TAM41_SCHPO
ID TAM41_SCHPO Reviewed; 393 AA.
AC O74339;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 106.
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 Name=tam41; ORFNames=SPBC1A4.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=972 / ATCC 24843, and JY3;
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
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 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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20110.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAA20110.3; ALT_FRAME; Genomic_DNA.
DR PIR; T39854; T39854.
DR RefSeq; NP_595808.3; NM_001021711.3.
DR PDB; 6IG2; X-ray; 2.88 A; A/B/C/D=28-319.
DR PDB; 6IG4; X-ray; 2.26 A; A/B=28-319.
DR PDBsum; 6IG2; -.
DR PDBsum; 6IG4; -.
DR AlphaFoldDB; O74339; -.
DR SMR; O74339; -.
DR STRING; 4896.SPBC1A4.06c.1; -.
DR MaxQB; O74339; -.
DR PaxDb; O74339; -.
DR GeneID; 2540640; -.
DR KEGG; spo:SPBC1A4.06c; -.
DR PomBase; SPBC1A4.06c; tam41.
DR eggNOG; KOG2986; Eukaryota.
DR HOGENOM; CLU_030279_1_1_1; -.
DR InParanoid; O74339; -.
DR BRENDA; 2.7.7.41; 5613.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:O74339; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:1901612; F:cardiolipin binding; IDA:PomBase.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:PomBase.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:PomBase.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:PomBase.
DR GO; GO:0007006; P:mitochondrial membrane organization; IC:PomBase.
DR InterPro; IPR015222; Tam41.
DR PANTHER; PTHR13619; PTHR13619; 1.
DR Pfam; PF09139; Tam41_Mmp37; 1.
DR PIRSF; PIRSF028840; Mmp37; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..393
FT /note="Phosphatidate cytidylyltransferase, mitochondrial"
FT /id="PRO_0000248361"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6IG4"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 191..212
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 219..236
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:6IG4"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:6IG4"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:6IG4"
SQ SEQUENCE 393 AA; 45235 MW; 379829C1A68BDCE4 CRC64;
MIFGKTHFLS YNILRYSTKR WMNRHSYSHH AKCTVAQLLK QNLLTFENQR IQPEEELKEN
LTKVVNYFQA PIDVAVGYGS GVFRQAGYSQ KENPMIDFIF QVEDPVKWHK INLQQNPSHY
SFVKNFGPGF VSTLQESFGT GVYYNTHVEV EGNIIKYGVT SKKDVYEDLK NWNTMYLAGR
FQKPVVILKG EDEFYKENSY NLSSALHVGL LMLADRFTEF DLYKTIVSLS YLGDIRMSFF
AENPRKVENI VSKQIAFFRK LYLPLLYAEP GVHFIESSEV LKSMDPSDNS RYLSFHQNIT
KDSISRLLNG LPLNLVKILG LKPDTSSFEK CAELMLTNQI STRSLLISKS IKKLTSFSIL
TQSIKGIFTA GVIRSFVYVY AKLKKGLLSK WGR
