ID   PMEB_PECPM              Reviewed;         400 AA.
AC   P55743; K4FUN6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Pectinesterase B;
DE            Short=PE B;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase B;
GN   Name=pemB; OrderedLocusNames=W5S_4605;
OS   Pectobacterium parmentieri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=1905730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=23045508; DOI=10.1128/jb.00681-12;
RA   Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA   Paulin L., Pirhonen M., Palva T., Holm L.;
RT   "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL   J. Bacteriol. 194:6004-6004(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-400.
RC   STRAIN=SCC3193;
RA   Heikinheimo R., Mae A., Flego D., Pirhonen M., Koiv V., Palva E.T.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR   EMBL; CP003415; AFI92651.1; -; Genomic_DNA.
DR   EMBL; X80475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_014702023.1; NZ_QESW01000003.1.
DR   AlphaFoldDB; P55743; -.
DR   SMR; P55743; -.
DR   STRING; 1905730.W5S_4605; -.
DR   EnsemblBacteria; AFI92651; AFI92651; W5S_4605.
DR   KEGG; pec:W5S_4605; -.
DR   PATRIC; fig|1166016.3.peg.4667; -.
DR   eggNOG; COG4677; Bacteria.
DR   HOGENOM; CLU_012243_5_0_6; -.
DR   OrthoDB; 1095798at2; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000008044; Chromosome.
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; Hydrolase.
FT   CHAIN           1..400
FT                   /note="Pectinesterase B"
FT                   /id="PRO_0000215046"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            227
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        223
FT                   /note="L -> R (in Ref. 2; X80475)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  44446 MW;  D23CCCF011E4C4E5 CRC64;
     MTKTTYPGTA YRPILSEQEA DRFTLPHYFT RRGHDGHSDT DVWQPTSIEV DPATPWVVGP
     QVGVDGATHG TVQQAVNAAL RAQQDRPCID IKLLPGIYTG AVYIPADAPP LTLFGTGEQP
     NDVVIQLALD SMFSPATYRE TVNSHGEYQP GDPAWYMYDL CASKQNATID TICAAVVWSQ
     SDNLQMKNLT VVNALLDSVD GRAHQAVALR TDGDKIQLER VRLIGRQDTF FVNTSNLRNE
     YVTDRYSRAY IKDSYIEGDV DYVFGRATAV FDRVHFHTVS SRGAKDIHVF APDSMPWAQY
     GFLAVSCRFT GDEGFSGGRK AKLGRAWDQG ARQTGYQPNK TANGQLVIRD STIDASYDRE
     QPWGVAATTA RPFAGNVDSA RNLDDVQFNR LWEYNNIDEV