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Q47474 (PMEB_DICD3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pectinesterase B

Short name=PE B
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase B
Gene names
Name:pemB
Ordered Locus Names:Dda3937_03435
OrganismDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) [Complete proteome] [HAMAP]
Taxonomic identifier198628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in the degradation of methylated oligogalacturonides present in the periplasm.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Cell outer membrane; Lipid-anchor.

Induction

By pectin.

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Keywords
   Cellular componentCell membrane
Cell outer membrane
Membrane
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   PTMLipoprotein
Palmitate
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell wall

Inferred from electronic annotation. Source: InterPro

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 433412Pectinesterase B
PRO_0000023499

Sites

Active site2591Proton donor By similarity
Active site2921Nucleophile By similarity
Binding site2021Substrate By similarity
Binding site2361Substrate By similarity
Binding site3561Substrate By similarity
Binding site3581Substrate By similarity

Amino acid modifications

Lipidation221N-palmitoyl cysteine Ref.1
Lipidation221S-diacylglycerol cysteine Probable

Experimental info

Sequence conflict245 – 25814DRVQL…LLSRQ → ESGATGKCPPAQPS in CAA59151. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q47474 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 73C2B9E8ED50281F

FASTA43347,190
        10         20         30         40         50         60 
MSLTHYSGLA AAVSMSLILT ACGGQTPNSA RFQPVFPGTV SRPVLSAQEA GRFTPQHYFA 

        70         80         90        100        110        120 
HGGEYAKPVA DGWTPTPIDT SRVTAAYVVG PRAGVAGATH TSIQQAVNAA LRQHPGQTRV 

       130        140        150        160        170        180 
YIKLLPGTYT GTVYVPEGAP PLTLFGAGDR PEQVVVSLAL DSMMSPADYR ARVNPHGQYQ 

       190        200        210        220        230        240 
PADPAWYMYN ACATKAGATI NTTCSAVMWS QSNDFQLKNL TVVNALLDTV DSGTHQAVAL 

       250        260        270        280        290        300 
RTDGDRVQLE NVRLLSRQDT FFVNTSDRQN SYVTDHYSRA YIKDSYIEGD VDYVFGRATA 

       310        320        330        340        350        360 
VFDRVRFHTV SSRGSKEAYV FAPDSIPSVK YGFLVINSQL TGDNGYRGAQ KAKLGRAWDQ 

       370        380        390        400        410        420 
GAKQTGYLPG KTANGQLVIR DSTIDSSYDL ANPWGAAATT DRPFKGNISP QRDLDDIHFN 

       430 
RLWEYNTQVL LHE 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of pectin methylesterase B, an outer membrane lipoprotein of Erwinia chrysanthemi 3937."
Shevchik V.E., Condemine G., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.
Mol. Microbiol. 19:455-466(1996) [PubMed: 8830237] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PALMITOYLATION.
Strain: 3937.
[2]"Complete genome sequence of Dickeya dadantii 3937."
International Erwinia Consortium
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 3937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84665 Genomic DNA. Translation: CAA59151.1.
CP002038 Genomic DNA. Translation: ADM98093.1.
PIRS70914.
RefSeqYP_003882650.1. NC_014500.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9733317.
GenomeReviewsGene locus Dda3937_03435 in contig CP002038_GR.
KEGGddd:Dda3937_03435.
PATRIC42316098. VBIDicDad25310_1873.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
KOK01051.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMEB_DICD3
AccessionPrimary (citable) accession number: Q47474
Secondary accession number(s): E0SL58
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 30, 2010
Last modified: January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families