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Database: UniProt
Entry: M4BAR0_HYAAE
LinkDB: M4BAR0_HYAAE
Original site: M4BAR0_HYAAE 
ID   M4BAR0_HYAAE            Unreviewed;       305 AA.
AC   M4BAR0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP803370, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|Proteomes:UP000011713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP803370}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP803370};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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; JH598070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4BAR0; -.
DR   STRING; 559515.M4BAR0; -.
DR   EnsemblProtists; HpaT803370; HpaP803370; HpaG803370.
DR   VEuPathDB; FungiDB:HpaG803370; -.
DR   eggNOG; ENOG502RY96; Eukaryota.
DR   HOGENOM; CLU_044863_0_1_1; -.
DR   InParanoid; M4BAR0; -.
DR   OMA; VCTRFNG; -.
DR   Proteomes; UP000011713; 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   Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..305
FT                   /note="Probable pectate lyase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012474962"
SQ   SEQUENCE   305 AA;  32302 MW;  7ED9ABC7E8466BA3 CRC64;
     MRSFVALVAF SYALASHPIT AITTAEEEVT MSRLRRYKGG GRRLIGDLVD TTPWREGYTP
     GEVNAVQDQE ERTHGVWPLS AGTVVLHRPG IVGSTYSFDG GMKTFKRRNV DFESGVKMTK
     QNAVFVVQAG GVLRNVIIAG GGGVFCETHN CALVNVWFKD SVQAALHINS GTGITTVTGG
     GAKNVAGRVI FGQASGTVVV SGGFHMEHSG MLFESCSTCG PVKRGIVVDG VVSVNPTAEL
     IRVNSNYNDR GTIASATITT TDADYPVCTR YNGGVVPQKL GAGAFPPICS FSRSNVKIKP
     VEQAV
//
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