ID PME1_SOLLC Reviewed; 546 AA. AC P14280; Q43145; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 5. DT 02-SEP-2026, entry version 171. DE RecName: Full=Pectinesterase 1; DE Short=PE 1; DE EC=3.1.1.11; DE AltName: Full=Pectin methylesterase 1; DE Flags: Precursor; GN Name=PME1.9; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; OC Solanum subgen. Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ailsa Craig; TISSUE=Pericarp; RX PubMed=8018878; DOI=10.1007/bf00023246; RA Hall L.N., Bird C.R., Picton S., Tucker G.A., Seymour G.B., Grierson D.; RT "Molecular characterisation of cDNA clones representing pectin esterase RT isozymes from tomato."; RL Plant Mol. Biol. 25:313-318(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-546. RC STRAIN=cv. Rutgers; RA Turner L.A., Kausch K.D., Handa A.K.; RT "Isolation and nucleotide sequence of two cDNAs corresponding to tomato RT fruit pectin methylesterase genes."; RL (er) Plant Gene Register PGR96-035(1996). RN [3] RP PROTEIN SEQUENCE OF 230-546. RX PubMed=3732279; DOI=10.1111/j.1432-1033.1986.tb09775.x; RA Markovic O., Joernvall H.; RT "Pectinesterase. The primary structure of the tomato enzyme."; RL Eur. J. Biochem. 158:455-462(1986). RN [4] RP SEQUENCE REVISION. RX PubMed=2089377; RA Markovic O., Joernvall H.; RT "Tomato and Aspergillus niger pectinesterases. Correlation of differences RT in existing reports: large species variations."; RL Protein Seq. Data Anal. 3:513-515(1990). RN [5] RP SEQUENCE REVISION. RA Markovic O., Joernvall H.; RL Submitted (MAR-1996) to UniProtKB. RN [6] RP DISULFIDE BONDS. RX PubMed=1303747; DOI=10.1002/pro.5560011007; RA Markovic O., Joernvall H.; RT "Disulfide bridges in tomato pectinesterase: variations from RT pectinesterases of other species; conservation of possible active site RT segments."; RL Protein Sci. 1:1288-1292(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 230-546 IN COMPLEX WITH KIWI PMEI. RX PubMed=14635125; DOI=10.1002/prot.10487; RA D'Avino R., Camardella L., Christensen T.M., Giovane A., Servillo L.; RT "Tomato pectin methylesterase: modeling, fluorescence, and inhibitor RT interaction studies-comparison with the bacterial (Erwinia chrysanthemi) RT enzyme."; RL Proteins 53:830-839(2003). CC -!- FUNCTION: Pectinesterase may play a role in cell wall metabolism during CC fruit growth and development prior to ripening and may be required for CC preparing cell walls for softening by polygalacturonase during fruit CC ripening. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = CC [(1->4)-alpha-D-galacturonosyl](n) + n methanol + n H(+); 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. CC -!- DEVELOPMENTAL STAGE: In ripening fruit. 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}. 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 EMBL; X74638; CAA52703.1; -; mRNA. DR EMBL; U50986; AAB67740.1; -; mRNA. DR PIR; A25010; A25010. DR PIR; S46527; S46527. DR RefSeq; NP_001234151.1; NM_001247222.2. DR PDB; 1XG2; X-ray; 1.90 A; A=230-546. DR AlphaFoldDB; P14280; -. DR MDposit; P14280; -. DR SMR; P14280; -. DR STRING; 4081.P14280; -. DR PaxDb; 4081-P14280; -. DR GeneID; 544090; -. DR KEGG; sly:544090; -. DR eggNOG; ENOG502QUQ5; Eukaryota. DR HOGENOM; CLU_012243_9_2_1; -. DR InParanoid; P14280; -. DR OrthoDB; 2019149at2759; -. DR PhylomeDB; P14280; -. DR BioCyc; MetaCyc:MONOMER-16134; -. DR BRENDA; 3.1.1.11; 3101. DR UniPathway; UPA00545; UER00823. DR EvolutionaryTrace; P14280; -. DR Proteomes; UP000004994; Unplaced. 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 CDD; cd15799; PMEI-like_4; 1. DR FunFam; 2.160.20.10:FF:000001; Pectinesterase; 1. DR FunFam; 1.20.140.40:FF:000015; Pectinesterase 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 InterPro; IPR018040; Pectinesterase_Tyr_AS. DR NCBIfam; TIGR01614; PME_inhib; 1. DR PANTHER; PTHR31707; PECTINESTERASE; 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; PS00800; PECTINESTERASE_1; 1. DR PROSITE; PS00503; PECTINESTERASE_2; 1. DR PDBsum; 1XG2; -. PE 1: Evidence at protein level; KW 3D-structure; Aspartyl esterase; Cell wall; KW Cell wall biogenesis/degradation; Direct protein sequencing; KW Disulfide bond; Fruit ripening; Hydrolase; Reference proteome; Secreted; KW Signal; Zymogen. FT SIGNAL 1..39 FT /evidence="ECO:0000255" FT PROPEP 40..229 FT /evidence="ECO:0000269|PubMed:3732279" FT /id="PRO_0000023486" FT CHAIN 230..546 FT /note="Pectinesterase 1" FT /id="PRO_0000023487" FT ACT_SITE 361 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040" FT ACT_SITE 382 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 338 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 450 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 452 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 360 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT DISULFID 327..354 FT /evidence="ECO:0000269|PubMed:1303747" FT DISULFID 395..429 FT /evidence="ECO:0000269|PubMed:1303747" FT CONFLICT 204 FT /note="F -> L (in Ref. 2; AAB67740)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="A -> S (in Ref. 2; AAB67740)" FT /evidence="ECO:0000305" FT CONFLICT 430 FT /note="N -> D (in Ref. 2; AAB67740)" FT /evidence="ECO:0000305" FT CONFLICT 440 FT /note="V -> L (in Ref. 2; AAB67740)" FT /evidence="ECO:0000305" FT CONFLICT 519 FT /note="M -> I (in Ref. 2; AAB67740)" FT /evidence="ECO:0000305" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 242..246 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 262..266 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 268..272 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:1XG2" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:1XG2" FT TURN 302..305 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 313..316 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 322..325 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 367..374 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 376..382 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 389..394 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 396..399 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 408..413 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 423..428 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 430..433 FT /evidence="ECO:0007829|PDB:1XG2" FT TURN 435..437 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:1XG2" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 457..462 FT /evidence="ECO:0007829|PDB:1XG2" FT TURN 479..485 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 487..492 FT /evidence="ECO:0007829|PDB:1XG2" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 515..518 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 519..521 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 523..526 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 530..533 FT /evidence="ECO:0007829|PDB:1XG2" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:1XG2" SQ SEQUENCE 546 AA; 60066 MW; 4FEDF511FF075DCB CRC64; MANPQQPLLI KTHKQNPIIS FKILSFVITL FVALFLVAPY QVEIKHSNLC KTAQDSQLCL SYVSDLISNE IVTTESDGHS ILMKFLVNYV HQMNNAIPVV RKMKNQINDI RQHGALTDCL ELLDQSVDFA SDSIAAIDKR SRSEHANAQS WLSGVLTNHV TCLDELDSFT KAMINGTNLE ELISRAKVAL AMLASLTTQD EDVFMTVLGK MPSWVSSMDR KLMESSGKDI IANAVVAQDG TGDYQTLAEA VAAAPDKSKT RYVIYVKRGT YKENVEVASN KMNLMIVGDG MYATTITGSL NVVDGSTTFR SATLAAVGQG FILQDICIQN TAGPAKDQAV ALRVGADMSV INRCRIDAYQ DTLYAHSQRQ FYRDSYVTGT VDFIFGNAAV VFQKCQLVAR KPGKYQQNMV TAQGRTDPNQ ATGTSIQFCN IIASSDLEPV LKEFPTYLGR PWKEYSRTVV MESYLGGLIN PAGWAEWDGD FALKTLYYGE FMNNGPGAGT SKRVKWPGYH VITDPAKAMP FTVAKLIQGG SWLRSTGVAY VDGLYD //