P0A8K1 (PSD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	b4160, JW4121

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Phosphatidyl-L-serine = phosphatidylethanolamine + CO2. HAMAP MF_00662
Cofactor	Pyruvoyl group.
Pathway	Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. HAMAP MF_00662
Subunit structure	Multimer of the heterodimer.
Subcellular location	Cell membrane; Peripheral membrane protein HAMAP MF_00662.
Sequence similarities	Belongs to the phosphatidylserine decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell membrane Membrane
Ligand	Pyruvate
Molecular function	Decarboxylase Lyase
PTM	Formylation Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatidylserine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 253	253	Phosphatidylserine decarboxylase beta chain HAMAP MF_00662		PRO_0000029647
	Chain	254 – 322	69	Phosphatidylserine decarboxylase alpha chain HAMAP MF_00662		PRO_0000029648
Sites
	Site	253 – 254	2	Cleavage (non-hydrolytic)
Amino acid modifications
	Modified residue	1	1	N-formylmethionine HAMAP MF_00662
	Modified residue	254	1	Pyruvic acid (Ser) HAMAP MF_00662
Experimental info
	Mutagenesis	254	1	S → A: No processing of the proenzyme, complete loss of activity. Ref.5
	Mutagenesis	254	1	S → C: Reduced processing, 16% wild-type activity. Ref.5
	Mutagenesis	254	1	S → T: Reduced processing, 2% wild-type activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P0A8K1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 45195A6689610599	FASTA	322	35,934
	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

References

	« Hide 'large scale' referencesShow '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
EMBL GenBank DDBJ	J03916 Genomic DNA. Translation: AAA83896.1. U14003 Genomic DNA. Translation: AAA97059.1. U00096 Genomic DNA. Translation: AAC77120.1. AP009048 Genomic DNA. Translation: BAE78164.1.
PIR	A29234.
RefSeq	NP_418584.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A8K1.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A8K1. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002126; EBESCP00000002126; EBESCG00000001742. EBESCT00000016054; EBESCP00000015345; EBESCG00000015114.
GeneID	948673.
GenomeReviews	Gene locus JW4121 in contig AP009048_GR. Gene locus b4160 in contig U00096_GR.
KEGG	ecj:JW4121. eco:b4160.
PATRIC	32123893. VBIEscCol129921_4294.
Organism-specific databases
EchoBASE	EB0768.
EcoGene	EG10775. psd.
Phylogenomic databases
eggNOG	COG0688.
GeneTree	EBGT00050000010432.
HOGENOM	HBG302256.
OMA	SMATVWH.
PhylomeDB	P0A8K1.
ProtClustDB	PRK00044.
Enzyme and pathway databases
BioCyc	EcoCyc:PSD-MONOMER. MetaCyc:PSD-MONOMER.
Gene expression databases
Genevestigator	P0A8K1.
Family and domain databases
HAMAP	MF_00662. PS_decarb_type1. [Tree]
InterPro	IPR003817. PS_Dcarbxylase. IPR005221. PS_decarb. [Graphical view]
KO	K01613.
PANTHER	PTHR10067. PS_decarb. 1 hit.
Pfam	PF02666. PS_Dcarbxylase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00163. PS_decarb. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PSD_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program