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Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (CDP-DAG synthase) (Mitochondrial import protein MMP37) (Mitochondrial matrix protein of 37 kDa) (Mitochondrial translocator assembly and maintenance protein 41)

 TAM41_YEAST             Reviewed;         385 AA.
P53230; D6VUI3; Q45U38;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 127.
RecName: Full=Phosphatidate cytidylyltransferase, mitochondrial;
EC=2.7.7.41;
AltName: Full=CDP-diacylglycerol synthase;
Short=CDP-DAG synthase;
AltName: Full=Mitochondrial import protein MMP37;
AltName: Full=Mitochondrial matrix protein of 37 kDa;
AltName: Full=Mitochondrial translocator assembly and maintenance protein 41;
Flags: Precursor;
Name=TAM41; Synonyms=MMP37; OrderedLocusNames=YGR046W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-8 AND ALA-127.
STRAIN=SK1;
PubMed=16273108; DOI=10.1038/ng1674;
Deutschbauer A.M., Davis R.W.;
"Quantitative trait loci mapped to single-nucleotide resolution in
yeast.";
Nat. Genet. 37:1333-1340(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14690591; DOI=10.1016/S1097-2765(03)00476-3;
Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
Yates J.R. III, Davis T.N.;
"Assigning function to yeast proteins by integration of
technologies.";
Mol. Cell 12:1353-1365(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16943180; DOI=10.1083/jcb.200603087;
Tamura Y., Harada Y., Yamano K., Watanabe K., Ishikawa D., Ohshima C.,
Nishikawa S., Yamamoto H., Endo T.;
"Identification of Tam41 maintaining integrity of the TIM23 protein
translocator complex in mitochondria.";
J. Cell Biol. 174:631-637(2006).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16790493; DOI=10.1091/mbc.E06-04-0366;
Gallas M.R., Dienhart M.K., Stuart R.A., Long R.M.;
"Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial
matrix protein with a role in mitochondrial protein import.";
Mol. Biol. Cell 17:4051-4062(2006).
[9]
FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
PubMed=19114592; DOI=10.1083/jcb.200806048;
Kutik S., Rissler M., Guan X.L., Guiard B., Shui G., Gebert N.,
Heacock P.N., Rehling P., Dowhan W., Wenk M.R., Pfanner N.,
Wiedemann N.;
"The translocator maintenance protein Tam41 is required for
mitochondrial cardiolipin biosynthesis.";
J. Cell Biol. 183:1213-1221(2008).
[10]
PATHWAY.
PubMed=20485265; DOI=10.1038/emboj.2010.98;
Osman C., Haag M., Wieland F.T., Brugger B., Langer T.;
"A mitochondrial phosphatase required for cardiolipin biosynthesis:
the PGP phosphatase Gep4.";
EMBO J. 29:1976-1987(2010).
[11]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, COFACTOR, AND MUTAGENESIS OF 130-TYR--SER-132
AND ASP-220.
PubMed=23623749; DOI=10.1016/j.cmet.2013.03.018;
Tamura Y., Harada Y., Nishikawa S., Yamano K., Kamiya M., Shiota T.,
Kuroda T., Kuge O., Sesaki H., Imai K., Tomii K., Endo T.;
"Tam41 is a CDP-diacylglycerol synthase required for cardiolipin
biosynthesis in mitochondria.";
Cell Metab. 17:709-718(2013).
-!- FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG)
from phosphatidic acid (PA) in the mitochondrial inner membrane.
Required for the biosynthesis of the dimeric phospholipid
cardiolipin, which stabilizes supercomplexes of the mitochondrial
respiratory chain in the mitochondrial inner membrane.
{ECO:0000269|PubMed:16790493, ECO:0000269|PubMed:16943180,
ECO:0000269|PubMed:19114592, ECO:0000269|PubMed:23623749}.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-
1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
Evidence={ECO:0000269|PubMed:23623749};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:23623749};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:23623749};
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:23623749};
Note=Magnesium. Also active with cobalt or copper.
{ECO:0000269|PubMed:23623749};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.76 mM for CTP {ECO:0000269|PubMed:23623749};
KM=0.067 mM for nitrobenzoxadiazole-phosphatidate
{ECO:0000269|PubMed:23623749};
Vmax=68 nmol/min/mg enzyme {ECO:0000269|PubMed:23623749};
pH dependence:
Optimum pH is 7-9. {ECO:0000269|PubMed:23623749};
-!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
{ECO:0000269|PubMed:19114592, ECO:0000269|PubMed:20485265}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16790493,
ECO:0000269|PubMed:16943180, ECO:0000269|PubMed:23623749};
Peripheral membrane protein {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:16790493, ECO:0000269|PubMed:16943180,
ECO:0000269|PubMed:23623749}; Matrix side
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16790493,
ECO:0000269|PubMed:16943180, ECO:0000269|PubMed:23623749}.
-!- DISRUPTION PHENOTYPE: Deficient in cardiolipin. Blocked in the
import of presequence-containing proteins as well as of non-
cleavable carrier proteins into mitochondria.
{ECO:0000269|PubMed:19114592}.
-!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TAM41 family. {ECO:0000305}.
-!- CAUTION: Was initially identified as protein involved in the
translocation of transit peptide-containing proteins across the
mitochondrial inner membrane by its role in maintaining the
integrity and stability of the inner membrane translocase TIM23
complex (PubMed:16943180, PubMed:16790493). It has later been
shown that this phenotype can be attributed to the pleiotropic
effects of mitochondria lacking cardiolipin (PubMed:19114592).
{ECO:0000305|PubMed:16790493, ECO:0000305|PubMed:16943180,
ECO:0000305|PubMed:19114592}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ115391; AAZ22461.1; -; Genomic_DNA.
EMBL; Z72831; CAA97045.1; -; Genomic_DNA.
EMBL; BK006941; DAA08144.1; -; Genomic_DNA.
PIR; S64340; S64340.
RefSeq; NP_011560.3; NM_001181175.3.
ProteinModelPortal; P53230; -.
SMR; P53230; -.
BioGrid; 33293; 146.
DIP; DIP-1622N; -.
IntAct; P53230; 26.
MINT; P53230; -.
STRING; 4932.YGR046W; -.
SwissLipids; SLP:000000240; -.
MaxQB; P53230; -.
PaxDb; P53230; -.
PRIDE; P53230; -.
EnsemblFungi; YGR046W_mRNA; YGR046W_mRNA; YGR046W.
GeneID; 852937; -.
KEGG; sce:YGR046W; -.
SGD; S000003278; TAM41.
GeneTree; ENSGT00390000000616; -.
HOGENOM; HOG000205225; -.
InParanoid; P53230; -.
KO; K17807; -.
OMA; LKDLATW; -.
OrthoDB; EOG092C3DJW; -.
BioCyc; YEAST:G3O-30764-MONOMER; -.
UniPathway; UPA00557; UER00614.
PRO; PR:P53230; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:SGD.
GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:SGD.
GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR015222; Tam41.
PANTHER; PTHR13619; PTHR13619; 2.
Pfam; PF09139; Tam41_Mmp37; 2.
PIRSF; PIRSF028840; Mmp37; 1.
1: Evidence at protein level;
Complete proteome; Lipid biosynthesis; Lipid metabolism; Magnesium;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Nucleotidyltransferase; Phospholipid biosynthesis;
Phospholipid metabolism; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 34 Mitochondrion. {ECO:0000255}.
CHAIN 35 385 Phosphatidate cytidylyltransferase,
mitochondrial.
/FTId=PRO_0000202796.
VARIANT 8 8 G -> S (in strain: SK1).
{ECO:0000269|PubMed:16273108}.
VARIANT 127 127 V -> A (in strain: SK1).
{ECO:0000269|PubMed:16273108}.
MUTAGEN 130 132 YGS->AAA: Completely abolishes the
enzymatic activity.
{ECO:0000269|PubMed:23623749}.
MUTAGEN 220 220 D->A: Completely abolishes the enzymatic
activity. {ECO:0000269|PubMed:23623749}.
SEQUENCE 385 AA; 44200 MW; A0E9DDCB1F8E8043 CRC64;
MLRVSENGLR FLLKCHSTNV SMFNRLLSTQ IKEGRSSIDD AGIIPDGTIN ERPNHYIEGI
TKGSDLDLLE KGIRKTDEMT SNFTNYMYKF HRLPPNYGSN QLITIDKELQ KELDGVMSSF
KAPCRFVFGY GSGVFEQAGY SKSHSKPQID IILGVTYPSH FHSINMRQNP QHYSSLKYFG
SEFVSKFQQI GAGVYFNPFA NINGHDVKYG VVSMETLLKD IATWNTFYLA GRLQKPVKIL
KNDLRVQYWN QLNLKAAATL AKHYTLEKNN NKFDEFQFYK EITALSYAGD IRYKLGGENP
DKVNNIVTKN FERFQEYYKP IYKEVVLNDS FYLPKGFTLK NTQRLLLSRI SKSSALQTIK
GVFTAGITKS IKYAWAKKLK SMRRS


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