ID A0A177C0X5_9PLEO Unreviewed; 518 AA.
AC A0A177C0X5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=pectin lyase {ECO:0000256|ARBA:ARBA00039082};
DE EC=4.2.2.10 {ECO:0000256|ARBA:ARBA00039082};
GN ORFNames=CC84DRAFT_277152 {ECO:0000313|EMBL:OAG01145.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG01145.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG01145.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG01145.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441558; OAG01145.1; -; Genomic_DNA.
DR RefSeq; XP_018031510.1; XM_018185728.1.
DR AlphaFoldDB; A0A177C0X5; -.
DR STRING; 1460663.A0A177C0X5; -.
DR GeneID; 28769214; -.
DR InParanoid; A0A177C0X5; -.
DR OrthoDB; 65895at2759; -.
DR Proteomes; UP000077069; 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:UP000077069};
KW Secreted {ECO:0000256|RuleBase:RU361173};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..518
FT /note="pectin lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008057568"
FT DOMAIN 465..501
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 380..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 52149 MW; 31064533EE9F3E94 CRC64;
MRYSLAAALL AASQTAAQSV VGTAYGFANG VTGGGDAEAV TVSSVDELAK LLADDTARTI
VINGELDFTG TSATGAGCDR KSCSASNGGQ LYLGDLSCGG SDNVAVSSIT YDAAGPEPLK
VGSNKSILGN GKGVLIGKGL ELADGASNVI IQGLEFKNIN PGVVWGGDAL GFKGNNDGVW
VDHNKFSLVG RMFIVSHYAP TRLTISNNEF DGTTTTSASC NGNHYWTMMF YGDGDQVTLD
KNYYHNVAGR APKLGEDGTT GTFHAVNNFF SNMKGHAFDA YQGASALIEG NVFEAVSQPN
TDKAAGSSTL YTVPDASAAS ACSSALGRAC EVNSVDASSG KLAALKANSV LSTFSKIKDV
LVEPLAASEV AAHVKANAGP AGLASAGTTP SKVVGDEATA SSTAPTAPVS SSVEDVPAAT
SKAAATSKAA APVASEKPAA SSPVAAQPTP TPSTGSGSGS GSSSGTVAAY GQCGGKGFTG
ATKCVSGYTC IKQNDWYSQC IAASAKFRRN FGPFAKKR
//
