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Protein

Phosphatidylserine decarboxylase proenzyme

Gene

psd

Organism
Wolbachia pipientis wVitA
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).UniRule annotation

Catalytic activityi

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.UniRule annotation

Pathwayi: phosphatidylethanolamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphatidylserine decarboxylase proenzyme (psd)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei186Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylaseUniRule annotationSAAS annotation, Lyase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesisUniRule annotationSAAS annotation, Phospholipid metabolism
LigandPyruvateUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00558; UER00616.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine decarboxylase proenzymeUniRule annotation (EC:4.1.1.65UniRule annotation)
Cleaved into the following 2 chains:
Phosphatidylserine decarboxylase beta chainUniRule annotation
Phosphatidylserine decarboxylase alpha chainUniRule annotation
Gene namesi
Name:psdUniRule annotation
ORF Names:N499_0643Imported
OrganismiWolbachia pipientis wVitAImported
Taxonomic identifieri1379786 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia
Proteomesi
  • UP000188951 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cell membrane UniRule annotationSAAS annotation; Peripheral membrane protein UniRule annotationSAAS annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei12 – 34HelicalSequence analysisAdd BLAST23

GO - Cellular componenti

Keywords - Cellular componenti

Cell membraneUniRule annotationSAAS annotation, Membrane

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei186Pyruvic acid (Ser); by autocatalysisUniRule annotation1

Post-translational modificationi

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei185 – 186Cleavage (non-hydrolytic); by autocatalysisUniRule annotation2

Keywords - PTMi

ZymogenUniRule annotation

Interactioni

Subunit structurei

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.UniRule annotationSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.SAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Family and domain databases

HAMAPiMF_00664. PS_decarb_PSD_A. 1 hit.
InterProiView protein in InterPro
IPR003817. PS_Dcarbxylase.
IPR033175. PSD-A.
PANTHERiPTHR35809. PTHR35809. 1 hit.
PfamiView protein in Pfam
PF02666. PS_Dcarbxylase. 1 hit.
TIGRFAMsiTIGR00164. PS_decarb_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A0A1V2N550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCFGLPNINR EGYSFIVVSF IVTCIAFSIS WGFGVTCLFP TLLCTYFFRD
60 70 80 90 100
PARAVPNNKN LILSPADGVI SKIEEVNYPL SAENGEEKKF TLVSIFLSVL
110 120 130 140 150
NVHVNRIPIS GTIKEMSYKK GKFVSAMSNR SSNENEKQVI VIEYEKGKEI
160 170 180 190 200
IVEQIAGLIA RRIVCNLGIS QNVKAGERFG IIRFGSRVNI YVPADTEVRV
210 220 230
SEGQTVIGGE TIIANLNKEN VQEKLTFDVI
Length:230
Mass (Da):25,537
Last modified:June 7, 2017 - v1
Checksum:iBDA9E9E86159BA02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MUJM01000064 Genomic DNA. Translation: ONI57695.1.
RefSeqiWP_007548750.1. NZ_MUJM01000064.1.

Genome annotation databases

GeneIDi29555573.

Similar proteinsi

Entry informationi

Entry nameiA0A1V2N550_WOLPI
AccessioniPrimary (citable) accession number: A0A1V2N550
Entry historyiIntegrated into UniProtKB/TrEMBL: June 7, 2017
Last sequence update: June 7, 2017
Last modified: March 28, 2018
This is version 9 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteomeImported