Reviewed, UniProtKB/Swiss-Prot Q9FK05 (PME61_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 61
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 61
        Alternative name(s):
            Pectin methylesterase inhibitor 61
    2- Recommended name:
            Pectinesterase 61
                Short name=PE 61
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 61
              Short name=AtPME61
            AtPMEpcrF

Gene names

Name:	PME61
Synonyms:	ARATH61
Ordered Locus Names:	At5g53370
ORF Names:	K19E1.17

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 › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
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.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Expressed in siliques, floral stems and rosettes leaves. Ref.3 Ref.5
Developmental stage	Expressed throughout silique development. Ref.5
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	Membrane
Domain	Transmembrane
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Phosphoprotein
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 integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 587	587	Probable pectinesterase/pectinesterase inhibitor 61		PRO_0000371707
Regions
	Transmembrane	35 – 55	21	Potential
	Region	69 – 223	155	Pectinesterase inhibitor 61
	Region	273 – 571	299	Pectinesterase 61
Sites
	Active site	402	1	Proton donor; for pectinesterase activity By similarity
	Active site	423	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	349	1	Substrate; for pectinesterase activity By similarity
	Binding site	379	1	Substrate; for pectinesterase activity By similarity
	Binding site	491	1	Substrate; for pectinesterase activity By similarity
	Binding site	493	1	Substrate; for pectinesterase activity By similarity
	Site	401	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	539	1	Phosphoserine Ref.6
	Disulfide bond	416 ↔ 436		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FK05-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A60B9271DE489DBD	FASTA	587	64,241
	10 20 30 40 50 60 MGYDRLGPSG PSNPNQKDPA TSLPELQKKT KTKLILFTLA VLVVGVVCFG IFAGIRAVDS 70 80 90 100 110 120 GKTEPKLTRK PTQAISRTCS KSLYPNLCID TLLDFPGSLT ADENELIHIS FNATLQKFSK 130 140 150 160 170 180 ALYTSSTITY TQMPPRVRSA YDSCLELLDD SVDALTRALS SVVVVSGDES HSDVMTWLSS 190 200 210 220 230 240 AMTNHDTCTD GFDEIEGQGG EVKDQVIGAV KDLSEMVSNC LAIFAGKVKD LSGVPVVNNR 250 260 270 280 290 300 KLLGTEETEE LPNWLKREDR ELLGTPTSAI QADITVSKDG SGTFKTIAEA IKKAPEHSSR 310 320 330 340 350 360 RFVIYVKAGR YEEENLKVGR KKTNLMFIGD GKGKTVITGG KSIADDLTTF HTATFAATGA 370 380 390 400 410 420 GFIVRDMTFE NYAGPAKHQA VALRVGGDHA VVYRCNIIGY QDALYVHSNR QFFRECEIYG 430 440 450 460 470 480 TVDFIFGNAA VILQSCNIYA RKPMAQQKIT ITAQNRKDPN QNTGISIHAC KLLATPDLEA 490 500 510 520 530 540 SKGSYPTYLG RPWKLYSRVV YMMSDMGDHI DPRGWLEWNG PFALDSLYYG EYMNKGLGSG 550 560 570 580 IGQRVKWPGY HVITSTVEAS KFTVAQFISG SSWLPSTGVS FFSGLSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"Characterization of the pectin methylesterase-like gene AtPME3: a new member of a gene family comprising at least 12 genes in Arabidopsis thaliana." Micheli F., Holliger C., Goldberg R., Richard L. Gene 220:13-20(1998) [PubMed: 9767082] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"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.
[5]	"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.
[6]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB013388 Genomic DNA. Translation: BAB09799.1. AF360340 mRNA. Translation: AAK28637.1. AY051077 mRNA. Translation: AAK93754.1.
IPI	IPI00530003.
RefSeq	NP_200149.1.
UniGene	At.24561 At.29558
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMR	Q9FK05. Positions 73-224, 267-585.
ModBase	Search...
Proteomic databases
PRIDE	Q9FK05.
Genome annotation databases
GeneID	835418.
GenomeReviews	Gene locus AT5G53370 in contig BA000015_GR.
KEGG	ath:AT5G53370.
NMPDR	fig|3702.1.peg.27231.
Organism-specific databases
GeneFarm	298. 8.
TAIR	At5g53370.
Phylogenomic databases
eggNOG	COG4677.
HOGENOM	HBG747179.
InParanoid	Q9FK05.
OMA	ISIHACK.
Gene expression databases
ArrayExpress	Q9FK05.
Genevestigator	Q9FK05.
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]
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

PME61_ARATH

Accession

Primary (citable) accession number: Q9FK05

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)