PELA_NEOFI
ID PELA_NEOFI Reviewed; 378 AA.
AC A1CYC2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Probable pectin lyase A;
DE Short=PLA;
DE EC=4.2.2.10;
DE Flags: Precursor;
GN Name=pelA; ORFNames=NFIA_033080;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW23742.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS027686; EAW23742.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001265639.1; XM_001265638.1.
DR AlphaFoldDB; A1CYC2; -.
DR SMR; A1CYC2; -.
DR STRING; 331117.A1CYC2; -.
DR EnsemblFungi; EAW23742; EAW23742; NFIA_033080.
DR GeneID; 4592857; -.
DR KEGG; nfi:NFIA_033080; -.
DR eggNOG; ENOG502QXM6; Eukaryota.
DR OMA; QDDWCEN; -.
DR OrthoDB; 1267775at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0047490; F:pectin lyase activity; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
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; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..378
FT /note="Probable pectin lyase A"
FT /id="PRO_0000394344"
FT ACT_SITE 254
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..100
FT /evidence="ECO:0000250"
FT DISULFID 90..224
FT /evidence="ECO:0000250"
FT DISULFID 321..329
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 39318 MW; AFF89A671924F95C CRC64;
MKYQGLLAIA GCIASASAVS VSGAAEGFAK GVTGGGSATA VYPSTTAELV SYLGDSEARV
IVLTKTFDFT GTEGTTTATG CAPWGTASAC QLAINQNDWC TNYEPDAPSV SVTYDNAGTL
GITVKSNKSL LGSGSSGVIK GKGLRIVSGA SNIIIQNIAI TDINPKYVWG GDAITINNAD
MVWIDHVTTA RIGRQHLVLG TSASNRVTIS NNYFNGVSSY SATCDGYHYW GIYLDGSNDL
VTMKGNYIYH FSGRSPKVQG NTLLHAVNNY WYDSSGHAFE IGSGGYVLAE GNVFQNIDTI
VESPVDGQLF TSPDSTTNKV CSTYLGHVCQ VNGFGSSGTF SQADTGFLSN FAGKNIASAS
AYTVVQSSVP SSAGQGKI