ID   B0RL92_XANCB            Unreviewed;       325 AA.
AC   B0RL92;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 83.
DE   RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE            EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN   Name=pme1 {ECO:0000313|EMBL:CAP49460.1};
GN   ORFNames=XCCB100_0130 {ECO:0000313|EMBL:CAP49460.1};
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP49460.1, ECO:0000313|Proteomes:UP000001188};
RN   [1] {ECO:0000313|EMBL:CAP49460.1, ECO:0000313|Proteomes:UP000001188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100 {ECO:0000313|EMBL:CAP49460.1,
RC   ECO:0000313|Proteomes:UP000001188};
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA   Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA   Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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         Evidence={ECO:0000256|RuleBase:RU000589};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5. {ECO:0000256|RuleBase:RU000589}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family.
CC       {ECO:0000256|ARBA:ARBA00008891}.
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DR   EMBL; AM920689; CAP49460.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RL92; -.
DR   KEGG; xca:xcc-b100_0130; -.
DR   HOGENOM; CLU_012243_3_1_6; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:TreeGrafter.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR   FunFam; 2.160.20.10:FF:000052; 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; IPR006311; TAT_signal.
DR   PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR   PANTHER; PTHR31321:SF57; PECTINESTERASE 53-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW   ECO:0000256|RuleBase:RU000589};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000589};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001188};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00648,
KW   ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           31..325
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00648,
FT                   ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5005122397"
FT   DOMAIN          36..308
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   325 AA;  34195 MW;  D7DFA5DD46F3CDBB CRC64;
     MQPHRRIVLR TLAASALLAG LSLGSGAAIA ADPVYTVAKQ GSAGYRTVQA AIDAAVQGGK
     RAQINIGAGT YQELIVVPSN APALKLTGAG ATQTVITYDN YASRINPATG AAYGTSGSSS
     VIIAGNDFTA EQLSFGNHAG PVGQAVAVRV DGDRAAFRNV RFLGYQDTLY LRGAKLSYFL
     DCYVEGTVDF VFGAGTALFE NVQLHSLGDG YLTAASTPQE SARGFVFRNA RVTAASGVSR
     VHLGRPWRPY ASVSFITSQL GAHIVPEGWN NWGNAANEAT ARYSEYQNTG AGANPSRRVK
     WSRQLTAAQA AALDRSTVLG SWRPF
//