ID A0A167E5U2_9PEZI Unreviewed; 485 AA.
AC A0A167E5U2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=pectin lyase {ECO:0000256|ARBA:ARBA00039082};
DE EC=4.2.2.10 {ECO:0000256|ARBA:ARBA00039082};
GN ORFNames=CI238_12420 {ECO:0000313|EMBL:KZL84739.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84739.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL84739.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84739.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pectinolytic enzymes 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.
CC {ECO:0000256|ARBA:ARBA00037631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00036818};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|ARBA:ARBA00010980, ECO:0000256|RuleBase:RU361173}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL84739.1}.
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DR EMBL; LFIW01000808; KZL84739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167E5U2; -.
DR STRING; 1573173.A0A167E5U2; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR PANTHER; PTHR31683:SF67; PECTIN LYASE F-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR SMART; SM00656; Amb_all; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Secreted {ECO:0000256|RuleBase:RU361173};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..485
FT /note="pectin lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007885599"
FT DOMAIN 435..471
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 374..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..424
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 50109 MW; 2E0D9ECC408E99FF CRC64;
MRFSTSVILA AAAATTASAQ AVVGKAYGFA AGVTGGGNAA AATPSSAEEL AEWLSDDTPR
TIVIDKEYDF TGKSATGEGC DRKSCSSTNG GQLYLGDLSC GSSDNTVATV TYDVAGTEPL
IVGSNKSILG VGGKGVLNGK GLRIKADAKN VIVQGLEITN LNPGVVWGGD ALDLQGGNDG
VWIDHCKFSL VGRQFIVSHY DGSRATISNN EFDGVTETSA TCNGNHYWTM MLNGDGDQIT
LDKNYFHDVS GRAPKLGDGG TFQATNNLFS NMKGHTFELY SGTVALIEGN AFEAVDTPYN
GEAFSNSFNV PDASTASACK SQIGRACAVN SVDSSSGDFK ALSGTNALST FSKLTDYLVE
PVAATGVASL VKGSAGPSNL EASSAATPAP ATDAGETTEE EEEEEEPAVV EEPATVEEPA
AEEPATEENT APSGETAQQW GQCGGNNWTG PTACVAGTSC VVQNEWYSQC LSSAARRSMK
SLRRL
//
