ID A0A0D9XPJ2_9ORYZ Unreviewed; 494 AA.
AC A0A0D9XPJ2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR11G03900.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR11G03900.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR11G03900.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR11G03900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 -!- 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 AlphaFoldDB; A0A0D9XPJ2; -.
DR STRING; 77586.A0A0D9XPJ2; -.
DR EnsemblPlants; LPERR11G03900.1; LPERR11G03900.1; LPERR11G03900.
DR Gramene; LPERR11G03900.1; LPERR11G03900.1; LPERR11G03900.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000032180; Chromosome 11.
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 NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF149; PECTINESTERASE_PECTINESTERASE INHIBITOR 17-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; 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 Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 27..494
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005115576"
FT DOMAIN 22..145
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 494 AA; 52454 MW; 200F807FDE367695 CRC64;
MAPSDAISAI HVLSFLLLIL PRAISAVDIP SHDDSVQVAM DQAARALAMT RAARRSDPRD
DVARHGATQA WSDCDQLVSF AVAHLNRTAA AAVASPSDVA TWLSAARTTV NTCLDGFAEL
GASPAPDFAA ALANVSRLVT DALRRESTEN GSASSTRVVT HDDGRMFPLD DMARPGDADV
VVAKDGTGHF RTVGDAINAV AVARRSNGDG ERIVVYVKAG VYNENVEVWT NNLVLIGDGI
GRTVITGCRS VRQGYTTFSS ATFAVNADGF VASGVTFRNT AGAGSSQAVA LRASGDRLAF
YRCSIEGHQD TLYAHTLRQF YRECVVAGTV DFIFGNAAAV LQRCSIRVRR PPFPGQPAVV
TAQGRVDRFE RTGFAIHGGR VTASARFGAT APFVAYLGRP WKEYSRVVYM EVYMDGTVDA
AGWLAWDGTE FAQSTAFYGE YRNFGPGSGT SGRVRWGGYH VISDPGQASE FTAGDLVNAG
SWLGSTGVPF TPGL
//
