PME_DAUCA
ID PME_DAUCA Reviewed; 319 AA.
AC P83218;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Pectinesterase;
DE Short=PE;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
OS Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC STRAIN=cv. Tiptop; TISSUE=Root;
RX PubMed=11964128; DOI=10.1007/s00018-002-8442-6;
RA Markovic O., Cederlund E., Griffiths W.J., Lipka T., Joernvall H.;
RT "Characterization of carrot pectin methylesterase.";
RL Cell. Mol. Life Sci. 59:513-518(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND CHARACTERIZATION.
RX PubMed=11943159; DOI=10.1016/s0014-5793(02)02372-4;
RA Johansson K., El-Ahmad M., Friemann R., Joernvall H., Markovic O.,
RA Eklund H.;
RT "Crystal structure of plant pectin methylesterase.";
RL FEBS Lett. 514:243-249(2002).
CC -!- FUNCTION: Catalyzes the deesterification of methyl-esterified D-
CC galactosiduronic acid units in pectic compounds. It participates in
CC modulating cell wall during fruit ripening, cell wall extension during
CC pollen germination, and in defense mechanisms against pathogens.
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 -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1GQ8; X-ray; 1.75 A; A=2-319.
DR PDBsum; 1GQ8; -.
DR AlphaFoldDB; P83218; -.
DR SMR; P83218; -.
DR PRIDE; P83218; -.
DR BRENDA; 3.1.1.11; 1841.
DR UniPathway; UPA00545; UER00823.
DR EvolutionaryTrace; P83218; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
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; 2.160.20.10; -; 1.
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; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl esterase; Cell wall;
KW Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Pyrrolidone carboxylic acid; Secreted.
FT CHAIN 1..319
FT /note="Pectinesterase"
FT /id="PRO_0000215045"
FT ACT_SITE 136
FT /note="Proton donor"
FT ACT_SITE 157
FT /note="Nucleophile"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11964128"
FT DISULFID 150..170
FT /evidence="ECO:0000250"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1GQ8"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1GQ8"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1GQ8"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1GQ8"
FT TURN 254..260
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1GQ8"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1GQ8"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1GQ8"
SQ SEQUENCE 319 AA; 34254 MW; 359675FF36FD7625 CRC64;
QSSTVTPNVV VAADGSGDYK TVSEAVAAAP EDSKTRYVIR IKAGVYRENV DVPKKKKNIM
FLGDGRTSTI ITASKNVQDG STTFNSATVA AVGAGFLARD ITFQNTAGAA KHQAVALRVG
SDLSAFYRCD ILAYQDSLYV HSNRQFFINC FIAGTVDFIF GNAAVVLQDC DIHARRPGSG
QKNMVTAQGR TDPNQNTGIV IQKSRIGATS DLQPVQSSFP TYLGRPWKEY SRTVVMQSSI
TNVINPAGWF PWDGNFALDT LYYGEYQNTG AGAATSGRVT WKGFKVITSS TEAQGFTPGS
FIAGGSWLKA TTFPFSLGL
