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Protein

Phosphatidylserine decarboxylase proenzyme

Gene

psd

Organism
Rhizobium etli (strain CIAT 652)
Status
Reviewed-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

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.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 sitei190Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
LigandPyruvate

Enzyme and pathway databases

BioCyciRETL491916:G1GBZ-1464-MONOMER
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 alpha chainUniRule annotation
Phosphatidylserine decarboxylase beta chainUniRule annotation
Gene namesi
Name:psdUniRule annotation
Ordered Locus Names:RHECIAT_CH0001480
OrganismiRhizobium etli (strain CIAT 652)
Taxonomic identifieri491916 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
Proteomesi
  • UP000008817 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001314861 – 189Phosphatidylserine decarboxylase beta chainUniRule annotationAdd BLAST189
ChainiPRO_1000131487190 – 232Phosphatidylserine decarboxylase alpha chainUniRule annotationAdd BLAST43

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei190Pyruvic 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
Sitei189 – 190Cleavage (non-hydrolytic); by autocatalysisUniRule annotation2

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi491916.RHECIAT_CH0001480

Structurei

3D structure databases

SMRiB3PUR0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41071I4 Bacteria
COG0688 LUCA
HOGENOMiHOG000229359
KOiK01613
OMAiVSIFMSP
OrthoDBiPOG091H01PZ

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.

B3PUR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFNTVRNT IVPVHKEGYP FVAAFFVASL ILGWIFKPLF WIGMIFTLWC
60 70 80 90 100
AYFFRDPERV TPQDDDLVIS PADGKVSAIQ MVTPPAELDL GSEPMLRISV
110 120 130 140 150
FMNVFNCHVN RAPMRGRIVS INYRSGSFVN AELDKASEDN ERNGLVIETK
160 170 180 190 200
HGQIGVVQIA GLVARRILCW ANTNEPMDAG ERFGLIRFGS RLDVFLPAGA
210 220 230
APRVSLGQTA IAGETVIAEF ASAKGPVISR RS
Length:232
Mass (Da):25,575
Last modified:September 2, 2008 - v1
Checksum:iCC3DF4D7D555FDCD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001074 Genomic DNA Translation: ACE90459.1
RefSeqiWP_012483280.1, NC_010994.1

Genome annotation databases

EnsemblBacteriaiACE90459; ACE90459; RHECIAT_CH0001480
KEGGirec:RHECIAT_CH0001480

Similar proteinsi

Entry informationi

Entry nameiPSD_RHIE6
AccessioniPrimary (citable) accession number: B3PUR0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: April 25, 2018
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health