ID   PELA_ASPOR              Reviewed;         379 AA.
AC   Q2TXM4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Probable pectin lyase A;
DE            Short=PLA;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA; ORFNames=AO090010000087;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007175; BAE65999.1; -; Genomic_DNA.
DR   RefSeq; XP_001827132.1; XM_001827080.1.
DR   AlphaFoldDB; Q2TXM4; -.
DR   SMR; Q2TXM4; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   EnsemblFungi; BAE65999; BAE65999; AO090010000087.
DR   GeneID; 5999266; -.
DR   KEGG; aor:AO090010000087; -.
DR   VEuPathDB; FungiDB:AO090010000087; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; QDDWCEN; -.
DR   Proteomes; UP000006564; Chromosome 8.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..379
FT                   /note="Probable pectin lyase A"
FT                   /id="PRO_0000394341"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  39513 MW;  D0BFBDE05C5CA040 CRC64;
     MKFALLSGVA AGLLPVVSAV SVSGAAEGFA KGVTGGGSAA AVYPTTTDEL VSYLGDSSPR
     VIVLDRTFDF TGTEGTTTAT GCAPWGTAAA CQLAINQNDW CTNYQPDAPS VSVTYDNAGI
     LGITVASDKT ILGSGSSGVI KGKGLRIVSG ASNIIIQNIA ITDLNPKYVW GGDAITLNDA
     DMVWIDHVTT ARIGRQHLVL GNDADNRVTV SNSYFNGVSD YSATCDGYAY WGIYFAGSSD
     LITFKGNYIH HFSGRSPKVQ ENTLLHAVNN YWYDSTGHAF EIGAGGYVLA EGNVFQNIDT
     PVQSPIEGQL FTSPDTNTNT VCATYLGRNC EVNGFGSSGT FSQADTAFLV NFEGKNIASA
     SPYADAQSSV PSSAGQGNL