ID   PELC_ASPOR              Reviewed;         375 AA.
AC   Q2UCT7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Probable pectin lyase C;
DE            Short=PLC;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelC; ORFNames=AO090012000451;
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}.
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; AP007161; BAE60628.1; -; Genomic_DNA.
DR   RefSeq; XP_001727467.1; XM_001727415.1.
DR   AlphaFoldDB; Q2UCT7; -.
DR   SMR; Q2UCT7; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   EnsemblFungi; BAE60628; BAE60628; AO090012000451.
DR   GeneID; 5987941; -.
DR   KEGG; aor:AO090012000451; -.
DR   VEuPathDB; FungiDB:AO090012000451; -.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; QNIMITN; -.
DR   Proteomes; UP000006564; Chromosome 4.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..375
FT                   /note="Probable pectin lyase C"
FT                   /id="PRO_0000394350"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..220
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  39345 MW;  2F6D64A33E2EF048 CRC64;
     MKITSTIPAV LLGLAPLSAA VSVSGSAEGF ASGVTGGGDA EAQIPSDIDE LKEWLTDDTP
     RVIVLDKEYD FTESEGTTSG TVCASWGTGS GCQKIIQDDC GDSPSSQATW YTAGTTGIDV
     ASDKTILGDG DKGVIKGKGL RFRDGVSNII VQNIEISDLN PEYVWGGDAL YFDGSDLIWI
     DHVTTARTGR QHYTFGYETN TRITLSNNFI NGETTYSTGC DGYTYWTFEM VGEADQITLQ
     NNYIYMTAGR SPALSGGTLL HAVNNVWEKN NGHALEGGDA GARGIFEGNA WIGVSTIVGD
     YAGRLFNAPD SSSAGDCESA LGRACEVNAV SDSGDLTAYT DTSFFSDFSG LTIAPATSAT
     DAQSSVPNNA GMGKL