Q43111 (PME3_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase 3
Short name=PE 3
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 3

Gene names

Name:

MPE3

Organism

Phaseolus vulgaris (Kidney bean) (French bean)

Taxonomic identifier

3885 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length	581 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	May have roles in the deposition of pectin in developing tissues and in the wall loosening and cell separation that occurs in cell expansion, fruit ripening and abscission.
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
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Glycoprotein
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 – 55	55	Potential
	Chain	56 – 581	526	Pectinesterase 3		PRO_0000023496
Sites
	Active site	401	1	Proton donor By similarity
	Active site	422	1	Nucleophile By similarity
	Binding site	348	1	Substrate By similarity
	Binding site	378	1	Substrate By similarity
	Binding site	486	1	Substrate By similarity
	Binding site	488	1	Substrate By similarity
	Site	400	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	101	1	N-linked (GlcNAc...) Potential
	Glycosylation	156	1	N-linked (GlcNAc...) Potential
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	268	1	N-linked (GlcNAc...) Potential
	Glycosylation	477	1	N-linked (GlcNAc...) Potential
	Disulfide bond	415 ↔ 435		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43111 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CDB0621372E59BFE	FASTA	581	63,588
	10 20 30 40 50 60 MDTIKSFKGY GKVNELEQQA YEKKTRKRLI IIAVSSIVLI AVIIAAVAGV VIHNRNSESS 70 80 90 100 110 120 PSSDSVPQTE LSPAASLKAV CDTTRYPSSC FSSISSLPES NTTDPELLFK LSLRVAIDEL 130 140 150 160 170 180 SSFPSKLRAN AEQDARLQKA IDVCSSVFGD ALDRLNDSIS ALGTVAGRIA SSASVSNVET 190 200 210 220 230 240 WLSAALTDQD TCLDAVGELN STAARGALQE IETAMRNSTE FASNSLAIVT KILGLLSRFE 250 260 270 280 290 300 TPIHHRRLLG FPEWLGAAER RLLEEKNNDS TPDAVVAKDG SGQFKTIGEA LKLVKKKSEE 310 320 330 340 350 360 RFSVYVKEGR YVENIDLDKN TWNVMIYGDG KDKTFVVGSR NFMDGTPTFE TATFAVKGKG 370 380 390 400 410 420 FIAKDIGFVN NAGASKHQAV ALRSGSDRSV FFRCSFDGFQ DTLYAHSNRQ FYRDCDITGT 430 440 450 460 470 480 IDFIFGNAAV VFQSCKIMPR QPLPNQFNTI TAQGKKDPNQ NTGIIIQKST ITPFGNNLTA 490 500 510 520 530 540 PTYLGRPWKD FSTTVIMQSD IGALLNPVGW MSWVPNVEPP TTIFYAEYQN SGPGADVSQR 550 560 570 580 VKWAGYKPTI TDRNAEEFTV QSFIQGPEWL PNAAVQFDST L

References

[1]	"Characterization of pectinases and pectin methylesterase cDNAs in pods of green beans (Phaseolus vulgaris L.)." Ebbelaar C.E.M., Tucker G.A., Laats J.M., van Dijk C., Stolle-Smits T., Recourt K. Plant Mol. Biol. 31:1141-1151(1996) [PubMed: 8914530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Masai.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X85216 mRNA. Translation: CAA59482.1.
PIR	S53105.
3D structure databases
ProteinModelPortal	Q43111.
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

PME3_PHAVU

Accession

Primary (citable) accession number: Q43111

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program