ID   PELA_ASPCL              Reviewed;         378 AA.
AC   A1CFS2;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Probable pectin lyase A;
DE            Short=PLA;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA; ORFNames=ACLA_094210;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027052; EAW11721.1; -; Genomic_DNA.
DR   RefSeq; XP_001273147.1; XM_001273146.1.
DR   AlphaFoldDB; A1CFS2; -.
DR   SMR; A1CFS2; -.
DR   EnsemblFungi; EAW11721; EAW11721; ACLA_094210.
DR   GeneID; 4704779; -.
DR   KEGG; act:ACLA_094210; -.
DR   VEuPathDB; FungiDB:ACLA_094210; -.
DR   eggNOG; ENOG502QXM6; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; QDDWCEN; -.
DR   OrthoDB; 1267775at2759; -.
DR   Proteomes; UP000006701; 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   Lyase; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..378
FT                   /note="Probable pectin lyase A"
FT                   /id="PRO_0000394337"
FT   ACT_SITE        254
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;  39450 MW;  0F9CEA6FF18ED4D4 CRC64;
     MKYASFLALV GFITSTSAIG VSGAAEGFAK GVTGGGSATP VYPSTTAELV SYLTDSQPRV
     IVLTKTFDFT NTEGSTTATG CAPWGTAPGC QLAINQNDWC KNYQSSAPSV SVTYDNAGVL
     GMTVASDKTL LGSGSSGVIK GKGLRVVSGA KNIIIQNVAI TDINPKYVWG GDAITIDNAD
     MVWIDHVTTA RIGRQHLVLG TSASNRVTIS NSYFNGVSSY SATCDGYHYW GIYLTGSNDL
     VTMKGNYIHH FSGRSPKIQG NTLLHAVNNY WYDSTGHAFE IGSGGYVLAE GNVFQNIKTI
     VEPPVGGQLF TSPNSNTNQA CSAYLGHVCQ VNGFGSSGPF SQADTGLLSK FSGKNVASAS
     AYTVAQSRVP SSAGQGKL