PME1_SOLLC
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 03-AUG-2022, entry version 157.
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 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.
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}.
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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 PDBsum; 1XG2; -.
DR AlphaFoldDB; P14280; -.
DR SMR; P14280; -.
DR STRING; 4081.Solyc07g064170.2.1; -.
DR PaxDb; P14280; -.
DR PRIDE; P14280; -.
DR GeneID; 544090; -.
DR KEGG; sly:544090; -.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; P14280; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; P14280; -.
DR BioCyc; MetaCyc:MON-16134; -.
DR BRENDA; 3.1.1.11; 3101.
DR UniPathway; UPA00545; UER00823.
DR EvolutionaryTrace; P14280; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P14280; baseline.
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; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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 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
