ID   PMEA_ASPFC              Reviewed;         324 AA.
AC   B0Y9F9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable pectinesterase A;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase A;
DE   Flags: Precursor;
GN   Name=pmeA; ORFNames=AFUB_080890;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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: Involved in maceration and soft-rotting of plant tissue.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC         Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR   EMBL; DS499600; EDP48652.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y9F9; -.
DR   SMR; B0Y9F9; -.
DR   EnsemblFungi; EDP48652; EDP48652; AFUB_080890.
DR   VEuPathDB; FungiDB:AFUB_080890; -.
DR   HOGENOM; CLU_012243_1_2_1; -.
DR   PhylomeDB; B0Y9F9; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR033131; Pectinesterase_Asp_AS.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase; Cell wall biogenesis/degradation; Glycoprotein;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..324
FT                   /note="Probable pectinesterase A"
FT                   /id="PRO_0000394079"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        186
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   324 AA;  34558 MW;  5323FE08306F7FAF CRC64;
     MYLPSLVLGL LGFGLTASTS PIEERSNRSK APAGCLTVGS SGTYATIGAA LSALGSSTSD
     ACIFIGAGTY QEQITIDYKG KLTMYGETTD TSSYKQNLVT ITHSISSPEA GSLDKSATVN
     VRSDGFKMYN INVINGYGKG AQAVTLVANA DKLGFYGCSF VGYQDTLYAK AGRQYYSNCY
     IEGAVDYIFG DASAWFGECD LVSVGPGYIT AMSRTTADET TWYAIDHCNI YGKPGVDLTS
     AVYLGRPWRV LARVIFQNSQ LSNIINPKGW SPMATGATPL YYEYNNKGAG ADTSKREYES
     PISGAVSIAT VLGGGWNSWV DTTY