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Database: UniProt
Entry: X0KVF8_FUSOX
LinkDB: X0KVF8_FUSOX
Original site: X0KVF8_FUSOX 
ID   X0KVF8_FUSOX            Unreviewed;       240 AA.
AC   X0KVF8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE            EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
GN   ORFNames=FOTG_14255 {ECO:0000313|EMBL:EXM17563.1};
OS   Fusarium oxysporum f. sp. vasinfectum 25433.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM17563.1};
RN   [1] {ECO:0000313|EMBL:EXM17563.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM17563.1};
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 Cotton.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXM17563.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM17563.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum Cotton.";
RL   Submitted (MAR-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}.
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DR   EMBL; KK035214; EXM17563.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0KVF8; -.
DR   HOGENOM; CLU_044863_3_1_1; -.
DR   Proteomes; UP000030701; 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:EXM17563.1};
KW   Secreted {ECO:0000256|RuleBase:RU367009};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..240
FT                   /note="Pectate lyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012135884"
SQ   SEQUENCE   240 AA;  24873 MW;  45C0A180305704E1 CRC64;
     MKYTAILALA GVSSAAVTKT LPKSAGATSF PTAVPVKGSY DGGMKRFERS PSVCQGQTET
     GEKDAMFILE NGATLSNVII GASQAEGVHC KGTCTLNNVW WADVCEDAVT LKQTSGTSYI
     NGGGAFHASD KIVQFNGRGT VQIKDFYAED YGKLVRSCGN CKDNGGPRNV VISGSVAVDG
     GVLCGINTNY GDTCKITSSC QNKGKYCDRY EGNSSGAEPS KIGSGPDGKY CTTSGVTTSC
//
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