PME3_PHAVU
ID PME3_PHAVU Reviewed; 581 AA.
AC Q43111;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Pectinesterase 3;
DE Short=PE 3;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 3;
DE Flags: Precursor;
GN Name=MPE3;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Masai;
RX PubMed=8914530; DOI=10.1007/bf00040831;
RA Ebbelaar C.E.M., Tucker G.A., Laats J.M., van Dijk C., Stolle-Smits T.,
RA Recourt K.;
RT "Characterization of pectinases and pectin methylesterase cDNAs in pods of
RT green beans (Phaseolus vulgaris L.).";
RL Plant Mol. Biol. 31:1141-1151(1996).
CC -!- FUNCTION: May have roles in the deposition of pectin in developing
CC tissues and in the wall loosening and cell separation that occurs in
CC cell expansion, fruit ripening and abscission.
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 -!- 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; X85216; CAA59482.1; -; mRNA.
DR PIR; S53105; S53105.
DR AlphaFoldDB; Q43111; -.
DR SMR; Q43111; -.
DR STRING; 3885.XP_007135363.1; -.
DR EnsemblPlants; ESW07357; ESW07357; PHAVU_010G123100g.
DR Gramene; ESW07357; ESW07357; PHAVU_010G123100g.
DR eggNOG; ENOG502QVK0; Eukaryota.
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 SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 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..55
FT /evidence="ECO:0000255"
FT CHAIN 56..581
FT /note="Pectinesterase 3"
FT /id="PRO_0000023496"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 400
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..435
FT /evidence="ECO:0000250"
SQ SEQUENCE 581 AA; 63588 MW; CDB0621372E59BFE CRC64;
MDTIKSFKGY GKVNELEQQA YEKKTRKRLI IIAVSSIVLI AVIIAAVAGV VIHNRNSESS
PSSDSVPQTE LSPAASLKAV CDTTRYPSSC FSSISSLPES NTTDPELLFK LSLRVAIDEL
SSFPSKLRAN AEQDARLQKA IDVCSSVFGD ALDRLNDSIS ALGTVAGRIA SSASVSNVET
WLSAALTDQD TCLDAVGELN STAARGALQE IETAMRNSTE FASNSLAIVT KILGLLSRFE
TPIHHRRLLG FPEWLGAAER RLLEEKNNDS TPDAVVAKDG SGQFKTIGEA LKLVKKKSEE
RFSVYVKEGR YVENIDLDKN TWNVMIYGDG KDKTFVVGSR NFMDGTPTFE TATFAVKGKG
FIAKDIGFVN NAGASKHQAV ALRSGSDRSV FFRCSFDGFQ DTLYAHSNRQ FYRDCDITGT
IDFIFGNAAV VFQSCKIMPR QPLPNQFNTI TAQGKKDPNQ NTGIIIQKST ITPFGNNLTA
PTYLGRPWKD FSTTVIMQSD IGALLNPVGW MSWVPNVEPP TTIFYAEYQN SGPGADVSQR
VKWAGYKPTI TDRNAEEFTV QSFIQGPEWL PNAAVQFDST L
