PELD_ASPOR
ID PELD_ASPOR Reviewed; 375 AA.
AC Q2TXS4; Q8X1X1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Pectin lyase 2;
DE Short=PL2;
DE EC=4.2.2.10;
DE AltName: Full=Pectin lyase D;
DE Short=PLD;
DE Flags: Precursor;
GN Name=pel2; Synonyms=pelD; ORFNames=AO090010000030;
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], GLYCOSYLATION, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=KBN616;
RX PubMed=16233008; DOI=10.1263/jbb.91.378;
RA Kitamoto N., Yoshino-Yasuda S., Ohmiya K., Tsukagoshi N.;
RT "A second pectin lyase gene (pel2) from Aspergillus oryzae KBN616: its
RT sequence analysis and overexpression, and characterization of the gene
RT products.";
RL J. Biosci. Bioeng. 91:378-381(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).
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:16233008}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. Stable over a wide pH range of 3.0 to 7.0.
CC {ECO:0000269|PubMed:16233008};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Stable up to 55 degrees
CC Celsius but inactivated rapidly above 55 degrees Celsius.
CC {ECO:0000269|PubMed:16233008};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
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DR EMBL; AB029323; BAB82468.1; -; Genomic_DNA.
DR EMBL; AP007175; BAE65949.1; -; Genomic_DNA.
DR RefSeq; XP_001827082.1; XM_001827030.1.
DR AlphaFoldDB; Q2TXS4; -.
DR SMR; Q2TXS4; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR iPTMnet; Q2TXS4; -.
DR EnsemblFungi; BAE65949; BAE65949; AO090010000030.
DR GeneID; 5999216; -.
DR KEGG; aor:AO090010000030; -.
DR VEuPathDB; FungiDB:AO090010000030; -.
DR HOGENOM; CLU_021980_0_1_1; -.
DR OMA; NIGRQHI; -.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..375
FT /note="Pectin lyase 2"
FT /id="PRO_0000394353"
FT ACT_SITE 255
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16233008"
FT DISULFID 82..101
FT /evidence="ECO:0000250"
FT DISULFID 91..225
FT /evidence="ECO:0000250"
FT DISULFID 321..329
FT /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="G -> A (in Ref. 1; BAB82468)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> R (in Ref. 1; BAB82468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 39230 MW; 913954C9EA4130D4 CRC64;
MKYAAVLTTV AALASRALGA GVSGTAEGFA SSATGGGSAT AVYPTTTDEL VSYLGDDEAR
VIVLSQTFDF TNTEGTTTET GCAPWGTGSA CQVAINKDDW CTNYESSAPS TSVTYDNAGS
LGITVNSNKS LIGEGTKGVI KGKGLRIVNG VENVIIQNIA VTDINPKYVW GGDAITINQA
DLVWIDHVTT ARIGRQHYVL GTEADNRVTL SNNYIDGESD YSATCDGHHY WNVYLDGSSD
KVTMKGNYFY KTSGRAPKVQ GNTYLHAVNN YWNDNSNHAF EIGSGGYVLA EGNTFADVTA
AVEDSSFEGE LFSSSSDADT CSSYIGRACK ANSFTNSGDL SGTTVDVLSK FKGETVATAD
TASTAPASNA GQGNL
