PGLR2_ASPNC
ID PGLR2_ASPNC Reviewed; 362 AA.
AC A2R5S4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable endopolygalacturonase II;
DE Short=EPG-II;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 2;
DE AltName: Full=Polygalacturonase II;
DE Short=PG-II;
DE AltName: Full=Polygalacturonase X2;
DE Flags: Precursor;
GN Name=pgaII; Synonyms=pg2; ORFNames=An15g05370;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AM270345; CAK42510.1; -; Genomic_DNA.
DR RefSeq; XP_001397067.1; XM_001397030.1.
DR AlphaFoldDB; A2R5S4; -.
DR SMR; A2R5S4; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2R5S4; -.
DR EnsemblFungi; CAK42510; CAK42510; An15g05370.
DR GeneID; 4988138; -.
DR KEGG; ang:ANI_1_728134; -.
DR VEuPathDB; FungiDB:An15g05370; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase 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; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..27
FT /evidence="ECO:0000255"
FT /id="PRO_0000393632"
FT CHAIN 28..362
FT /note="Probable endopolygalacturonase II"
FT /id="PRO_5000221069"
FT REPEAT 156..186
FT /note="PbH1 1"
FT REPEAT 209..229
FT /note="PbH1 2"
FT REPEAT 238..259
FT /note="PbH1 3"
FT REPEAT 267..289
FT /note="PbH1 4"
FT REPEAT 301..322
FT /note="PbH1 5"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..45
FT /evidence="ECO:0000250"
FT DISULFID 203..219
FT /evidence="ECO:0000250"
FT DISULFID 329..334
FT /evidence="ECO:0000250"
FT DISULFID 353..362
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 37684 MW; 952A79F612BC8000 CRC64;
MHSFASLLAY GLVAGATFAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL NNIEVPAGTT
LDLTGLTSGT KVIFEGTTTF QYEEWAGPLI SMSGEHITVT GASGHLINCD GARWWDGKGT
SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM AFSVQANDIT FTDVTINNAD GDTQGGHNTD
AFDVGNSVGV NIIKPWVHNQ DDCLAVNSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN
VTIEHSTVSN SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP
TNGVTIQDVK LESVTGSVDS GATEIYLLCG SGSCSDWTWD DVKVTGGKKS TACKNFPSVA
SC
