ID   PLYE_ASPFN              Reviewed;         257 AA.
AC   B8NX10;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable pectate lyase E;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=plyE; ORFNames=AFLA_121970;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963485; EED45968.1; -; Genomic_DNA.
DR   RefSeq; XP_002384904.1; XM_002384863.1.
DR   AlphaFoldDB; B8NX10; -.
DR   SMR; B8NX10; -.
DR   STRING; 5059.CADAFLAP00012769; -.
DR   EnsemblFungi; EED45968; EED45968; AFLA_121970.
DR   VEuPathDB; FungiDB:AFLA_121970; -.
DR   eggNOG; ENOG502QU39; Eukaryota.
DR   HOGENOM; CLU_044863_3_1_1; -.
DR   OMA; KCTGQVE; -.
DR   Proteomes; UP000001875; 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..257
FT                   /note="Probable pectate lyase E"
FT                   /id="PRO_0000394582"
SQ   SEQUENCE   257 AA;  27320 MW;  5483562852F6A5B7 CRC64;
     MYQKLLLVPL LLTSALASPH DASSHQKFHQ LNERAAFPIP ASKGSQTFKE PYYVKGTYDG
     GMKTFGRGVK CTGQKEGGDK DAVFIVADGG ILRNAIIGAD QIEGVHCEGS CTIENVWWQE
     VCEDALTFKG TGTGVHKVIG GGAQGADDKV IQHNSGGSAI IQDFTVQNFG KLYRSCGNCK
     KQFKRTVQIS GVKASNGKTL VGINPNLGDS ATIDGCASSV KEICVEYEGT DNNGKEPKKA
     HSGPSNTCKF KEPLASC