ID A0A067L1W8_JATCU Unreviewed; 543 AA.
AC A0A067L1W8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=JCGZ_04732 {ECO:0000313|EMBL:KDP38089.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP38089.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP38089.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP38089.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin.
CC {ECO:0000256|RuleBase:RU000589}.
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|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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000256|ARBA:ARBA00007786}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000256|ARBA:ARBA00006027}.
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DR EMBL; KK914370; KDP38089.1; -; Genomic_DNA.
DR RefSeq; XP_012072269.1; XM_012216879.1.
DR AlphaFoldDB; A0A067L1W8; -.
DR STRING; 180498.A0A067L1W8; -.
DR GeneID; 105634094; -.
DR KEGG; jcu:105634094; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
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 CDD; cd15798; PMEI-like_3; 1.
DR Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
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; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF152; PECTINESTERASE_PECTINESTERASE INHIBITOR 6-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Cell wall {ECO:0000256|RuleBase:RU000589};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU000589};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Secreted {ECO:0000256|RuleBase:RU000589}.
FT DOMAIN 23..177
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 543 AA; 60238 MW; 5227227890ACD3F5 CRC64;
MDKNKIVQAI FYLSFLFYSL GFIDGATIAS CSQTPYPEIC NHFMNTNILE TEKDQTPFTF
RDQSLLVTMN HAIKAHQMIL SLEMNDSFDE KAKLARADCV ELYEDTIDHL NRSLFVSSSN
NNNPVDSQTW LSAANTNLQT CQNGFTEFNL TSNYLESLLL PDMLSNFSKL LSNSLAINKE
NYYISPLYNS KTVHPGSSGG GGRKLLHDDE FPWWVSVTDR KLLQSSPEAD IVVAQDGSGN
YKTIGEAVAA SATRRSGNKR FVIYVKKGVY KEYVEIKNSM NNLMLIGDGI DATIVTGNKN
NQDGSTTFRS ATFAVSGEGF IAKDITFENT AGPQKHQAVA LRSGSDFSVF YSCSFKGYQD
TLYVYSQRQF YRDCDIYGTV DFIFGNAVVV FQNCNIYVRK PMSGQKNTVT AQARTDPNEN
TGIIIHNSRV TAASDLRPVQ GSFKSYLGRP WQEYSRTVIL KSNLDGLIDP AGWLPWSGNF
ALSTLYYAEY MNSGSGASTG DRVKWPGYHV ITKVTDAGKF TVGNFLAGDS WIPATGVPFD
SGL
//
