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Reviewed, UniProtKB/Swiss-Prot P15922 (PEHX_ERWCH)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Exo-poly-alpha-D-galacturonosidase
      Short name=Exo-PG
    EC=3.2.1.82
Gene names
Name: pehX
OrganismErwinia chrysanthemi
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Contributes significantly to bacterial utilization of polygalacturonate and the induction of pectate lyase in the presence of extracellular pectic polymers.

Catalytic activity

Hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate.

Subcellular location

Secreted. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 28 family.

Contains 1 fibronectin type-III domain.

Contains 4 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionexo-poly-alpha-galacturonosidase activity

Inferred from electronic annotation. Source: EC

polygalacturonase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 602575Exo-poly-alpha-D-galacturonosidase
PRO_0000024824

Regions

Domain29 – 143115Fibronectin type-III

Sites

Active site3951Proton donor By similarity
Active site4281 By similarity

Sequences

Sequence LengthMass (Da)Tools
P15922-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: C7F44689C343B34B

FASTA60264,444
        10         20         30         40         50         60 
MKVITFSRRS ALASIVATCL MSTPALAATA QAPQKLQIPT LSYDDHSVML VWDTPEDTSN 

        70         80         90        100        110        120 
ITDYQIYQNG QLIGLASQNN DKNSPAKPYI SAFYKSDAAN FHHRIVLQNA KVDGLKAGTD 

       130        140        150        160        170        180 
YQFTVRTVYA DGTTSNDSNT VTTTTTAVPK VINITQYGAK GDGTTLNTSA IQKAIDACPT 

       190        200        210        220        230        240 
GCRIDVPAGV FKTGALWLKS DMTLNLLQGA TLLGSDNAAD YPDAYKIYSY VSQVRPASLL 

       250        260        270        280        290        300 
NAIDKNSSAV GTFKNIRIVG KGIIDGNGWK RSADAKDELG NTLPQYVKSD NSKVSKDGIL 

       310        320        330        340        350        360 
AKNQVAAAVA TGMDTKTAYS QRRSSLVTLR GVQNAYIADV TIRNPANHGI MFLESENVVE 

       370        380        390        400        410        420 
NSVIHQTFNA NNGDGVEFGN SQNIMVFNSV FDTGDDSINF AAGMGQDAQK QEPSQNAWLF 

       430        440        450        460        470        480 
NNFFRHGHGA VVLGSHTGAG IVDVLAENNV ITQNDVGLRA KSAPAIGGGA HGIVFRNSAM 

       490        500        510        520        530        540 
KNLAKQAVIV TLSYADNNGT IDYTPAKVPA RFYDFTVKNV TVQDSTGSNP AIEITGDSSK 

       550        560        570        580        590        600 
DIWHSQFIFS NMKLSGVSPT SISDLSDSQF NNLTFSNLRS GSSPWKFGTV KNVTVDGKTV 


TP 

« Hide

References

[1]"Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16."
He S.Y., Collmer A.
J. Bacteriol. 172:4988-4995(1990) [PubMed: 2168372] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-40, SUBCELLULAR LOCATION.
Strain: EC16.
[2]"Proposed acquisition of an animal protein domain by bacteria."
Bork P., Doolittle R.F.
Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992) [PubMed: 1409594] [Abstract]
Cited for: DOMAIN FIBRONECTIN TYPE-III.

Cross-references

Sequence databases

M31308 Genomic DNA. Translation: AAA24842.1.
PIRA36715.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH28. Glycoside Hydrolase Family 28.

Enzyme and pathway databases

BRENDA3.2.1.82. 1459.

Family and domain databases

InterProIPR003961. FN_III.
IPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00041. fn3. 1 hit.
PF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00710. PbH1. 3 hits.
[Graphical view]
PROSITEPS50853. FN3. 1 hit.
PS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEHX_ERWCH
AccessionPrimary (citable) accession number: P15922
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents