ID A0A010QM42_9PEZI Unreviewed; 237 AA.
AC A0A010QM42;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN ORFNames=CFIO01_03096 {ECO:0000313|EMBL:EXF77775.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF77775.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF77775.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF77775.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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|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:EXF77775.1}.
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DR EMBL; JARH01000682; EXF77775.1; -; Genomic_DNA.
DR RefSeq; XP_007598615.1; XM_007598553.1.
DR AlphaFoldDB; A0A010QM42; -.
DR STRING; 1445577.A0A010QM42; -.
DR KEGG; cfj:CFIO01_03096; -.
DR eggNOG; ENOG502QSM3; Eukaryota.
DR HOGENOM; CLU_044863_3_1_1; -.
DR OrthoDB; 66064at2759; -.
DR Proteomes; UP000020467; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367009};
KW Lyase {ECO:0000256|RuleBase:RU367009, ECO:0000313|EMBL:EXF77775.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367009}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT CHAIN 21..237
FT /note="Pectate lyase"
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT /id="PRO_5025087104"
SQ SEQUENCE 237 AA; 25244 MW; 73B0AD95EEA5C791 CRC64;
MQFLKFGLVP MLAALPSAFA CNGYTGGVPK ATGTVTSKSY IEIKAGQVYD GKWQRFDRGS
GACGGQSEGD YKDSVFYIQA GGTLKNAIIG KNQAEGVHCN GHCTLEFVWF EDVCEDAISI
KNDKAGTQSW IVGGGAYHAS DKVIQHNGCG TVNVINYYVE DYGKLYRSCG NCKTQCKRNV
YMEGVTAKNG GELAGINLTY KDTATLKNVC ADTKTKCQMY NGCAGGCEPS KAGTCSG
//
