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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei212 – 2121Proton donorPROSITE-ProRule annotation
Active sitei234 – 2341PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881H → P: Reduces activity by 98.2%. Lowers affinity for substrate 50-fold. 1 Publication
Mutagenesisi191 – 1911D → A: Loss of activity. No effect on Km for substrate. 1 Publication
Mutagenesisi212 – 2132DD → EE: Loss of activity. No effect on Km for substrate. 1 Publication
Mutagenesisi212 – 2132DD → NN: Loss of activity. No effect on Km for substrate. 1 Publication
Mutagenesisi267 – 2671R → A: Loss of activity. Lowers affinity for substrate over 10-fold. 1 Publication
Mutagenesisi269 – 2691K → E: Reduces activity by 99.87%. Lowers affinity for substrate over 10-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 373349PolygalacturonasePRO_0000024786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 42
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Disulfide bondi214 ↔ 230
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence analysis
Disulfide bondi340 ↔ 345
Disulfide bondi364 ↔ 371

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314Combined sources
Helixi32 – 343Combined sources
Helixi35 – 417Combined sources
Beta strandi43 – 475Combined sources
Beta strandi58 – 603Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 775Combined sources
Beta strandi87 – 948Combined sources
Beta strandi96 – 994Combined sources
Beta strandi104 – 1063Combined sources
Helixi109 – 1113Combined sources
Beta strandi127 – 14317Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi150 – 1589Combined sources
Beta strandi160 – 17011Combined sources
Helixi172 – 1743Combined sources
Turni179 – 1835Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi199 – 20911Combined sources
Beta strandi214 – 23320Combined sources
Beta strandi236 – 24510Combined sources
Beta strandi248 – 27124Combined sources
Beta strandi276 – 30227Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi313 – 32917Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi345 – 3528Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi366 – 3694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG8X-ray1.73A25-373[»]
ProteinModelPortaliQ07181.
SMRiQ07181. Positions 25-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07181.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati136 – 15823PbH1 1Add
BLAST
Repeati159 – 19739PbH1 2Add
BLAST
Repeati198 – 21922PbH1 3Add
BLAST
Repeati220 – 24021PbH1 4Add
BLAST
Repeati249 – 27022PbH1 5Add
BLAST
Repeati278 – 30023PbH1 6Add
BLAST
Repeati312 – 33322PbH1 7Add
BLAST
Repeati345 – 36925PbH1 8Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG8X-ray1.73A25-373[»]
ProteinModelPortaliQ07181.
SMRiQ07181. Positions 25-373.
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...

Publicationsi

  1. "Cloning and characterization of a gene encoding the endopolygalacturonase of Fusarium moniliforme."
    Caprari C., Richter A., Bergmann C., Lo Cicero S., Salvi G., Cervone F., de Lorenzo G.
    Mycol. Res. 97:497-505(1993)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)."
    Federici L., Caprari C., Mattei B., Savino C., Di Matteo A., De Lorenzo G., Cervone F., Tsernoglou D.
    Proc. Natl. Acad. Sci. U.S.A. 98:13425-13430(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 25-373, MUTAGENESIS OF HIS-188; ASP-191; 212-ASP-ASP-213; ARG-267 AND LYS-269.

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: October 14, 2015
This is version 85 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.