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Protein

Pectinesterase A

Gene

pemA

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in maceration and soft-rotting of plant tissue.By similarity

Catalytic activityi

Pectin + n H2O = n methanol + pectate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091SubstrateBy similarity
Binding sitei153 – 1531SubstrateBy similarity
Sitei177 – 1771Transition state stabilizerBy similarity
Active sitei178 – 1781Proton donor
Active sitei199 – 1991Nucleophile
Binding sitei219 – 2191SubstrateBy similarity
Binding sitei226 – 2261SubstrateBy similarity
Binding sitei230 – 2301SubstrateBy similarity
Binding sitei267 – 2671SubstrateBy similarity
Binding sitei269 – 2691SubstrateBy similarity
Binding sitei272 – 2721Substrate; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  1. aspartyl esterase activity Source: UniProtKB-KW
  2. pectinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall modification Source: InterPro
  2. pectin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BRENDAi3.1.1.11. 2141.
SABIO-RKP0C1A8.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectinesterase A (EC:3.1.1.11)
Short name:
PE A
Alternative name(s):
Pectin methylesterase A
Gene namesi
Name:pemA
Synonyms:pem
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. cell wall Source: InterPro
  2. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 366342Pectinesterase APRO_0000023498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi192 ↔ 212

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 443Combined sources
Helixi45 – 506Combined sources
Beta strandi54 – 574Combined sources
Beta strandi59 – 635Combined sources
Beta strandi65 – 684Combined sources
Beta strandi72 – 743Combined sources
Beta strandi79 – 846Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 935Combined sources
Helixi108 – 1114Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1319Combined sources
Helixi135 – 1395Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi165 – 17410Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1918Combined sources
Beta strandi193 – 21119Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi278 – 2814Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi315 – 3184Combined sources
Helixi320 – 3223Combined sources
Beta strandi323 – 3297Combined sources
Beta strandi337 – 3415Combined sources
Helixi346 – 3494Combined sources
Helixi350 – 3523Combined sources
Helixi354 – 3585Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJVX-ray2.37A/B25-366[»]
SMRiP0C1A8. Positions 25-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1A8.

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C1A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA
60 70 80 90 100
SAPAGSTPFV ILIKNGVYNE RLTITRNNLL LKGESRNGAV IAAATAAGTL
110 120 130 140 150
KSDGSKWGTA GSSTITISAK DFSAQSLTIR NDFDFPANQA KSDSDSSKIK
160 170 180 190 200
DTQAVALYVT KSGDRAYFKD VSLVGYQDTL YVSGGRSFFS DCRISGTVDF
210 220 230 240 250
IFGDGTALFN NCDLVSRYRA DVKSGNVSGY LTAPSTNINQ KYGLVITNSR
260 270 280 290 300
VIRESDSVPA KSYGLGRPWH PTTTFSDGRY ADPNAIGQTV FLNTSMDNHI
310 320 330 340 350
YGWDKMSGKD KNGNTIWFNP EDSRFFEYKS YGAGAAVSKD RRQLTDAQAA
360
EYTQSKVLGD WTPTLP
Length:366
Mass (Da):39,319
Last modified:April 18, 2006 - v1
Checksum:iDA7DD9A45290660B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00549 Genomic DNA. Translation: CAA68628.1.
PIRiS03770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00549 Genomic DNA. Translation: CAA68628.1.
PIRiS03770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJVX-ray2.37A/B25-366[»]
SMRiP0C1A8. Positions 25-366.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BRENDAi3.1.1.11. 2141.
SABIO-RKP0C1A8.

Miscellaneous databases

EvolutionaryTraceiP0C1A8.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374."
    Plastow G.S.
    Mol. Microbiol. 2:247-254(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B374.
  2. "Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site."
    Jenkins J., Mayans O., Smith D., Worboys K., Pickersgill R.W.
    J. Mol. Biol. 305:951-960(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 25-366.
    Strain: B374.

Entry informationi

Entry nameiPMEA_DICCH
AccessioniPrimary (citable) accession number: P0C1A8
Secondary accession number(s): P07863
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: April 1, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.