ID T0L703_COLGC Unreviewed; 416 AA.
AC T0L703;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN ORFNames=CGLO_17300 {ECO:0000313|EMBL:EQB44000.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB44000.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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 -!- 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 -!- 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}.
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:EQB44000.1}.
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DR EMBL; AMYD01004130; EQB44000.1; -; Genomic_DNA.
DR AlphaFoldDB; T0L703; -.
DR STRING; 1237896.T0L703; -.
DR HOGENOM; CLU_044863_2_2_1; -.
DR OMA; QGNWNLN; -.
DR OrthoDB; 2472266at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
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 PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR Pfam; PF03211; Pectate_lyase; 1.
DR PRINTS; PR01228; EGGSHELL.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EQB44000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..416
FT /note="Probable pectate lyase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004579780"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 40692 MW; 0D3B80614555CFA7 CRC64;
MASRLVLFTL AALGAANPIN PGGRDAERPA RRHIGGVGHL ARAVMAPQQA KVEVRFAGPG
GGGPGNNGSC EDDGSDVGSK ADPSTDKSKD KSKDKTKDKS KDKSKDKSKD KNKDKNKDKG
SGSGSGSGSG SGSGSGSGSG SGGSKSGGGK SGGSTGGGGS SSGGGGAYLG GGGSSANNGT
TPGGGGGSSG GGGGLQKTFP TPAGTENLSA VKTITGVFDG GMKLFDRVPS TCTGGEGNRN
DAAFILEDGA TLSNAIIGGG AGEGVQCVGS CTLENVWWDK VCEDAATFRQ TGGKSTVRGG
GARGGSDKVF QHNGGGEVEV IDFYAQNIGQ LYRSCGNCKE QTARTSTFTN IYVDGAKTIV
HVNGNLGDKA TVNGACILGG ATVCKNSKGV TGGGEPGDAP NDPNVCSETN VKTSGC
//
