ID A0A4Q4WQ46_9PEZI Unreviewed; 244 AA.
AC A0A4Q4WQ46;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN ORFNames=DL769_011092 {ECO:0000313|EMBL:RYP49303.1};
OS Monosporascus sp. CRB-8-3.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211644 {ECO:0000313|EMBL:RYP49303.1, ECO:0000313|Proteomes:UP000292472};
RN [1] {ECO:0000313|EMBL:RYP49303.1, ECO:0000313|Proteomes:UP000292472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRB-8-3 {ECO:0000313|EMBL:RYP49303.1,
RC ECO:0000313|Proteomes:UP000292472};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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 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|ARBA:ARBA00004613,
CC 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:RYP49303.1}.
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DR EMBL; QJNZ01001486; RYP49303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4WQ46; -.
DR STRING; 2211644.A0A4Q4WQ46; -.
DR OrthoDB; 441042at2759; -.
DR Proteomes; UP000292472; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:TreeGrafter.
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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367009};
KW Lyase {ECO:0000256|RuleBase:RU367009};
KW Reference proteome {ECO:0000313|Proteomes:UP000292472};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367009}.
SQ SEQUENCE 244 AA; 25508 MW; EAA21E4F559CB6F4 CRC64;
MKFTATVVTS SILASVSGQT LNIPTRSGSI ISLDSPMVIS GSRDFSNQEY DRGRDCDTDE
ETGSDSAVFI LENGASISNV IIGERALEGV HCRGSCTLTN VWFRDVCEDA ISALGTGDVL
IRGGGAQDAQ DKVVQHNGRG TVTIRDYTVV NAGKLYRSCG DCTNNGGPRN VVVQNARVRG
MTSELVGINS NYGDTATISG SCGVSKKTCQ EYKGVNKGDG SSSKVSTTAN CRGDQGKLSA
LPAC
//
