ID G2XKU9_PHYCP Unreviewed; 343 AA.
AC G2XKU9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Pectinesterase {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
GN Name=pcpme2 {ECO:0000313|EMBL:ACO54868.1};
OS Phytophthora capsici.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4784 {ECO:0000313|EMBL:ACO54868.1};
RN [1] {ECO:0000313|EMBL:ACO54868.1}
RP NUCLEOTIDE SEQUENCE.
RA Jia Y.J., Zhang X.G.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACO54868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21259289; DOI=10.1002/jobm.201000317;
RA Li P., Feng B., Wang H., Tooley P.W., Zhang X.;
RT "Isolation of nine Phytophthora capsici pectin methylesterase genes which
RT are differentially expressed in various plant species.";
RL J. Basic Microbiol. 51:61-70(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00001440,
CC ECO:0000256|RuleBase:RU000589};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184,
CC ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; FJ213426; ACO54868.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XKU9; -.
DR VEuPathDB; FungiDB:DVH05_002251; -.
DR BRENDA; 3.1.1.11; 11828.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF125; PECTINESTERASE A; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 20..343
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005131567"
FT DOMAIN 46..316
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 343 AA; 36958 MW; B2112A6EEF70D720 CRC64;
MQIFTPLVVL TGLVAGALAQ QTCTGPNART EPPAGAVVVD ATGAYKNSVK TVSEGVAKLD
PHTTSEQTVF VRPGVYNEQV FVAPLSGPLV LQGFTCDATS YSSNEVTITQ GKAQKDIPAT
VTGESRNDMT STVRFYSDNV KVYNLNIANT AGNVGQALAV NVNATDYGFY ACNLTGYQDT
VLADKGRELY ARTYINGATD FVFGRYAQAW FEKCDIETIG TGFITASGRE SESSSATYVF
NKARVFGKSG VNSTVLGRPW RPFARVIWQN SELGDVVKPE GWAKWDATSS TDKVIFKEFN
NVGPGAATAN RVAFSGQLDA PVAINEVLGE GYETEWWVDM TYL
//
