ID   PELF_ASPFC              Reviewed;         386 AA.
AC   B0Y0L8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Probable pectin lyase E;
DE            Short=PLE;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelE; ORFNames=AFUB_057770;
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}.
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DR   EMBL; DS499597; EDP51759.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y0L8; -.
DR   SMR; B0Y0L8; -.
DR   EnsemblFungi; EDP51759; EDP51759; AFUB_057770.
DR   VEuPathDB; FungiDB:AFUB_057770; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   PhylomeDB; B0Y0L8; -.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..386
FT                   /note="Probable pectin lyase E"
FT                   /id="PRO_0000394356"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..334
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  41355 MW;  3B501F9E72C20F92 CRC64;
     MKTAVLSLFL ALQTYARVTG SPSGFAAGTT GGGSATPAAP SSLDELVQWI TDDKPRVILI
     DRTWDFIGTE GTTTGKCCSM PSTTVCSGGT SKGQAWIQDH CDGGSWVSCK YDNAALTPLD
     VGSNKSIVGV GNKGVIKGKG LRVRNGNKNV IIQNIHITNL NPQYVWGGDA ITLDNADKVW
     IDHNKISLIG RQFIVSGWGK AGHVTISNNE FDGRTSWSAG CNGKHYWTLL LLGEQDYYTF
     QGNWLHDVSG RAPHMGTDHT KSQIFFHGVN NYFQNVGGHA FDVDTNTWVL LEGNYFENVN
     TPLTDTSLRA GGKLYTTSTV AAAGACQDKL GYICEWNRLA GSGAWKDRTD ADVKTKAAAF
     KSSLVGHYPV ADVPAKVVAN AGVGKL