_1_1; -.
DR   OMA; KIVPCQK; -.
DR   OrthoDB; 1066001at2759; -.
DR   BRENDA; 4.2.2.2; 504.
DR   Proteomes; UP000006702; 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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..234
FT                   /note="Probable pectate lyase F"
FT                   /id="PRO_0000394592"
SQ   SEQUENCE   234 AA;  24861 MW;  50D6ABB90B2348D3 CRC64;
     MWSSIAALPV LVPVALACLG YEGGVPTPTA HYSNSAVIEV AAGQVFDAGW AKYDRGSGAC
     NDQSEGDWKD AVFYLHSGAT LKNVIIGANQ AEGVHCDGPC TLQFVWFEDV CEDAITIKND
     KAGQETWIIG GGAYHASDKI VQHNGCGTVN IINFYAEDYG KVYRSCGNCD NQCKRNVYVE
     GTTARDGGEV VGINLNYGDT ATLKNVCADA DHPCVFYDGC AGDCEPKKVG YCSG