Q42608 (PME_BRACM) 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	Brassica campestris (Field mustard)
Taxonomic identifier	3711 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica

Protein attributes

Sequence length	571 AA.
Sequence status	Fragment.
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.
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
Molecular function	Aspartyl esterase Hydrolase
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
	Chain	‹1 – 571	›571	Pectinesterase/pectinesterase inhibitor		PRO_0000215044
Regions
	Region	27 – 178	152	Pectinesterase inhibitor
	Region	259 – 558	300	Pectinesterase
	Compositional bias	245 – 254	10	Poly-Gly
Sites
	Active site	389	1	Proton donor; for pectinesterase activity By similarity
	Active site	410	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	336	1	Substrate; for pectinesterase activity By similarity
	Binding site	366	1	Substrate; for pectinesterase activity By similarity
	Binding site	479	1	Substrate; for pectinesterase activity By similarity
	Binding site	481	1	Substrate; for pectinesterase activity By similarity
	Site	388	1	Transition state stabilizer By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q42608 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 88B56AB6254D87C7	FASTA	571	61,711
	10 20 30 40 50 60 LLVVGVAIGV VTFVNKGGGA GGDKTLNSHQ KAVESLCASA TDKGSCAKTL DPVKSDDPSK 70 80 90 100 110 120 LIKAFMLATK DAVTKSTNFT ASTEEGMGKN MNATSKAVLD YCKRVLMYAL EDLETIVEEM 130 140 150 160 170 180 GEDLQQSGSK MDQLKQWLTG VFNYQTDCID DIEESELRKV MGEGIRHSKI LSSNAIDIFH 190 200 210 220 230 240 ALTTAMSQMN VKVDDMKKGN LGETPAPDRD LLEDLDQKGL PKWHSDKDRK LMAQAGRPGA 250 260 270 280 290 300 PADEGIGEGG GGGGKIKPTH VVAKDGSGQF KTISEAVKAC PEKNPGRCII YIKAGVYKEQ 310 320 330 340 350 360 VTIPKKVNNV FMFGDGATQT IITFDRSVGL SPGTTTSLSG TVQVESEGFM AKWIGFQNTA 370 380 390 400 410 420 GPLGNQAVAF RVNGDRAVIF NCRFDGYQDT LYVNNGRQFY RNIVVSGTVD FINGKSATVI 430 440 450 460 470 480 QNSLILCRKG SPGQTNHVTA DGKQKGKAVK IGIVLHNCRI MADKELEADR LTVKSYLGRP 490 500 510 520 530 540 WKPFATTAVI GTEIGDLIQP TGWNEWQGEK FHLTATYVEF NNRGPGANPA ARVPWAKMAK 550 560 570 SAAEVERFTV ANWLTPANWI QEANVTVQLG L

References

[1]	Kim H.U., Park B.S., Lee J.Y., Jin Y.M., Chung T.Y., Kang S.K. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Anther.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L48178 mRNA. Translation: AAB04617.1.
PIR	T52325.
3D structure databases
ProteinModelPortal	Q42608.
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. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME_BRACM

Accession

Primary (citable) accession number: Q42608

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program