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Q9CZ42

- NNRD_MOUSE

UniProt

Q9CZ42 - NNRD_MOUSE

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Protein

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

Gene

Carkd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Kineticsi

  1. KM=2.8 µM for (S)-NADHX1 Publication
  2. KM=2.5 µM for (S)-NADPHX1 Publication
  3. KM=1.8 µM for ATP1 Publication

Vmax=0.43 µmol/min/mg enzyme toward (S)-NADHX1 Publication

Vmax=1.6 µmol/min/mg enzyme toward (S)-NADPHX1 Publication

Vmax=0.26 µmol/min/mg enzyme toward ATP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491NAD(P)HX; via amide nitrogenUniRule annotation
Binding sitei271 – 2711NAD(P)HXUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi242 – 2465ATPUniRule annotation
Nucleotide bindingi261 – 27010ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent NAD(P)H-hydrate dehydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nicotinamide nucleotide metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

ATP-binding, NAD, NADP, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent (S)-NAD(P)H-hydrate dehydrataseUniRule annotation (EC:4.2.1.93UniRule annotation)
Alternative name(s):
ATP-dependent NAD(P)HX dehydrataseUniRule annotation
Carbohydrate kinase domain-containing proteinUniRule annotation
Gene namesi
Name:Carkd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1913353. Carkd.

Subcellular locationi

Mitochondrion 1 PublicationUniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionUniRule annotationAdd
BLAST
Chaini43 – 343301ATP-dependent (S)-NAD(P)H-hydrate dehydratasePRO_0000337022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-acetyllysine1 Publication
Modified residuei81 – 811Phosphotyrosine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CZ42.
PaxDbiQ9CZ42.
PRIDEiQ9CZ42.

PTM databases

PhosphoSiteiQ9CZ42.

Expressioni

Gene expression databases

BgeeiQ9CZ42.
ExpressionAtlasiQ9CZ42. baseline.
GenevestigatoriQ9CZ42.

Interactioni

Protein-protein interaction databases

IntActiQ9CZ42. 3 interactions.
MINTiMINT-4126105.

Structurei

3D structure databases

ProteinModelPortaliQ9CZ42.
SMRiQ9CZ42. Positions 52-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 340292YjeF C-terminalUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni202 – 2087NAD(P)HXUniRule annotation

Sequence similaritiesi

Belongs to the NnrD/CARKD family.UniRule annotation
Contains 1 YjeF C-terminal domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0063.
HOGENOMiHOG000163126.
HOVERGENiHBG057182.
InParanoidiQ9CZ42.
KOiK17757.
PhylomeDBiQ9CZ42.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01965. NADHX_dehydratase.
InterProiIPR029056. Ribokinase-like.
IPR000631. YjeF_C.
[Graphical view]
PfamiPF01256. Carb_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00196. yjeF_cterm. 1 hit.
PROSITEiPS51383. YJEF_C_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CZ42-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAVHACGAAA AVVALLSAAI ALQWSPLYAV LQRALSLHTA HATKDMENLF
60 70 80 90 100
QLVRNIVPAL TSKKHKGQDG RIGIVGGCQE YTGAPYFAGI SALKVGADLT
110 120 130 140 150
HVFCAREAAP VIKSYSPELI VHPVLDSSNA VEEVEKWLPR LHALVVGPGL
160 170 180 190 200
GRDDLLLNNV RGILESTKAR DIPVVIDADG LWLVAQQPAL IHSYHKAILT
210 220 230 240 250
PNHVEFSRLW EAVLSSPMDS NDLKGSTLKL SQALGNITVV QKGEQDLISN
260 270 280 290 300
GQQVLVCNQE GSSRRCGGQG DLLSGSLGVM VHWALRAGPE KTNGSSPLLV
310 320 330 340
AAWGACTLTR ECNRQAFQKY GRSTTTTDMI TEVGTAFSRL FTT
Length:343
Mass (Da):36,717
Last modified:June 1, 2001 - v1
Checksum:iD0202FE6716F80D5
GO
Isoform 2 (identifier: Q9CZ42-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Show »
Length:298
Mass (Da):32,152
Checksum:i45454F0628FFD33D
GO
Isoform 3 (identifier: Q9CZ42-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:327
Mass (Da):35,217
Checksum:i871CFDE6941678A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031H → N in BAB22531. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform 2. 2 PublicationsVSP_033831Add
BLAST
Alternative sequencei1 – 2929MAVHA…SPLYA → MGFRCVAIRACGG in isoform 3. 1 PublicationVSP_033832Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS57604.1. [Q9CZ42-3]
RefSeqiNP_001177286.1. NM_001190357.1.
NP_081271.2. NM_026995.4.
UniGeneiMm.64911.

Genome annotation databases

GeneIDi69225.
KEGGimmu:69225.
UCSCiuc009kvf.2. mouse. [Q9CZ42-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS57604.1. [Q9CZ42-3 ]
RefSeqi NP_001177286.1. NM_001190357.1.
NP_081271.2. NM_026995.4.
UniGenei Mm.64911.

3D structure databases

ProteinModelPortali Q9CZ42.
SMRi Q9CZ42. Positions 52-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9CZ42. 3 interactions.
MINTi MINT-4126105.

PTM databases

PhosphoSitei Q9CZ42.

Proteomic databases

MaxQBi Q9CZ42.
PaxDbi Q9CZ42.
PRIDEi Q9CZ42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 69225.
KEGGi mmu:69225.
UCSCi uc009kvf.2. mouse. [Q9CZ42-1 ]

Organism-specific databases

CTDi 55739.
MGIi MGI:1913353. Carkd.

Phylogenomic databases

eggNOGi COG0063.
HOGENOMi HOG000163126.
HOVERGENi HBG057182.
InParanoidi Q9CZ42.
KOi K17757.
PhylomeDBi Q9CZ42.

Miscellaneous databases

ChiTaRSi Carkd. mouse.
NextBioi 328919.
PROi Q9CZ42.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZ42.
ExpressionAtlasi Q9CZ42. baseline.
Genevestigatori Q9CZ42.

Family and domain databases

Gene3Di 3.40.1190.20. 1 hit.
HAMAPi MF_01965. NADHX_dehydratase.
InterProi IPR029056. Ribokinase-like.
IPR000631. YjeF_C.
[Graphical view ]
Pfami PF01256. Carb_kinase. 1 hit.
[Graphical view ]
SUPFAMi SSF53613. SSF53613. 1 hit.
TIGRFAMsi TIGR00196. yjeF_cterm. 1 hit.
PROSITEi PS51383. YJEF_C_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  4. 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.

Entry informationi

Entry nameiNNRD_MOUSE
AccessioniPrimary (citable) accession number: Q9CZ42
Secondary accession number(s): Q9CQX9, Q9D7G7, Q9DC93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3