(data stored in ACNUC7421 zone)

SWISSPROT: NADK_RHOOB

ID   NADK_RHOOB              Reviewed;         320 AA.
AC   C1ASY3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
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=ROP_06680;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH48915.1; -; Genomic_DNA.
DR   RefSeq; WP_012687918.1; NC_012522.1.
DR   SMR; C1ASY3; -.
DR   STRING; 632772.ROP_06680; -.
DR   EnsemblBacteria; BAH48915; BAH48915; ROP_06680.
DR   KEGG; rop:ROP_06680; -.
DR   PATRIC; fig|632772.20.peg.728; -.
DR   eggNOG; ENOG4105F91; Bacteria.
DR   eggNOG; COG0061; LUCA.
DR   HOGENOM; HOG000227223; -.
DR   KO; K00858; -.
DR   OMA; VNLGHVG; -.
DR   OrthoDB; POG091H02D1; -.
DR   Proteomes; UP000002212; 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; C1ASY3.
DR   SWISS-2DPAGE; C1ASY3.
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    320       NAD kinase.
FT                                /FTId=PRO_1000133578.
FT   NP_BIND      96     97       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   NP_BIND     170    171       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   NP_BIND     211    216       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00361}.
FT   BINDING     101    101       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
FT   BINDING     200    200       NAD. {ECO:0000255|HAMAP-Rule:MF_00361}.
SQ   SEQUENCE   320 AA;  34458 MW;  56EAFD812FCCEDE2 CRC64;
     MSGGSSGGQQ REREILLVAH PGRAEITETA RRVGKIFERA GIGMRVLVDE VDSTRIEPMD
     GMAADEFLVP GLEVTIVQAG PDAALGCEMV LVLGGDGTFL RAAELAQAAS IPVLGINLGR
     IGFLAETEAE HLDEALGQVV RREYRIEHRM TLDVLVRVDD EIIERGWALN EASIENRSRL
     GVLEVVLEVD GRPVSAFGCD GVLISTPTGS TAYAFSAGGP VVWPELEALL VVPSNAHALF
     ARPLVTSPES LIAVETVAGS HDGLVFCDGR RTLELPAGAR VEVVRGKEPV RWVRLDSAPF
     ADRMVRKFEL PVTGWRGRKP
//

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