(data stored in ACNUC9435 zone)

SWISSPROT: NADK1_LISIN

ID   NADK1_LISIN             Reviewed;         264 AA.
AC   Q92D53;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=NAD kinase 1 {ECO:0000255|HAMAP-Rule:MF_00361};
DE            EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE   AltName: Full=ATP-dependent NAD kinase 1 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=lin0967;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC       NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC       Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC       adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
DR   EMBL; AL596167; CAC96198.1; -; Genomic_DNA.
DR   PIR; AF1553; AF1553.
DR   RefSeq; WP_003766243.1; NC_003212.1.
DR   SMR; Q92D53; -.
DR   STRING; 272626.lin0967; -.
DR   EnsemblBacteria; CAC96198; CAC96198; CAC96198.
DR   KEGG; lin:lin0967; -.
DR   eggNOG; ENOG4105F91; Bacteria.
DR   eggNOG; COG0061; LUCA.
DR   HOGENOM; HOG000275803; -.
DR   KO; K00858; -.
DR   OMA; NGIERMS; -.
DR   OrthoDB; 1463423at2; -.
DR   BioCyc; GCF_000195795:LIN_RS04940-MONOMER; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.200.30; -; 1.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   HAMAP; MF_00361; NAD_kinase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q92D53.
DR   SWISS-2DPAGE; Q92D53.
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase.
FT   CHAIN           1..264
FT                   /note="NAD kinase 1"
FT                   /id="PRO_0000120628"
FT   NP_BIND         45..46
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   NP_BIND         122..123
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   NP_BIND         161..166
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         148
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         150
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         185
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   264 AA;  29975 MW;  0257FCE110222AE6 CRC64;
     MKYMITSKGD EKSDLLRLNM IAGFGEYDME YDEIEPEIVI SIGGDGTFLS AFHQYEERLD
     EIAFIGIHTG HLGFYADWRP AEADKLVKLL AKGEYQKVSY PLLKTTVKYG IGKKEAEYLA
     LNESTVKSSG GPFVVDVVIN DLHFERFRGD GLCMSTPSGT TAYNKSLGGA LMHPSIEAMQ
     LTEMASINNR VYRTIGSPLV FPKHHVVSLQ PVNDKDFQIS VDHLSILHRD VQEIRYEVSA
     KKVHFARFRS FPFWRRVHDS FIED
//

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