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 27-MAR-2024, entry version 92. 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 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; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 PANTHER; PTHR31707; PECTINESTERASE; 1. DR PANTHER; PTHR31707:SF3; PECTINESTERASE_PECTINESTERASE INHIBITOR 3; 1. DR Pfam; PF01095; Pectinesterase; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 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 //