C3F857 (C3F857_BACTU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Probable inorganic polyphosphate/ATP-NAD kinase 2 HAMAP MF_00361
Short name=Poly(P)/ATP NAD kinase 2 HAMAP MF_00361
EC=2.7.1.23 HAMAP MF_00361

Gene names

Name:	ppnK2 HAMAP MF_00361
ORF Names:	bthur0007_44980 EMBL EEM57697.1

Organism

Bacillus thuringiensis serovar monterrey BGSC 4AJ1 EMBL EEM57697.1

Taxonomic identifier

527022 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

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

General annotation (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. HAMAP MF_00361 SAAS SAAS002504
Catalytic activity	ATP + NAD+ = ADP + NADP+. HAMAP MF_00361 SAAS SAAS002504
Cofactor	Divalent metal ions By similarity. HAMAP MF_00361 SAAS SAAS002504
Subcellular location	Cytoplasm By similarity HAMAP MF_00361 SAAS SAAS002504.
Sequence similarities	Belongs to the NAD kinase family. HAMAP MF_00361

Ontologies

Keywords
Cellular component	Cytoplasm HAMAP MF_00361 SAAS SAAS002504
Ligand	ATP-binding HAMAP MF_00361 SAAS SAAS002504 NAD HAMAP MF_00361 SAAS SAAS002504 NADP HAMAP MF_00361 SAAS SAAS002504 Nucleotide-binding
Molecular function	Kinase HAMAP MF_00361 SAAS SAAS002504 Transferase
Gene Ontology (GO)
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: HAMAP metal ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	C3F857 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: 22C017138F19C795	FASTA	267	30,365
	10 20 30 40 50 60 MADRRNLFFF YGDDKAKLVE KMKPIYRILE ENGFTILDHP KNANAIVSVG DDATFLQAVR 70 80 90 100 110 120 KTGFREDCLY AGISTKDEIS FYCDFHIDHV DTALQEITKN EIEVRKYPTI EVDVDGSTSF 130 140 150 160 170 180 HCLNEFSLRS SIIKTFVVDV HVDDLYFETF RGDGLVVSTP TGSTAYNKSL RGAVVDPLIP 190 200 210 220 230 240 CFQVSELASL NNNTYRTLGS PFILNHERTL TLKLRPDGND YPVIGMDNEA LSIKQVEKAV 250 260 VRLSDKQIKT VKLKNNSFWE KVQRTFL

References

[1]

"Annotation of the Bacillus thuringiensis BGSC 4AJ1 genome." Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E. Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BGSC 4AJ1 EMBL EEM57697.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACNE01000106 Genomic DNA. Translation: EEM57697.1.
3D structure databases
ProteinModelPortal	C3F857.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000396233; EBBACP00000393657; EBBACG00000397189.
PATRIC	28909301. VBIBacThu130558_0749.
Family and domain databases
HAMAP	MF_00361. NAD_kinase. [Tree]
InterPro	IPR016064. ATP-NAD_kinase_PpnK-typ. IPR017438. ATP-NAD_kinase_PpnK-typ_a/b. IPR017437. ATP-NAD_kinase_PpnK-typ_all-b. IPR002504. polyP/ATP_NADK_prd. [Graphical view]
Gene3D	G3DSA:2.60.200.30. ATP-NAD_kinase_PpnK-typ. 1 hit. G3DSA:3.40.50.10330. ATP-NAD_kinase_PpnK-typ_a/b. 1 hit.
PANTHER	PTHR20275. ATP_NADK. 1 hit.
Pfam	PF01513. NAD_kinase. 1 hit. [Graphical view]
SUPFAM	SSF111331. ATP-NAD_kinase_PpnK-typ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

C3F857_BACTU

Accession

Primary (citable) accession number: C3F857

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)