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Database: UniProt
Entry: H0EWL4_GLAL7
LinkDB: H0EWL4_GLAL7
Original site: H0EWL4_GLAL7 
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
//
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