ID   PELA_COLGL              Reviewed;         380 AA.
AC   Q00374;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Pectin lyase;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=PNLA;
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8181749; DOI=10.1016/0378-1119(94)90369-7;
RA   Templeton M.D., Sharrock K.R., Bowen J.K., Crowhurst R.N., Rikkerink E.H.;
RT   "The pectin lyase-encoding gene (pnl) family from Glomerella cingulata:
RT   characterization of pnlA and its expression in yeast.";
RL   Gene 142:141-146(1994).
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   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; L22857; AAA21817.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00374; -.
DR   SMR; Q00374; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
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   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   Glycoprotein; Lyase; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..380
FT                   /note="Pectin lyase"
FT                   /id="PRO_0000024899"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   380 AA;  39326 MW;  3DF9A99FBB482053 CRC64;
     MRSASILSAA LAAFAPLASA ADAVSGAAEG FAKGVTGGGS ATPVYPSTTA ELASYLKDSS
     ARVIVLTKTF DFTGTEGTTT ETGCAPYGTA AACQVAINKD NWCTNYQPNA PKVSVSYDKA
     PFNPLIVGSN KSLIGQGSKG VIKGKGLRIT NSAKNVIIQN IHITNLNPKY VWGGDAISLD
     GTDLVWFDHV KTSLIGRQHI VLGNGASNRV TISNNEIDGS TSWSATCDNH HYWGVYLTGS
     NDMVTFSKNY IHHTSGRSPK IAGNSLVHIS GNYFYANSGH AMEADAGAKV VLEGNVFQNV
     VAAMQSGLAG KVFSSPDANT NAQCSSYLGH TCQLNAYGSS GSLSGSDTSI LSSFSGKNVA
     ATVTANDAKN VPNTAGFGKI