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Database: UniProt
Entry: A0A1X1Q8Q1_9FIRM
LinkDB: A0A1X1Q8Q1_9FIRM
Original site: A0A1X1Q8Q1_9FIRM 
ID   A0A1X1Q8Q1_9FIRM        Unreviewed;       275 AA.
AC   A0A1X1Q8Q1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=D081_0056 {ECO:0000313|EMBL:ORU01237.1};
OS   Anaerovibrio sp. JC8.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORU01237.1, ECO:0000313|Proteomes:UP000192538};
RN   [1] {ECO:0000313|EMBL:ORU01237.1, ECO:0000313|Proteomes:UP000192538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC8 {ECO:0000313|EMBL:ORU01237.1,
RC   ECO:0000313|Proteomes:UP000192538};
RA   Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT   "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT   bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT   effect of hydrogen.";
RL   Submitted (OCT-2012) 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}.
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:ORU01237.1}.
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DR   EMBL; ANBM01000001; ORU01237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1Q8Q1; -.
DR   STRING; 1240085.D081_0056; -.
DR   OrthoDB; 9799199at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000192538; 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   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
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        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   275 AA;  29348 MW;  DF96ED18522F38FE CRC64;
     MLTRIITGII GIILAALVIQ NGGTVFAGAV LLLAFGAWYE YCNAFQQKGY KPTLVTGMVM
     ISIMWAGGFL GSTGMLVGAA MLSALVIMLL TVLNHDKFDV LSAVISVAGV FYIGLSFVHL
     VMLRFIGEEA YIATSLGDFQ LGCALVWVAL IGTWASDTFA YFAGCFLGKH KLCEKISPKK
     TIEGFIGGLV GTTASVAGLG VFFGFDVVVM AVLGFFICVV ATLGDLVESV VKRYTGIKDS
     GNVIPGHGGI WDRFDSVIYT VPFVYYFLYC ARIAG
//
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