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Database: UniProt
Entry: L1NK62_9NEIS
LinkDB: L1NK62_9NEIS
Original site: L1NK62_9NEIS 
ID   L1NK62_9NEIS            Unreviewed;       302 AA.
AC   L1NK62;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   03-MAY-2023, entry version 56.
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=HMPREF9120_02588 {ECO:0000313|EMBL:EKY03726.1};
OS   Neisseria sp. oral taxon 020 str. F0370.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY03726.1, ECO:0000313|Proteomes:UP000010457};
RN   [1] {ECO:0000313|EMBL:EKY03726.1, ECO:0000313|Proteomes:UP000010457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0370 {ECO:0000313|EMBL:EKY03726.1,
RC   ECO:0000313|Proteomes:UP000010457};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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:EKY03726.1}.
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DR   EMBL; AMER01000199; EKY03726.1; -; Genomic_DNA.
DR   RefSeq; WP_009427242.1; NZ_KB291153.1.
DR   AlphaFoldDB; L1NK62; -.
DR   STRING; 1127694.HMPREF9120_02588; -.
DR   PATRIC; fig|1127694.3.peg.2403; -.
DR   HOGENOM; CLU_008831_0_1_4; -.
DR   OrthoDB; 9774737at2; -.
DR   Proteomes; UP000010457; 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   Reference proteome {ECO:0000313|Proteomes:UP000010457};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00361}.
FT   ACT_SITE        78
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         78..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         152..153
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         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   302 AA;  33498 MW;  E249938AE04654EF CRC64;
     MITEFKRIGI VTRPQTPQIE ECLHDLLGFL LAEKIEVFVD CESVEGGVVR PEDLAQCRIT
     DKDNIGRECS LIIVLGGDGT FLSAARKAAP FRIPLIGVNQ GHLGFLTQVP REEMLQQIGG
     MLTGKHLPEE RILLETDLIR EGECVQQSLA LNDVVISRGG AGQMIEFETF INREFVYTQR
     SDGLIVSTPT GSTAYALAAG GPILQASLRA FTLVPICPQS MTNRPIAVSD TCEIDILITK
     AGDARAHFDG QSYTDIQSGD ILRIRRYRHS LRVLHPVGYS YYKTLRQKLH WGEQLVPISQ
     HD
//
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