ID A0A1I3E934_9PLAN Unreviewed; 337 AA.
AC A0A1I3E934;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938};
GN ORFNames=SAMN05421753_104126 {ECO:0000313|EMBL:SFH95466.1};
OS Planctomicrobium piriforme.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomicrobium.
OX NCBI_TaxID=1576369 {ECO:0000313|EMBL:SFH95466.1, ECO:0000313|Proteomes:UP000199518};
RN [1] {ECO:0000313|Proteomes:UP000199518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26348 {ECO:0000313|Proteomes:UP000199518};
RA Varghese N., Submissions S.;
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|RuleBase:RU003938};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {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; FOQD01000004; SFH95466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3E934; -.
DR STRING; 1576369.SAMN05421753_104126; -.
DR OrthoDB; 9799199at2; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000199518; Unassembled WGS sequence.
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; PTHR43535; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43535:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 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:SFH95466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199518};
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 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 337 AA; 37435 MW; 8437118E4618C278 CRC64;
MPQWITEWTR GWTRLEHLTP EVGITLVAIA VALVIASILT RILKRIRPER DDTELRQRVR
TWWVIAWMFG AAILISPATS TIFLAFVSFL ALKEYFSLIP TRRADRRVLF WAYLSIPVQY
YLAYTAWYGM FVVFIPVYLF LFLPARMVAI GQTEGFLRSI GTLHWGLMTT VFSLSHTAMM
LMLSVGASPR IAPEWPGNSQ TTAPGVALLV LLIVLTQFND VAQYVWGKSL GRIRVVPKVS
PGKTLAGLLG GIGSTTLLAA LLGPWLTILN LKMAIFAGML IAVSGFAGDL SISALKRDLG
VKDSGSILPG HGGILDRVDS LTYTAPLFFH FIYYFYG
//
