PGLRB_ASPOR
ID PGLRB_ASPOR Reviewed; 363 AA.
AC P35335; A4L7I0; Q2UI78;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Endopolygalacturonase B;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase B;
DE AltName: Full=Polygalacturonase B;
DE Flags: Precursor;
GN Name=pgaB; Synonyms=pecB; ORFNames=AO090023000161;
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].
RC STRAIN=KBN616;
RX PubMed=8359678; DOI=10.1111/j.1574-6968.1993.tb06358.x;
RA Kitamoto N., Kimura T., Kito Y., Ohmiya K., Tsukagoshi N.;
RT "Structural features of a polygalacturonase gene cloned from Aspergillus
RT oryzae KBN616.";
RL FEMS Microbiol. Lett. 111:37-42(1993).
RN [2]
RP SEQUENCE REVISION TO 337-338.
RA Kitamoto N.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-363, AND FUNCTION.
RX PubMed=18562768; DOI=10.1104/pp.108.116962;
RA Zhao Q., Yuan S., Wang X., Zhang Y., Zhu H., Lu C.;
RT "Restoration of mature etiolated cucumber hypocotyl cell wall
RT susceptibility to expansin by pretreatment with fungal pectinases and EGTA
RT in vitro.";
RL Plant Physiol. 147:1874-1885(2008).
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:18562768}.
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; D14282; BAA03244.2; -; Genomic_DNA.
DR EMBL; AP007157; BAE58737.1; -; Genomic_DNA.
DR EMBL; EF452420; ABO38858.1; -; mRNA.
DR RefSeq; XP_001820739.1; XM_001820687.2.
DR AlphaFoldDB; P35335; -.
DR SMR; P35335; -.
DR STRING; 510516.P35335; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGA28A_ASPOR; -.
DR EnsemblFungi; BAE58737; BAE58737; AO090023000161.
DR GeneID; 5992741; -.
DR KEGG; aor:AO090023000161; -.
DR VEuPathDB; FungiDB:AO090023000161; -.
DR HOGENOM; CLU_040116_0_0_1; -.
DR OMA; GSTIKFM; -.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..28
FT /evidence="ECO:0000255"
FT /id="PRO_0000024780"
FT CHAIN 29..363
FT /note="Endopolygalacturonase B"
FT /id="PRO_0000024781"
FT REPEAT 158..187
FT /note="PbH1 1"
FT REPEAT 188..209
FT /note="PbH1 2"
FT REPEAT 210..230
FT /note="PbH1 3"
FT REPEAT 239..260
FT /note="PbH1 4"
FT REPEAT 268..290
FT /note="PbH1 5"
FT REPEAT 302..347
FT /note="PbH1 6"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..46
FT /evidence="ECO:0000250"
FT DISULFID 204..220
FT /evidence="ECO:0000250"
FT DISULFID 330..335
FT /evidence="ECO:0000250"
FT DISULFID 354..363
FT /evidence="ECO:0000250"
FT CONFLICT 358
FT /note="S -> P (in Ref. 4; ABO38858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 37651 MW; 83DC803AE2865504 CRC64;
MQLLQSSVIA ATVGAALVAA VPVELKARDS CTFTSAADAK SGKTSCSTIT LSNIEVPAGE
TLDLTGLNDG TTVIFSGETT FGYKEWEGPL ISVSGTNIKV QQASGAKIDG DGSRWWDGKG
GNGGKTKPKF FYAHKLDSSS ITGLQIYNTP VQGFSIQSDN LNITDVTIDN SAGTAEGHNT
DAFDVGSSTY INIDGATVYN QDDCLAINSG SHITFTNGYC DGGHGLSIGS VGGRSDNTVE
DVTISNSKVV NSQNGVRIKT VYDATGTVSN VKFEDITLSG ITKYGLIVEQ DYENGSPTGT
PTNGIKVSDI TFDKVTGTVE SDATDIYILC GSGSCTDWTW SGVSITGGKT SSKCENVSTG
ASC
