NADK_ARCFU
ID NADK_ARCFU Reviewed; 249 AA.
AC O30297;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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}; OrderedLocusNames=AF_2373;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH ATP AND NAD,
RP FUNCTION, AND SUBUNIT.
RX PubMed=16242716; DOI=10.1016/j.jmb.2005.09.026;
RA Liu J., Lou Y., Yokota H., Adams P.D., Kim R., Kim S.H.;
RT "Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex
RT with ATP, NAD, or NADP.";
RL J. Mol. Biol. 354:289-303(2005).
CC -!- FUNCTION: Involved in the regulation of the intracellular balance
CC between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of
CC NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC adenosine moiety of NAD to yield NADP. {ECO:0000269|PubMed:16242716}.
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16242716}.
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}.
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DR EMBL; AE000782; AAB91287.1; -; Genomic_DNA.
DR PIR; E69546; E69546.
DR RefSeq; WP_010879860.1; NC_000917.1.
DR PDB; 1SUW; X-ray; 2.45 A; A/B/C/D=1-249.
DR PDB; 1Z0S; X-ray; 1.70 A; A/B/C/D=1-249.
DR PDB; 1Z0U; X-ray; 2.00 A; A/B=1-249.
DR PDB; 1Z0Z; X-ray; 2.85 A; A/B/C/D=1-249.
DR PDBsum; 1SUW; -.
DR PDBsum; 1Z0S; -.
DR PDBsum; 1Z0U; -.
DR PDBsum; 1Z0Z; -.
DR AlphaFoldDB; O30297; -.
DR SMR; O30297; -.
DR STRING; 224325.AF_2373; -.
DR EnsemblBacteria; AAB91287; AAB91287; AF_2373.
DR GeneID; 1485603; -.
DR KEGG; afu:AF_2373; -.
DR eggNOG; arCOG01348; Archaea.
DR HOGENOM; CLU_008831_0_3_2; -.
DR OMA; VAPYTLY; -.
DR OrthoDB; 104144at2157; -.
DR PhylomeDB; O30297; -.
DR BRENDA; 2.7.1.23; 414.
DR EvolutionaryTrace; O30297; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..249
FT /note="NAD kinase"
FT /id="PRO_0000120697"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 49..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 115..116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:16242716"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 156..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:16242716"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:16242716"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1Z0S"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1Z0U"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 108..123
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 137..152
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:1Z0S"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 212..224
FT /evidence="ECO:0007829|PDB:1Z0S"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1Z0S"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1Z0S"
SQ SEQUENCE 249 AA; 27868 MW; E07E3163BD14FC7B CRC64;
MRAAVVYKTD GHVKRIEEAL KRLEVEVELF NQPSEELENF DFIVSVGGDG TILRILQKLK
RCPPIFGINT GRVGLLTHAS PENFEVELKK AVEKFEVERF PRVSCSAMPD VLALNEIAVL
SRKPAKMIDV ALRVDGVEVD RIRCDGFIVA TQIGSTGYAF SAGGPVVEPY LECFILIPIA
PFRFGWKPYV VSMERKIEVI AEKAIVVADG QKSVDFDGEI TIEKSEFPAV FFKNEKRFRN
LFGKVRSIG
