ID K1E598_9MICO Unreviewed; 304 AA.
AC K1E598;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
DE EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361};
DE AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
GN Name=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=B277_11490 {ECO:0000313|EMBL:EKA60597.1}, CWN80_14195
GN {ECO:0000313|EMBL:RWU81487.1};
OS Janibacter hoylei PVAS-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA60597.1, ECO:0000313|Proteomes:UP000004474};
RN [1] {ECO:0000313|EMBL:RWU81487.1, ECO:0000313|Proteomes:UP000288711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU81487.1,
RC ECO:0000313|Proteomes:UP000288711};
RX PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT the upper atmosphere.";
RL Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN [2] {ECO:0000313|EMBL:EKA60597.1, ECO:0000313|Proteomes:UP000004474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA60597.1,
RC ECO:0000313|Proteomes:UP000004474};
RX PubMed=23144385; DOI=10.1128/JB.01728-12;
RA Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA Shouche Y.S.;
RT "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT Stratospheric Air.";
RL J. Bacteriol. 194:6629-6630(2012).
RN [3] {ECO:0000313|EMBL:RWU81487.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU81487.1};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001262, ECO:0000256|HAMAP-
CC Rule:MF_00361};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00361};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00361}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKA60597.1}.
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DR EMBL; ALWX01000051; EKA60597.1; -; Genomic_DNA.
DR EMBL; PIPF01000014; RWU81487.1; -; Genomic_DNA.
DR RefSeq; WP_007928220.1; NZ_PIPF01000014.1.
DR AlphaFoldDB; K1E598; -.
DR STRING; 1210046.B277_11490; -.
DR PATRIC; fig|1210046.3.peg.2206; -.
DR eggNOG; COG0061; Bacteria.
DR OrthoDB; 9774737at2; -.
DR Proteomes; UP000004474; Unassembled WGS sequence.
DR Proteomes; UP000288711; Unassembled WGS sequence.
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; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 PANTHER; PTHR20275; NAD KINASE; 1.
DR PANTHER; PTHR20275:SF0; NAD KINASE; 1.
DR Pfam; PF01513; NAD_kinase; 1.
DR Pfam; PF20143; NAD_kinase_C; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00361};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00361};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00361};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 76..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 150..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 191..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 304 AA; 32314 MW; 3D8A5CEAB9B97868 CRC64;
MSATRRRVLL LAHPGRPEAL EVAIGVADRL TEAGIEVRLP AGELADTTLG RHPVVVVHDG
DDPAADVELV VVLGGDGTIL RGAETARSAN VPVLGVNLGH VGFLAEAERE DVEATVDHIV
ERAYDVEERM ALDVVATLDG REIARSWALN EVTVEKASRE RMLVLTVEID GRPLSTWGCD
GVVMATPTGS TAYAFSAGGP VVWPGVEAML VVPISAHALF ARPLVVAPTS DLAVDLVPGT
EGYGVLWCDG RRAVDLPPGA RIEVSRSAQP VRLARLSRSP FTDRLVAKFD LSVHGWRGRS
RQGG
//
