ID   POS5_YEAST              Reviewed;         414 AA.
AC   Q06892; Q08928;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=NADH kinase POS5, mitochondrial;
DE            EC=2.7.1.86;
DE   Flags: Precursor;
GN   Name=POS5; OrderedLocusNames=YPL188W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gruenbein R., Krems B., Entian K.-D.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=2547755;
RA   Iwahashi Y., Hitoshio A., Tajima N., Nakamura T.;
RT   "Characterization of NADH kinase from Saccharomyces cerevisiae.";
RL   J. Biochem. 105:588-593(1989).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12727869; DOI=10.1093/emboj/cdg211;
RA   Outten C.E., Culotta V.C.;
RT   "A novel NADH kinase is the mitochondrial source of NADPH in
RT   Saccharomyces cerevisiae.";
RL   EMBO J. 22:2015-2024(2003).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12912900; DOI=10.1128/EC.2.4.809-820.2003;
RA   Strand M.K., Stuart G.R., Longley M.J., Graziewicz M.A.,
RA   Dominick O.C., Copeland W.C.;
RT   "POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH
RT   kinase required for stability of mitochondrial DNA.";
RL   Eukaryot. Cell 2:809-820(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Phosphorylates both NADH and NAD(+), with a twofold
CC       preference for NADH. Anti-oxidant factor and key source of the
CC       cellular reductant NADPH.
CC   -!- CATALYTIC ACTIVITY: ATP + NADH = ADP + NADPH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=105 uM for NADH;
CC         KM=2.1 mM for ATP;
CC       pH dependence:
CC         Optimum pH is 8.5;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Present with 4650 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
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DR   EMBL; X84260; CAA59017.1; -; Genomic_DNA.
DR   EMBL; Z73544; CAA97900.1; -; Genomic_DNA.
DR   PIR; S65200; S65200.
DR   RefSeq; NP_015136.1; -.
DR   DIP; DIP:5503N; -.
DR   IntAct; Q06892; 6.
DR   Ensembl; YPL188W; Saccharomyces cerevisiae.
DR   GeneID; 855913; -.
DR   GenomeReviews; U00094_GR; YPL188W.
DR   KEGG; sce:YPL188W; -.
DR   NMPDR; fig|4932.3.peg.6265; -.
DR   CYGD; YPL188w; -.
DR   SGD; S000006109; POS5.
DR   HOGENOM; Q06892; -.
DR   OMA; Q06892; GFNSSFR.
DR   BRENDA; 2.7.1.86; 250.
DR   NextBio; 980625; -.
DR   GermOnline; YPL188W; Saccharomyces cerevisiae.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0042736; F:NADH kinase activity; IDA:SGD.
DR   GO; GO:0006741; P:NADP biosynthetic process; IDA:SGD.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; ATP_NADK.
DR   Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1.
DR   PANTHER; PTHR20275; ATP_NADK; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Kinase; Mitochondrion; NAD; NADP;
KW   Nucleotide-binding; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    414       NADH kinase POS5, mitochondrial.
FT                                /FTId=PRO_0000120715.
FT   CONFLICT     37     38       KP -> EA (in Ref. 1; CAA59017).
FT   CONFLICT    180    180       S -> L (in Ref. 1; CAA59017).
FT   CONFLICT    329    329       V -> D (in Ref. 1; CAA59017).
FT   CONFLICT    343    343       I -> S (in Ref. 1; CAA59017).
FT   CONFLICT    398    401       LGFN -> CRIH (in Ref. 1; CAA59017).
SQ   SEQUENCE   414 AA;  46247 MW;  002CFC271A67B557 CRC64;
     MFVRVKLNKP VKWYRFYSTL DSHSLKLQSG SKFVKIKPVN NLRSSSSADF VSPPNSKLQS
     LIWQNPLQNV YITKKPWTPS TREAMVEFIT HLHESYPEVN VIVQPDVAEE ISQDFKSPLE
     NDPNRPHILY TGPEQDIVNR TDLLVTLGGD GTILHGVSMF GNTQVPPVLA FALGTLGFLS
     PFDFKEHKKV FQEVISSRAK CLHRTRLECH LKKKDSNSSI VTHAMNDIFL HRGNSPHLTN
     LDIFIDGEFL TRTTADGVAL ATPTGSTAYS LSAGGSIVSP LVPAILMTPI CPRSLSFRPL
     ILPHSSHIRI KIGSKLNQKP VNSVVKLSVD GIPQQDLDVG DEIYVINEVG TIYIDGTQLP
     TTRKTENDFN NSKKPKRSGI YCVAKTENDW IRGINELLGF NSSFRLTKRQ TDND
//