Skip Header

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

P39822 (PSD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BSU02290
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length263 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
Reference 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 – 229229Phosphatidylserine decarboxylase beta chain By similarity
PRO_0000029631
Chain230 – 26334Phosphatidylserine decarboxylase alpha chain By similarity
PRO_0000029632

Sites

Site229 – 2302Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue2301Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
P39822 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3FF57686313D0F6F

FASTA26329,690
        10         20         30         40         50         60 
MFNTAVKILY RSLIELTNHR LSSYLIKGFC ESKISKPVIP LFSKHFRLNW DDVDGTAADY 

        70         80         90        100        110        120 
GSLSELFIRQ INLERRPVSK EAHAVVSPVD GVVQTVGIIN PNQTFTVKGK DYSFAELTGC 

       130        140        150        160        170        180 
KSADHQYNGG YFVVLYLSPR HYHRFHSPIS CRYQKLAELG NRSYPVNQLG LKYGKDVLSK 

       190        200        210        220        230        240 
NYRFVYELNS GSRNVLMIPV GAMNINSIVQ TNTRTELEIG EELGYFSFGS TVILVFEKDA 

       250        260 
FQPSAHLAEG QEVQVGELIG YEE

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase."
Matsumoto K., Okada M., Horikoshi Y., Matsuzaki H., Kishi T., Itaya M., Shibuya I.
J. Bacteriol. 180:100-106(1998) [PubMed: 9422599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome."
Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D38022 Genomic DNA. Translation: BAA07226.1.
AB006424 Genomic DNA. Translation: BAA33126.1.
AL009126 Genomic DNA. Translation: CAB12023.1.
PIRB69683.
RefSeqNP_388111.1. NC_000964.3.

3D structure databases

ProteinModelPortalP39822.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003510; EBBACP00000003510; EBBACG00000003503.
GeneID938431.
GenomeReviewsGene locus BSU02290 in contig AL009126_GR.
KEGGbsu:BSU02290.
NMPDRfig|224308.1.peg.230.
PATRIC18972007. VBIBacSub10457_0232.

Organism-specific databases

GenoListBSU02290. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001988.
HOGENOMHBG302256.
OMANKREWSI.
PhylomeDBP39822.
ProtClustDBPRK03140.

Enzyme and pathway databases

BioCycBSUB:BSU02290-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_BACSU
AccessionPrimary (citable) accession number: P39822
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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