ID   PME_ASPNG               Reviewed;         331 AA.
AC   P17872;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 107.
DE   RecName: Full=Pectinesterase;
DE            Short=PE;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase;
DE   Flags: Precursor;
GN   Name=pme1;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=RH 5344;
RX   PubMed=2377474; DOI=10.1093/nar/18.14.4262;
RA   Khanh N.Q., Albrecht H., Ruttkowski E., Loeffler F., Gottschalk M.,
RA   Jany K.-D.;
RT   "Nucleotide and derived amino acid sequence of a pectinesterase cDNA
RT   isolated from Aspergillus niger strain RH 5344.";
RL   Nucleic Acids Res. 18:4262-4262(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RH 5344;
RX   PubMed=1937044; DOI=10.1016/0378-1119(91)90567-u;
RA   Khanh N.Q., Ruttkowski E., Leidinger K., Albrecht H., Gottschalk M.;
RT   "Characterization and expression of a genomic pectin methyl esterase-
RT   encoding gene in Aspergillus niger.";
RL   Gene 106:71-77(1991).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n methanol + n H(+);
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.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR   EMBL; X52902; CAA37084.1; -; mRNA.
DR   EMBL; X54145; CAA38084.1; -; Genomic_DNA.
DR   PIR; JT0589; JT0589.
DR   AlphaFoldDB; P17872; -.
DR   SMR; P17872; -.
DR   VEuPathDB; FungiDB:An03g06310; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1137796; -.
DR   VEuPathDB; FungiDB:ATCC64974_75710; -.
DR   VEuPathDB; FungiDB:M747DRAFT_364154; -.
DR   eggNOG; ENOG502QSQ4; Eukaryota.
DR   OMA; AAGHQNQ; -.
DR   BioCyc; MetaCyc:MONOMER-20553; -.
DR   UniPathway; UPA00545; UER00823.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   FunFam; 2.160.20.10:FF:000014; Pectinesterase; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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   InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR   PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR   PANTHER; PTHR31321:SF127; PECTINESTERASE; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00800; PECTINESTERASE_1; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   1: Evidence at protein level;
KW   Aspartyl esterase; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..331
FT                   /note="Pectinesterase"
FT                   /id="PRO_0000023473"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        182
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            160
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  35715 MW;  25B52150884C797A CRC64;
     MVKSILASVL FAATALAASR MTAPSGAIVV AKSGGDYDTI SAAVDALSTT STETQTIFIE
     EGSYDEQVYI PALSGKLIVY GQTEDTTTYT SNLVNITHAI ALADVDNDDE TATLRNYAEG
     SAIYNLNIAN TCGQACHQAL AVSAYASEQG YYACQFTGYQ DTLLAETGYQ VYAGTYIEGA
     VDFIFGQHAR AWFHECDIRV LEGPSSASIT ANGRSSESDD SYYVIHKSTV AAADGNDVSS
     GTYYLGRPWS QYARVCFQKT SMTDVINHLG WTEWSTSTPN TENVTFVEYG NTGTGAEGPR
     ANFSSELTEP ITISWLLGSD WEDWVDTSYI N
//