ID A0A1G7DCN3_9ACTN Unreviewed; 303 AA.
AC A0A1G7DCN3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373, ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN ORFNames=SAMN04489747_3538 {ECO:0000313|EMBL:SDE48545.1};
OS Auraticoccus monumenti.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Auraticoccus.
OX NCBI_TaxID=675864 {ECO:0000313|EMBL:SDE48545.1, ECO:0000313|Proteomes:UP000198546};
RN [1] {ECO:0000313|EMBL:SDE48545.1, ECO:0000313|Proteomes:UP000198546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MON 2.2 {ECO:0000313|EMBL:SDE48545.1,
RC ECO:0000313|Proteomes:UP000198546};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698,
CC ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|RuleBase:RU003938}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC ECO:0000256|RuleBase:RU003938}.
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DR EMBL; LT629688; SDE48545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7DCN3; -.
DR STRING; 675864.SAMN04489747_3538; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000198546; Chromosome i.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU003938};
KW Reference proteome {ECO:0000313|Proteomes:UP000198546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003938};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 30981 MW; E1C54C3AF2E2CEC3 CRC64;
MSDPDIPPGS ASPPRAHTPP AGPDHGRAGR NLPAAIGVGV GLGALLLLSL WKFQLGFAVF
VAVALAQGAV EIGQALRRLQ MHAAVVPIVA GTFLIVVGSY FAGQRDVAPA SSTSILLGAM
GLTVLAALIW RMPGGQEGYV KDVAASLFII AYVPLLGAFV SLMLAGENGS LRVLTFIAVV
VASDVGGYAV GVLVGRHPMA PRISPKKSWE GFAGSMVLGC VVAVLMVTLT LDAPLWVGLV
VGATLVGIGV CGDLIESLIK RDVGIKDMSS ILPGHGGVMD RLDSLLVAAP VAWLAMYLLI
PGG
//
