ID N1QBX5_PSEFD Unreviewed; 216 AA.
AC N1QBX5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU367009};
DE Flags: Fragment;
GN ORFNames=MYCFIDRAFT_23004 {ECO:0000313|EMBL:EME89711.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME89711.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME89711.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME89711.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446555; EME89711.1; -; Genomic_DNA.
DR RefSeq; XP_007919672.1; XM_007921481.1.
DR AlphaFoldDB; N1QBX5; -.
DR STRING; 383855.N1QBX5; -.
DR GeneID; 19338392; -.
DR KEGG; pfj:MYCFIDRAFT_23004; -.
DR eggNOG; ENOG502QU39; Eukaryota.
DR HOGENOM; CLU_044863_3_1_1; -.
DR OrthoDB; 66064at2759; -.
DR Proteomes; UP000016932; 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:EME89711.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EME89711.1"
FT NON_TER 216
FT /evidence="ECO:0000313|EMBL:EME89711.1"
SQ SEQUENCE 216 AA; 22361 MW; 11BA3EF22FD1DB41 CRC64;
LPASSGSSAL DAVQTIAAGQ SFDGGMVMYD RGVECTGQAE GGSSDAVFYL EAGASISNVI
IGPNQAEGIH CFGECTLSNV WWSAVCEDAF TIKEQDAGAT TTITGGGAFG AEDKVLQHNG
GGTLSVSGFT VETFGKLYRS CGNCDEMFER HVILDDITAT DGKSLAGINS NYGDTATFTN
IVVSGISDIC VEYEGNDTGE EPEKTSSGPS DYCIYS
//
