ID A0A1Y2F496_PROLT Unreviewed; 239 AA.
AC A0A1Y2F496;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
DE EC=2.7.8.11 {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
GN ORFNames=BCR37DRAFT_122131 {ECO:0000313|EMBL:ORY77765.1};
OS Protomyces lactucae-debilis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Protomycetaceae; Protomyces.
OX NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY77765.1, ECO:0000313|Proteomes:UP000193685};
RN [1] {ECO:0000313|EMBL:ORY77765.1, ECO:0000313|Proteomes:UP000193685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-1054 {ECO:0000313|EMBL:ORY77765.1,
RC ECO:0000313|Proteomes:UP000193685};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC Evidence={ECO:0000256|PIRNR:PIRNR000848};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|PIRNR:PIRNR000848, ECO:0000256|RuleBase:RU003750}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY77765.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFI01000019; ORY77765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2F496; -.
DR STRING; 56484.A0A1Y2F496; -.
DR OMA; CRMYASV; -.
DR OrthoDB; 5472855at2759; -.
DR Proteomes; UP000193685; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1.
DR PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000848};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000848};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000848};
KW Reference proteome {ECO:0000313|Proteomes:UP000193685};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000848};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 239 AA; 27177 MW; E5B581F8970FAE05 CRC64;
MPGHSIQSSV RSENVYLFIP NIIGFSRIIL AFVSLYYMPF HPKYCTITYS ISCLLDAFDG
WAARKFHQST KFGAVLDMVT DRCTTGCLLC FLSAAYPAYT FVFQLLVTLD LASHYIHMYS
TLNQGVTSHK KIPADQAWIL RLYYGNNVVL FLFCAFNELF FVALYLLHFP PRADSPPFFG
RHWNIDFSWP MAIALVSAGP CFIKQWISLV QLINASNALV ELDVEERAEA RRLAGGKKQ
//
