GenomeNet

Database: UniProt
Entry: X0LHM8_FUSOX
LinkDB: X0LHM8_FUSOX
Original site: X0LHM8_FUSOX 
ID   X0LHM8_FUSOX            Unreviewed;       233 AA.
AC   X0LHM8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-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=FOTG_11315 {ECO:0000313|EMBL:EXM20667.1};
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:EXM20667.1};
RN   [1] {ECO:0000313|EMBL:EXM20667.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM20667.1};
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:EXM20667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM20667.1};
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 (MAY-2012) 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; JH657951; EXM20667.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0LHM8; -.
DR   SMR; X0LHM8; -.
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:EXM20667.1};
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_5025073808"
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
//
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