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Protein

Endopolygalacturonase B

Gene

pgaB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.1 Publication

Catalytic activityi

Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei202 – 2021Proton donorPROSITE-ProRule annotation
Active sitei224 – 2241PROSITE-ProRule annotation

GO - Molecular functioni

  • galacturan 1,4-alpha-galacturonidase activity Source: UniProtKB
  • polygalacturonase activity Source: UniProtKB

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • pectin catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28A_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Endopolygalacturonase B (EC:3.2.1.15)
Alternative name(s):
Pectinase B
Polygalacturonase B
Gene namesi
Name:pgaB
Synonyms:pecB
ORF Names:AO090023000161
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiFungiDB:AO090023000161.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 288Sequence analysisPRO_0000024780
Chaini29 – 363335Endopolygalacturonase BPRO_0000024781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 46By similarity
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi204 ↔ 220By similarity
Disulfide bondi330 ↔ 335By similarity
Disulfide bondi354 ↔ 363By similarity
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP35335.
SMRiP35335. Positions 30-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati158 – 18730PbH1 1Add
BLAST
Repeati188 – 20922PbH1 2Add
BLAST
Repeati210 – 23021PbH1 3Add
BLAST
Repeati239 – 26022PbH1 4Add
BLAST
Repeati268 – 29023PbH1 5Add
BLAST
Repeati302 – 34746PbH1 6Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated
Contains 6 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000193107.
KOiK01184.
OMAiVQGFSIQ.
OrthoDBiEOG71VT3J.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 6 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLLQSSVIA ATVGAALVAA VPVELKARDS CTFTSAADAK SGKTSCSTIT
60 70 80 90 100
LSNIEVPAGE TLDLTGLNDG TTVIFSGETT FGYKEWEGPL ISVSGTNIKV
110 120 130 140 150
QQASGAKIDG DGSRWWDGKG GNGGKTKPKF FYAHKLDSSS ITGLQIYNTP
160 170 180 190 200
VQGFSIQSDN LNITDVTIDN SAGTAEGHNT DAFDVGSSTY INIDGATVYN
210 220 230 240 250
QDDCLAINSG SHITFTNGYC DGGHGLSIGS VGGRSDNTVE DVTISNSKVV
260 270 280 290 300
NSQNGVRIKT VYDATGTVSN VKFEDITLSG ITKYGLIVEQ DYENGSPTGT
310 320 330 340 350
PTNGIKVSDI TFDKVTGTVE SDATDIYILC GSGSCTDWTW SGVSITGGKT
360
SSKCENVSTG ASC
Length:363
Mass (Da):37,651
Last modified:May 2, 2006 - v2
Checksum:i83DC803AE2865504
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581S → P in ABO38858 (PubMed:18562768).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14282 Genomic DNA. Translation: BAA03244.2.
AP007157 Genomic DNA. Translation: BAE58737.1.
EF452420 mRNA. Translation: ABO38858.1.
RefSeqiXP_001820739.1. XM_001820687.2.

Genome annotation databases

EnsemblFungiiCADAORAT00007309; CADAORAP00007163; CADAORAG00007309.
GeneIDi5992741.
KEGGiaor:AOR_1_276144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14282 Genomic DNA. Translation: BAA03244.2.
AP007157 Genomic DNA. Translation: BAE58737.1.
EF452420 mRNA. Translation: ABO38858.1.
RefSeqiXP_001820739.1. XM_001820687.2.

3D structure databases

ProteinModelPortaliP35335.
SMRiP35335. Positions 30-361.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28A_ASPOR.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00007309; CADAORAP00007163; CADAORAG00007309.
GeneIDi5992741.
KEGGiaor:AOR_1_276144.

Organism-specific databases

EuPathDBiFungiDB:AO090023000161.

Phylogenomic databases

HOGENOMiHOG000193107.
KOiK01184.
OMAiVQGFSIQ.
OrthoDBiEOG71VT3J.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 6 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural features of a polygalacturonase gene cloned from Aspergillus oryzae KBN616."
    Kitamoto N., Kimura T., Kito Y., Ohmiya K., Tsukagoshi N.
    FEMS Microbiol. Lett. 111:37-42(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KBN616.
  2. Kitamoto N.
    Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 337-338.
  3. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.
  4. "Restoration of mature etiolated cucumber hypocotyl cell wall susceptibility to expansin by pretreatment with fungal pectinases and EGTA in vitro."
    Zhao Q., Yuan S., Wang X., Zhang Y., Zhu H., Lu C.
    Plant Physiol. 147:1874-1885(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-363, FUNCTION.

Entry informationi

Entry nameiPGLRB_ASPOR
AccessioniPrimary (citable) accession number: P35335
Secondary accession number(s): A4L7I0, Q2UI78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 2, 2006
Last modified: April 13, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.