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Protein

Endopolygalacturonase I

Gene

pgaI

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 5 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 sitei219 – 2191Proton donor
Active sitei241 – 2411

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.

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 aculeatus
Taxonomic identifieri5053 [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 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 3919Sequence analysisPRO_0000024762Add
BLAST
Chaini40 – 378339Endopolygalacturonase IPRO_0000024763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 61
Glycosylationi44 – 441O-linked (Man...)1 Publication
Glycosylationi46 – 461O-linked (Man...)1 Publication
Glycosylationi48 – 481O-linked (Man...)1 Publication
Glycosylationi52 – 521O-linked (Man...)1 Publication
Glycosylationi53 – 531O-linked (Man...)1 Publication
Glycosylationi55 – 551O-linked (Man...)1 Publication
Glycosylationi57 – 571O-linked (Man...)1 Publication
Glycosylationi62 – 621O-linked (Man...)1 Publication
Glycosylationi63 – 631O-linked (Man...)1 Publication
Glycosylationi73 – 731O-linked (Man...)1 Publication
Disulfide bondi221 ↔ 237
Glycosylationi258 – 2581N-linked (GlcNAc...)1 Publication
Disulfide bondi345 ↔ 350
Disulfide bondi369 ↔ 378

Keywords - PTMi

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

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 465Combined sources
Helixi47 – 493Combined sources
Helixi50 – 578Combined sources
Helixi58 – 603Combined sources
Beta strandi62 – 687Combined sources
Beta strandi77 – 793Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi122 – 1243Combined sources
Helixi127 – 1293Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi146 – 15813Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 1893Combined sources
Turni190 – 1934Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi221 – 23414Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi255 – 26814Combined sources
Beta strandi270 – 2789Combined sources
Beta strandi284 – 30926Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi322 – 33413Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi350 – 36415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA5X-ray2.00A40-378[»]
1IB4X-ray2.00A/B40-378[»]
ProteinModelPortaliO74213.
SMRiO74213. Positions 40-378.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74213.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati174 – 20431PbH1 1Add
BLAST
Repeati205 – 22622PbH1 2Add
BLAST
Repeati227 – 24721PbH1 3Add
BLAST
Repeati256 – 27722PbH1 4Add
BLAST
Repeati285 – 30723PbH1 5Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated
Contains 5 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. 5 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.

O74213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLNTTLLVS LALGAASVLA SPAPPAITAP PTAEEIAKRA TTCTFSGSNG
60 70 80 90 100
ASSASKSKTS CSTIVLSNVA VPSGTTLDLT KLNDGTHVIF SGETTFGYKE
110 120 130 140 150
WSGPLISVSG SDLTITGASG HSINGDGSRW WDGEGGNGGK TKPKFFAAHS
160 170 180 190 200
LTNSVISGLK IVNSPVQVFS VAGSDYLTLK DITIDNSDGD DNGGHNTDAF
210 220 230 240 250
DIGTSTYVTI SGATVYNQDD CVAVNSGENI YFSGGYCSGG HGLSIGSVGG
260 270 280 290 300
RSDNTVKNVT FVDSTIINSD NGVRIKTNID TTGSVSDVTY KDITLTSIAK
310 320 330 340 350
YGIVVQQNYG DTSSTPTTGV PITDFVLDNV HGSVVSSGTN ILISCGSGSC
360 370
SDWTWTDVSV SGGKTSSKCT NVPSGASC
Length:378
Mass (Da):38,528
Last modified:November 1, 1998 - v1
Checksum:iDC5B9B6E1D2059C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054893 mRNA. Translation: AAC23565.1.
AJ581480 mRNA. Translation: CAE46193.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054893 mRNA. Translation: AAC23565.1.
AJ581480 mRNA. Translation: CAE46193.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA5X-ray2.00A40-378[»]
1IB4X-ray2.00A/B40-378[»]
ProteinModelPortaliO74213.
SMRiO74213. Positions 40-378.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO74213.

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. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGLR1_ASPAC
AccessioniPrimary (citable) accession number: O74213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1998
Last modified: October 14, 2015
This is version 79 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

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.