GenomeNet

Database: UniProt
Entry: I4N8P8_9PSED
LinkDB: I4N8P8_9PSED
Original site: I4N8P8_9PSED 
ID   I4N8P8_9PSED            Unreviewed;       271 AA.
AC   I4N8P8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=PMM47T1_04979 {ECO:0000313|EMBL:EIK97838.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK97838.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK97838.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK97838.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(2012).
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}.
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:EIK97838.1}.
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; AJWX01000003; EIK97838.1; -; Genomic_DNA.
DR   RefSeq; WP_008366374.1; NZ_AJWX01000003.1.
DR   AlphaFoldDB; I4N8P8; -.
DR   STRING; 1179778.PMM47T1_04979; -.
DR   PATRIC; fig|1179778.3.peg.996; -.
DR   eggNOG; COG0575; Bacteria.
DR   OrthoDB; 9799199at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000004339; Unassembled WGS sequence.
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:UP000004339};
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        28..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   271 AA;  29050 MW;  549E00F87D365863 CRC64;
     MLKQRIITAL ILLPIALCGF FLLEGASFAL FIGLVVTLGG WEWARLAGFE RQPARVGFAA
     VVAVALFFLY LSPALAPFVL AAALIWWGVA TFLVLTFPRT SEHWGSVACK LLIGFLILLP
     AWQGLVLIKA QEQGNWLILA VMVLVWAADI GAYFSGRAFG KAKLAPQVSP GKSWAGFYGG
     MAVSLLITLV VGQVRHWGVG ETILCLMGAA IVVALSVVGD LTESMFKRRA GIKDSSNLLP
     GHGGILDRID SLTAAIPVFA VLLWMANWSA L
//
DBGET integrated database retrieval system