(data stored in ACNUC7421 zone)

SWISSPROT: NADK_SULIK

ID   NADK_SULIK              Reviewed;         249 AA.
AC   C4KJF1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 41.
DE   RecName: Full=NAD kinase {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 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361};
GN   OrderedLocusNames=M164_0035;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance
CC       of 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: ATP + NAD(+) = ADP + NADP(+).
CC       {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; CP001402; ACR40671.1; -; Genomic_DNA.
DR   RefSeq; WP_012710214.1; NC_012726.1.
DR   SMR; C4KJF1; -.
DR   EnsemblBacteria; ACR40671; ACR40671; M164_0035.
DR   GeneID; 8759874; -.
DR   KEGG; sid:M164_0035; -.
DR   HOGENOM; HOG000270621; -.
DR   KO; K00858; -.
DR   OMA; VNLGHVG; -.
DR   OrthoDB; POG093Z0ENK; -.
DR   BioCyc; SISL426118:GI01-35-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
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_dom_1.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase.
DR   InterPro; IPR002504; NADK.
DR   PANTHER; PTHR20275; PTHR20275; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJF1.
DR   SWISS-2DPAGE; C4KJF1.
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    249       NAD kinase.
FT                                /FTId=PRO_1000205426.
FT   NP_BIND      45     46       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   NP_BIND     110    111       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   NP_BIND     149    154       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   ACT_SITE     45     45       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00361}.
FT   BINDING      50     50       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   BINDING     138    138       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
SQ   SEQUENCE   249 AA;  27978 MW;  8C86C7F578839319 CRC64;
     MRVKIVSKPT SQLNNIIEKI KNISTKLGFE VVDKDFDYVI AVGGDGTLLR AVKQNKPVIA
     VKAGRRGLLM DVPVDKFEEA LLRLKKGDYE EEEYMLLEMI YNDKVELGFN EVGILYDRPE
     AIKVGISFDT ERVSVEGDGV LVSTPQGSSG WGMSATNSLL YKDLSAIEII FVNPIFYYLR
     SVVIPPKPLT LRLEDKGYPQ TARAVVDGEV VTLIKTNQEI TVRVSQRKAK ILRFFKLDLI
     GEVLHAYHI
//

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