ID   PELA_ASPFC              Reviewed;         378 AA.
AC   B0XT36;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Probable pectin lyase A;
DE            Short=PLA;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA; ORFNames=AFUB_017880;
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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS499595; EDP53745.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XT36; -.
DR   SMR; B0XT36; -.
DR   PRIDE; B0XT36; -.
DR   EnsemblFungi; EDP53745; EDP53745; AFUB_017880.
DR   VEuPathDB; FungiDB:AFUB_017880; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   PhylomeDB; B0XT36; -.
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: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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..378
FT                   /note="Probable pectin lyase A"
FT                   /id="PRO_0000394338"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        321..329
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  39382 MW;  5EB5AABB67B03F37 CRC64;
     MKYQDLLAIA GCIANAGAVS VSGAAEGFAK GVTGGGSATA VYPSTTAELV SYLGDSEARV
     IVLTKTFDFT GTEGTTTATG CAPWGTASAC QLAINQNNWC TNYEPNAPSV SVTYDNAGIL
     GITVKSNKSL IGSGSSGVIK GKGLRIVSGA SNIIIQNIAI TDINPKYVWG GDAITIDNAD
     MVWIDHVTTA RIGRQHLVLG TSASNRVTIS NNYFNGVSSY SATCDGYHYW GIYLDGSNDL
     VTMKGNYIYH FSGRSPKVQG NTLLHAVNNY WYDSSGHAFE IGSGGYVLAE GNVFQNIDTI
     VQSPVDGQLF TSPDSNTNKV CSTYLGHVCQ VNGFGSSGTF SQADTGFLSN FAGKNIASAS
     AYTAVQSTVP SSAGQGKI