P09607 (PME21_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase 2.1
Short name=PE 2.1
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 2.1

Gene names

Name:

PME2.1

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	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 Glycoprotein Zymogen
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 – ?		Potential
	Propeptide	? – 233		Potential		PRO_0000023488
	Chain	234 – 550	317	Pectinesterase 2.1		PRO_0000023489
Sites
	Active site	365	1	Proton donor By similarity
	Active site	386	1	Nucleophile By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	342	1	Substrate By similarity
	Binding site	454	1	Substrate By similarity
	Binding site	456	1	Substrate By similarity
	Site	364	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Disulfide bond	331 ↔ 358		By similarity
	Disulfide bond	399 ↔ 433		By similarity
Experimental info
	Sequence conflict	377 – 378	2	RD → QS in CAA30746. Ref.3
	Sequence conflict	377 – 378	2	RD → QS in CAA01257. Ref.3
	Sequence conflict	468	1	Y → S in CAA30746. Ref.3
	Sequence conflict	468	1	Y → S in CAA01257. Ref.3
	Sequence conflict	515	1	V → C in AAB67739. Ref.2
	Sequence conflict	550	1	D → DYSDIKLLFVYVTRHL in CAA30746. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09607 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 7ABB7CC37E849DE7	FASTA	550	60,500
	10 20 30 40 50 60 MATPQQPLLT KTHKQNSIIS FKILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS 70 80 90 100 110 120 QLCLSYVSDL ISNEIVTSDS DGLSILKKFL VYSVHQMNNA IPVVRKIKNQ INDIREQGAL 130 140 150 160 170 180 TDCLELLDLS VDLVCDSIAA IDKRSRSEHA NAQSWLSGVL TNHVTCLDEL DSFTKAMING 190 200 210 220 230 240 TNLDELISRA KVALAMLASV TTPNDEVLRP GLGKMPSWVS SRDRKLMESS GKDIGANAVV 250 260 270 280 290 300 AKDGTGKYRT LAEAVAAAPD KSKTRYVIYV KRGTYKENVE VSSRKMNLMI IGDGMYATII 310 320 330 340 350 360 TGSLNVVDGS TTFHSATLAA VGKGFILQDI CIQNTAGPAK HQAVALRVGA DKSVINRCRI 370 380 390 400 410 420 DAYQDTLYAH SQRQFYRDSY VTGTIDFIFG NAAVVFQKCQ LVARKPGKYQ QNMVTAQGRT 430 440 450 460 470 480 DPNQATGTSI QFCDIIASPD LKPVVKEFPT YLGRPWKKYS RTVVMESYLG GLIDPSGWAE 490 500 510 520 530 540 WHGDFALKTL YYGEFMNNGP GAGTSKRVKW PGYHVITDPA EAMSFTVAKL IQGGSWLRST 550 DVAYVDGLYD

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]. Strain: cv. Rutgers. Tissue: Fruit.
[3]	"Identification and sequence determination of a cDNA clone for tomato pectin esterase." Ray J., Knapp J., Grierson D., Bird C., Schuch W. Eur. J. Biochem. 174:119-124(1988) [PubMed: 3371355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-550.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74639 mRNA. Translation: CAA52704.1. U50985 mRNA. Translation: AAB67739.1. X07910 mRNA. Translation: CAA30746.1. A15983 Unassigned RNA. Translation: CAA01257.1.
PIR	S46528.
RefSeq	NP_001233948.1. NM_001247019.1.
UniGene	Les.3630.
3D structure databases
ProteinModelPortal	P09607.
SMR	P09607. Positions 234-550.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	544289.
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

PME21_SOLLC

Accession

Primary (citable) accession number: P09607
Secondary accession number(s): Q43144, Q43777

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program