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Database: UniProt
Entry: F2Y9V8_GLORO
LinkDB: F2Y9V8_GLORO
Original site: F2Y9V8_GLORO 
ID   F2Y9V8_GLORO            Unreviewed;       142 AA.
AC   F2Y9V8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   RecName: Full=pectate lyase {ECO:0000256|ARBA:ARBA00012272};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
DE   Flags: Fragment;
GN   Name=pel1 {ECO:0000313|EMBL:AEA08777.1};
OS   Globodera rostochiensis (Golden nematode worm) (Heterodera rostochiensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=31243 {ECO:0000313|EMBL:AEA08777.1};
RN   [1] {ECO:0000313|EMBL:AEA08777.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Libelice {ECO:0000313|EMBL:AEA08810.1}, Obersteibach
RC   {ECO:0000313|EMBL:AEA08783.1}, and Trenta
RC   {ECO:0000313|EMBL:AEA08777.1};
RA   Geric Stare B.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pectinolytic enzyme consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins. Favors pectate, the
CC       anion, over pectin, the methyl ester. {ECO:0000256|ARBA:ARBA00025679}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000256|ARBA:ARBA00006463}.
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DR   EMBL; HQ850157; AEA08777.1; -; Genomic_DNA.
DR   EMBL; HQ850163; AEA08783.1; -; Genomic_DNA.
DR   EMBL; HQ850175; AEA08795.1; -; Genomic_DNA.
DR   EMBL; HQ850176; AEA08796.1; -; Genomic_DNA.
DR   EMBL; HQ850190; AEA08810.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Y9V8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:AEA08777.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEA08777.1"
FT   NON_TER         142
FT                   /evidence="ECO:0000313|EMBL:AEA08777.1"
SQ   SEQUENCE   142 AA;  15156 MW;  AA33F4B821D58376 CRC64;
     GGSGILNGAC DVKNGKMKYL MVLKHGVTIK NAIINTPGLG IYCEGSCVLE NIYYKKLCYH
     ATGFGYKSTG TSYTYQVIGG AGQGSPDKYF TQSGRGTTII KNFCAEGKYG KVWCSCGNCI
     DQMPRSVQIS NTKIQGPGLA II
//
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