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Q9CZ42 (NNRD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent (S)-NAD(P)H-hydrate dehydratase

EC=4.2.1.93
Alternative name(s):
ATP-dependent NAD(P)HX dehydratase
Carbohydrate kinase domain-containing protein
Gene names
Name:Carkd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Ref.6

Catalytic activity

ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH. HAMAP-Rule MF_03157

ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = ADP + phosphate + NADPH.

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03157

Subcellular location

Mitochondrion Ref.4.

Sequence similarities

Belongs to the NnrD/CARKD family.

Contains 1 YjeF C-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.8 µM for (S)-NADHX Ref.6

KM=2.5 µM for (S)-NADPHX

KM=1.8 µM for ATP

Vmax=0.43 µmol/min/mg enzyme toward (S)-NADHX

Vmax=1.6 µmol/min/mg enzyme toward (S)-NADPHX

Vmax=0.26 µmol/min/mg enzyme toward ATP

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnicotinamide nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from direct assay Ref.4. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent NAD(P)H-hydrate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CZ42-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9CZ42-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
Isoform 3 (identifier: Q9CZ42-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MAVHACGAAAAVVALLSAAIALQWSPLYA → MGFRCVAIRACGG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion Potential
Chain43 – 343301ATP-dependent (S)-NAD(P)H-hydrate dehydratase HAMAP-Rule MF_03157
PRO_0000337022

Regions

Domain49 – 340292YjeF C-terminal
Nucleotide binding242 – 2465ATP By similarity
Nucleotide binding261 – 27010ATP By similarity
Region202 – 2087NAD(P)HX By similarity

Sites

Binding site1491NAD(P)HX; via amide nitrogen By similarity
Binding site2711NAD(P)HX By similarity

Amino acid modifications

Modified residue631N6-acetyllysine Ref.7
Modified residue811Phosphotyrosine Ref.3 Ref.5

Natural variations

Alternative sequence1 – 4545Missing in isoform 2.
VSP_033831
Alternative sequence1 – 2929MAVHA…SPLYA → MGFRCVAIRACGG in isoform 3.
VSP_033832

Experimental info

Sequence conflict2031H → N in BAB22531. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D0202FE6716F80D5

FASTA34336,717
        10         20         30         40         50         60 
MAVHACGAAA AVVALLSAAI ALQWSPLYAV LQRALSLHTA HATKDMENLF QLVRNIVPAL 

        70         80         90        100        110        120 
TSKKHKGQDG RIGIVGGCQE YTGAPYFAGI SALKVGADLT HVFCAREAAP VIKSYSPELI 

       130        140        150        160        170        180 
VHPVLDSSNA VEEVEKWLPR LHALVVGPGL GRDDLLLNNV RGILESTKAR DIPVVIDADG 

       190        200        210        220        230        240 
LWLVAQQPAL IHSYHKAILT PNHVEFSRLW EAVLSSPMDS NDLKGSTLKL SQALGNITVV 

       250        260        270        280        290        300 
QKGEQDLISN GQQVLVCNQE GSSRRCGGQG DLLSGSLGVM VHWALRAGPE KTNGSSPLLV 

       310        320        330        340 
AAWGACTLTR ECNRQAFQKY GRSTTTTDMI TEVGTAFSRL FTT 

« Hide

Isoform 2 [UniParc].

Checksum: 45454F0628FFD33D
Show »

FASTA29832,152
Isoform 3 [UniParc].

Checksum: 871CFDE6941678A4
Show »

FASTA32735,217

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Brain and Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Liver.
[3]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[4]"A mitochondrial protein compendium elucidates complex I disease biology."
Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., Ong S.E., Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., Vidal M., Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.
Cell 134:112-123(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair."
Marbaix A.Y., Noel G., Detroux A.M., Vertommen D., Van Schaftingen E., Linster C.L.
J. Biol. Chem. 286:41246-41252(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003048 mRNA. Translation: BAB22531.1.
AK009254 mRNA. Translation: BAB26172.1.
AK012456 mRNA. Translation: BAB28251.1.
AK013028 mRNA. Translation: BAB28607.1.
AK013069 mRNA. Translation: BAB28632.1.
AK013420 mRNA. Translation: BAB28847.1.
AK154142 mRNA. Translation: BAE32403.1.
AK171034 mRNA. Translation: BAE42200.1.
BC019538 mRNA. Translation: AAH19538.1.
BC021955 mRNA. Translation: AAH21955.1.
CCDSCCDS57604.1. [Q9CZ42-3]
RefSeqNP_001177286.1. NM_001190357.1.
NP_081271.2. NM_026995.4.
UniGeneMm.64911.

3D structure databases

ProteinModelPortalQ9CZ42.
SMRQ9CZ42. Positions 52-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CZ42. 3 interactions.
MINTMINT-4126105.

PTM databases

PhosphoSiteQ9CZ42.

Proteomic databases

MaxQBQ9CZ42.
PaxDbQ9CZ42.
PRIDEQ9CZ42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID69225.
KEGGmmu:69225.
UCSCuc009kvf.2. mouse. [Q9CZ42-1]

Organism-specific databases

CTD55739.
MGIMGI:1913353. Carkd.

Phylogenomic databases

eggNOGCOG0063.
HOGENOMHOG000163126.
HOVERGENHBG057182.
InParanoidQ9CZ42.
KOK17757.
PhylomeDBQ9CZ42.

Gene expression databases

BgeeQ9CZ42.
GenevestigatorQ9CZ42.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
HAMAPMF_01965. NADHX_dehydratase.
InterProIPR029056. Ribokinase-like.
IPR000631. YjeF_C.
[Graphical view]
PfamPF01256. Carb_kinase. 1 hit.
[Graphical view]
SUPFAMSSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00196. yjeF_cterm. 1 hit.
PROSITEPS51383. YJEF_C_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCARKD. mouse.
NextBio328919.
PROQ9CZ42.
SOURCESearch...

Entry information

Entry nameNNRD_MOUSE
AccessionPrimary (citable) accession number: Q9CZ42
Secondary accession number(s): Q9CQX9, Q9D7G7, Q9DC93
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot