TAM41_CAEBR
ID TAM41_CAEBR Reviewed; 321 AA.
AC Q61X59; A8WW89;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Phosphatidate cytidylyltransferase, mitochondrial;
DE EC=2.7.7.41 {ECO:0000250|UniProtKB:P53230};
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDP-DAG synthase;
DE AltName: Full=Mitochondrial translocator assembly and maintenance protein 41 homolog;
DE Short=TAM41;
GN ORFNames=CBG04116;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from
CC phosphatidic acid (PA) in the mitochondrial inner membrane. Required
CC for the biosynthesis of the dimeric phospholipid cardiolipin, which
CC stabilizes supercomplexes of the mitochondrial respiratory chain in the
CC mitochondrial inner membrane. {ECO:0000250|UniProtKB:P53230}.
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:0000250|UniProtKB:P53230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Note=Magnesium. Also active with cobalt or copper.
CC {ECO:0000250|UniProtKB:P53230};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000250|UniProtKB:P53230}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P53230}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53230}; Matrix side
CC {ECO:0000250|UniProtKB:P53230}.
CC -!- SIMILARITY: Belongs to the TAM41 family. {ECO:0000305}.
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DR EMBL; HE600956; CAP24898.1; -; Genomic_DNA.
DR RefSeq; XP_002639511.1; XM_002639465.1.
DR AlphaFoldDB; Q61X59; -.
DR SMR; Q61X59; -.
DR STRING; 6238.CBG04116; -.
DR EnsemblMetazoa; CBG04116.1; CBG04116.1; WBGene00026852.
DR GeneID; 8581504; -.
DR KEGG; cbr:CBG_04116; -.
DR CTD; 8581504; -.
DR WormBase; CBG04116; CBP01061; WBGene00026852; -.
DR eggNOG; KOG2986; Eukaryota.
DR HOGENOM; CLU_030279_1_2_1; -.
DR InParanoid; Q61X59; -.
DR OMA; HYSFLKF; -.
DR OrthoDB; 1145430at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR015222; Tam41.
DR PANTHER; PTHR13619; PTHR13619; 1.
DR Pfam; PF09139; Tam41_Mmp37; 1.
DR PIRSF; PIRSF028840; Mmp37; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..321
FT /note="Phosphatidate cytidylyltransferase, mitochondrial"
FT /id="PRO_0000248358"
SQ SEQUENCE 321 AA; 36705 MW; EB39B920EC8BFD94 CRC64;
MDEYRELISV LPLDTVEYAF AYGSGAIQQK DENKAEKMVD FVVVTKDAQE FHKANIAKNP
QHYSLLRLLG PKMLEKIQCN FAARVYYNTH VNVGKRKIKY GIISYENVKQ DLLDWRWIYI
SGRLHKPVLD VIKPKDDMCD LVTENRRSAL HSALLLLPES FTLKQLFHQI VGLSYTGDFR
MIVGEDKNKI MKIVEGNYEE LMRVYEPLMN DDARLSVMSP AKVIQDGSTT AIYHRLNLLP
SEVLNQIQKN MNKAQKRQRD AEEVIFSLAH RHDVAATVET AIGGIIRPIS FSQTAKNAFS
AGMTRSVIYS LAKMSKFLKS K