ID H0EWL4_GLAL7 Unreviewed; 364 AA.
AC H0EWL4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN ORFNames=M7I_7184 {ECO:0000313|EMBL:EHK97044.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97044.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK97044.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(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:EHK97044.1}.
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DR EMBL; AGUE01000211; EHK97044.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EWL4; -.
DR HOGENOM; CLU_044863_2_1_1; -.
DR InParanoid; H0EWL4; -.
DR Proteomes; UP000005446; 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 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, ECO:0000313|EMBL:EHK97044.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367009}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT CHAIN 20..364
FT /note="Pectate lyase"
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT /id="PRO_5025073496"
FT REGION 57..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 36302 MW; 7903EFDF8A26811F CRC64;
MKFSNVQLAI LAFSLGVSAA PSNKYTGAIF ARECDDEVTS TAVSSATFTA PVNLAAETSE
ATTKKASKTS KAKTTKTKAT EATTATDAAD DADDVDADVT TTSKAKSASA TPAASDAASS
KTGKASSAAT TASPTTGSSS GSSGGSLPAS SGTSVLSAAQ TIAAGGSFDG GMTMFDRGVS
CTGQAEGGDS DAVFNIEEGG SLSNVIIGPN QIEGVHCQGA CTLTNVWWSA VCEDAFTIKL
QDAGATTTIN GGGAFGAEDK VIQHNGAGTV VINDFTADTF GKLYRSCGNC KASNERHVVM
KGVSASNGDI LVGINSNFGD TATLDGSKIT SVKTVCQEFE GTTPGNEPAT VDTKTSCLGA
DGQL
//