POS5_YEAST
ID POS5_YEAST Reviewed; 414 AA.
AC Q06892; D6W3I1; Q08928;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=NADH kinase POS5, mitochondrial;
DE EC=2.7.1.86 {ECO:0000269|PubMed:12727869};
DE Flags: Precursor;
GN Name=POS5; OrderedLocusNames=YPL188W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
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 204508 / S288c;
RX 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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2547755; DOI=10.1093/oxfordjournals.jbchem.a122709;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
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 Saccharomyces
RT cerevisiae.";
RL EMBO J. 22:2015-2024(2003).
RN [6]
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., Dominick O.C.,
RA Copeland W.C.;
RT "POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase
RT required for stability of mitochondrial DNA.";
RL Eukaryot. Cell 2:809-820(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX 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 [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Phosphorylates both NADH and NAD(+), with a twofold
CC preference for NADH. Anti-oxidant factor and key source of the cellular
CC reductant NADPH. {ECO:0000269|PubMed:12727869,
CC ECO:0000269|PubMed:12912900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NADH = ADP + H(+) + NADPH; Xref=Rhea:RHEA:12260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:456216; EC=2.7.1.86;
CC Evidence={ECO:0000269|PubMed:12727869};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12261;
CC Evidence={ECO:0000305|PubMed:12727869};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=105 uM for NADH {ECO:0000269|PubMed:2547755};
CC KM=2.1 mM for ATP {ECO:0000269|PubMed:2547755};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:2547755};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:12727869, ECO:0000269|PubMed:12912900,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 4650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
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DR EMBL; X84260; CAA59017.1; -; Genomic_DNA.
DR EMBL; Z73544; CAA97900.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11247.1; -; Genomic_DNA.
DR PIR; S65200; S65200.
DR RefSeq; NP_015136.1; NM_001184002.1.
DR PDB; 3AFO; X-ray; 2.00 A; A/B=27-414.
DR PDBsum; 3AFO; -.
DR AlphaFoldDB; Q06892; -.
DR SMR; Q06892; -.
DR BioGRID; 35995; 58.
DR DIP; DIP-5503N; -.
DR IntAct; Q06892; 3.
DR STRING; 4932.YPL188W; -.
DR MaxQB; Q06892; -.
DR PaxDb; Q06892; -.
DR PRIDE; Q06892; -.
DR EnsemblFungi; YPL188W_mRNA; YPL188W; YPL188W.
DR GeneID; 855913; -.
DR KEGG; sce:YPL188W; -.
DR SGD; S000006109; POS5.
DR VEuPathDB; FungiDB:YPL188W; -.
DR eggNOG; KOG2178; Eukaryota.
DR HOGENOM; CLU_008831_10_2_1; -.
DR InParanoid; Q06892; -.
DR OMA; IPKYQES; -.
DR BioCyc; MetaCyc:G3O-34081-MON; -.
DR BioCyc; YEAST:G3O-34081-MON; -.
DR BRENDA; 2.7.1.23; 984.
DR BRENDA; 2.7.1.86; 984.
DR PRO; PR:Q06892; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06892; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
DR GO; GO:0042736; F:NADH kinase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR HAMAP; MF_00361; NAD_kinase; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Mitochondrion; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..414
FT /note="NADH kinase POS5, mitochondrial"
FT /id="PRO_0000120715"
FT CONFLICT 37..38
FT /note="KP -> EA (in Ref. 1; CAA59017)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> L (in Ref. 1; CAA59017)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> D (in Ref. 1; CAA59017)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="I -> S (in Ref. 1; CAA59017)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..401
FT /note="LGFN -> CRIH (in Ref. 1; CAA59017)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:3AFO"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 220..231
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 248..261
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:3AFO"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:3AFO"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:3AFO"
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
