PME_MEDSA
ID PME_MEDSA Reviewed; 447 AA.
AC Q42920;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor;
DE AltName: Full=Pectin methylesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase;
DE Short=PE;
DE EC=3.1.1.11;
DE AltName: Full=P65;
DE AltName: Full=Pectin methylesterase;
DE Flags: Precursor;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C2-4; TISSUE=Pollen;
RA Qiu X., Erickson L.;
RT "A pollen-specific cDNA (P65) encoding a putative pectin esterase in
RT Alfalfa.";
RL (er) Plant Gene Register PGR95-094(1995).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Microspores and pollen.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the uninucleate microspore,
CC reaching a maximum in mature pollen.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
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DR EMBL; U28148; AAA91128.1; -; mRNA.
DR PIR; T09414; T09414.
DR AlphaFoldDB; Q42920; -.
DR SMR; Q42920; -.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 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 Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..447
FT /note="Pectinesterase/pectinesterase inhibitor"
FT /id="PRO_0000023494"
FT REGION ?..83
FT /note="Pectinesterase inhibitor"
FT REGION 131..427
FT /note="Pectinesterase"
FT ACT_SITE 259
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 280
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 206
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 273..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 49133 MW; E191BB8E3EB3400A CRC64;
MEICNEVLDY AVDGIHKSVG TLDQFDFHKL SEYAFDLKVW LTGTLSHQQT CLDGFANTTT
KAGETMTKVL KTSMELSSNA IDMMDAVSRI LKGFDTSQYS VSRRLLSDDG IPSWVNDGHR
RLLAGGNVQP NAVVAQDGSG QFKTLTDALK TVPPKNAVPF VIHVKAGVYK ETVNVAKEMN
YVTVIGDGPT KTKFTGSLNY ADGINTYNTA TFGVNGANFM AKDIGFENTA GTGKHQAVAL
RVTADQAIFY NCQMDGFQDT LYVQSQRQFY RDCSISGTID FVFGERFGVF QNCKLVCRLP
AKGQQCLVTA GGREKQNSAS ALVFQSSHFT GEPALTSVTP KVSYLGRPWK QYSKVVIMDS
TIDAIFVPEG YMPWMGSAFK ETCTYYEYNN KGPGADTNLR VKWHGVKVLT SNVAAEYYPG
KFFEIVNATA RDTWIVKSGV PYSLGPM
