Reviewed, UniProtKB/Swiss-Prot Q9MAL0 (PME57_ARATH)

Names and origin

Protein names

Recommended name:
    Putative pectinesterase 57
      Short name=PE 57
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 57
      Short name=AtPME57

Gene names

Name:	PME57
Synonyms:	ARATH57
Ordered Locus Names:	At1g44980
ORF Names:	F27F5.7

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	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Sequence similarities	Belongs to the pectinesterase family.
Sequence caution	The sequence AAF69174.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Molecular function	Aspartyl esterase Hydrolase
PTM	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: InterPro
Molecular function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW 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 – 246	246	Putative pectinesterase 57		PRO_0000371705
Sites
	Active site	205	1	Proton donor By similarity
	Active site	226	1	Nucleophile By similarity
	Binding site	152	1	Substrate By similarity
	Site	204	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Glycosylation	174	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9MAL0-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 278E69BBC60B7B39	FASTA	246	27,743
	10 20 30 40 50 60 MAMIGVMEDS KLHEDMENDM LGDLTSRARE ALALFISISL RDNTELNLVV PNGPSWLSHV 70 80 90 100 110 120 DKKDLYLNDE TLKKITDILV AKDVTGNYNI VNVAIAAAPQ HSQKRFVIYI KTSIYVEIVV 130 140 150 160 170 180 IGNMKSNLTL IADGQDSTII TFNLSSSNSK RTFNTATFAS NGDGFIRVDM CFRNTTWPVK 190 200 210 220 230 240 GPVVTLRVNG DMSIIYRCRV EEYQDALYPH KNRQCYREYF LMDTVDFICG NAAAVFQFCQ IVHMDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007915 Genomic DNA. Translation: AAF69174.1. Sequence problems.
IPI	IPI00518651.
PIR	H96508.
RefSeq	NP_175118.2.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Genome annotation databases
GeneID	841063.
GenomeReviews	Gene locus AT1G44980 in contig CT485782_GR.
Organism-specific databases
TAIR	At1g44980.
Gene expression databases
Genevestigator	Q9MAL0.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF01095. Pectinesterase. 1 hit. [Graphical view]
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME57_ARATH

Accession

Primary (citable) accession number: Q9MAL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	October 13, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)