ID K3VZG6_FUSPC Unreviewed; 233 AA.
AC K3VZG6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN ORFNames=FPSE_07485 {ECO:0000313|EMBL:EKJ72365.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ72365.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ72365.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ72365.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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 ECO:0000256|RuleBase:RU367009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000695,
CC ECO:0000256|RuleBase:RU367009};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|RuleBase:RU367009};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367009}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463, ECO:0000256|RuleBase:RU367009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKJ72365.1}.
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DR EMBL; AFNW01000195; EKJ72365.1; -; Genomic_DNA.
DR RefSeq; XP_009258878.1; XM_009260603.1.
DR AlphaFoldDB; K3VZG6; -.
DR EnsemblFungi; EKJ72365; EKJ72365; FPSE_07485.
DR GeneID; 20366103; -.
DR KEGG; fpu:FPSE_07485; -.
DR eggNOG; ENOG502QSM3; Eukaryota.
DR HOGENOM; CLU_044863_3_1_1; -.
DR OrthoDB; 66064at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR Pfam; PF03211; Pectate_lyase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367009};
KW Lyase {ECO:0000256|RuleBase:RU367009};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367009}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT CHAIN 19..233
FT /note="Pectate lyase"
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT /id="PRO_5025074765"
SQ SEQUENCE 233 AA; 24604 MW; E61D393896122E12 CRC64;
MHAPSILAVL SALPAAMACL GYTGGVPKAT GTKSLSAPRY LKKGEVFDAK WVRYDRGVKC
SGQSEGGEKD AVFVLEDGAT LRNVVIGANQ KEGVHCLGAC NLEFVWFEDV CEDAITIKGS
GTANIIGGGA YKAADKVIQH NGCGHVNIVN FYANDYGKVY RSCGNCKGNS KCKRSVHMEG
VTAVNGGELI GINTNLGDKA TYKNNCFPKT QCQGYKGCDK ANGECEPSKA SKC
//
