NADK_PSEAE
ID NADK_PSEAE Reviewed; 295 AA.
AC Q9HZC0;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PA3088;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06476.1; -; Genomic_DNA.
DR PIR; D83259; D83259.
DR RefSeq; NP_251778.1; NC_002516.2.
DR RefSeq; WP_003091343.1; NZ_QZGE01000009.1.
DR PDB; 7MH7; X-ray; 2.61 A; A=1-295.
DR PDBsum; 7MH7; -.
DR AlphaFoldDB; Q9HZC0; -.
DR SMR; Q9HZC0; -.
DR STRING; 287.DR97_4848; -.
DR PaxDb; Q9HZC0; -.
DR PRIDE; Q9HZC0; -.
DR EnsemblBacteria; AAG06476; AAG06476; PA3088.
DR GeneID; 882736; -.
DR KEGG; pae:PA3088; -.
DR PATRIC; fig|208964.12.peg.3240; -.
DR PseudoCAP; PA3088; -.
DR HOGENOM; CLU_008831_0_1_6; -.
DR InParanoid; Q9HZC0; -.
DR OMA; VNLGHVG; -.
DR PhylomeDB; Q9HZC0; -.
DR BioCyc; PAER208964:G1FZ6-3141-MON; -.
DR Proteomes; UP000002438; 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:0051287; F:NAD binding; IEA:UniProt.
DR GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IBA:GO_Central.
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..295
FT /note="NAD kinase"
FT /id="PRO_0000120646"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 72..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 146..147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 187..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7MH7"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:7MH7"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 121..134
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 137..151
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 168..181
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7MH7"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:7MH7"
FT STRAND 257..271
FT /evidence="ECO:0007829|PDB:7MH7"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:7MH7"
SQ SEQUENCE 295 AA; 32140 MW; 2567446028BAA419 CRC64;
MEPFRNIGII GRLGSTQVLD TIRRLKKFLI DRHLHVILED TIAEVLPGHG LQTCSRKIMG
EICDLVVVVG GDGSMLGAAR ALARHKVPVL GINRGSLGFL TDIRPDELEA KVGEVLDGQY
IVESRFLLDA QVRRGIDSMG QGDALNDVVL HPGKSTRMIE FELYIDGQFV CSQKADGLIV
ATPTGSTAYA LSAGGPIMHP KLDAIVIVPM YPHMLSSRPI VVDGNSELKI VVSPNMQIYP
QVSCDGQNHF TCAPGDTVTI SKKPQKLRLI HPIDHNYYEI CRTKLGWGSR LGGGD
