PGLRC_ASPNC
ID PGLRC_ASPNC Reviewed; 384 AA.
AC A2QL39;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable endopolygalacturonase C;
DE Short=PGC;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 3;
DE AltName: Full=Pectinase C;
DE AltName: Full=Polygalacturonase C;
DE AltName: Full=Polygalacturonase III;
DE Short=PG-III;
DE Flags: Precursor;
GN Name=pgaC; ORFNames=An05g02440;
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; AM270106; CAK44905.1; -; Genomic_DNA.
DR RefSeq; XP_001390812.1; XM_001390775.1.
DR AlphaFoldDB; A2QL39; -.
DR SMR; A2QL39; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QL39; -.
DR EnsemblFungi; CAK44905; CAK44905; An05g02440.
DR GeneID; 4980981; -.
DR KEGG; ang:ANI_1_312044; -.
DR VEuPathDB; FungiDB:An05g02440; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7L.
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; 4.
DR SUPFAM; SSF51126; SSF51126; 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..40
FT /evidence="ECO:0000255"
FT /id="PRO_0000393660"
FT CHAIN 41..384
FT /note="Probable endopolygalacturonase C"
FT /id="PRO_5000220025"
FT REPEAT 176..207
FT /note="PbH1 1"
FT REPEAT 208..229
FT /note="PbH1 2"
FT REPEAT 254..280
FT /note="PbH1 3"
FT REPEAT 288..310
FT /note="PbH1 4"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..63
FT /evidence="ECO:0000250"
FT DISULFID 224..240
FT /evidence="ECO:0000250"
FT DISULFID 349..354
FT /evidence="ECO:0000250"
FT DISULFID 373..382
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 40573 MW; 51DF161789E09D96 CRC64;
MVRQLILISS LLAAVAVRAA PADPAHPMVT EAPDVNLVEK RATTCTFSGS EGASKASKSK
TSCSTIYLSD VAVPSGTTLD LSDLNDGTHV IFQGETTFGY EEWEGPLVRV SGTDITVEGE
SDAVLNGDGS RWWDGEGGNG GKTKPKFFYA HDLTSSTIKS IYIENSPVQV FSIDGSTDLT
MTDITVDNTD GDTDDLAANT DGFDIGESTY ITITGAEIYN QDDCVAINSG ENIYFSASVC
SGGHGLSIGS VGGRDDNTVK NVTFYDVNVL KSQQAIRIKT IYGDTGSVSE VTYHEIAFSD
ATDYGIVIEQ NYDDTSKTPT TGVPITDFVL ENIVGTCEDD DCTEVYIACG DGSCSDWTWT
GVSVTGGSVS DDCLNVPSGI SCDL
