ID D0NV94_PHYIT Unreviewed; 486 AA.
AC D0NV94;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN ORFNames=PITG_17207 {ECO:0000313|EMBL:EEY66566.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY66566.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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}.
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DR EMBL; DS028167; EEY66566.1; -; Genomic_DNA.
DR RefSeq; XP_002897085.1; XM_002897039.1.
DR AlphaFoldDB; D0NV94; -.
DR STRING; 403677.D0NV94; -.
DR EnsemblProtists; PITG_17207T0; PITG_17207T0; PITG_17207.
DR GeneID; 9468687; -.
DR KEGG; pif:PITG_17207; -.
DR VEuPathDB; FungiDB:PITG_17207; -.
DR eggNOG; ENOG502S4FB; Eukaryota.
DR HOGENOM; CLU_027689_0_0_1; -.
DR InParanoid; D0NV94; -.
DR OMA; PLCKNTT; -.
DR OrthoDB; 69515at2759; -.
DR Proteomes; UP000006643; Partially assembled 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; 2.
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; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EEY66566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..486
FT /note="Probable pectate lyase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003013684"
SQ SEQUENCE 486 AA; 52185 MW; 1A9E0D601E77A00B CRC64;
MVKSFAPFVT SAALLLAVAT SASLPNGSWP ASKGTVQYSK AYVVKAGEVF DGKMKTFERS
DVSCEGQSES GADTAVFNVE AGGHLKNVII GKNQMEGVHC DKHDCIIENV WWDDVCEDAL
SVKGGTASSV TKVIGGGARY ADDKVIQHNG FGTVDIDGFY GEDISKLYRS CGTCGNRPKK
VSVSNTYVLN PTNAIVTVNK NWGDQATLHN VWVKSSKPTV KVCQWSQGNA NGEPKMLGHG
PSNPLCKNTT ASVPDGTWPA STGIVRYKKP YTIKAGEVFD GKMQTFERSD ITCSGGEGQK
DTAVFLVEAG GTLKNAIIGK NQKEGVHCDY HDCTIENVWW DDVCEDALSI KGGSASSVTT
VTNCGARYAE DKVVQHNGYG TVKIKGFFAQ EFGRLYRSCG TCGNIPRKVT VENVYAIDPL
VSVVTVNKNN NDQATLKNIF VKTTDGKKNV KVCQWSQASK TPSNVGDGPS GKLCQYSTSD
VHINED
//
