Reviewed, UniProtKB/Swiss-Prot Q43867 (PME1_ARATH)

Names and origin

Protein names

Recommended name:
    Pectinesterase 1
      Short name=PE 1
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 1
      Short name=AtPME1

Gene names

Name:	PME1
Synonyms:	ARATH65
Ordered Locus Names:	At1g53840
ORF Names:	T18A20.7

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	586 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 in siliques. Ref.6
Developmental stage	Expressed throughout silique development. Ref.6
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	Complete proteome
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 plasma membrane Inferred from direct assay. Source: TAIR
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 – 49	49	Potential
	Chain	50 – 586	537	Pectinesterase 1		PRO_0000023474
Regions
	Compositional bias	248 – 251	4	Poly-Arg
Sites
	Active site	408	1	Proton donor By similarity
	Active site	429	1	Nucleophile By similarity
	Binding site	355	1	Substrate By similarity
	Binding site	385	1	Substrate By similarity
	Binding site	492	1	Substrate By similarity
	Binding site	494	1	Substrate By similarity
	Site	407	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	154	1	N-linked (GlcNAc...) Potential
	Glycosylation	201	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Glycosylation	466	1	N-linked (GlcNAc...) Potential
	Disulfide bond	422 ↔ 442		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43867-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EF2752BCC535BE99	FASTA	586	64,149
	10 20 30 40 50 60 MDSVNSFKGY GKVDEAQDLA LKKKTRKRLL LLSISVVVLI AVIIAAVVAT VVHKNKNEST 70 80 90 100 110 120 PSPPPELTPS TSLKAICSVT RFPESCISSI SKLPSSNTTD PETLFKLSLK VIIDELDSIS 130 140 150 160 170 180 DLPEKLSKET EDERIKSALR VCGDLIEDAL DRLNDTVSAI DDEEKKKTLS SSKIEDLKTW 190 200 210 220 230 240 LSATVTDHET CFDSLDELKQ NKTEYANSTI TQNLKSAMSR STEFTSNSLA IVSKILSALS 250 260 270 280 290 300 DLGIPIHRRR RLMSHHHQQS VDFEKWARRR LLQTAGLKPD VTVAGDGTGD VLTVNEAVAK 310 320 330 340 350 360 VPKKSLKMFV IYVKSGTYVE NVVMDKSKWN VMIYGDGKGK TIISGSKNFV DGTPTYETAT 370 380 390 400 410 420 FAIQGKGFIM KDIGIINTAG AAKHQAVAFR SGSDFSVYYQ CSFDGFQDTL YPHSNRQFYR 430 440 450 460 470 480 DCDVTGTIDF IFGSAAVVFQ GCKIMPRQPL SNQFNTITAQ GKKDPNQSSG MSIQRCTISA 490 500 510 520 530 540 NGNVIAPTYL GRPWKEFSTT VIMETVIGAV VRPSGWMSWV SGVDPPASIV YGEYKNTGPG 550 560 570 580 SDVTQRVKWA GYKPVMSDAE AAKFTVATLL HGADWIPATG VINQLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterisation of a putative pectin methylesterase cDNA in Arabidopsis thaliana (L.)." Richard L., Qin L.X., Gadal P., Goldberg R. FEBS Lett. 355:135-139(1994) [PubMed: 7982486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Shoot.
[2]	"Clustered genes within the genome of Arabidopsis thaliana encoding pectin methylesterase-like enzymes." Richard L., Qin L.X., Goldberg R. Gene 170:207-211(1996) [PubMed: 8666246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Pectin methylesterases: sequence-structural features and phylogenetic relationships." Markovic O., Janecek S. Carbohydr. Res. 339:2281-2295(2004) [PubMed: 15337457] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"Comprehensive expression profiling of the pectin methylesterase gene family during silique development in Arabidopsis thaliana." Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F., Guerineau F., Pelloux J. Planta 224:782-791(2006) [PubMed: 16622707] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X81585 mRNA. Translation: CAA57275.1. U25649 Genomic DNA. Translation: AAC50024.1. AC009324 Genomic DNA. Translation: AAF02857.1. AY054197 mRNA. Translation: AAL06858.1.
IPI	IPI00543108.
PIR	JC4778.
RefSeq	NP_175787.1.
UniGene	At.24997
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Proteomic databases
PRIDE	Q43867.
Genome annotation databases
GeneID	841821.
GenomeReviews	Gene locus AT1G53840 in contig CT485782_GR.
KEGG	ath:AT1G53840.
NMPDR	fig|3702.1.peg.4888.
Organism-specific databases
GeneFarm	133. 8.
TAIR	At1g53840.
Phylogenomic databases
OMA	KTWLSAT.
Enzyme and pathway databases
BRENDA	3.1.1.11. 302.
Gene expression databases
ArrayExpress	Q43867.
Genevestigator	Q43867.
GermOnline	AT1G53840. Arabidopsis thaliana.
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

PME1_ARATH

Accession

Primary (citable) accession number: Q43867

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)