ID W7MR14_GIBM7 Unreviewed; 621 AA.
AC W7MR14;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=pectin lyase {ECO:0000256|ARBA:ARBA00039082};
DE EC=4.2.2.10 {ECO:0000256|ARBA:ARBA00039082};
GN ORFNames=FVEG_12209 {ECO:0000313|EMBL:EWG53873.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG53873.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG53873.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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}.
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DR EMBL; DS022260; EWG53873.1; -; Genomic_DNA.
DR RefSeq; XP_018760064.1; XM_018901558.1.
DR AlphaFoldDB; W7MR14; -.
DR EnsemblFungi; FVEG_12209T0; FVEG_12209T0; FVEG_12209.
DR GeneID; 30069669; -.
DR KEGG; fvr:FVEG_12209; -.
DR VEuPathDB; FungiDB:FVEG_12209; -.
DR eggNOG; ENOG502SJIR; Eukaryota.
DR HOGENOM; CLU_021980_0_1_1; -.
DR OMA; YFHATNN; -.
DR OrthoDB; 65895at2759; -.
DR Proteomes; UP000009096; Chromosome 4.
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:UP000009096};
KW Secreted {ECO:0000256|RuleBase:RU361173};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..621
FT /note="pectin lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004896818"
FT DOMAIN 574..610
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 382..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 63946 MW; F9886CD6B2253098 CRC64;
MRLQSITAIL AAAATASAQS VSGKAYGFAA GVTGGEGEAV TPSSAEELAT LLADDTPRVI
YLNKEFDFTG DVKTGAGCDR KSCSASNGGQ LYLGDLSCGG DDNVAVSSIA YDAAGPEPLP
VGSNKSIIGN GKAVLKGKGL SIKKGSKNVI VQGIEFTDIN PGVVWGGDAL ELKGLNDGVW
IDHCKFSKVG RMFIVSHYDG SRLTISNSEF DGVTDTSASC NGNHYWTMMF YGEGDQVTLD
RNHFHDVAGR APKLGEPGTN GYFHATNNYF QNMKGHAFDA YQGANAIIEG NVFDGVDTPI
TKEAASVSTL FVADESSASA CQSALGRACE PNSATSSGDL PSLKGESGLN AVAKNKDNII
TPVSASEVTA LVLGSVGPAN VGSGSNSGSG SDSAPSQSPE SGNDATETAP ESTPEAVNEQ
EETETEPVEN AEVKPVASED CEEETDATPS KTEEKPVAPG DCDDEIEAAA DSSSETEQKP
AASATPSKQT SSSSDECDEE PKAEAKPAAT GDCDDEIEAA ADTTASATPS KQTSSSNDEC
DEEPKAEAKP VATGDCDEGE TSEAAAESSS STGSTAQMYG QCGGKNWTGA TMCPSGTSCK
KMNDYYSQCI GSNSRVRRYV Q
//
