ID G4ZB47_PHYSP Unreviewed; 266 AA.
AC G4ZB47;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN ORFNames=PHYSODRAFT_329885 {ECO:0000313|EMBL:EGZ22013.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ22013.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ22013.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ22013.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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; JH159153; EGZ22013.1; -; Genomic_DNA.
DR RefSeq; XP_009524730.1; XM_009526435.1.
DR AlphaFoldDB; G4ZB47; -.
DR STRING; 1094619.G4ZB47; -.
DR EnsemblProtists; EGZ22013; EGZ22013; PHYSODRAFT_329885.
DR GeneID; 20646013; -.
DR KEGG; psoj:PHYSODRAFT_329885; -.
DR InParanoid; G4ZB47; -.
DR OMA; ISACDAY; -.
DR Proteomes; UP000002640; Unassembled 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; 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 Lyase {ECO:0000313|EMBL:EGZ22013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
SQ SEQUENCE 266 AA; 28970 MW; D62A5BCCFF85E1C7 CRC64;
MTGQAGLPTL SLISTGLTVC RVRFSVSGPI LPYPLCYFCF FWWQELLDAH RAIKAGEVFD
GKMQTFERSD ITCTDGEGQK DSAVFLVEAG GTLKNAIIGK NQKEGVHCDD HDCTIENVWW
DDVCEDALSI KGGTASSVTT VTNCGARYAS DKVVQHNGYG TVKINGFFAQ EFGKLYRSCG
TCGDIPRTVT VENVYAIDPL VSLVTVNKNY NDQATLKNIY VKTTDGKGDV KVCQWSQGSK
TPSNLGDGPS GTLCQYTESD VHINEK
//
