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Q9CZ42

- NNRD_MOUSE

UniProt

Q9CZ42 - NNRD_MOUSE

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    Magnesium.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

    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

    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.
    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

    MAVHACGAAA AVVALLSAAI ALQWSPLYAV LQRALSLHTA HATKDMENLF    50
    QLVRNIVPAL TSKKHKGQDG RIGIVGGCQE YTGAPYFAGI SALKVGADLT 100
    HVFCAREAAP VIKSYSPELI VHPVLDSSNA VEEVEKWLPR LHALVVGPGL 150
    GRDDLLLNNV RGILESTKAR DIPVVIDADG LWLVAQQPAL IHSYHKAILT 200
    PNHVEFSRLW EAVLSSPMDS NDLKGSTLKL SQALGNITVV QKGEQDLISN 250
    GQQVLVCNQE GSSRRCGGQG DLLSGSLGVM VHWALRAGPE KTNGSSPLLV 300
    AAWGACTLTR ECNRQAFQKY GRSTTTTDMI TEVGTAFSRL FTT 343
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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

    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: October 1, 2014
    This is version 98 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