P65770 (NADK2_LISMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD kinase 2
EC=2.7.1.23

Alternative name(s):
ATP-dependent NAD kinase 2

Gene names

Name:	nadK2
Ordered Locus Names:	lmo1586

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP By similarity. HAMAP-Rule MF_00361
Catalytic activity	ATP + NAD+ = ADP + NADP+. HAMAP-Rule MF_00361
Cofactor	Divalent metal ions By similarity. HAMAP-Rule MF_00361
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00361.
Sequence similarities	Belongs to the NAD kinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding NAD NADP Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD metabolic process Inferred from electronic annotation. Source: InterPro NADP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ kinase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 267	267	NAD kinase 2 HAMAP-Rule MF_00361		PRO_0000120633
Regions
	Nucleotide binding	50 – 51	2	NAD By similarity
	Nucleotide binding	122 – 123	2	NAD By similarity
	Nucleotide binding	162 – 167	6	NAD By similarity
Sites
	Active site	50	1	Proton acceptor By similarity
	Binding site	55	1	NAD By similarity
	Binding site	149	1	NAD By similarity
	Binding site	151	1	NAD By similarity
	Binding site	186	1	NAD; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P65770 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 69512B6100D49F73	FASTA	267	30,499
	10 20 30 40 50 60 MAKTIFYFSY RKTEELHAKA KELKKITTDY GYELTDDYQK ANVIISIGGD GAFLKSVRET 70 80 90 100 110 120 GFRQDCLYAG IALTEQLGQY CDFHINQLDE IIKAAIEDRW LVRRYPTIYG TVNNTKAFYV 130 140 150 160 170 180 LNEFNIRSSI IRTLTMDLYI NDSHFETFRG DGMVISTPTG STAYNKSVNG SIVDPLLPSM 190 200 210 220 230 240 QVSELASINN NKFRTLGSSF ILSPKRKLRI EIASEEGNNE FPMIGMDSEA LSIQHVHEVN 250 260 LEVGDRFINI IKLPKNSFWD KVKRNFL

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591979 Genomic DNA. Translation: CAC99664.1.
PIR	AB1273.
RefSeq	NP_465111.1. NC_003210.1.
3D structure databases
ProteinModelPortal	P65770.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	169963.lmo1586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC99664; CAC99664; CAC99664.
GeneID	987765.
KEGG	lmo:lmo1586.
PATRIC	20312303. VBILisMon69206_1628.
Organism-specific databases
GenoList	LMO1586.
Phylogenomic databases
eggNOG	COG0061.
HOGENOM	HOG000275803.
KO	K00858.
OMA	DDLHFET.
OrthoDB	EOG6PZXDR.
PhylomeDB	P65770.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1586-MONOMER.
Family and domain databases
Gene3D	2.60.200.30. 1 hit. 3.40.50.10330. 1 hit.
HAMAP	MF_00361. NAD_kinase.
InterPro	IPR017438. ATP-NAD_kinase_dom_1. IPR016064. ATP-NAD_kinase_PpnK-typ. IPR017437. ATP-NAD_kinase_PpnK-typ_all-b. IPR002504. PolyP/ATP_NADK. [Graphical view]
PANTHER	PTHR20275. PTHR20275. 1 hit.
Pfam	PF01513. NAD_kinase. 1 hit. [Graphical view]
SUPFAM	SSF111331. SSF111331. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADK2_LISMO

Accession

Primary (citable) accession number: P65770
Secondary accession number(s): Q92BC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program