ID   PELA_ASPFU              Reviewed;         380 AA.
AC   Q4WV10;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Probable pectin lyase A;
DE            Short=PLA;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA; ORFNames=AFUA_5G10380;
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 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}.
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DR   EMBL; AAHF01000003; EAL91566.1; -; Genomic_DNA.
DR   RefSeq; XP_753604.1; XM_748511.1.
DR   AlphaFoldDB; Q4WV10; -.
DR   SMR; Q4WV10; -.
DR   EnsemblFungi; EAL91566; EAL91566; AFUA_5G10380.
DR   GeneID; 3511320; -.
DR   KEGG; afm:AFUA_5G10380; -.
DR   VEuPathDB; FungiDB:Afu5g10380; -.
DR   eggNOG; ENOG502QXM6; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   InParanoid; Q4WV10; -.
DR   OMA; CRPWGTG; -.
DR   OrthoDB; 1267775at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..380
FT                   /note="Probable pectin lyase A"
FT                   /id="PRO_0000394340"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        323..331
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  39783 MW;  0912999222E3EEAC CRC64;
     MRYTSLFTAV TAALASTAAA VGVSGAAEGF AKGVTGGGNA SPVYPKTNDE LVSYLGDSQA
     RVIVLTKTFD FRGTEGTTSG TGCAPWGTNA KCQLAINQNS WCDNYQPNAP KVSVSYDNAG
     VLGITVNSNK SLIGQGSAGV IKGKGLRIVS GAKNVIIQNI AITDINPKYV WGGDAITINN
     ADLVWIDHVT TARIGRQHIV LGTQADNRIT ISNCYIDGVT DYSATCNGYH YWGIYLDGSN
     DMVTMKGNYI YHTSGRSPKV QGNTLLHAVN NYWYDNAGHA FEIGSGAYVV AEGNVFQNVK
     AVAESPISGK LFSSPDASTN KVCSSYLGHT CQINGFGSSG AFSQADTDIL SKFKGKNIAS
     AAAYNTVVSS VTANAGNGKL