Q42920 (PME_MEDSA) 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): P65 Pectin methylesterase
Organism	Medicago sativa (Alfalfa)
Taxonomic identifier	3879 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	447 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	Microspores and pollen.
Developmental stage	Expression begins in the uninucleate microspore, reaching a maximum in mature pollen.
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 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 – ?		Potential
	Chain	? – 447		Pectinesterase/pectinesterase inhibitor		PRO_0000023494
Regions
	Region	? – 83		Pectinesterase inhibitor
	Region	131 – 427	297	Pectinesterase
Sites
	Active site	259	1	Proton donor; for pectinesterase activity By similarity
	Active site	280	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	206	1	Substrate; for pectinesterase activity By similarity
	Binding site	236	1	Substrate; for pectinesterase activity By similarity
	Binding site	347	1	Substrate; for pectinesterase activity By similarity
	Binding site	349	1	Substrate; for pectinesterase activity By similarity
	Site	258	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential
	Disulfide bond	273 ↔ 293		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42920 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E191BB8E3EB3400A	FASTA	447	49,133
	10 20 30 40 50 60 MEICNEVLDY AVDGIHKSVG TLDQFDFHKL SEYAFDLKVW LTGTLSHQQT CLDGFANTTT 70 80 90 100 110 120 KAGETMTKVL KTSMELSSNA IDMMDAVSRI LKGFDTSQYS VSRRLLSDDG IPSWVNDGHR 130 140 150 160 170 180 RLLAGGNVQP NAVVAQDGSG QFKTLTDALK TVPPKNAVPF VIHVKAGVYK ETVNVAKEMN 190 200 210 220 230 240 YVTVIGDGPT KTKFTGSLNY ADGINTYNTA TFGVNGANFM AKDIGFENTA GTGKHQAVAL 250 260 270 280 290 300 RVTADQAIFY NCQMDGFQDT LYVQSQRQFY RDCSISGTID FVFGERFGVF QNCKLVCRLP 310 320 330 340 350 360 AKGQQCLVTA GGREKQNSAS ALVFQSSHFT GEPALTSVTP KVSYLGRPWK QYSKVVIMDS 370 380 390 400 410 420 TIDAIFVPEG YMPWMGSAFK ETCTYYEYNN KGPGADTNLR VKWHGVKVLT SNVAAEYYPG 430 440 KFFEIVNATA RDTWIVKSGV PYSLGPM

References

[1]	"A pollen-specific cDNA (P65) encoding a putative pectin esterase in Alfalfa." Qiu X., Erickson L. Plant Gene Register PGR95-094 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. C2-4. Tissue: Pollen.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U28148 mRNA. Translation: AAA91128.1.
PIR	T09414.
3D structure databases
ProteinModelPortal	Q42920.
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]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit. SSF101148. Pectinesterase_inhib. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME_MEDSA

Accession

Primary (citable) accession number: Q42920

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program