Q9CZ42 (NNRD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	ATP-binding NAD NADP Nucleotide-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nicotinamide nucleotide metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	mitochondrion Inferred from direct assay Ref.4. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent NAD(P)H-hydrate dehydratase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion Potential
	Chain	43 – 343	301	ATP-dependent (S)-NAD(P)H-hydrate dehydratase HAMAP-Rule MF_03157		PRO_0000337022
Regions
	Domain	49 – 340	292	YjeF C-terminal
	Nucleotide binding	242 – 246	5	ATP By similarity
	Nucleotide binding	261 – 270	10	ATP By similarity
	Region	202 – 208	7	NAD(P)HX By similarity
Sites
	Binding site	149	1	NAD(P)HX; via amide nitrogen By similarity
	Binding site	271	1	NAD(P)HX By similarity
Amino acid modifications
	Modified residue	81	1	Phosphotyrosine Ref.3 Ref.5
Natural variations
	Alternative sequence	1 – 45	45	Missing in isoform 2.		VSP_033831
	Alternative sequence	1 – 29	29	MAVHA…SPLYA → MGFRCVAIRACGG in isoform 3.		VSP_033832
Experimental info
	Sequence conflict	203	1	H → N in BAB22531. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D0202FE6716F80D5	FASTA	343	36,717
	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
	Isoform 2 [UniParc]. Checksum: 45454F0628FFD33D	FASTA	298	32,152
	10 20 30 40 50 60 MENLFQLVRN IVPALTSKKH KGQDGRIGIV GGCQEYTGAP YFAGISALKV GADLTHVFCA 70 80 90 100 110 120 REAAPVIKSY SPELIVHPVL DSSNAVEEVE KWLPRLHALV VGPGLGRDDL LLNNVRGILE 130 140 150 160 170 180 STKARDIPVV IDADGLWLVA QQPALIHSYH KAILTPNHVE FSRLWEAVLS SPMDSNDLKG 190 200 210 220 230 240 STLKLSQALG NITVVQKGEQ DLISNGQQVL VCNQEGSSRR CGGQGDLLSG SLGVMVHWAL 250 260 270 280 290 RAGPEKTNGS SPLLVAAWGA CTLTRECNRQ AFQKYGRSTT TTDMITEVGT AFSRLFTT
	Isoform 3 [UniParc]. Checksum: 871CFDE6941678A4	FASTA	327	35,217
	10 20 30 40 50 60 MGFRCVAIRA CGGVLQRALS LHTAHATKDM ENLFQLVRNI VPALTSKKHK GQDGRIGIVG 70 80 90 100 110 120 GCQEYTGAPY FAGISALKVG ADLTHVFCAR EAAPVIKSYS PELIVHPVLD SSNAVEEVEK 130 140 150 160 170 180 WLPRLHALVV GPGLGRDDLL LNNVRGILES TKARDIPVVI DADGLWLVAQ QPALIHSYHK 190 200 210 220 230 240 AILTPNHVEF SRLWEAVLSS PMDSNDLKGS TLKLSQALGN ITVVQKGEQD LISNGQQVLV 250 260 270 280 290 300 CNQEGSSRRC GGQGDLLSGS LGVMVHWALR AGPEKTNGSS PLLVAAWGAC TLTRECNRQA 310 320 FQKYGRSTTT TDMITEVGTA FSRLFTT

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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: IDENTIFICATION BY MASS SPECTROMETRY, 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, MASS SPECTROMETRY. 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.
+	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.
IPI	IPI00112032. IPI00894581. IPI00895023.
RefSeq	NP_001177286.1. NM_001190357.1. NP_081271.2. NM_026995.4.
UniGene	Mm.64911.
3D structure databases
ProteinModelPortal	Q9CZ42.
SMR	Q9CZ42. Positions 52-275.
ModBase	Search...
PTM databases
PhosphoSite	Q9CZ42.
Proteomic databases
PaxDb	Q9CZ42.
PRIDE	Q9CZ42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	69225.
KEGG	mmu:69225.
UCSC	uc009kvf.2. mouse.
Organism-specific databases
CTD	55739.
MGI	MGI:1913353. Carkd.
Phylogenomic databases
eggNOG	COG0063.
HOGENOM	HOG000163126.
HOVERGEN	HBG057182.
InParanoid	Q9CZ42.
OrthoDB	EOG49CQ85.
Gene expression databases
Bgee	Q9CZ42.
Genevestigator	Q9CZ42.
Family and domain databases
HAMAP	MF_01965. NADHX_dehydratase.
InterPro	IPR026599. NnrD/CARKD. IPR000631. YjeF_C_carb_kinase-rel. [Graphical view]
Pfam	PF01256. Carb_kinase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00196. yjeF_cterm. 1 hit.
PROSITE	PS01049. YJEF_C_1. False negative. PS01050. YJEF_C_2. False negative. PS51383. YJEF_C_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CARKD. mouse.
NextBio	328919.
SOURCE	Search...

Entry information

Entry name

NNRD_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program