P37530 (DGK_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyguanosine kinase
Short name=DGUO kinase
Short name=dGK
EC=2.7.1.113

Gene names

Name:	dgk
Synonyms:	yaaG
Ordered Locus Names:	BSU00150

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an essential role in generating the deoxyribonucleotide precursors dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP. Ref.3
Catalytic activity	ATP + deoxyguanosine = ADP + dGMP.
Enzyme regulation	Inhibited by deoxyguanosine at concentrations above 30 µM only with UTP as phosphate donor. dGTP is a potent competitive inhibitor. Ref.3
Subunit structure	Homodimer. Ref.3
Miscellaneous	Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.
Sequence similarities	Belongs to the DCK/DGK family.
Biophysicochemical properties	Kinetic parameters: KM=0.6 µM for deoxyguanosine (with UTP at pH 7.8 and at 37 degrees Celsius) Ref.3 KM=1.7 µM for deoxyguanosine (with CTP at pH 7.8 and at 37 degrees Celsius) KM=6.5 µM for deoxyguanosine (with ATP at pH 7.8 and at 37 degrees Celsius) KM=10.4 µM for deoxyguanosine (with GTP at pH 7.8 and at 37 degrees Celsius) KM=6 µM for UTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=35 µM for CTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=36 µM for ATP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=46 µM for GTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) Vmax=8.1 µmol/min/mg enzyme toward deoxyguanosine (with 0.5 mM UTP at pH 7.8 and at 37 degrees Celsius) pH dependence: Optimum pH is around pH 9 (with saturating concentrations of dGuo and UTP). At pH 7.5 and 11.5 more than 80% of maximal activity is still observed. At pH 6.0, 60% activity remains, whereas the enzyme is completely inactive below pH 5.6.
Mass spectrometry	Molecular mass is 24147 Da from positions 1 - 207. Determined by ESI. Ref.3

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW deoxyguanosine kinase activity Inferred from electronic annotation. Source: EC phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Deoxyguanosine kinase		PRO_0000049431
Regions
	Nucleotide binding	11 – 19	9	ATP By similarity
Sites
	Active site	86	1	Proton acceptor Potential
	Binding site	35	1	Substrate By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	147	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37530 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 0F77C6B31E9AA331	FASTA	207	24,145
	10 20 30 40 50 60 MNTAPFIAIE GPIGAGKTTL ATMLSQKFGF PMINEIVEDN PYLDKFYDNI KEWSFQLEMF 70 80 90 100 110 120 FLCHRYKQLE DTSDHFLKKG QPVIADYHIY KNVIFAERTL SPHQLEKYKK IYHLLTDDLP 130 140 150 160 170 180 KPNFIIYIKA SLPTLLHRIE KRGRPFEKKI ETSYLEQLIS DYEVAIKQLQ EADPELTVLT 190 200 VDGDSKDFVL NKSDFERIAA HVKELIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor." Andersen R.B., Neuhard J. J. Biol. Chem. 276:5518-5524(2001) [PubMed: 11078735] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, NOMENCLATURE, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D26185 Genomic DNA. Translation: BAA05251.1. AL009126 Genomic DNA. Translation: CAB11791.1.
PIR	S66045.
RefSeq	NP_387896.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P37530.
SMR	P37530. Positions 5-203.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003729; EBBACP00000003729; EBBACG00000003722.
GeneID	937037.
GenomeReviews	Gene locus BSU00150 in contig AL009126_GR.
KEGG	bsu:BSU00150.
NMPDR	fig|224308.1.peg.15.
PATRIC	18971491. VBIBacSub10457_0016.
Organism-specific databases
GenoList	BSU00150. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000000907.
HOGENOM	HBG725501.
OMA	FAKDRIF.
PhylomeDB	P37530.
ProtClustDB	CLSK2460881.
Enzyme and pathway databases
BioCyc	BSUB:BSU00150-MONOMER.
Family and domain databases
InterPro	IPR002624. Deoxynucleoside_kinase. [Graphical view]
KO	K15518.
PANTHER	PTHR10513. dNK. 1 hit.
Pfam	PF01712. dNK. 1 hit. [Graphical view]
PIRSF	PIRSF000705. DNK. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DGK_BACSU

Accession

Primary (citable) accession number: P37530

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program