PGLR1_ASPNC
ID PGLR1_ASPNC Reviewed; 368 AA.
AC A2QAH3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable endopolygalacturonase I;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 1;
DE AltName: Full=Polygalacturonase I;
DE Short=PG-I;
DE Flags: Precursor;
GN Name=pgaI; Synonyms=pg1, pga1; ORFNames=An01g11520;
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; AM269981; CAK44054.1; -; Genomic_DNA.
DR RefSeq; XP_001389562.1; XM_001389525.1.
DR AlphaFoldDB; A2QAH3; -.
DR SMR; A2QAH3; -.
DR Allergome; 8269; Asp n Pectinase.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QAH3; -.
DR EnsemblFungi; CAK44054; CAK44054; An01g11520.
DR GeneID; 4978020; -.
DR KEGG; ang:ANI_1_1554014; -.
DR VEuPathDB; FungiDB:An01g11520; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..31
FT /evidence="ECO:0000255"
FT /id="PRO_0000393621"
FT CHAIN 32..368
FT /note="Probable endopolygalacturonase I"
FT /id="PRO_5000219447"
FT REPEAT 140..161
FT /note="PbH1 1"
FT REPEAT 162..192
FT /note="PbH1 2"
FT REPEAT 193..214
FT /note="PbH1 3"
FT REPEAT 244..265
FT /note="PbH1 4"
FT REPEAT 273..295
FT /note="PbH1 5"
FT REPEAT 307..352
FT /note="PbH1 6"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..50
FT /evidence="ECO:0000250"
FT DISULFID 209..225
FT /evidence="ECO:0000250"
FT DISULFID 335..340
FT /evidence="ECO:0000250"
FT DISULFID 359..368
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 38108 MW; CD9B46A9A99B5102 CRC64;
MHSYQLLGLA AVGSLVSAAP APSRVSEFAK KASTCTFTSA SEASESISSC SDVVLSSIEV
PAGETLDLSD AADGSTITFE GTTSFGYKEW KGPLIRFGGK DLTVTMADGA VIDGDGSRWW
DSKGTNGGKT KPKFMYIHDV EDSTFKGINI KNTPVQAISV QATNVHLNDF TIDNSDGDDN
GGHNTDGFDI SESTGVYISG ATVKNQDDCI AINSGESISF TGGTCSGGHG LSIGSVGGRD
DNTVKNVTIS DSTVSNSANG VRIKTIYKET GDVSEITYSN IQLSGITDYG IVIEQDYENG
SPTGTPSTGI PITDVTVDGV TGTLEDDATQ VYILCGDGSC SDWTWSGVDL SGGKTSDKCE
NVPSGASC
