ID   PGLRD_ASPNG             Reviewed;         495 AA.
AC   Q9P4W2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=10675564; DOI=10.1016/s0014-5793(00)01173-x;
RA   Parenicova L., Kester H.C., Benen J.A., Visser J.;
RT   "Characterization of a novel endopolygalacturonase from Aspergillus niger
RT   with unique kinetic properties.";
RL   FEBS Lett. 467:333-336(2000).
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.
CC       {ECO:0000269|PubMed:10675564}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; Y18806; CAB72931.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4W2; -.
DR   SMR; Q9P4W2; -.
DR   STRING; 5061.CADANGAP00007721; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28D_ASPNG; -.
DR   VEuPathDB; FungiDB:An09g03260; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1180726; -.
DR   VEuPathDB; FungiDB:ATCC64974_10360; -.
DR   VEuPathDB; FungiDB:M747DRAFT_306785; -.
DR   eggNOG; ENOG502QW1P; Eukaryota.
DR   BioCyc; MetaCyc:MON-20557; -.
DR   BRENDA; 3.2.1.15; 518.
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; Repeat; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..495
FT                   /note="Endopolygalacturonase D"
FT                   /id="PRO_5000147353"
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