NPPNK_METMP
ID NPPNK_METMP Reviewed; 566 AA.
AC Q6LX63;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bifunctional NADP phosphatase/NAD kinase;
DE Includes:
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};
DE AltName: Full=Poly(P)-dependent NAD kinase;
DE Short=PPNK;
DE Includes:
DE RecName: Full=NADP phosphatase;
DE Short=NADPase;
DE Short=pNPPase;
DE EC=3.1.3.-;
GN OrderedLocusNames=MMP1489;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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 the phosphorylation and dephosphorylation of NAD and
CC NADP, respectively. Although it shows conflicting dual activities and
CC is able to supply NADP, it seems that its physiological role is to
CC prevent excess accumulation of NADP (By similarity). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the inositol
CC monophosphatase superfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD kinase
CC family. {ECO:0000305}.
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DR EMBL; BX950229; CAF31045.1; -; Genomic_DNA.
DR RefSeq; WP_011171433.1; NC_005791.1.
DR AlphaFoldDB; Q6LX63; -.
DR SMR; Q6LX63; -.
DR STRING; 267377.MMP1489; -.
DR EnsemblBacteria; CAF31045; CAF31045; MMP1489.
DR GeneID; 2761729; -.
DR KEGG; mmp:MMP1489; -.
DR PATRIC; fig|267377.15.peg.1526; -.
DR eggNOG; arCOG01348; Archaea.
DR HOGENOM; CLU_445249_0_0_2; -.
DR OMA; VIVPICP; -.
DR OrthoDB; 23762at2157; -.
DR BioCyc; MMAR267377:MMP_RS07655-MON; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0003951; F:NAD+ kinase activity; ISS:UniProtKB.
DR GO; GO:0019178; F:NADP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0006553; P:lysine metabolic process; IEA:InterPro.
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; IPR021175; Bifunctional_PpnK_predicted.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR Pfam; PF00459; Inositol_P; 1.
DR Pfam; PF01513; NAD_kinase; 1.
DR PIRSF; PIRSF036641; Bifunctional_PpnK_predicted; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; NAD; NADP; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..566
FT /note="Bifunctional NADP phosphatase/NAD kinase"
FT /id="PRO_0000229718"
FT REGION 1..283
FT /note="NADP phosphatase"
FT REGION 275..566
FT /note="NAD kinase"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 355..356
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 360
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 430..431
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 441
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 458
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 460
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 468
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 471..476
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 528
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ SEQUENCE 566 AA; 62594 MW; 1BE5DAC1288E60B0 CRC64;
MDMLEMALNI AKDIEKSVKP LIGWEKSNEV VKIGADGTPT KRIDLIAENV AINSIEKVCS
AILISEEIGF KRIGKNKPEY VIVLDPVDGT YNSLKDIPFY SAAVAIGRID KFADNLEELI
NNLKMKDLEV GVVRNIATGD TYYAEKGKGA HFLRKGEKKS ISISNSSNLK DSSIGLFAHD
ISIDTLKFIK DRRFRRIRLF GSIALEMCYV AKGALDAFIN VNETTRLCDI AAGYVIIKEA
GGIVTDKNGQ EVNLDLDVNS KVSVICSNEM LHKKLVGIFG NRWRIKPTNF GIISRIDNEE
SIEVADNVIK YLDSKGIKYE LDSSTYNALK NRLTKKCDII SNIEEISHMI SIGGDGTVLR
ASKMIEGNEI PMVCINMGTV GFLTEFNKDE IFSAIDSIIC GSYKVEKRTK LMGFAKLSDG
KQHILNDSLN EVVITTKNPA KMMHFEVYID GSLVEDVRAD GIIVSTPNGS TAYSLSSGGP
IIEPTVEGFV IVPICPFKLS SRPLVVNANS EIKIKLLKKS TYVVIDGNTE FEAKKGDEII
LRKSESNAYF VKGDNFYNKL KKLSLM
