P83947 (PME1_FICPW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Pectinesterase/pectinesterase inhibitor Including the following 2 domains: Pectinesterase inhibitor Alternative name(s): Pectin methylesterase inhibitor Pectinesterase Short name=PE EC=3.1.1.11 Alternative name(s): Pectin methylesterase
Organism	Ficus pumila var. awkeotsang (Jelly fig) (Ficus awkeotsang)
Taxonomic identifier	204231 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Moraceae › Ficus

Protein attributes

Sequence length	545 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.2 Ref.3
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Secreted › cell wall Probable.
Post-translational modification	N-glycosylated. Ref.3
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 cell wall organization 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 – 37	37	Potential
	Propeptide	38 – 228	191			PRO_0000023484
	Chain	229 – 545	317	Pectinesterase/pectinesterase inhibitor		PRO_0000023485
Regions
	Region	38 – 191	154	Pectinesterase inhibitor
	Region	232 – 530	299	Pectinesterase
Sites
	Active site	360	1	Proton donor; for pectinesterase activity By similarity
	Active site	381	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	307	1	Substrate; for pectinesterase activity By similarity
	Binding site	337	1	Substrate; for pectinesterase activity By similarity
	Binding site	449	1	Substrate; for pectinesterase activity By similarity
	Binding site	451	1	Substrate; for pectinesterase activity By similarity
	Site	359	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	135	1	N-linked (GlcNAc...) Potential
	Glycosylation	375	1	N-linked (GlcNAc...) (complex)
	Disulfide bond	326 ↔ 353		By similarity
	Disulfide bond	394 ↔ 428		By similarity
Experimental info
	Sequence conflict	249	1	A → H AA sequence Ref.2
	Sequence conflict	255	1	D → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P83947 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: CF7B40DF36655D93	FASTA	545	60,602
	10 20 30 40 50 60 MEINQPNLLE ASKSCYSKIT FFLLVISFAA LVSTGFSSPE LSLHHKICDQ SVNKESCLAM 70 80 90 100 110 120 ISEVTGLNMA DHRNLLKSFL EKTTPRIQKA FETANDASRR INNPQERTAL LDCAELMDLS 130 140 150 160 170 180 KERVVDSISI LFHQNLTTRS HEDLHVWLSG VLTNHVTCLD GLEEGSTDYI KTLMESHLNE 190 200 210 220 230 240 LILRARTSLA IFVTLFPAKS NVIEPVTGNF PTWVTAGDRR LLQTLGKDIE PDIVVAKDGS 250 260 270 280 290 300 GDYETLNEAV AAIPDNSKKR VIVLVRTGIY EENVDFGYQK KNVMLVGEGM DYTIITGSRN 310 320 330 340 350 360 VVDGSTTFDS ATVAAVGDGF IAQDICFQNT AGPEKYQAVA LRIGADETVI NRCRIDAYQD 370 380 390 400 410 420 TLYPHNYRQF YRDRNITGTV DFIFGNAAVV FQNCNLIPRK QMKGQENTIT AQGRTDPNQN 430 440 450 460 470 480 TGTSIQNCEI FASADLEPVE DTFKSYLGRP WKEYSRTVVM ESYISDVIDP AGWLEWDRDF 490 500 510 520 530 540 ALKTLFYGEY RNGGPGSGTS ERVKWPGYHV ITSPEVAEQF TVAELIQGGS WLGSTGVDYT AGLYA

References

[1]	"Cloning and expression of an acidic pectin methylesterase from jelly fig (Ficus awkeotsang)." Ding J.L.C., Lee T.T.T., Wang M.M.C., Tai S.S.K., Tzen J.T.C. J. Agric. Food Chem. 48:3052-3057(2000) [PubMed: 10898664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 229-239. Tissue: Pericarp.
[2]	"Purification and characterization of pectinmethylesterase from Ficus awkeotsang makino achenes." Lin T.-P., Liu C.-C., Chen S.-W., Wang W.-Y. Plant Physiol. 91:1445-1453(1989) [PubMed: 16667199] [Abstract] Cited for: PROTEIN SEQUENCE OF 229-256, CATALYTIC ACTIVITY. Tissue: Pericarp.
[3]	"Purification and glycosylation analysis of an acidic pectin methylesterase in jelly fig (Ficus awkeotsang) achenes." Ding J.L.C., Hsu J.S.F., Wang M.M.C., Tzen J.T.C. J. Agric. Food Chem. 50:2920-2925(2002) [PubMed: 11982420] [Abstract] Cited for: CATALYTIC ACTIVITY, GLYCOSYLATION. Tissue: Pericarp.

Cross-references

3D structure databases
ProteinModelPortal	P83947.
SMR	P83947. Positions 234-544.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit. SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMs	TIGR01614. PME_inhib. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME1_FICPW

Accession

Primary (citable) accession number: P83947

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program