ID   A0A2N0UTD6_9FIRM        Unreviewed;       285 AA.
AC   A0A2N0UTD6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   11-DEC-2019, entry version 8.
DE   RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS01084339};
DE            EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS01084342};
DE   AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
GN   Name=ppnK {ECO:0000313|EMBL:PKD30272.1};
GN   Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN   ORFNames=DW802_06625 {ECO:0000313|EMBL:RHD25156.1}, DW960_07090
GN   {ECO:0000313|EMBL:RGZ96551.1}, RB5AMG_00677
GN   {ECO:0000313|EMBL:PKD30272.1};
OS   Ruminococcus bromii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD30272.1, ECO:0000313|Proteomes:UP000233562};
RN   [1] {ECO:0000313|EMBL:PKD30272.1, ECO:0000313|Proteomes:UP000233562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AMG {ECO:0000313|EMBL:PKD30272.1,
RC   ECO:0000313|Proteomes:UP000233562};
RX   PubMed=29159997;
RA   Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., Walker A.W.,
RA   Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., Louis P., Koropatkin N.,
RA   Cockburn D., Kibler R., Cooper P.J., Sandoval C., Crost E., Juge N.,
RA   Bayer E.A., Flint H.J.;
RT   "Sporulation capability and amylosome conservation among diverse human
RT   colonic and rumen isolates of the keystone starch-degrader Ruminococcus
RT   bromii.";
RL   Environ. Microbiol. 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:RGZ96551.1, ECO:0000313|Proteomes:UP000284544, ECO:0000313|Proteomes:UP000285083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM32-13AC {ECO:0000313|EMBL:RHD25156.1,
RC   ECO:0000313|Proteomes:UP000284544}, and AM46-2BH
RC   {ECO:0000313|EMBL:RGZ96551.1, ECO:0000313|Proteomes:UP000285083};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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, ECO:0000256|SAAS:SAAS01092643}.
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|HAMAP-Rule:MF_00361,
CC         ECO:0000256|SAAS:SAAS01120179};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00361,
CC         ECO:0000256|SAAS:SAAS01092646};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361,
CC       ECO:0000256|SAAS:SAAS01092648}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00361, ECO:0000256|SAAS:SAAS01084379}.
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:PKD30272.1}.
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DR   EMBL; NNBY01000031; PKD30272.1; -; Genomic_DNA.
DR   EMBL; QSEV01000005; RGZ96551.1; -; Genomic_DNA.
DR   EMBL; QSIY01000001; RHD25156.1; -; Genomic_DNA.
DR   Proteomes; UP000233562; Unassembled WGS sequence.
DR   Proteomes; UP000284544; Unassembled WGS sequence.
DR   Proteomes; UP000285083; 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: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   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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361,
KW   ECO:0000256|SAAS:SAAS01084347};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS01092644};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00103427,
KW   ECO:0000313|EMBL:PKD30272.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00103431};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00103470};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361,
KW   ECO:0000256|SAAS:SAAS01084333};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00361,
KW   ECO:0000256|SAAS:SAAS00103430, ECO:0000313|EMBL:PKD30272.1}.
FT   NP_BIND         69..70
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   NP_BIND         141..142
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   NP_BIND         182..187
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         74
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         152
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         169
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         171
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   285 AA;  31754 MW;  B1156BD2D40B3ADA CRC64;
     MKFALVVNLS KERAIKYAKK ISLFLLDKNA EIAMIEECSQ YFKGIHIHYS KNITELFEYC
     DMAITVGGDG TIIHAAKYAA KADKQLIGVN VGRLGFAADV EPHEYEQLER LITGDYTTEE
     RILLDVEVIK EDGSKHYLAV NDAVVARGQL SKTIDLHLTL DGDEISKYRA DGLLFATPTG
     STAYSLSAGG PILAPKMECI LMTPVCPHSL FSRSVLFSGE SELSVHVKIP EECCCVLTID
     GEKNVPVLAT DRVVIRKSDL KLKLALLHNR NFYKLLNEKL KERDF
//