NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).

Comments

FUNCTION: Catalyzes the phosphorylation of NAD to NADP. Utilizes ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus (By similarity).
CATALYTIC ACTIVITY: ATP + NAD⁺ = ADP + NADP⁺.
COFACTOR: Divalent metal ions (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the NAD kinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AP006841; BAD50710.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_101244.1; -.

3D structure databases

ModBase

Q64P72.

Enzyme and pathway databases

BioCyc

BFRA295405:BF3968-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from HAMAP).
GO:0003951;	Molecular function: NAD+ kinase activity (inferred from electronic annotation from HAMAP).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00361; -; 1.
PBIL [Tree]

InterPro

IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
IPR002504; ATP_NADK.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1.

PANTHER

PTHR20275; ATP_NADK; 1.

Pfam

PF01513; NAD_kinase; 1.
Pfam graphical view of domain structure.

ProtoNet

Q64P72.

Genome annotation databases

3085049; -.

AP006841_GR; BF3968.

bfr:BF3968; -.

fig|295405.3.peg.4021; -.

Phylogenomic databases

HOGENOM

Q64P72; -.

Genome annotation databases

CMR

Q64P72; BF3968.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Kinase; NAD; NADP; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 290`	`290`		`Probable inorganic polyphosphate/ATP-NAD kinase.`	`PRO_0000229608`

Sequence information

Length: 290 AA [This is the length of the unprocessed precursor]

Molecular weight: 32355 Da [This is the MW of the unprocessed precursor]

CRC64: C3448F310C87837C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFAIFGNTY QAKKSSHAAT LFKLLEKHGA EICVCREFHR FLKSDLKLNV KADDLFDENN 

        70         80         90        100        110        120 
FDADMVISIG GDGTFLKAAR RVGNKGIPIL GINTGRLGFL ADVSPEEMEE TIEEVYQNHY 

       130        140        150        160        170        180 
TVEERSVLQL LCDDKHLQNS PYALNEIAIL KRDSSSMISI RTAINGAHLT TYQADGLIIA 

       190        200        210        220        230        240 
TPTGSTAYSL SVGGPIIVPH SKTIAITPVA PHSLNVRPIV ICDDWEITLD VESRSHNFLV 

       250        260        270        280        290 
AIDGSSETCK ETTRLTIRRA DYSIKVVKRF YHIFFDTLRT KMMWGADSRV

Q64P72 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools