PSS_ENCCU
ID PSS_ENCCU Reviewed; 384 AA.
AC Q95ZE2; Q8SQY0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase;
GN Name=PSS; OrderedLocusNames=ECU11_0620;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11560410; DOI=10.1006/expr.2001.4635;
RA El Alaoui H., Bata J., Peyret P., Vivares C.P.;
RT "Encephalitozoon cuniculi (Microspora): characterization of phospholipid
RT metabolic pathway potentially linked to therapeutics.";
RL Exp. Parasitol. 98:171-179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 1/2.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD25972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ310089; CAC51024.1; -; Genomic_DNA.
DR EMBL; AL590450; CAD25972.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_586368.1; NM_001042201.1.
DR AlphaFoldDB; Q95ZE2; -.
DR STRING; 284813.Q95ZE2; -.
DR GeneID; 860021; -.
DR KEGG; ecu:ECU11_0620; -.
DR HOGENOM; CLU_035066_6_0_1; -.
DR InParanoid; Q95ZE2; -.
DR OrthoDB; 847100at2759; -.
DR UniPathway; UPA00558; UER00615.
DR Proteomes; UP000000819; Chromosome XI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; PTHR10414; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..384
FT /note="CDP-diacylglycerol--serine O-
FT phosphatidyltransferase"
FT /id="PRO_0000056800"
SQ SEQUENCE 384 AA; 42874 MW; C5E5A6FA2A496D92 CRC64;
MKMEPDEVSS LRKHRFVGTD NSILGRYVLH HYTNWMLEKI PAFVAPNMLT LCGLIAMVAS
LALTLAFDPC LCSPPAFLSL ANFLLMFVYF TCDNLDGAQA RKTGSGSSLG QLFDHGVDSC
CALITSIALS STFGFGLSPK FLIFTLAVMV QFYLAGIEEK FTGRFVLGRI SGASEGVVFA
MGAHLATFLC GKRLFRHLFS DNFLWPVKKI YSSILGTDNF SAVSVIIGTA LVFNTASTLI
SIEFKMHFPR RLLLYSTILR VMSFVTSFVI LHNTLSTESL WIRHLNILMF GQIFSIKYVN
EVCSYIIRRD PFLFTPPYLM YLTVSAVLQL QYLKEFRETL VAISFLLSSM YYLLVALRII
ITFKEALGIS FLSITTSDKS KAGG
