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Protein

Endo-polygalacturonase

Gene

pehA

Organism
Pectobacterium sp. (strain SCC3193)
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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei249Proton donorPROSITE-ProRule annotation1
Active sitei277Curated1

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:
Endo-polygalacturonase (EC:3.2.1.15)
Gene namesi
Name:pehA
Ordered Locus Names:W5S_3318
OrganismiPectobacterium sp. (strain SCC3193)
Taxonomic identifieri1166016 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaePectobacterium
Proteomesi
  • UP000008044 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000002475924 – 402Endo-polygalacturonaseAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 62
Disulfide bondi115 ↔ 125

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 45Combined sources6
Beta strandi48 – 50Combined sources3
Helixi52 – 59Combined sources8
Beta strandi67 – 71Combined sources5
Beta strandi73 – 81Combined sources9
Beta strandi90 – 93Combined sources4
Beta strandi98 – 101Combined sources4
Helixi106 – 108Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi128 – 133Combined sources6
Beta strandi138 – 140Combined sources3
Beta strandi142 – 146Combined sources5
Beta strandi154 – 158Combined sources5
Helixi162 – 170Combined sources9
Beta strandi179 – 184Combined sources6
Beta strandi186 – 196Combined sources11
Beta strandi202 – 207Combined sources6
Beta strandi209 – 219Combined sources11
Beta strandi229 – 234Combined sources6
Beta strandi236 – 242Combined sources7
Beta strandi244 – 246Combined sources3
Beta strandi251 – 256Combined sources6
Beta strandi263 – 273Combined sources11
Beta strandi275 – 277Combined sources3
Beta strandi279 – 300Combined sources22
Beta strandi302 – 308Combined sources7
Turni311 – 313Combined sources3
Beta strandi316 – 329Combined sources14
Beta strandi331 – 337Combined sources7
Beta strandi350 – 361Combined sources12
Beta strandi366 – 370Combined sources5
Beta strandi378 – 386Combined sources9
Beta strandi392 – 401Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHEX-ray1.90A27-402[»]
ProteinModelPortaliP26509.
SMRiP26509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26509.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK01184.
OMAiYQDITSK.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[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.

P26509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYQSGKRVL SLSLGLIGLF SASAWASDSR TVSEPKTPSS CTTLKADSST
60 70 80 90 100
ATSTIQKALN NCDQGKAVRL SAGSTSVFLS GPLSLPSGVS LLIDKGVTLR
110 120 130 140 150
AVNNAKSFEN APSSCGVVDK NGKGCDAFIT AVSTTNSGIY GPGTIDGQGG
160 170 180 190 200
VKLQDKKVSW WELAADAKVK KLKQNTPRLI QINKSKNFTL YNVSLINSPN
210 220 230 240 250
FHVVFSDGDG FTAWKTTIKT PSTARNTDGI DPMSSKNITI AYSNIATGDD
260 270 280 290 300
NVAIKAYKGR AETRNISILH NDFGTGHGMS IGSETMGVYN VTVDDLKMNG
310 320 330 340 350
TTNGLRIKSD KSAAGVVNGV RYSNVVMKNV AKPIVIDTVY EKKEGSNVPD
360 370 380 390 400
WSDITFKDVT SETKGVVVLN GENAKKPIEV TMKNVKLTSD STWQIKNVNV

KK
Length:402
Mass (Da):42,853
Last modified:August 1, 1992 - v1
Checksum:iC1902D8C5388B6B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51701 Genomic DNA. Translation: CAA35998.1.
CP003415 Genomic DNA. Translation: AFI91392.1.
PIRiS11772.
RefSeqiWP_014700877.1. NC_017845.1.

Genome annotation databases

EnsemblBacteriaiAFI91392; AFI91392; W5S_3318.
KEGGipec:W5S_3318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51701 Genomic DNA. Translation: CAA35998.1.
CP003415 Genomic DNA. Translation: AFI91392.1.
PIRiS11772.
RefSeqiWP_014700877.1. NC_017845.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHEX-ray1.90A27-402[»]
ProteinModelPortaliP26509.
SMRiP26509.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFI91392; AFI91392; W5S_3318.
KEGGipec:W5S_3318.

Phylogenomic databases

KOiK01184.
OMAiYQDITSK.

Miscellaneous databases

EvolutionaryTraceiP26509.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGLR2_PECSS
AccessioniPrimary (citable) accession number: P26509
Secondary accession number(s): K4FKA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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.