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Protein

Phosphatidylserine decarboxylase proenzyme 3

Gene

psd3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980).UniRule annotation1 Publication

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. CDP-diacylglycerol--serine O-phosphatidyltransferase (pps1)
  2. Phosphatidylserine decarboxylase proenzyme 3 (psd3), Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (psd1), Phosphatidylserine decarboxylase proenzyme 2, mitochondrial (psd2)
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 sitei769Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei825Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei912Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei912Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activityUniRule annotation1

GO - Molecular functioni

  • phosphatidylserine decarboxylase activity Source: PomBase
  • phospholipid binding Source: PomBase

GO - Biological processi

  • phosphatidylcholine biosynthetic process Source: PomBase
  • phosphatidylethanolamine biosynthetic process Source: PomBase

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00558; UER00616

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine decarboxylase proenzyme 31 Publication (EC:4.1.1.65UniRule annotation)
Cleaved into the following 2 chains:
Gene namesi
Name:psd31 Publication
ORF Names:SPAC31G5.15Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC31G5.15
PomBaseiSPAC31G5.15 psd3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003039541 – 967Phosphatidylserine decarboxylase proenzyme 3Add BLAST967
ChainiPRO_00004168371 – 911Phosphatidylserine decarboxylase 3 beta chainCuratedAdd BLAST911
ChainiPRO_0000416838912 – 967Phosphatidylserine decarboxylase 3 alpha chainCuratedAdd BLAST56

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei912Pyruvic 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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei911 – 912Cleavage (non-hydrolytic); by autocatalysisUniRule annotation2

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiO14111
PaxDbiO14111
PRIDEiO14111

PTM databases

iPTMnetiO14111

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279608, 8 interactors
STRINGi4896.SPAC31G5.15.1

Structurei

3D structure databases

SMRiO14111
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini269 – 357C2UniRule annotationAdd BLAST89

Domaini

The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.UniRule annotation

Sequence similaritiesi

Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.UniRule annotation

Phylogenomic databases

InParanoidiO14111
KOiK01613
OMAiPICHQPR
OrthoDBiEOG092C5DKH

Family and domain databases

Gene3Di2.60.40.150, 1 hit
HAMAPiMF_00663 PS_decarb_PSD_B_type2, 1 hit
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR003817 PS_Dcarbxylase
IPR033177 PSD
IPR033179 PSD_type2_pro
PANTHERiPTHR10067 PTHR10067, 1 hit
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF02666 PS_Dcarbxylase, 1 hit
SMARTiView protein in SMART
SM00239 C2, 1 hit
TIGRFAMsiTIGR00163 PS_decarb, 1 hit
PROSITEiView protein in PROSITE
PS50004 C2, 1 hit

Sequencei

Sequence statusi: Complete.

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

O14111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFTKSCRSA NTLRKGIKNG KLILKIIVND IDNVESCLSG DESNDSKKSS
60 70 80 90 100
ASFYMKLKYG SYRALADNIL STDENRKEDI AVFDVPLPNG LQIDTFTLCL
110 120 130 140 150
YRKSKWKKQI VGEAYIGIQA LLLSTNPDET CKYPVISPPS GRNKENQSPS
160 170 180 190 200
HQICNLSLKW IIYDPEDADA DSKTLAKAWL QQIKMNQTSI DPMSNISKSL
210 220 230 240 250
KELEVDNVES DLEDSSFIAE PDSSIPPSES SVSISTDTGK ETPPSKSKKS
260 270 280 290 300
SNQPYVSIGE GNSDLLGFVF LEIISVSNLP PLKNVFRTGF DMDPFVITAF
310 320 330 340 350
SKNIFRTKWL RHNLNPVYNE KFLFEVGAFE SNYDLVFKVV DHDKMSLNDS
360 370 380 390 400
IAVGSFNVQS IINSSAQVDP ETGLYSFNIE TSSPSQDTSS KAEDSPTVQK
410 420 430 440 450
IADDFSSAVG KDLRTDIIEQ IIPLTLCCKH DFSTPRDVKL SFKAMFFPIA
460 470 480 490 500
ALRQKFWRVM LAQYGDIEDG HIGKLGMYAV LDTLGSNIPN SMVDDIYTEL
510 520 530 540 550
SSKNHDDTSD SITVDEAVIC LERLVDLVCH QDQQATQTPQ SPSSNEESGP
560 570 580 590 600
GTPTQTSDQY EDSEDSRNFP SKLYLVYLSN CPLCLKFKLS KVNQQKATVH
610 620 630 640 650
LATCASHDWK RVDRLMMTSY VSLNQAQRRW FSKAFAKVVY GSSKVGSTSA
660 670 680 690 700
TTLVQNRQTG QIQEEKMNAY VRIGIRLLYR GIRNRRIEGS KVKKILRSLT
710 720 730 740 750
LKQGMKYDSP ISVKEIKPFI RFFDLNMNEV DMPVGGFKTF NEFFYRKLKP
760 770 780 790 800
GSRPCAFPDN PDILVSPADS RIVAYECIEK ATTYWIKGTE FTVERLLGYS
810 820 830 840 850
NEAQRFVGGS ICISRLAPQD YHRFHSPVNG CIGPITKIEG QYYTVNPMAI
860 870 880 890 900
RSYLDVFGEN VRVLIPIDSN EFGKVMLVAV GAMMVGSTVL TVDEGKIVQR
910 920 930 940 950
SDELGYFKFG GSTVITLFEP NVTSFDEDLL RNSKTKIETL VKMGERIGQK
960
IDPNKPTDAE DHSKSDS
Length:967
Mass (Da):108,213
Last modified:April 18, 2012 - v2
Checksum:i5B2115FB91FA42BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAB11699.2
PIRiT38632
RefSeqiNP_594016.2, NM_001019442.2

Genome annotation databases

EnsemblFungiiSPAC31G5.15.1; SPAC31G5.15.1:pep; SPAC31G5.15
GeneIDi2543178
KEGGispo:SPAC31G5.15

Similar proteinsi

Entry informationi

Entry nameiPSD3_SCHPO
AccessioniPrimary (citable) accession number: O14111
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 18, 2012
Last modified: March 28, 2018
This is version 114 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health