P14280 (PME1_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase 1
Short name=PE 1
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 1

Gene names

Name:

PME1.9

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening.
Catalytic activity	Pectin + n H2O = n methanol + pectate.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Secreted › cell wall.
Developmental stage	In ripening fruit.
Miscellaneous	The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.
Sequence similarities	In the N-terminal section; belongs to the PMEI family. In the C-terminal section; belongs to the pectinesterase family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Fruit ripening
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW ripening Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW enzyme inhibitor activity Inferred from electronic annotation. Source: InterPro pectinesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 39

39

Potential

Propeptide

40 – 229

190

PRO_0000023486

Chain

230 – 546

317

Pectinesterase 1

PRO_0000023487

Sites

Active site

361

1

Proton donor By similarity

Active site

382

1

Nucleophile By similarity

Binding site

308

1

Substrate By similarity

Binding site

338

1

Substrate By similarity

Binding site

450

1

Substrate By similarity

Binding site

452

1

Substrate By similarity

Site

360

1

Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond

327 ↔ 354

Ref.6

Disulfide bond

395 ↔ 429

Ref.6

Experimental info

Sequence conflict

204

1

F → L in AAB67740. Ref.2

Sequence conflict

278

1

A → S in AAB67740. Ref.2

Sequence conflict

430

1

N → D in AAB67740. Ref.2

Sequence conflict

440

1

V → L in AAB67740. Ref.2

Sequence conflict

519

1

M → I in AAB67740. Ref.2

Secondary structure

1

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546

Helix Strand Turn

Details...

Beta strand

233 – 236

4

Beta strand

242 – 246

5

Helix

247 – 253

7

Beta strand

262 – 266

5

Beta strand

268 – 272

5

Beta strand

275 – 277

3

Beta strand

283 – 289

7

Turn

291 – 293

3

Beta strand

294 – 298

5

Turn

302 – 305

4

Helix

309 – 311

3

Beta strand

313 – 316

4

Beta strand

322 – 325

4

Beta strand

327 – 330

4

Helix

334 – 336

3

Beta strand

341 – 344

4

Beta strand

349 – 353

5

Beta strand

355 – 357

3

Beta strand

363 – 365

3

Beta strand

367 – 374

8

Beta strand

376 – 382

7

Beta strand

384 – 386

3

Beta strand

389 – 394

6

Beta strand

396 – 399

4

Beta strand

408 – 413

6

Beta strand

423 – 428

6

Beta strand

430 – 433

4

Turn

435 – 437

3

Helix

438 – 440

3

Turn

441 – 443

3

Beta strand

446 – 449

4

Beta strand

457 – 462

6

Turn

479 – 485

7

Beta strand

487 – 492

6

Beta strand

509 – 512

4

Helix

515 – 518

4

Helix

519 – 521

3

Helix

523 – 526

4

Helix

530 – 533

4

Helix

534 – 536

3

Sequences

	Sequence		Length	Mass (Da)
	P14280 [UniParc]. Last modified July 15, 1999. Version 5. Checksum: 4FEDF511FF075DCB	FASTA	546	60,066
	10 20 30 40 50 60 MANPQQPLLI KTHKQNPIIS FKILSFVITL FVALFLVAPY QVEIKHSNLC KTAQDSQLCL 70 80 90 100 110 120 SYVSDLISNE IVTTESDGHS ILMKFLVNYV HQMNNAIPVV RKMKNQINDI RQHGALTDCL 130 140 150 160 170 180 ELLDQSVDFA SDSIAAIDKR SRSEHANAQS WLSGVLTNHV TCLDELDSFT KAMINGTNLE 190 200 210 220 230 240 ELISRAKVAL AMLASLTTQD EDVFMTVLGK MPSWVSSMDR KLMESSGKDI IANAVVAQDG 250 260 270 280 290 300 TGDYQTLAEA VAAAPDKSKT RYVIYVKRGT YKENVEVASN KMNLMIVGDG MYATTITGSL 310 320 330 340 350 360 NVVDGSTTFR SATLAAVGQG FILQDICIQN TAGPAKDQAV ALRVGADMSV INRCRIDAYQ 370 380 390 400 410 420 DTLYAHSQRQ FYRDSYVTGT VDFIFGNAAV VFQKCQLVAR KPGKYQQNMV TAQGRTDPNQ 430 440 450 460 470 480 ATGTSIQFCN IIASSDLEPV LKEFPTYLGR PWKEYSRTVV MESYLGGLIN PAGWAEWDGD 490 500 510 520 530 540 FALKTLYYGE FMNNGPGAGT SKRVKWPGYH VITDPAKAMP FTVAKLIQGG SWLRSTGVAY VDGLYD

References

[1]	"Molecular characterisation of cDNA clones representing pectin esterase isozymes from tomato." Hall L.N., Bird C.R., Picton S., Tucker G.A., Seymour G.B., Grierson D. Plant Mol. Biol. 25:313-318(1994) [PubMed: 8018878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Ailsa Craig. Tissue: Pericarp.
[2]	"Isolation and nucleotide sequence of two cDNAs corresponding to tomato fruit pectin methylesterase genes." Turner L.A., Kausch K.D., Handa A.K. Plant Gene Register PGR96-035 Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-546. Strain: cv. Rutgers.
[3]	"Pectinesterase. The primary structure of the tomato enzyme." Markovic O., Joernvall H. Eur. J. Biochem. 158:455-462(1986) [PubMed: 3732279] [Abstract] Cited for: PROTEIN SEQUENCE OF 230-546.
[4]	"Tomato and Aspergillus niger pectinesterases. Correlation of differences in existing reports: large species variations." Markovic O., Joernvall H. Protein Seq. Data Anal. 3:513-515(1990) [PubMed: 2089377] [Abstract] Cited for: SEQUENCE REVISION.
[5]	Markovic O., Joernvall H. Submitted (MAR-1996) to UniProtKB Cited for: SEQUENCE REVISION.
[6]	"Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments." Markovic O., Joernvall H. Protein Sci. 1:1288-1292(1992) [PubMed: 1303747] [Abstract] Cited for: DISULFIDE BONDS.
[7]	"Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies-comparison with the bacterial (Erwinia chrysanthemi) enzyme." D'Avino R., Camardella L., Christensen T.M., Giovane A., Servillo L. Proteins 53:830-839(2003) [PubMed: 14635125] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 230-546 IN COMPLEX WITH KIWI PMEI.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X74638 mRNA. Translation: CAA52703.1.
U50986 mRNA. Translation: AAB67740.1.

PIR

A25010.
S46527.

RefSeq

NP_001234151.1. NM_001247222.1.

UniGene

Les.3122.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XG2	X-ray	1.90	A	230-546	[»]

ProteinModelPortal

P14280.

SMR

P14280. Positions 230-546.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

544090.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16134.

Family and domain databases

InterPro

IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.

Pfam

PF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]

SUPFAM

SSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.

TIGRFAMs

TIGR01614. PME_inhib. 1 hit.

PROSITE

PS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PME1_SOLLC

Accession

Primary (citable) accession number: P14280
Secondary accession number(s): Q43145

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 15, 1999
Last modified:	December 14, 2011
This is version 105 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program