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Reviewed, UniProtKB/Swiss-Prot Q8RJP2 (RHIE_DICD3)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Rhamnogalacturonate lyase
      Short name=Rhamnogalacturonase
    EC=4.2.2.-
Gene names
Name: rhiE
OrganismDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Taxonomic identifier198628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Is required for the full virulence of E.chrysanthemi strain 3937 as it is involved in rotting of plant tissue.

Catalytic activity

Cleaves the alpha-1,4 linkage of RG-I backbone between a rhamnose and a galacturonate, thereby creating an unsaturated bond between carbons 4 and 5 of the galacturonate residue.

Subcellular location

Secreted. Note: Via the type II out secretion pathway.

Induction

By rhamnose.

Miscellaneous

Contrary to other proteins secreted by the Out pathway, rhiE contains no disulfide bond.

Sequence similarities

Belongs to the polysaccharide lyase 4 family.

Caution

Both Met-1 and Met-3 seem to be able to act as initiation codons.

biophysicochemical properties

pH dependence:

Optimum pH is 6.0.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

lyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 578551Rhamnogalacturonate lyase
PRO_0000024914

Sequences

Sequence LengthMass (Da)Tools
Q8RJP2-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 82B177C96ABA1C47

FASTA57864,978
        10         20         30         40         50         60 
MHMNKPLQAW RTPLLTLIFV LPLTATGAVK LTLDGMNSTL DNGLLKVRFG ADGSAKEVWK 

        70         80         90        100        110        120 
GGTNLISRLS GAARDPDKNR SFYLDYYSGG VNEFVPERLE VIKQTPDQVH LAYIDDQNGK 

       130        140        150        160        170        180 
LRLEYHLIMT RDVSGLYSYV VAANTGSAPV TVSELRNVYR FDATRLDTLF NSIRRGTPLL 

       190        200        210        220        230        240 
YDELEQLPKV QDETWRLPDG SVYSKYDFAG YQRESRYWGV MGNGYGAWMV PASGEYYSGD 

       250        260        270        280        290        300 
ALKQELLVHQ DAIILNYLTG SHFGTPDMVA QPGFEKLYGP WLLYINQGND RELVADVSRR 

       310        320        330        340        350        360 
AEHERASWPY RWLDDARYPR QRATVSGRLR TEAPHATVVL NSSAENFDIQ TTGYLFSART 

       370        380        390        400        410        420 
NRDGRFSLSN VPPGEYRLSA YADGGTQIGL LAQQTVRVEG KKTRLGQIDA RQPAPLAWAI 

       430        440        450        460        470        480 
GQADRRADEF RFGDKPRQYR WQTEVPADLT FEIGKSRERK DWYYAQTQPG SWHILFNTRT 

       490        500        510        520        530        540 
PEQPYTLNIA IAAASNNGMT TPASSPQLAV KLNGQLLTTL KYDNDKSIYR GAMQSGRYHE 

       550        560        570 
AHIPLPAGAL QQGGNRITLE LLGGMVMYDA ITLTETPQ 

« Hide

References

[1]"Rhamnogalacturonate lyase RhiE is secreted by the out system in Erwinia chrysanthemi."
Laatu M., Condemine G.
J. Bacteriol. 185:1642-1649(2003) [PubMed: 12591882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION.

Cross-references

Sequence databases

AJ438339 Genomic DNA. Translation: CAD27359.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyPL4. Polysaccharide Lyase Family 4.

Family and domain databases

InterProIPR010325. Rhamnogal_lyase.
[Graphical view]
PfamPF06045. Rhamnogal_lyase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHIE_DICD3
AccessionPrimary (citable) accession number: Q8RJP2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 37 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

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