ID A0A022QAM3_ERYGU Unreviewed; 533 AA.
AC A0A022QAM3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=MIMGU_mgv1a004327mg {ECO:0000313|EMBL:EYU24971.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU24971.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU24971.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
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; KI632098; EYU24971.1; -; Genomic_DNA.
DR RefSeq; XP_012852303.1; XM_012996849.1.
DR AlphaFoldDB; A0A022QAM3; -.
DR STRING; 4155.A0A022QAM3; -.
DR GeneID; 105971919; -.
DR KEGG; egt:105971919; -.
DR eggNOG; ENOG502QU67; Eukaryota.
DR OMA; GLFVIYV; -.
DR OrthoDB; 668039at2759; -.
DR PhylomeDB; A0A022QAM3; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
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:SF45; PECTINESTERASE_PECTINESTERASE INHIBITOR 60-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}; Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 22..533
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005101176"
FT DOMAIN 27..179
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 533 AA; 58584 MW; D2AD35D68B981E52 CRC64;
MAKLSLFFFF FSYVCSHAVF ADDDVSIKKG TISWWCSTTP HPDPCNHFIM MGRYNPNQHN
PITRQDFRTL TIQAAMERAI HVQTRAKNLC FQGKSKRKKT VHRDCYNLIG NTIHQLNTTF
RSIQKTSNAT SDAQTWLSAA LTNVEICRSG SHDLKIAARF RSPILSGYVS ELISNSLAAN
GALILAANND PDSGRRFPGR VTPGNRKLLQ VSALVLKANV TVSPDGSGQF RSIQAAIDYA
TSKRVGDGRV VVYVKKGVYE ENILINRTMN KVTLVGDGVK HTVITGSRSV SGGFTTYSSA
TVGVDGAGFM ARGITFRNTA GPEKGQAVAL RSASDLSVFY ACAFEGYQDT LFVHAQRQFF
KSCHIYGTVD IIFGNAAVVI QNSVIYVRKP LVGQANMITA QGRGDPFQNT GISIHNCRVM
PAPDLKPVVG SFKTYLGRPW QQYSRTVIMK SYLDGLVEPE GWSRWGDSDF ALSTLYYGEY
KNFGPAGSLE NRVNWTGYHA ITNPDEASRF TVRSLVAGRA WLPATGVPFI AGL
//
