ID J7IRQ1_DESMD Unreviewed; 282 AA.
AC J7IRQ1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938};
GN OrderedLocusNames=Desmer_2391 {ECO:0000313|EMBL:AFQ44315.1};
OS Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS NCIMB 13706 / S10).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ44315.1, ECO:0000313|Proteomes:UP000005262};
RN [1] {ECO:0000313|EMBL:AFQ44315.1, ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
RN [2] {ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL Submitted (AUG-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|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; CP003629; AFQ44315.1; -; Genomic_DNA.
DR RefSeq; WP_014903229.1; NC_018515.1.
DR AlphaFoldDB; J7IRQ1; -.
DR STRING; 768704.Desmer_2391; -.
DR KEGG; dmi:Desmer_2391; -.
DR eggNOG; COG4589; Bacteria.
DR HOGENOM; CLU_037294_2_0_9; -.
DR OrthoDB; 9799199at2; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000005262; 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; 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938,
KW ECO:0000313|EMBL:AFQ44315.1};
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 5..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 282 AA; 31218 MW; A80D131B150CC525 CRC64;
MILRAYLFFL CVIILIFSLA YVKKSRETVL RVASFFGILN VFSLASILGV KAVFGLVSLI
LLLSLYELGK NYHLKYPILL ALIVAGCYGL MLSFASYLIY FIPPFLLLVA LTFAGTLKMI
RNPFYVYCFG VMFLAVSAAS LVALYSLNPD TLWFLVAMLA FNDVTGYFAG RKFGKTLVFK
VLSPKKTLEG YLGGLGGLLA GLVLFHTIIP VLAETTLFQN AILLITIFIV GNAGDLVFSK
IKRSVGIKDF SNFLPGHGGI LDRFDSTFTV SPLLFMFLYY LN
//
