PME_RALSL
ID PME_RALSL Reviewed; 396 AA.
AC P24791;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Pectinesterase;
DE Short=PE;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
DE Flags: Precursor;
GN Name=pme;
OS Ralstonia solanacearum (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15369 / DSM 50905 / ICPB PS 138;
RX PubMed=2045776; DOI=10.1099/00221287-137-1-131;
RA Spoek A., Stubenrauch G., Schoergendorfer K., Schwab H.;
RT "Molecular cloning and sequencing of a pectinesterase gene from Pseudomonas
RT solanacearum.";
RL J. Gen. Microbiol. 137:131-140(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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M62803; AAA25984.1; -; Genomic_DNA.
DR PIR; A49747; A49747.
DR RefSeq; WP_003277586.1; NZ_CDMD01000001.1.
DR AlphaFoldDB; P24791; -.
DR SMR; P24791; -.
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 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; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..396
FT /note="Pectinesterase"
FT /id="PRO_0000023501"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 41016 MW; 82E2AFC4C0B54AB4 CRC64;
MQSTTLYLKT AAFLGGCSLF AATALAATST ATRPQLSNAD ARAYTIASYM ASFGTIGSLT
TDNWDPTGGV GAVSGFRANY AVAADGSAQY KTVQAAIDAA VADGGVARKY ISVKAGTYNE
LVCVPESAPP ITLYSLDANA NNTVIVYNNA NPTPASGAKT NPCMGTSSNA TVGTVRSATA
MVRASNFNAR NLTFKNSYVE GTFADNNQSA VALAVRGDKA ILENVSVIGN QDTLYLGATN
NTMVIRAYFK NSFIQGDTDF IFGAGTAVFH GCTIQYTAAR LGARATSYVF APSTAPDNPH
GFLAINSTFN ATGNASNNST HLGRAWDQGV SGTSAYINGS SPNGQVVIRD SSLGAHIRLA
DPWGPSTAGR PYCSSKCAYS ANRFFEYNNT GAGSGN
