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P0C1A8

- PMEA_DICCH

UniProt

P0C1A8 - PMEA_DICCH

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Protein

Pectinesterase A

Gene
pemA, pem
Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed - Annotation score: 5 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 – 1091Substrate By similarity
Binding sitei153 – 1531Substrate By similarity
Sitei177 – 1771Transition state stabilizer By similarity
Active sitei178 – 1781Proton donor
Active sitei199 – 1991Nucleophile
Binding sitei219 – 2191Substrate By similarity
Binding sitei226 – 2261Substrate By similarity
Binding sitei230 – 2301Substrate By similarity
Binding sitei267 – 2671Substrate By similarity
Binding sitei269 – 2691Substrate By similarity
Binding sitei272 – 2721Substrate; via amide nitrogen and carbonyl oxygen By 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

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 – 324
Beta strandi36 – 405
Beta strandi42 – 443
Helixi45 – 506
Beta strandi54 – 574
Beta strandi59 – 635
Beta strandi65 – 684
Beta strandi72 – 743
Beta strandi79 – 846
Turni86 – 883
Beta strandi89 – 935
Helixi108 – 1114
Beta strandi114 – 1174
Beta strandi119 – 1213
Beta strandi123 – 1319
Helixi135 – 1395
Beta strandi156 – 1594
Beta strandi165 – 17410
Beta strandi180 – 1823
Beta strandi184 – 1918
Beta strandi193 – 21119
Beta strandi213 – 2164
Beta strandi229 – 2346
Beta strandi244 – 2485
Beta strandi250 – 2556
Beta strandi263 – 2664
Beta strandi272 – 2754
Beta strandi278 – 2814
Beta strandi288 – 2936
Beta strandi300 – 3023
Beta strandi306 – 3094
Beta strandi315 – 3184
Helixi320 – 3223
Beta strandi323 – 3297
Beta strandi337 – 3415
Helixi346 – 3494
Helixi350 – 3523
Helixi354 – 3585

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJVX-ray2.37A/B25-366[»]
ProteinModelPortaliP0C1A8.
SMRiP0C1A8. Positions 25-366.

Miscellaneous databases

EvolutionaryTraceiP0C1A8.

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.

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

MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA    50
SAPAGSTPFV ILIKNGVYNE RLTITRNNLL LKGESRNGAV IAAATAAGTL 100
KSDGSKWGTA GSSTITISAK DFSAQSLTIR NDFDFPANQA KSDSDSSKIK 150
DTQAVALYVT KSGDRAYFKD VSLVGYQDTL YVSGGRSFFS DCRISGTVDF 200
IFGDGTALFN NCDLVSRYRA DVKSGNVSGY LTAPSTNINQ KYGLVITNSR 250
VIRESDSVPA KSYGLGRPWH PTTTFSDGRY ADPNAIGQTV FLNTSMDNHI 300
YGWDKMSGKD KNGNTIWFNP EDSRFFEYKS YGAGAAVSKD RRQLTDAQAA 350
EYTQSKVLGD WTPTLP 366
Length:366
Mass (Da):39,319
Last modified:April 18, 2006 - v1
Checksum:iDA7DD9A45290660B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00549 Genomic DNA. Translation: CAA68628.1.
PIRiS03770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00549 Genomic DNA. Translation: CAA68628.1 .
PIRi S03770.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QJV X-ray 2.37 A/B 25-366 [» ]
ProteinModelPortali P0C1A8.
SMRi P0C1A8. Positions 25-366.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00545 ; UER00823 .
SABIO-RK P0C1A8.

Miscellaneous databases

EvolutionaryTracei P0C1A8.

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view ]
Pfami PF01095. Pectinesterase. 1 hit.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 1 hit.
PROSITEi PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1988) [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(2001) [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 16, 2014
This is version 38 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

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