Reviewed, UniProtKB/Swiss-Prot O04887 (PME2_CITSI)

Names and origin

Protein names

Recommended name:
    Pectinesterase 2
      Short name=PE 2
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase

Gene names

Name:

PECS-2.1

Organism

Citrus sinensis (Sweet orange)

Taxonomic identifier

2711 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Sapindales › Rutaceae › Citrus

Protein attributes

Sequence length	510 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	Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity.
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 Probable.
Tissue specificity	Expressed at low levels in young leaves, young bark, young fruit, mature fruit vesicles, shoots and flower buds, young bark and juice vesicles. In both leaf and fruit abscission zones, and mature leaves, expression was initially undetectable but increased markedly following ethylene treatment. Ref.1
Induction	By ethylene. Ref.1
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
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro
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 – 19	19	Potential
	Chain	20 – 510	491	Pectinesterase 2		PRO_0000023481
Sites
	Active site	328	1	Proton donor By similarity
	Active site	349	1	Nucleophile By similarity
	Binding site	275	1	Substrate By similarity
	Binding site	305	1	Substrate By similarity
	Binding site	416	1	Substrate By similarity
	Binding site	418	1	Substrate By similarity
	Site	327	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	110	1	N-linked (GlcNAc...) Potential
	Glycosylation	158	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential
	Glycosylation	385	1	N-linked (GlcNAc...) Potential
	Disulfide bond	342 ↔ 362		By similarity
Experimental info
	Sequence conflict	130	1	T → S in AAB57671. Ref.1
	Sequence conflict	166	1	T → A in AAB57671. Ref.1
	Sequence conflict	387	1	S → N in AAB57671. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O04887-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: BD4D57D0376A2035	FASTA	510	56,328
	10 20 30 40 50 60 MALRILITVS LVLFSLSHTS FGYSPEEVKS WCGKTPNPQP CEYFLTQKTD VTSIKQDTDF 70 80 90 100 110 120 YKISLQLALE RATTAQSRTY TLGSKCRNER EKAAWEDCRE LYELTVLKLN QTSNSSPGCT 130 140 150 160 170 180 KVDKQTWLST ALTNLETCRA SLEDLGVPEY VLPLLSNNVT KLISNTLSLN KVPYNEPSYK 190 200 210 220 230 240 DGFPTWVKPG DRKLLQTTPR ANIVVAQDGS GNVKTIQEAV AAASRAGGSR YVIYIKAGTY 250 260 270 280 290 300 NENIEVKLKN IMFVGDGIGK TIITGSKSVG GGATTFKSAT VAVVGDNFIA RDITIRNTAG 310 320 330 340 350 360 PNNHQAVALR SGSDLSVFYR CSFEGYQDTL YVHSQRQFYR ECDIYGTVDF IFGNAAVVLQ 370 380 390 400 410 420 NCNIFARKPP NRTNTLTAQG RTDPNQSTGI IIHNCRVTAA SDLKPVQSSV KTFLGRPWKQ 430 440 450 460 470 480 YSRTVYIKTF LDSLINPAGW MEWSGDFALN TLYYAEYMNT GPGSSTANRV KWRGYHVLTS 490 500 510 PSQVSQFTVG NFIAGNSWLP ATNVPFTSGL

References

[1]	"Genetics and expression of two pectinesterase genes in Valencia orange." Nairn C.J., Lewandowski D.J., Burns J.K. Physiol. Plantarum 102:226-235(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Valencia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U82975 Genomic DNA. Translation: AAB57669.1. U82977 mRNA. Translation: AAB57671.1.
PIR	T10491. T10494.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.11. 2265.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. 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]
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

PME2_CITSI

Accession

Primary (citable) accession number: O04887
Secondary accession number(s): O04889

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 1, 1997
Last modified:	September 22, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)