Skip Header

Contribute Send feedback
Read comments (?) or add your own

B2I1N9 (PSD_ACIBC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylserine decarboxylase proenzyme
EC=4.1.1.65

Cleaved into the following 2 chains:

  1. Phosphatidylserine decarboxylase alpha chain
  2. Phosphatidylserine decarboxylase beta chain
Gene names
Name:psd
Ordered Locus Names:ACICU_03578
OrganismAcinetobacter baumannii (strain ACICU) [Complete proteome] [HAMAP]
Taxonomic identifier405416 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyruvoyl group By similarity. HAMAP MF_00662

Pathway

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

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphatidylserine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Phosphatidylserine decarboxylase beta chain By similarity
PRO_1000131320
Chain250 – 28334Phosphatidylserine decarboxylase alpha chain By similarity
PRO_1000131321

Sites

Site249 – 2502Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue2501Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2I1N9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 119A3442F9CF7230

FASTA28331,272
        10         20         30         40         50         60 
MSFTSRLKKE LFIKAQNLVP QHQLSRVVGK VAASENPILK AAVIHAFKTK YGIDLSIAEQ 

        70         80         90        100        110        120 
GNALKYKSFN DFFTRALKDG VRLVDENPDS IVSPADGAIS QIGKITAGEV FQAKGQSFSV 

       130        140        150        160        170        180 
EKLIGDPQLA QPFQEGEFAT VYLSPRDYHR VHMPFSGTLT ETLYVPGELF SVNQVTAENV 

       190        200        210        220        230        240 
PGLFARNERM VCLFDTELGR MAVVLVGAMI VAGIETVATG KVKPSGRIEL QHHELKLEKG 

       250        260        270        280 
AELGRFYLGS TAIILFEKDK IEWEKRFKAE SVVVMGERMG HTI

« Hide

References

[1]"Whole-genome pyrosequencing of an epidemic multidrug-resistant Acinetobacter baumannii strain belonging to the European clone II group."
Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.
Antimicrob. Agents Chemother. 52:2616-2625(2008) [PubMed: 18411315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ACICU.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000863 Genomic DNA. Translation: ACC58887.1.
RefSeqYP_001848234.1. NC_010611.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2I1N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6236045.
GenomeReviewsGene locus ACICU_03578 in contig CP000863_GR.
KEGGabc:ACICU_03578.
PATRIC20715899. VBIAciBau103538_3598.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG302256.
OMAMCQSEAR.
ProtClustDBPRK00044.

Family and domain databases

HAMAPMF_00662. PS_decarb_type1.
[Tree]
InterProIPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
KOK01613.
PANTHERPTHR10067. PS_decarb. 1 hit.
PfamPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Entry information

Entry namePSD_ACIBC
AccessionPrimary (citable) accession number: B2I1N9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents