Skip Header

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

Q5QVW0 (PSD_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:IL2302
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length292 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 – 254254Phosphatidylserine decarboxylase beta chain By similarity
PRO_0000029669
Chain255 – 29238Phosphatidylserine decarboxylase alpha chain By similarity
PRO_0000029670

Sites

Site254 – 2552Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue2551Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QVW0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: ECAB3166B1A94206

FASTA29232,529
        10         20         30         40         50         60 
MAKTDKVKIF FQHVMPKHLI SRLIGKFAAA RAGWFTQLFI RWFIRQYKID MSEAIEESPK 

        70         80         90        100        110        120 
AYKTFNAFFT RHLKPELRPL EASESELAHP VDGAVSQLGD IENGRIFQAK GHDYSLQELL 

       130        140        150        160        170        180 
GGNEEDAKPF VDGKFATIYL APKDYHRIHM PCDGVLKKMI YVPGDLYSVN PLTAANVPNL 

       190        200        210        220        230        240 
FARNERVVAI FDTEVGPMSL VLVGATIVAS IGTVWSGTIT PPTGGRIQSW SYPTSGHSAI 

       250        260        270        280        290 
HLKKGEEMGH FKLGSTVVLT FAKDAIEFND ELKPLSVTRM GEVMAEIKES DD

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017340 Genomic DNA. Translation: AAV83134.1.
RefSeqYP_156683.1. NC_006512.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3173174.
GenomeReviewsGene locus IL2302 in contig AE017340_GR.
KEGGilo:IL2302.
NMPDRfig|283942.3.peg.2289.
PATRIC22142758. VBIIdiLoi21852_2313.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG302256.
OMASMATVWH.

Enzyme and pathway databases

BioCycILOI283942:IL2302-MONOMER.

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_IDILO
AccessionPrimary (citable) accession number: Q5QVW0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 41 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