Q9STY3 (PME33_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 33

Including the following 2 domains:

1. Pectinesterase inhibitor 33
   Alternative name(s):
   Pectin methylesterase inhibitor 33
2. Pectinesterase 33
   Short name=PE 33
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 33
   Short name=AtPME33

Gene names

Name:	PME33
Synonyms:	ARATH33
Ordered Locus Names:	At3g47400
ORF Names:	T21L8.150

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	594 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 By similarity.
Tissue specificity	Expressed in siliques. 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	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
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 – 22	22	Potential
	Chain	23 – 594	572	Probable pectinesterase/pectinesterase inhibitor 33		PRO_0000371685
Regions
	Region	78 – 237	160	Pectinesterase inhibitor 33
	Region	280 – 581	302	Pectinesterase 33
	Compositional bias	35 – 74	40	Pro-rich
Sites
	Active site	409	1	Proton donor; for pectinesterase activity By similarity
	Active site	430	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	356	1	Substrate; for pectinesterase activity By similarity
	Binding site	386	1	Substrate; for pectinesterase activity By similarity
	Binding site	498	1	Substrate; for pectinesterase activity By similarity
	Binding site	500	1	Substrate; for pectinesterase activity By similarity
	Site	408	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Glycosylation	226	1	N-linked (GlcNAc...) Potential
	Disulfide bond	423 ↔ 443		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9STY3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 97D0FB6592C8C965	FASTA	594	65,487
	10 20 30 40 50 60 MLRGIFHICL LASFLLLPFS SAVHDSGFTG GTDAPPPWDH NVSPPPETAP SPTPTSSPST 70 80 90 100 110 120 TSPPSPGPVA APSPINNGSV SGDMTWWCNK TPHAETCNYY FRKSSQNNIN LRPPRFRSEF 130 140 150 160 170 180 LRMLVKVALD QAVITHSQTV KFGPSCTNNQ RKAAWSDCVN LFQNTVAQLN RTLKGLNPAA 190 200 210 220 230 240 SSDVKCTDFD AQTWLSTAQT NIETCRSGSE DLNVSDFVMP VISNKNLSDL IGNCLAVNGV 250 260 270 280 290 300 LMKQHDHTTT ANHKEYFPSW VSRHERRLLV SASLAKSSPH LVVAQDRSGH FRSIQAAINF 310 320 330 340 350 360 AARRRFKSRF VIYVKKGVYR ENIDVGNDNH NIMLVGDGER KTIITSGRSV QHGYTTYNSA 370 380 390 400 410 420 TGGFGGQRFV AKDMTFINTA GPLRGQAVAV RSSSDLSVFY RVGIHGFQDT LYIHSQRQFF 430 440 450 460 470 480 RECYISGTID FIFGNAAVVF QNCMILVRRP LHGQANIITA QGRGDPFQNT GITIHSSRII 490 500 510 520 530 540 AASDLKPVIR AYKTYLGRPW QAYSRVTIMK TYIDNSISPL GWSPWLRGSN FALNTVFYGE 550 560 570 580 590 YKNFGPGSST RWRVRWKGFH AITSTAVASR FTVGSLIAGG SWLPATGVPF KSGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL096860 Genomic DNA. Translation: CAB51212.1. CP002686 Genomic DNA. Translation: AEE78277.1. AK227314 mRNA. No translation available.
IPI	IPI00534249.
PIR	T12995.
RefSeq	NP_190324.1. NM_114608.2.
UniGene	At.35810.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q9STY3.
SMR	Q9STY3. Positions 276-594.
ModBase	Search...
Proteomic databases
PRIDE	Q9STY3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G47400.1; AT3G47400.1; AT3G47400.
GeneID	823894.
GenomeReviews	Gene locus AT3G47400 in contig BA000014_GR.
KEGG	ath:AT3G47400.
NMPDR	fig|3702.1.peg.15961.
Organism-specific databases
GeneFarm	295. 8.
TAIR	At3g47400.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000027901.
HOGENOM	HBG747179.
InParanoid	Q9STY3.
OMA	TNIETCR.
PhylomeDB	Q9STY3.
ProtClustDB	CLSN2915696.
Gene expression databases
Genevestigator	Q9STY3.
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. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME33_ARATH

Accession

Primary (citable) accession number: Q9STY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program