ID   PGLRD_ASPOR             Reviewed;         492 AA.
AC   Q2UT29;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 77.
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=AO090005000186;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE55286.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007151; BAE55286.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001817288.2; XM_001817236.2.
DR   AlphaFoldDB; Q2UT29; -.
DR   SMR; Q2UT29; -.
DR   STRING; 510516.Q2UT29; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; BAE55286; BAE55286; AO090005000186.
DR   Proteomes; UP000006564; Chromosome 1.
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; 7.
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..492
FT                   /note="Probable endopolygalacturonase D"
FT                   /id="PRO_0000393662"
FT   REPEAT          216..238
FT                   /note="PbH1 1"
FT   REPEAT          258..280
FT                   /note="PbH1 2"
FT   REPEAT          281..319
FT                   /note="PbH1 3"
FT   REPEAT          320..341
FT                   /note="PbH1 4"
FT   REPEAT          371..392
FT                   /note="PbH1 5"
FT   REPEAT          400..422
FT                   /note="PbH1 6"
FT   REPEAT          434..478
FT                   /note="PbH1 7"
FT   ACT_SITE        334
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..166
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        461..466
FT                   /evidence="ECO:0000250"
FT   DISULFID        484..491
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  50732 MW;  CFA4356FA542D1BF CRC64;
     MKRSALILSF LPLVFGCDNP KSPGHSCASV YSVSSAAASS FCATFTASTV TATTGVPEAL
     LSNCDYKTKH LSSACSCLGT AAVPTVATPS SVSSVYITSA TATPTSFTFK TSTAHIVKVA
     KAATSSTAVV TTPVSVPTAS SSFTGNGGTT CTVTEYAAIS SAVASCSNIL LSDIYAPPSS
     TIDLQGLQTG AAVIFAGKTT FGDTADSDFD PIVVSGTSVT ITGVEGHVID GNGAAYWDGQ
     GSNGGSDKPD HFFVVKDMYN SRIENLYIQN WPVHCFEIES TEHLTVSGLT LNNSAGDAAN
     SKSDGDPAAH NSDGFDIKES SYFTLENTWV HNQDDCVAVT SGTDIVVDGM YCYGGHGLSI
     GSIGGKSDNT VNGVTFSNSQ VISSQNGCRI KTNSGETGEV YNIRYENITL SDISDYGIDV
     QQDYLNGGPT GEPTNGVTIA NVTFVDVTGT MSDGKDYYIL CGDDSCSNFV FDGVSITGGS
     GDSCNYPSTG CP