ID A0A1Z4R7T0_9CYAN Unreviewed; 294 AA.
AC A0A1Z4R7T0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN ORFNames=NIES4101_44540 {ECO:0000313|EMBL:BAZ38517.1};
OS Calothrix sp. NIES-4101.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ38517.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ38517.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ38517.1,
RC ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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|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; AP018280; BAZ38517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4R7T0; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000290974; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; PTHR47101:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47101; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 5, CHLOROPLASTIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938,
KW ECO:0000313|EMBL:BAZ38517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290974};
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 6..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 294 AA; 31776 MW; BC22038C2C9CD66B CRC64;
MPWTRIISGI IAIAIALTTT LLGGWYFTFT YVVIVYLGQN EFFDLVRAKS IAPAAKTTLV
VSLALLAIST VNVSLADAVL PLAGTFICFY LLFQPKIATI ADISASILGL FYTGYLPSFW
VRLRGIDSAN HTNLPLSGYL PVDWSDLFQR SQISSVPQGL CVTVLTFLCI WAADIGAYFV
GKYFGKTHLS DISPKKTVEG AVFGIGGSIV VATAGAYYLH WSHYILTGIS LGLLIGIASL
LGDLTESMLK RDAGVKDSGQ LIPGHGGILD RTDSYIFTAP IVYYFVTLLL PLLK
//