PGLR1_ASPOR
ID PGLR1_ASPOR Reviewed; 367 AA.
AC Q2UHL4; O93789;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=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, pgaB; ORFNames=AO090023000401;
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 [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=KBN616;
RX PubMed=9720204; DOI=10.1007/s002530051260;
RA Kitamoto N., Matsui J., Kawai Y., Kato A., Yoshino S., Ohmiya K.,
RA Tsukagoshi N.;
RT "Utilization of the TEF1-alpha gene (TEF1) promoter for expression of
RT polygalacturonase genes, pgaA and pgaB, in Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 50:85-92(1998).
RN [2]
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. {ECO:0000269|PubMed:9720204}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0: Stable between pH 3.0 and 7.0.
CC {ECO:0000269|PubMed:9720204};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:9720204};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AB007769; BAA34782.1; -; Genomic_DNA.
DR EMBL; AP007157; BAE58951.1; -; Genomic_DNA.
DR RefSeq; XP_001820953.1; XM_001820901.2.
DR AlphaFoldDB; Q2UHL4; -.
DR SMR; Q2UHL4; -.
DR STRING; 510516.Q2UHL4; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; BAE58951; BAE58951; AO090023000401.
DR GeneID; 5992955; -.
DR KEGG; aor:AO090023000401; -.
DR VEuPathDB; FungiDB:AO090023000401; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR OMA; EGSRWWD; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IDA:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA: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; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000393622"
FT CHAIN 31..367
FT /note="Endopolygalacturonase I"
FT /id="PRO_0000393623"
FT REPEAT 161..191
FT /note="PbH1 1"
FT REPEAT 192..213
FT /note="PbH1 2"
FT REPEAT 214..234
FT /note="PbH1 3"
FT REPEAT 243..264
FT /note="PbH1 4"
FT REPEAT 272..294
FT /note="PbH1 5"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..49
FT /evidence="ECO:0000250"
FT DISULFID 208..224
FT /evidence="ECO:0000250"
FT DISULFID 334..339
FT /evidence="ECO:0000250"
FT DISULFID 358..367
FT /evidence="ECO:0000250"
FT CONFLICT 136
FT /note="A -> G (in Ref. 1; BAA34782)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> Y (in Ref. 1; BAA34782)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 37798 MW; 98951FF0FC242576 CRC64;
MHFQLLGLAA LGSLAAAAPA PSRTSELVER GSSCTFTSAA QASASAKSCS NIVLKNIAVP
AGETLDLSKA KDGATITFEG TTTFGYKEWK GPLIRFGGNK ITVTQAAGAV IDGQGSRWWD
GKGTNGGKTK PKFIYAHKLQ SSTIKGLHVK NSPVQVFSVQ GNDVHLTDIT IDNSDGDNNG
GHNTDAFDVS ESNGVYITGA NVKNQDDCLA INSGENIEFT GATCSGGHGI SIGSIGNRDS
NTVKNVKVAD STVVDSDNGI RIKTISGATG SVSGVTYENI TLKNIKKNGI VIEQDYKNGG
PTGKPTTGVP ITDLTVNGVT GSVASKATPV YILCGKGSCS DWTWKGVSIS GGKKSDKCQN
IPSGASC
