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Protein

Endopolygalacturonase A

Gene

pgaA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

pH dependencei

Optimum pH is 2.0.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei229 – 2291PROSITE-ProRule annotation

GO - Molecular functioni

  • 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_ASPAW.

Names & Taxonomyi

Protein namesi
Recommended name:
Endopolygalacturonase A (EC:3.2.1.15)
Alternative name(s):
Pectinase A
Polygalacturonase A
Gene namesi
Name:pgaA
Synonyms:pecA, ppas
OrganismiAspergillus awamori (Black koji mold)
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 3213Sequence analysisPRO_0000393633Add
BLAST
Chaini33 – 370338Endopolygalacturonase APRO_0000393634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 50By similarity
Disulfide bondi209 ↔ 225By similarity
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi335 ↔ 340By similarity
Disulfide bondi359 ↔ 368By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ9P358.
SMRiQ9P358. Positions 33-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati162 – 19231PbH1 1Add
BLAST
Repeati193 – 21422PbH1 2Add
BLAST
Repeati215 – 23521PbH1 3Add
BLAST
Repeati244 – 26522PbH1 4Add
BLAST
Repeati273 – 29523PbH1 5Add
BLAST
Repeati307 – 35246PbH1 6Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

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.

Q9P358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSAKPLFCL ATLAGAALAA PAPSRATDFN KRSTCTFTDA ATASESKTSC
60 70 80 90 100
SDIVLKDITV PAGETLNLKD LNDGTTVTFE GTTTWEYEEW DGPLLRISGK
110 120 130 140 150
DITVTQSSDA VLNGNGAKWW DGEGTNGGKT KPKFFYAHDL DDSKISGLYI
160 170 180 190 200
KNTPVQAISV ESDNLVIEDV TIDNSDGDSE GGHNTDGFDI SESTYITITG
210 220 230 240 250
ATVKNQGDCV AINSGENIYF SGGTCSGGHG LSIGSVGGRD DNTVKNVTFI
260 270 280 290 300
DSTVSDSENG VRIKTVYDAT GTVEDITYSN IQLSGISDYG IVIEQDYENG
310 320 330 340 350
DPTGTPSNGV TISDVTLEDI TGSVDSDAVE IYILCGDGSC TDWTMSGIDI
360 370
TGGETSSDCE NVPSGASCSQ
Length:370
Mass (Da):38,661
Last modified:October 1, 2000 - v1
Checksum:iD329CE4AFC197057
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035082 Genomic DNA. Translation: BAA95408.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035082 Genomic DNA. Translation: BAA95408.1.

3D structure databases

ProteinModelPortaliQ9P358.
SMRiQ9P358. Positions 33-368.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28A_ASPAW.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Purification and characterization of acid-stable protopectinase produced by Aspergillus awamori in solid-state fermentation."
    Nagai M., Ozawa A., Katsuragi T., Sakai T.
    Biosci. Biotechnol. Biochem. 64:1337-1344(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-49, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 38854 / NBRC 4033.

Entry informationi

Entry nameiPGLRA_ASPAW
AccessioniPrimary (citable) accession number: Q9P358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 1, 2000
Last modified: October 14, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.