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Q06892 (POS5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH kinase POS5, mitochondrial
EC=2.7.1.86
Gene names
Name:POS5
Ordered Locus Names:YPL188W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates both NADH and NAD+, with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH. Ref.5 Ref.6

Catalytic activity

ATP + NADH = ADP + NADPH.

Subcellular location

Mitochondrion matrix Ref.5 Ref.6 Ref.7.

Miscellaneous

Present with 4650 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=105 µM for NADH Ref.4

KM=2.1 mM for ATP

pH dependence:

Optimum pH is 8.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 414NADH kinase POS5, mitochondrialPRO_0000120715

Experimental info

Sequence conflict37 – 382KP → EA in CAA59017. Ref.1
Sequence conflict1801S → L in CAA59017. Ref.1
Sequence conflict3291V → D in CAA59017. Ref.1
Sequence conflict3431I → S in CAA59017. Ref.1
Sequence conflict398 – 4014LGFN → CRIH in CAA59017. Ref.1

Secondary structure

1 ............................................................... 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06892 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 002CFC271A67B557

FASTA41446,247
        10         20         30         40         50         60 
MFVRVKLNKP VKWYRFYSTL DSHSLKLQSG SKFVKIKPVN NLRSSSSADF VSPPNSKLQS 

        70         80         90        100        110        120 
LIWQNPLQNV YITKKPWTPS TREAMVEFIT HLHESYPEVN VIVQPDVAEE ISQDFKSPLE 

       130        140        150        160        170        180 
NDPNRPHILY TGPEQDIVNR TDLLVTLGGD GTILHGVSMF GNTQVPPVLA FALGTLGFLS 

       190        200        210        220        230        240 
PFDFKEHKKV FQEVISSRAK CLHRTRLECH LKKKDSNSSI VTHAMNDIFL HRGNSPHLTN 

       250        260        270        280        290        300 
LDIFIDGEFL TRTTADGVAL ATPTGSTAYS LSAGGSIVSP LVPAILMTPI CPRSLSFRPL 

       310        320        330        340        350        360 
ILPHSSHIRI KIGSKLNQKP VNSVVKLSVD GIPQQDLDVG DEIYVINEVG TIYIDGTQLP 

       370        380        390        400        410 
TTRKTENDFN NSKKPKRSGI YCVAKTENDW IRGINELLGF NSSFRLTKRQ TDND

« Hide

References

« Hide 'large scale' references
[1]Gruenbein R., Krems B., Entian K.-D.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Characterization of NADH kinase from Saccharomyces cerevisiae."
Iwahashi Y., Hitoshio A., Tajima N., Nakamura T.
J. Biochem. 105:588-593(1989) [PubMed: 2547755] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]"A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae."
Outten C.E., Culotta V.C.
EMBO J. 22:2015-2024(2003) [PubMed: 12727869] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA."
Strand M.K., Stuart G.R., Longley M.J., Graziewicz M.A., Dominick O.C., Copeland W.C.
Eukaryot. Cell 2:809-820(2003) [PubMed: 12912900] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X84260 Genomic DNA. Translation: CAA59017.1.
Z73544 Genomic DNA. Translation: CAA97900.1.
BK006949 Genomic DNA. Translation: DAA11247.1.
PIRS65200.
RefSeqNP_015136.1. NM_001184002.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AFOX-ray2.00A/B27-414[»]
ProteinModelPortalQ06892.
SMRQ06892. Positions 27-408.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5503N.
IntActQ06892. 3 interactions.
MINTMINT-569331.
STRINGQ06892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL188W; YPL188W; YPL188W.
GeneID855913.
KEGGsce:YPL188W.
NMPDRfig|4932.3.peg.6265.

Organism-specific databases

CYGDYPL188w.
SGDS000006109. POS5.

Phylogenomic databases

eggNOGfuNOG04069.
GeneTreeEFGT00050000004217.
HOGENOMHBG328966.
OMAKTENDWI.
OrthoDBEOG45XC5K.

Enzyme and pathway databases

BRENDA2.7.1.86. 984.

Gene expression databases

ArrayExpressQ06892.
GenevestigatorQ06892.
GermOnlineYPL188W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR017438. ATP-NAD_kinase_PpnK-typ_a/b.
IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
IPR002504. polyP/ATP_NADK_prd.
[Graphical view]
Gene3DG3DSA:2.60.200.30. ATP-NAD_kinase_PpnK-typ. 1 hit.
G3DSA:3.40.50.10330. ATP-NAD_kinase_PpnK-typ_a/b. 1 hit.
PANTHERPTHR20275. ATP_NADK. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. ATP-NAD_kinase_PpnK-typ. 1 hit.
ProtoNetSearch...

Other

NextBio980625.

Entry information

Entry namePOS5_YEAST
AccessionPrimary (citable) accession number: Q06892
Secondary accession number(s): D6W3I1, Q08928
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: December 14, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents