PGLRE_ASPNC
ID PGLRE_ASPNC Reviewed; 378 AA.
AC A2QBB6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable endopolygalacturonase E;
DE Short=PGE;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 4;
DE AltName: Full=Pectinase E;
DE AltName: Full=Polygalacturonase E;
DE AltName: Full=Polygalacturonase IV;
DE Short=PG-IV;
DE Flags: Precursor;
GN Name=pgaE; ORFNames=An01g14670;
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; AM269993; CAK44164.1; -; Genomic_DNA.
DR RefSeq; XP_001389855.1; XM_001389818.2.
DR AlphaFoldDB; A2QBB6; -.
DR SMR; A2QBB6; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QBB6; -.
DR EnsemblFungi; CAK44164; CAK44164; An01g14670.
DR GeneID; 4977284; -.
DR KEGG; ang:ANI_1_1980014; -.
DR VEuPathDB; FungiDB:An01g14670; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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; 6.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..38
FT /evidence="ECO:0000255"
FT /id="PRO_0000393665"
FT CHAIN 39..378
FT /note="Probable endopolygalacturonase E"
FT /id="PRO_5000219495"
FT REPEAT 103..125
FT /note="PbH1 1"
FT REPEAT 174..204
FT /note="PbH1 2"
FT REPEAT 205..226
FT /note="PbH1 3"
FT REPEAT 256..277
FT /note="PbH1 4"
FT REPEAT 285..307
FT /note="PbH1 5"
FT REPEAT 317..345
FT /note="PbH1 6"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..61
FT /evidence="ECO:0000250"
FT DISULFID 221..237
FT /evidence="ECO:0000250"
FT DISULFID 345..350
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 39631 MW; 7A8D7FBDEB9AB758 CRC64;
MVTSSSVIVL TLWAALVSAS PVADPLVTPA PKLEDLEKRA TSCTFSGSEG ASSASKSKTS
CSTIVLSDVA VPSGTTLDLT DLNDGTHVIF EGETTFGYEE WSGPLVSVSG TDITVTGADG
AYLNGDGSRW WDGEGSNGGK TKPKFFYAHD LTSSTISGIY IQNSPVQVFS IDGSTYLTME
DITIDNTDGD DGEAANTDGF DIGDSTYITI TGANVYNQDD CVAVNSGENI YFSGGVCSGG
HGLSIGSVGG RSDNTVKNVT FYDSEIKSSQ NGVRIKTIYG DTGSVSEVTY KEITLSDITD
YGIVVEQNYD DTSKSPTDGI TIEDFVLDNV QGSVESSGTN IYIVCGSDSC TDWTWTDVDV
SGGKTSSDCE NVPDDISC
