PLYA_ASPFU
ID PLYA_ASPFU Reviewed; 321 AA.
AC Q4WIT0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable pectate lyase A;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN Name=plyA; ORFNames=AFUA_2G00760;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000008; EAL87175.1; -; Genomic_DNA.
DR RefSeq; XP_749213.1; XM_744120.1.
DR AlphaFoldDB; Q4WIT0; -.
DR SMR; Q4WIT0; -.
DR STRING; 746128.CADAFUBP00001740; -.
DR Allergome; 8991; Asp f PL.
DR EnsemblFungi; EAL87175; EAL87175; AFUA_2G00760.
DR GeneID; 3507249; -.
DR KEGG; afm:AFUA_2G00760; -.
DR VEuPathDB; FungiDB:Afu2g00760; -.
DR eggNOG; ENOG502S66G; Eukaryota.
DR HOGENOM; CLU_021894_1_0_1; -.
DR InParanoid; Q4WIT0; -.
DR OMA; NYWIDHV; -.
DR OrthoDB; 924221at2759; -.
DR BRENDA; 4.2.2.2; 508.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0070051; F:fibrinogen binding; IDA:AspGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate 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 Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycoprotein; Lyase; Metal-binding; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..321
FT /note="Probable pectate lyase A"
FT /id="PRO_0000394561"
FT ACT_SITE 220
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 33821 MW; C51CF450942FF666 CRC64;
MKFVATLIAC GLSGLALAAP TATVNSLGKR AADDAAFGYA SLNGGTTGGA GGTTTTVSSY
AAFTAAVSSD AKKVVYVSGP IKQSAKQVKV GSNTSIIGKD STAVLEGFGL LVKEKSNVII
RNLGVKKVLA ENGDAIGIQY SNNVWVDHVD VSSDRDHDKD YYDGLIDVTH AADYVTISNS
YIHDHWKASL VGHSDNNGDE DKGHLRVTYA NNYWSNINSR APSLRFGTGH IYNSYFENVS
DGINTRDGAQ VLVESNQFVG SSKALYSTDD GYAVERDNDF GGAKNTALQG TLTTVPYSYS
LLGSSKVKSA VVGVAGQTLK F
