ID A0A022QHW6_ERYGU Unreviewed; 531 AA.
AC A0A022QHW6;
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_mgv1a004362mg {ECO:0000313|EMBL:EYU28292.1};
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:EYU28292.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU28292.1, 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; KI631414; EYU28292.1; -; Genomic_DNA.
DR RefSeq; XP_012848231.1; XM_012992777.1.
DR AlphaFoldDB; A0A022QHW6; -.
DR STRING; 4155.A0A022QHW6; -.
DR GeneID; 105968155; -.
DR KEGG; egt:105968155; -.
DR eggNOG; ENOG502QRD0; Eukaryota.
DR OMA; YCEGLLS; -.
DR OrthoDB; 668039at2759; -.
DR PhylomeDB; A0A022QHW6; -.
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:SF11; PECTINESTERASE_PECTINESTERASE INHIBITOR 54-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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..26
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 27..531
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005101206"
FT DOMAIN 29..181
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 531 AA; 57357 MW; E72C811E15C8819F CRC64;
MATSKCIIQF PILFIILSCL IAVSCAANNE EPLIKRECGY TRYPTLCVQT LTATNDQNID
LLSALVNKTI HETNLPLSYF DSLIINSRLN SPAAQPIRTA IDDCDELMKM SLKRLNQAME
LLQKSPKNHK ADIQTWLSAA LTFQQTCKDT MEEHVASNAY VGKIYNKMDY LSELISNPLA
LVNRITGNPS ESPAGRRSLL QFPAWVSAGD RKLLQSTGAV KASAVVAKDG SGDFTTVSGA
IQAATGGRFV IYVKSGTYNE KINTNKDGIT LIGDGKYSTV ISGGSSVGKG SNLRGSATFT
ITGDGFIARD IGFQNTAGPE NHQAIALTVA SDHSVVYRCS ISGYQDTLYA LSLRQFYREC
DIYGTVDFIF GNAAAVFQSC TLVLRRPRNG GAFNTILANG RSDPGQNTGF SVQNCKITVG
ADFSPVKSSY DSYLGRPWKQ YSRAVVMQTN IDGEISSRGW AEWEGAAGST YRTLYFAEYE
NMGPGGATSG RVNWPGFEVI GTAEAAKFTV SNFIGGNSWL PSTGVTFVSG L
//
