Reviewed, UniProtKB/Swiss-Prot P83948 (PME3_CITSI)

Names and origin

Protein names	Recommended name:     Pectinesterase 3       Short name=PE 3     EC=3.1.1.11 Alternative name(s):     Pectin methylesterase 3
Organism	Citrus sinensis (Sweet orange)
Taxonomic identifier	2711 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Sapindales › Rutaceae › Citrus

Protein attributes

Sequence length	584 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	Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity.
Catalytic activity	Pectin + n H2O = n methanol + pectate. Ref.1
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Secreted › cell wall Ref.1.
Tissue specificity	In the peel, expression is localized to the region of the flavedo close to the oil glands, and to the innermost layer of the albedo. In the lamella, expression is localized to the cell layers opposing the fruit tissue, and to the parenchyma surrounding the vascular tissue. In the fruit vesicles, expression is restricted to the peripheral cell layers and stalk cells. High levels of expression are detected in the core matrix. 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
Technical term	Direct protein sequencing
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 – 50	50	Potential
	Propeptide	51 – 266	216	Potential		PRO_0000023482
	Chain	267 – 584	318	Pectinesterase 3		PRO_0000023483
Sites
	Active site	401	1	Proton donor By similarity
	Active site	422	1	Nucleophile By similarity
	Binding site	348	1	Substrate By similarity
	Binding site	378	1	Substrate By similarity
	Binding site	490	1	Substrate By similarity
	Binding site	492	1	Substrate By similarity
	Site	400	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Glycosylation	129	1	N-linked (GlcNAc...) Potential
	Glycosylation	226	1	N-linked (GlcNAc...) Potential
	Disulfide bond	415 ↔ 435		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83948-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E4C17683195311F6	FASTA	584	63,574
	10 20 30 40 50 60 MTRIKEFFTK LSESSTNQNI SNIPKKKKKL FLALFATLLV VAAVIGIVAG VNSRKNSGDN 70 80 90 100 110 120 GNEPHHAILK SSCSSTRYPD LCFSAIAAVP EASKKVTSQK DVIEMSLNIT TTAVEHNYFG 130 140 150 160 170 180 IQKLLKRTNL TKREKVALHD CLETIDETLD ELHKAVEDLE EYPNKKSLSQ HADDLKTLMS 190 200 210 220 230 240 AAMTNQGTCL DGFSHDDANK HVRDALSDGQ VHVEKMCSNA LAMIKNMTDT DMMIMRTSNN 250 260 270 280 290 300 RKLIEETSTV DGWPAWLSTG DRRLLQSSSV TPNVVVAADG SGNFKTVAAS VAAAPQGGTK 310 320 330 340 350 360 RYIIRIKAGV YRENVEVTKK HKNIMFIGDG RTRTIITGSR NVVDGSTTFK SATVAVVGEG 370 380 390 400 410 420 FLARDITFQN TAGPSKHQAV ALRVGADLSA FYNCDMLAYQ DTLYVHSNRQ FFVNCLIAGT 430 440 450 460 470 480 VDFIFGNAAA VLQNCDIHAR KPNSGQKNMV TAQGRADPNQ NTGIVIQKSR IGATSDLKPV 490 500 510 520 530 540 QGSFPTYLGR PWKEYSRTVI MQSSITDVIH PAGWHEWDGN FALNTLFYGE HQNAGAGAGT 550 560 570 580 SGRVKWKGFR VITSATEAQA FTPGSFIAGS SWLGSTGFPF SLGL

References

[1]

"Pectin methyl esterase from orange fruit: characterization and localization by in-situ hybridization and immunohistochemistry." Christensen T.M.I.E., Nielsen J.E., Kreiberg J.D., Rasmussen P., Mikkelsen J.D. Planta 206:493-503(1998) [PubMed: 9821684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 267-279; 302-305; 308-320; 323-330; 351-364; 393-404; 448-466; 469-506 AND 548-579, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Peelings.

Cross-references

3D structure databases
SMR	P83948. Positions 67-228, 266-584.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.11. 2265.
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]
SMART	SM00856. 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

PME3_CITSI

Accession

Primary (citable) accession number: P83948

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)