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Reviewed, UniProtKB/Swiss-Prot P0A8K1 (PSD_ECOLI)

Last modified November 3, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylserine decarboxylase proenzyme
    EC=4.1.1.65
Cleaved into the following 2 chains:
    1- Recommended name:
            Phosphatidylserine decarboxylase alpha chain
    2- Recommended name:
            Phosphatidylserine decarboxylase beta chain
Gene names
Name: psd
Ordered Locus Names: b4160, JW4121
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2. HAMAP MF_00662

Cofactor

Pyruvoyl group. HAMAP MF_00662

Pathway

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. HAMAP MF_00662

Subunit structure

Multimer of the heterodimer. HAMAP MF_00662

Subcellular location

Cell membrane; Peripheral membrane protein. HAMAP MF_00662

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMFormylation
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentextrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphatidylserine decarboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Phosphatidylserine decarboxylase beta chain HAMAP MF_00662
PRO_0000029647
Chain254 – 32269Phosphatidylserine decarboxylase alpha chain HAMAP MF_00662
PRO_0000029648

Sites

Site253 – 2542Cleavage (non-hydrolytic) HAMAP MF_00662

Amino acid modifications

Modified residue11N-formylmethionine HAMAP MF_00662
Modified residue2541Pyruvic acid (Ser) HAMAP MF_00662

Experimental info

Mutagenesis2541S → A: No processing of the proenzyme, complete loss of activity. Ref.5
Mutagenesis2541S → C: Reduced processing, 16% wild-type activity. Ref.5
Mutagenesis2541S → T: Reduced processing, 2% wild-type activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P0A8K1-1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 45195A6689610599

FASTA32235,934
        10         20         30         40         50         60 
MLNSFKLSLQ YILPKLWLTR LAGWGASKRA GWLTKLVIDL FVKYYKVDMK EAQKPDTASY 

        70         80         90        100        110        120 
RTFNEFFVRP LRDEVRPIDT DPNVLVMPAD GVISQLGKIE EDKILQAKGH NYSLEALLAG 

       130        140        150        160        170        180 
NYLMADLFRN GTFVTTYLSP RDYHRVHMPC NGILREMIYV PGDLFSVNHL TAQNVPNLFA 

       190        200        210        220        230        240 
RNERVICLFD TEFGPMAQIL VGATIVGSIE TVWAGTITPP REGIIKRWTW PAGENDGSVA 

       250        260        270        280        290        300 
LLKGQEMGRF KLGSTVINLF APGKVNLVEQ LESLSVTKIG QPLAVSTETF VTPDAEPAPL 

       310        320 
PAEEIEAEHD ASPLVDDKKD QV 

« Hide

References

« Hide 'large scale' references
[1]"Structural characterization of Escherichia coli phosphatidylserine decarboxylase."
Li Q.-X., Dowhan W.
J. Biol. Chem. 263:11516-11522(1988) [PubMed: 3042771] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli."
Li Q.-X., Dowhan W.
J. Biol. Chem. 265:4111-4115(1990) [PubMed: 2406271] [Abstract]
Cited for: MUTAGENESIS OF SER-254.
[6]"Phosphatidylserine decarboxylase from Escherichia coli."
Dowhan W., Li Q.-X.
Methods Enzymol. 209:348-359(1992) [PubMed: 1495415] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

J03916 Genomic DNA. Translation: AAA83896.1.
U14003 Genomic DNA. Translation: AAA97059.1.
U00096 Genomic DNA. Translation: AAC77120.1.
AP009048 Genomic DNA. Translation: BAE78164.1.
PIRA29234.
RefSeqAP_004663.1.
NP_418584.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP0A8K1.

Genome annotation databases

GeneID948673.
GenomeReviewsGene locus JW4121 in contig AP009048_GR.
Gene locus b4160 in contig U00096_GR.
KEGGecj:JW4121.
eco:b4160.

Organism-specific databases

EchoBASEEB0768.
EcoGeneEG10775. psd.
CMRSearch...

Phylogenomic databases

HOGENOMP0A8K1.
OMAINQDEME.

Enzyme and pathway databases

BioCycEcoCyc:PSD-MON.
MetaCyc:PSD-MON.

Gene expression databases

GenevestigatorP0A8K1.

Family and domain databases

HAMAPMF_00662.
[Tree]
InterProIPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
PANTHERPTHR10067. PS_decarb. 1 hit.
PfamPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Entry information

Entry namePSD_ECOLI
AccessionPrimary (citable) accession number: P0A8K1
Secondary accession number(s): P10740, Q2M6E2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents