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Reviewed, UniProtKB/Swiss-Prot Q9LFP5 (PEL19_ARATH)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Putative pectate lyase 19
    EC=4.2.2.2
Gene names
Ordered Locus Names: At5g15110
ORF Names: F2G14.230
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Cofactor

Binds 1 calcium ion. Required for its activity By similarity.

Pathway

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

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 472448Putative pectate lyase 19
PRO_0000024884

Sites

Active site3481 Potential
Metal binding2681Calcium By similarity
Metal binding2921Calcium By similarity
Metal binding2961Calcium By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9LFP5-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E0D84351D7F57D75

FASTA47253,851
        10         20         30         40         50         60 
MEMVRLSKLM FTFCIAVLIP TIRGNISELD EYWSQRADEA REFTLQAYHS DPYEIVDHFH 

        70         80         90        100        110        120 
ERHYDNSTDV TTPEEDGDAK PEEEEKEFIE MLGSSTNSTR RSLRGKGKGK WSKLKGPCTA 

       130        140        150        160        170        180 
SNPIDKCWRC RSDWAKRRKK LTRCVRGFGH RTTGGKRGRI YVVTSNLDED MVNPKPGTLR 

       190        200        210        220        230        240 
HAVIQKEPLW IIFKNDMSIR LNQELLINSH KTIDARGANV HVAHGAGITM QFVKNVIIHG 

       250        260        270        280        290        300 
LHIHHISESS GGMIRDSVDH FGMRTRADGD GLSIYGSSNI WLDHISMSKC QDGLIDAIVG 

       310        320        330        340        350        360 
STGITISNSH FTHHNDVMLL GAQNTNEADK HMQVTVAYNH FGKGLVQRMP RIRWGFVHVV 

       370        380        390        400        410        420 
NNDYTHWELY AIGGSQGPTI LSHGNRFIAP PHKPHYREVT KRDYASEDEW KHWNWRSDKD 

       430        440        450        460        470 
VFMNGAYFRQ SGNPQYKCAH TRQQMIKPKN GLAVSKLTKY AGALDCRVGR RC 

« Hide

References

[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

AL391146 Genomic DNA. Translation: CAC01830.1.
IPIIPI00944299.
PIRT51456.
UniGeneAt.50708

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Proteomic databases

PRIDEQ9LFP5.

Genome annotation databases

GenomeReviewsGene locus AT5G15110 in contig BA000015_GR.
KEGGath:AT5G15110.
NMPDRfig|3702.1.peg.23648.

Organism-specific databases

TAIRAt5g15110.

Phylogenomic databases

OMAGPCMATN.

Enzyme and pathway databases

BRENDA4.2.2.2. 302.

Gene expression databases

ArrayExpressQ9LFP5.
GenevestigatorQ9LFP5.
GermOnlineAT5G15110. Arabidopsis thaliana.

Family and domain databases

InterProIPR002022. Amb_allergen.
IPR018082. AmbAllergen.
IPR007524. Pec_lyase_N.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00544. Pec_lyase_C. 1 hit.
PF04431. Pec_lyase_N. 1 hit.
[Graphical view]
PRINTSPR00807. AMBALLERGEN.
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEL19_ARATH
AccessionPrimary (citable) accession number: Q9LFP5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

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