PLYC_ASPTN
ID PLYC_ASPTN Reviewed; 419 AA.
AC Q0CLG7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable pectate lyase C;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN Name=plyC; ORFNames=ATEG_05467;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
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DR EMBL; CH476600; EAU34536.1; -; Genomic_DNA.
DR RefSeq; XP_001214645.1; XM_001214645.1.
DR AlphaFoldDB; Q0CLG7; -.
DR SMR; Q0CLG7; -.
DR EnsemblFungi; EAU34536; EAU34536; ATEG_05467.
DR GeneID; 4320816; -.
DR VEuPathDB; FungiDB:ATEG_05467; -.
DR eggNOG; ENOG502QW7I; Eukaryota.
DR HOGENOM; CLU_016764_1_1_1; -.
DR OMA; GIHSMGT; -.
DR OrthoDB; 620007at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycoprotein; Lyase; Metal-binding; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..419
FT /note="Probable pectate lyase C"
FT /id="PRO_0000394572"
FT DOMAIN 261..296
FT /note="EF-hand"
FT REGION 350..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /evidence="ECO:0000255"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 419 AA; 44106 MW; 783DC36579BBFB88 CRC64;
MRLGIALFSL IGLCHSVSAL IAFPGAEGFG ANAVGGRQGE IYVVTNLNDS GEGSLRDAVS
ATDRIVVFAV GGVIEISDRI VVSKRVTILG QTAPGDGITV YGNGWSFSNA DDAIVRYIRI
RMGKVGDSGK DAITIAEGST MIFDHVSVSW GRDETFSISG TASNITIQNT IIAQGLETHS
CGGLIQTGGG VSLFRNLYID NKTRNPKVKG VNDFTNNVVY NWGGGGGYIA GDSSGDSYAN
IIGNYFISGP STSVTAFTRG NEYFHGYVET NYYDPDRDGT LNGNELGVSA SNYGGMALVD
TKYDYPAVEY QMTPGEAVNY VTGYVGASKV RDSVDTQLIA QVKSWGTKGE LISDEASMGG
PGDLDGGSPP TDSDGDGIPD DAETEIGSDP NTADSMELHS SGYTYVEMWA NSLVPSSYH
