ID X0CVC8_FUSOX Unreviewed; 233 AA.
AC X0CVC8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN ORFNames=FOQG_09714 {ECO:0000313|EMBL:EXK86442.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK86442.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK86442.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK86442.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH658385; EXK86442.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CVC8; -.
DR SMR; X0CVC8; -.
DR eggNOG; ENOG502QSM3; Eukaryota.
DR HOGENOM; CLU_044863_3_1_1; -.
DR Proteomes; UP000030663; 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:EXK86442.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367009}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT CHAIN 19..233
FT /note="Pectate lyase"
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT /id="PRO_5025093270"
SQ SEQUENCE 233 AA; 24586 MW; 90692185963F45A2 CRC64;
MHASSLLTLL TTLPAAMACL GYTGGVPKAT GTKSLSAPQY LKKGQVFDAK WVRYDRGVKC
SGQSEGGEKD AVFVLEDGAT LRNVVIGANQ KEGVHCLGAC NLEFVWFEDV CEDAISIKGS
GTANIIGGGA YKAADKVIQH NGCGHVNIVN FYANDYGKVY RSCGNCKGNS KCKRSVHMEG
VTAVNGGELI GINTNLGDKA TYSNNCYPKT QCQGYNGCDK SNGECEPSKA GKC
//
