ID A0A0E0QJR2_ORYRU Unreviewed; 560 AA.
AC A0A0E0QJR2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G18550.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI08G18550.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0QJR2; -.
DR STRING; 4529.A0A0E0QJR2; -.
DR EnsemblPlants; ORUFI08G18550.1; ORUFI08G18550.1; ORUFI08G18550.
DR Gramene; ORUFI08G18550.1; ORUFI08G18550.1; ORUFI08G18550.
DR eggNOG; ENOG502QRGV; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR OMA; NFIDGWT; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000008022; 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; cd15799; PMEI-like_4; 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 PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF213; PECTINESTERASE_PECTINESTERASE INHIBITOR 44-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 Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Secreted {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 27..560
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005116202"
FT DOMAIN 30..187
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT REGION 113..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 560 AA; 58721 MW; 6939B61EE7C88411 CRC64;
MASTCSSSIP QLILLLSLTV FLLANAHPMA PPSPPRKAAA PPTAAKGVTG ISPVLVSTLR
ETLDAIKNVA SIISSFPIGG ILGGGALRLS SAIADCLDLL DLSSDELSWS MSTTSSSSYQ
PTNAGAATSS HVGTGDARSD LRSWLGGALG NQDTCKEGLD DTGSVLGSLV GTALQTVTSL
LTDGLGQVAA GEASIAWSSS RRGLAEGGGA PHWLGARERR LLQMPVGPGG MPVDAVVAKD
GSGNYTTVSA AVDAAPTESA SRYVIYVKKG VYKETVDIKK KKWNLMLVGD GMGVTVISGH
RNYVDGYTTF RSATVAVNGK GFMARDVTFE NTAGPSKHQA VALRCDSDLS VFYRCGFEGY
QDTLYAHSLR QFYRDCRVSG TVDFVFGNAA AVFQNCTLAA RLPLPDQKNS VTAQGRLDGN
MTTGFAFQFC NVTADDDLQR ALAGGGNQSS AAAAAAATQT YLGRPWKQYS RVVFMQSYIG
AVVRPEGWLA WDGQFALDTL YYGEYMNTGP GAGVGGRVKW PGFHVMTSPA QAGNFTVAQF
IEGNMWLPPT GVKYTAGLTS
//
