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Protein

Polygalacturonase

Gene

PGA

Organism
Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
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)DescriptionActionsGraphical viewLength
Active sitei212Proton donorPROSITE-ProRule annotation1
Active sitei234PROSITE-ProRule annotation1

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

SABIO-RKQ07181.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28A_GIBMO.

Names & Taxonomyi

Protein namesi
Recommended name:
Polygalacturonase (EC:3.2.1.15)
Short name:
PG
Alternative name(s):
FmPG
Pectinase
Gene namesi
Name:PGA
OrganismiGibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Taxonomic identifieri5127 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium fujikuroi species complex

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi188H → P: Reduces activity by 98.2%. Lowers affinity for substrate 50-fold. 1 Publication1
Mutagenesisi191D → A: Loss of activity. No effect on Km for substrate. 1 Publication1
Mutagenesisi212 – 213DD → EE: Loss of activity. No effect on Km for substrate. 1 Publication2
Mutagenesisi212 – 213DD → NN: Loss of activity. No effect on Km for substrate. 1 Publication2
Mutagenesisi267R → A: Loss of activity. Lowers affinity for substrate over 10-fold. 1 Publication1
Mutagenesisi269K → E: Reduces activity by 99.87%. Lowers affinity for substrate over 10-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000002478625 – 373PolygalacturonaseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 42
Glycosylationi65N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi214 ↔ 230
Glycosylationi280N-linked (GlcNAc...)Sequence analysis1
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi340 ↔ 345
Disulfide bondi364 ↔ 371

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Helixi32 – 34Combined sources3
Helixi35 – 41Combined sources7
Beta strandi43 – 47Combined sources5
Beta strandi58 – 60Combined sources3
Beta strandi68 – 71Combined sources4
Beta strandi73 – 77Combined sources5
Beta strandi87 – 94Combined sources8
Beta strandi96 – 99Combined sources4
Beta strandi104 – 106Combined sources3
Helixi109 – 111Combined sources3
Beta strandi127 – 143Combined sources17
Beta strandi145 – 147Combined sources3
Beta strandi150 – 158Combined sources9
Beta strandi160 – 170Combined sources11
Helixi172 – 174Combined sources3
Turni179 – 183Combined sources5
Beta strandi192 – 197Combined sources6
Beta strandi199 – 209Combined sources11
Beta strandi214 – 233Combined sources20
Beta strandi236 – 245Combined sources10
Beta strandi248 – 271Combined sources24
Beta strandi276 – 302Combined sources27
Beta strandi304 – 307Combined sources4
Beta strandi313 – 329Combined sources17
Beta strandi333 – 339Combined sources7
Beta strandi345 – 352Combined sources8
Beta strandi354 – 356Combined sources3
Beta strandi366 – 369Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HG8X-ray1.73A25-373[»]
ProteinModelPortaliQ07181.
SMRiQ07181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07181.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati136 – 158PbH1 1Add BLAST23
Repeati159 – 197PbH1 2Add BLAST39
Repeati198 – 219PbH1 3Add BLAST22
Repeati220 – 240PbH1 4Add BLAST21
Repeati249 – 270PbH1 5Add BLAST22
Repeati278 – 300PbH1 6Add BLAST23
Repeati312 – 333PbH1 7Add BLAST22
Repeati345 – 369PbH1 8Add BLAST25

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated
Contains 8 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. 8 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.

Q07181-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRNIVSRLC SQLFALPSSS LQERDPCSVT EYSGLATAVS SCKNIVLNGF
60 70 80 90 100
QVPTGKQLDL SSLQNDSTVT FKGTTTFATT ADNDFNPIVI SGSNITITGA
110 120 130 140 150
SGHVIDGNGQ AYWDGKGSNS NSNQKPDHFI VVQKTTGNSK ITNLNIQNWP
160 170 180 190 200
VHCFDITGSS QLTISGLILD NRAGDKPNAK SGSLPAAHNT DGFDISSSDH
210 220 230 240 250
VTLDNNHVYN QDDCVAVTSG TNIVVSNMYC SGGHGLSIGS VGGKSDNVVD
260 270 280 290 300
GVQFLSSQVV NSQNGCRIKS NSGATGTINN VTYQNIALTN ISTYGVDVQQ
310 320 330 340 350
DYLNGGPTGK PTNGVKISNI KFIKVTGTVA SSAQDWFILC GDGSCSGFTF
360 370
SGNAITGGGK TSSCNYPTNT CPS
Length:373
Mass (Da):38,915
Last modified:October 1, 1994 - v1
Checksum:iD77BCACAC7FFBD8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02239 Genomic DNA. Translation: AAA74586.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02239 Genomic DNA. Translation: AAA74586.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HG8X-ray1.73A25-373[»]
ProteinModelPortaliQ07181.
SMRiQ07181.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28A_GIBMO.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ07181.

Miscellaneous databases

EvolutionaryTraceiQ07181.

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

Entry informationi

Entry nameiPGLR_GIBFU
AccessioniPrimary (citable) accession number: Q07181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 87 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.