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Protein

Phosphatidylserine decarboxylase proenzyme, mitochondrial

Gene

PISD

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.UniRule annotation

Catalytic activityi

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

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei191Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei267Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei378Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei378Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine decarboxylase proenzyme, mitochondrialUniRule 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:PISDUniRule annotation
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Chromosome 22

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini53 – 63Mitochondrial matrixUniRule annotationAdd BLAST11
Transmembranei64 – 82HelicalUniRule annotationAdd BLAST19
Topological domaini83 – 409Mitochondrial intermembraneUniRule annotationAdd BLAST327

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52MitochondrionSequence analysisAdd BLAST52
ChainiPRO_000043557353 – 409Phosphatidylserine decarboxylase proenzymeAdd BLAST357
ChainiPRO_000002983953 – 377Phosphatidylserine decarboxylase beta chainUniRule annotationAdd BLAST325
ChainiPRO_0000029840378 – 409Phosphatidylserine decarboxylase alpha chainUniRule annotationAdd BLAST32

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei378Pyruvic 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
Sitei377 – 378Cleavage (non-hydrolytic); by autocatalysisUniRule annotation2

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiQ5R8I8.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000013093.

Structurei

3D structure databases

SMRiQ5R8I8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2420. Eukaryota.
COG0688. LUCA.
GeneTreeiENSGT00390000013484.
HOVERGENiHBG039630.
InParanoidiQ5R8I8.
KOiK01613.
OMAiGLFCLNE.
OrthoDBiEOG091G09PP.
TreeFamiTF313148.

Family and domain databases

HAMAPiMF_03208. PS_decarb_PSD_B_type1_euk. 1 hit.
InterProiView protein in InterPro
IPR003817. PS_Dcarbxylase.
IPR033177. PSD.
IPR033661. PSD_type1_euk.
PANTHERiPTHR10067. PTHR10067. 1 hit.
PfamiView protein in Pfam
PF02666. PS_Dcarbxylase. 1 hit.
TIGRFAMsiTIGR00163. PS_decarb. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5R8I8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSVGHRCL GLLHGVAPWR SSLHPCEITA LSQSLQPLRK LPFRAFRTDA
60 70 80 90 100
RKIHTAPART MFLLRPVPIL LATGGGYAGY RQYEKYRERE LEKLGLEIPP
110 120 130 140 150
KLAGHWEVAL YKSVPTRLLS RAWGRLNQVE LPHWLRRPVY SLYIWTFGVN
160 170 180 190 200
MKEAAVEDLH HYRNLSEFFR RKLKPQARPV CGLHSVISPS DGRILNFGQV
210 220 230 240 250
KNCEVEQVKG VTYSLESFLG PRTCTEDLPF PPATSCDSFK NQLVTREGNE
260 270 280 290 300
LYHCVIYLAP GDYHCFHSPT DWTVSHRRHF PGSLMSVNPG MARWIKELFC
310 320 330 340 350
HNERVVLTGD WKHGFFSLTA VGATNVGSIR IYFDQDLHTN SPRHSKGSYN
360 370 380 390 400
DFSFVTHTNR EGVPMRKGEH LGEFNLGSTI VLIFEAPKDF NFQLKTGQKI

RFGEALGSL
Length:409
Mass (Da):46,601
Last modified:December 21, 2004 - v1
Checksum:iCE69C5D344644FE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859764 mRNA. Translation: CAH91922.1.
RefSeqiNP_001126113.1. NM_001132641.1.
UniGeneiPab.12977.

Genome annotation databases

EnsembliENSPPYT00000013627; ENSPPYP00000013093; ENSPPYG00000011738.
GeneIDi100173069.
KEGGipon:100173069.

Similar proteinsi

Entry informationi

Entry nameiPISD_PONAB
AccessioniPrimary (citable) accession number: Q5R8I8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 21, 2004
Last modified: March 15, 2017
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families