PGLRD_ASPNC
ID PGLRD_ASPNC Reviewed; 495 AA.
AC A2QTU0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Probable endopolygalacturonase D;
DE Short=PGD;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase D;
DE AltName: Full=Polygalacturonase D;
DE Flags: Precursor;
GN Name=pgaD; ORFNames=An09g03260;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270197; CAK40265.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QTU0; -.
DR SMR; A2QTU0; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QTU0; -.
DR EnsemblFungi; CAK40265; CAK40265; An09g03260.
DR HOGENOM; CLU_040116_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
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.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..495
FT /note="Probable endopolygalacturonase D"
FT /id="PRO_5000220437"
FT REPEAT 261..283
FT /note="PbH1 1"
FT REPEAT 284..322
FT /note="PbH1 2"
FT REPEAT 323..344
FT /note="PbH1 3"
FT REPEAT 374..395
FT /note="PbH1 4"
FT REPEAT 403..425
FT /note="PbH1 5"
FT REPEAT 469..492
FT /note="PbH1 6"
FT ACT_SITE 337
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..169
FT /evidence="ECO:0000250"
FT DISULFID 339..355
FT /evidence="ECO:0000250"
FT DISULFID 464..469
FT /evidence="ECO:0000250"
FT DISULFID 487..494
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 50783 MW; CF02F6E536721340 CRC64;
MKRSALLASF LPLALGCDSA ETHSCASAFS VSSAAAASFC ATFTASTVTA TTGVPDVFLS
NCDYKTKHLS SACSCLGTAD GSAPASTPAA PAVSSSSKVG KAPAVAATRT SAIPTTFHTT
AVRVPLSTSA AAAVTSQAVL PAQSSVAGNG GTTCTVTEYA SISSAVASCS NILLSNINAP
ASSTIDLTGL QTGAAVIFAG ETTFGDTYDS DFDPIVISGT DVTITGEEGH VINGNGEAYW
DGEGSNGGQD KPDHFIVVKD MYNSKIENLN ILNWPVHCFE IENTEYLTIS GLILNNTAGD
AANSKSDGDP AAHNTDGFDI KQSDFLTLSN SWVHNQDDCV AVTSGSSIVV DNLYCYGGHG
LSIGSIGGKS NNTVDGVTFS NSQVINSENG CRIKSNADTT GEVYNVKYEN ITLSGISDYG
IDIQQDYENG GATGDPTNGV KIENISFVNV KGTMSDGKDY YILCGDGSCS NFVFTDVDIT
GGSDDSCNYP SSGCP
