PME_ASPAC
ID PME_ASPAC Reviewed; 331 AA.
AC Q12535;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KSM 510;
RX PubMed=8920970; DOI=10.1042/bj3190705;
RA Christgau S., Kofod L.V., Halkier T., Andersen L.N., Hockauf M.,
RA Dorreich K., Dalboege H., Kauppinen S.;
RT "Pectin methyl esterase from Aspergillus aculeatus: expression cloning in
RT yeast and characterization of the recombinant enzyme.";
RL Biochem. J. 319:705-712(1996).
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 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.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; U49378; AAB42153.1; -; mRNA.
DR AlphaFoldDB; Q12535; -.
DR SMR; Q12535; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_1876912; -.
DR BRENDA; 3.1.1.11; 488.
DR UniPathway; UPA00545; UER00823.
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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall biogenesis/degradation; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..331
FT /note="Pectinesterase"
FT /id="PRO_0000023472"
FT ACT_SITE 162
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 161
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 35681 MW; 1F1C81BF1E32174F CRC64;
MVKSVLASAL FAVSALAASR TTAPSGAIVV AKSGGDYTTI GDAIDALSTS TTDTQTIFIE
EGTYDEQVYL PAMTGKVIIY GQTENTDSYA DNLVTITHAI SYEDAGESDD LTATFRNKAV
GSQVYNLNIA NTCGQACHQA LALSAWADQQ GYYGCNFTGY QDTLLAQTGN QLYINSYIEG
AVDFIFGQHA RAWFQNVDIR VVEGPTSASI TANGRSSETD TSYYVINKST VAAKEGDDVA
EGTYYLGRPW SEYARVVFQQ TSMTNVINSL GWTEWSTSTP NTEYVTFGEY ANTGAGSEGT
RASFAEKLDA KLTITDILGS DYTSWVDTSY F
