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Protein

Endopolygalacturonase I

Gene

pgaI

Organism
Aspergillus niger
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei207 – 2071Proton donorPROSITE-ProRule annotation
Active sitei229 – 2291Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BRENDAi3.2.1.15. 518.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28I_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Endopolygalacturonase I (EC:3.2.1.15)
Alternative name(s):
Pectinase 1
Polygalacturonase I
Short name:
PG-I
Gene namesi
Name:pgaI
Synonyms:pg1, pga1
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei8269. Asp n Pectinase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 3113Sequence analysisPRO_0000024768Add
BLAST
Chaini32 – 368337Endopolygalacturonase IPRO_0000024769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 50
Glycosylationi44 – 441O-linked (Man)1 Publication
Glycosylationi46 – 461O-linked (Man)1 Publication
Disulfide bondi209 ↔ 225
Glycosylationi246 – 2461N-linked (GlcNAc...)1 Publication
Disulfide bondi335 ↔ 340
Disulfide bondi359 ↔ 368

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP26213.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00001113.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 395Combined sources
Helixi40 – 467Combined sources
Helixi47 – 493Combined sources
Beta strandi51 – 577Combined sources
Beta strandi76 – 8510Combined sources
Beta strandi94 – 963Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi111 – 1133Combined sources
Helixi116 – 1183Combined sources
Turni124 – 1263Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi135 – 14713Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi158 – 16912Combined sources
Beta strandi171 – 1733Combined sources
Helixi177 – 1804Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi194 – 2007Combined sources
Beta strandi202 – 22221Combined sources
Beta strandi224 – 24017Combined sources
Beta strandi243 – 25614Combined sources
Beta strandi258 – 2669Combined sources
Beta strandi272 – 29827Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 32413Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi340 – 35415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHCX-ray1.70A/B/C/D/E/F33-368[»]
ProteinModelPortaliP26213.
SMRiP26213. Positions 33-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26213.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati140 – 16122PbH1 1Add
BLAST
Repeati162 – 19231PbH1 2Add
BLAST
Repeati193 – 21422PbH1 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

Phylogenomic databases

eggNOGiCOG5434. LUCA.

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.

P26213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSYQLLGLA AVGSLVSAAP APSRVSEFAK KASTCTFTSA SEASESISSC
60 70 80 90 100
SDVVLSSIEV PAGETLDLSD AADGSTITFE GTTSFGYKEW KGPLIRFGGK
110 120 130 140 150
DLTVTMADGA VIDGDGSRWW DSKGTNGGKT KPKFMYIHDV EDSTFKGINI
160 170 180 190 200
KNTPVQAISV QATNVHLNDF TIDNSDGDDN GGHNTDGFDI SESTGVYISG
210 220 230 240 250
ATVKNQDDCI AINSGESISF TGGTCSGGHG LSIGSVGGRD DNTVKNVTIS
260 270 280 290 300
DSTVSNSANG VRIKTIYKET GDVSEITYSN IQLSGITDYG IVIEQDYENG
310 320 330 340 350
SPTGTPSTGI PITDVTVDGV TGTLEDDATQ VYILCGDGSC SDWTWSGVDL
360
SGGKTSDKCE NVPSGASC
Length:368
Mass (Da):38,108
Last modified:May 1, 1992 - v1
Checksum:iCD9B46A9A99B5102
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58892 Genomic DNA. Translation: CAA41693.1.
PIRiS17980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58892 Genomic DNA. Translation: CAA41693.1.
PIRiS17980.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHCX-ray1.70A/B/C/D/E/F33-368[»]
ProteinModelPortaliP26213.
SMRiP26213. Positions 33-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00001113.

Protein family/group databases

Allergomei8269. Asp n Pectinase.
CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28I_ASPNG.

Proteomic databases

PaxDbiP26213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5434. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.15. 518.

Miscellaneous databases

EvolutionaryTraceiP26213.

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...

Entry informationi

Entry nameiPGLR1_ASPNG
AccessioniPrimary (citable) accession number: P26213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 11, 2015
This is version 96 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.