ID A0A067K5V6_JATCU Unreviewed; 316 AA.
AC A0A067K5V6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=JCGZ_19878 {ECO:0000313|EMBL:KDP27179.1};
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:KDP27179.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP27179.1, 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:KDP27179.1};
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 -!- 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; KK914862; KDP27179.1; -; Genomic_DNA.
DR RefSeq; XP_012084743.1; XM_012229353.1.
DR AlphaFoldDB; A0A067K5V6; -.
DR STRING; 180498.A0A067K5V6; -.
DR GeneID; 105644096; -.
DR KEGG; jcu:105644096; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000027138; Unassembled WGS sequence.
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:SF12; PECTINESTERASE 31; 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};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 7..296
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 316 AA; 35310 MW; 2F74EC36D219563B CRC64;
MAEKVLTVAQ DGSAEYKTVQ EAVDAVPENN ADRIVIRVAP GVYKQPVFVP KNKGMITMIG
SRPEDTILTW DNTAAKIEHH LDAEVIGKGT FGCGTVIVGG QDFIAENMTF ENAAPEGSHQ
AVAVRVSGDR SAFYNCRFLG WQDTLYLHQG KQYLRDCYIE GDVDFIFGNS TVLFEHCHIH
CKAAGFVTAQ SRKTAEDTTG FVFLRCVITG NGGPAYAYLG RPWGPFGRVL FAYTHMDACI
HNVGWHNWDN TENEKTACFY EYRCFGPGFT ADKRVDWSKQ LSNEEAEAYL KHEFVDPDPQ
QSWLAQKLGH RIPHNA
//
