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Reviewed, UniProtKB/Swiss-Prot P22751 (PELX_ERWCH)

Last modified April 14, 2009. Version 44. 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:
    Pectate disaccharide-lyase
    EC=4.2.2.9
Alternative name(s):
    Exopolygalacturonate lyase
      Short name=ExoPL
Gene names
Name: pelX
OrganismErwinia chrysanthemi
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin.

Cofactor

Calcium.

Sequence similarities

Belongs to the polysaccharide lyase 9 family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate disaccharide-lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1
Chain27 – 749723Pectate disaccharide-lyase
PRO_0000024935

Sequences

Sequence LengthMass (Da)Tools
P22751-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 449BB25C23F2A9B5

FASTA74982,240
        10         20         30         40         50         60 
MKYAASGLLS VALNSLLLLG SNQRFATQDV APVWRGIAFG QSTDVNFATN VLPEKVGVND 

        70         80         90        100        110        120 
VTINGKKLTV NDKADLSAPI TIESRGGKIA NTHDGLTFFY TQLPANVNFT LQSDVTVEQF 

       130        140        150        160        170        180 
GPESDAKPNA QEGAGLLVRD ILGVPRQEPL KEGYEEFPAA SNMVMNAIMT QDKKSKTEVK 

       190        200        210        220        230        240 
MQLISRNGVT QPWGNTNAEI TRTSYQEKIN LEQTPTFRLK LERTNDGFIT AYAPKGSDQW 

       250        260        270        280        290        300 
VSKTVKGADL VTHQDKDHYY VGFFASRNAK ITISNASLTT SPANTKPSAP FKAETTAPLL 

       310        320        330        340        350        360 
QVASSSLSTS DTYPVQARVN YNGTVEVFQN GKSLGKPQRV RAGDDFSLTT RLTQQKSDFK 

       370        380        390        400        410        420 
LVYIPSEGED KTAKETSFSV EKITLADARN LYVSPEGKAG NDGSKNAPLD IKTAINALPG 

       430        440        450        460        470        480 
GGTLWLMDGD YSATVIPVSA TQRKGMKTLM PVGKKAVFHG LQLNASYWKV KGIEITEKSF 

       490        500        510        520        530        540 
RIEGSHNQIE RLLAHHCDNT GIQVSSSDNV GRPLWASHNL ILNSESHSNQ HPSKKDADGF 

       550        560        570        580        590        600 
AVKMRVGEGN VIRGAFSHDN VDDGFDLFNK IEDGPNGAVM IENSISLNNT SNGFKLGGEG 

       610        620        630        640        650        660 
QPVAHQVKNS IAIGNHMDGF SDNFNPGALQ VSNNIALDNV RFNFIFRPSP YYGYEKQGIF 

       670        680        690        700        710        720 
KNNVSLRTQP GKYDDAVVGR LDASNYFIRI IERSTVRVRK SRRRITNPSR CQRSSAGMKK 

       730        740 
AACNWVIFCR RSNRHKTQRH RNRYPSTPA 

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References

[1]"Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product."
Brooks A.D., Yang He S., Gold S., Keen N.T., Collmer A., Hutcheson S.W.
J. Bacteriol. 172:6950-6958(1990) [PubMed: 2254266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-46.
Strain: EC16.

Cross-references

Sequence databases

M62739 Genomic DNA. Translation: AAA24850.1.
PIRA37839.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyPL9. Polysaccharide Lyase Family 9.

Enzyme and pathway databases

BRENDA4.2.2.9. 1459.

Family and domain databases

InterProIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
SMARTSM00710. PbH1. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePELX_ERWCH
AccessionPrimary (citable) accession number: P22751
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 14, 2009
This is version 44 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