PELB_ASPOR
ID PELB_ASPOR Reviewed; 381 AA.
AC Q2TWM1; A4L7H9; Q8X1X2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Pectin lyase 1;
DE Short=PL1;
DE EC=4.2.2.10;
DE AltName: Full=Pectin lyase B;
DE Short=PLB;
DE Flags: Precursor;
GN Name=pel1; Synonyms=pelB; ORFNames=AO090010000504;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=KBN616;
RX PubMed=11272833; DOI=10.1271/bbb.65.209;
RA Kitamoto N., Yoshino-Yasuda S., Ohmiya K., Tsukagoshi N.;
RT "Sequence analysis and overexpression of a pectin lyase gene (pel1) from
RT Aspergillus oryzae KBN616.";
RL Biosci. Biotechnol. Biochem. 65:209-212(2001).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-381, AND FUNCTION.
RX PubMed=18562768; DOI=10.1104/pp.108.116962;
RA Zhao Q., Yuan S., Wang X., Zhang Y., Zhu H., Lu C.;
RT "Restoration of mature etiolated cucumber hypocotyl cell wall
RT susceptibility to expansin by pretreatment with fungal pectinases and EGTA
RT in vitro.";
RL Plant Physiol. 147:1874-1885(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.
CC {ECO:0000269|PubMed:11272833, ECO:0000269|PubMed:18562768}.
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:0000305}.
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; AB029322; BAB82467.1; -; Genomic_DNA.
DR EMBL; AP007175; BAE66352.1; -; Genomic_DNA.
DR EMBL; EF452419; ABO38857.1; -; mRNA.
DR PIR; JC7650; JC7650.
DR RefSeq; XP_001827485.1; XM_001827433.1.
DR AlphaFoldDB; Q2TWM1; -.
DR SMR; Q2TWM1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblFungi; BAE66352; BAE66352; AO090010000504.
DR GeneID; 5999619; -.
DR KEGG; aor:AO090010000504; -.
DR VEuPathDB; FungiDB:AO090010000504; -.
DR HOGENOM; CLU_021980_0_1_1; -.
DR OMA; CRPWGTG; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0047490; F:pectin lyase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA: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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..381
FT /note="Pectin lyase 1"
FT /id="PRO_0000394347"
FT ACT_SITE 257
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..102
FT /evidence="ECO:0000250"
FT DISULFID 92..227
FT /evidence="ECO:0000250"
FT DISULFID 324..332
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="S -> T (in Ref. 1; BAB82467)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="A -> V (in Ref. 1; BAB82467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 39941 MW; 772A9499BBFD9F60 CRC64;
MKYASFIAAA AAALASAVSA AGVSGSAEGF AKGVTGGGSA TPVYPSTTDE LVSYLGDSEA
RVIILTKTFD FTNTEGTETS SGCAPWGTAS GCQLAINKDN WCTNYEPNAP TVSSITYNKA
GVLGITVNSN KSIVGQGSAG VIKGRGLRIV SGAKNVIIQN IAITDINPKY VWGGDAITLN
EADLVWIDHV TTARIARQHI VLGTQADNRV TISNSLIDGR TDYSATCNGH HYWGVYLDGS
NDMVTMMGNY FYYTSGRMPK VQGNTLLHAV NNYFHNIEGH AFEIGSGGYV LAEGNAFQNV
DAPVESPISG QLFSAPDATT NEQCKSVFGR ACQINAFGSS GSFSQADTAV ISKFSGKNIA
TAHLAQNIPK WVMANAGQGK L
