Q8NPA9 (DUT_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Short name=dUTPase
EC=3.6.1.23

Alternative name(s):
dUTP pyrophosphatase

Gene names

Name:	dut
Ordered Locus Names:	Cgl1905, cg2086

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA By similarity. HAMAP-Rule MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116
Sequence similarities	Belongs to the dUTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 149	149	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116		PRO_0000182855
Regions
	Region	66 – 68	3	Substrate binding By similarity
	Region	83 – 85	3	Substrate binding By similarity
Sites
	Binding site	79	1	Substrate By similarity
	Binding site	93	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NPA9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 05161933246D443D	FASTA	149	15,863
	10 20 30 40 50 60 MTDLAAIKIV RLDKELPLPK RAHRGDAGVD LHATTDAVIA PGHREIVGTG IAIALPLGTV 70 80 90 100 110 120 GLVHPRSGLA AREGLSIVNA PGTIDADYRG EIKVCLINLD PEKPIMITRG DRIAQLVIQK 130 140 VELVDFEEVE ELDDTVRGDQ GYGSTGKTA

References

[1]

"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB99298.1. BX927153 Genomic DNA. Translation: CAF20245.1.
RefSeq	NP_601111.1. NC_003450.3. YP_226146.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NPA9.
SMR	Q8NPA9. Positions 7-141.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg2086.
2D gel databases
World-2DPAGE	0001:Q8NPA9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB99298; BAB99298; BAB99298. CAF20245; CAF20245; cg2086.
GeneID	1019862. 3344413.
KEGG	cgb:cg2086. cgl:NCgl1830.
PATRIC	21495812. VBICorGlu203724_1842.
Phylogenomic databases
eggNOG	COG0756.
HOGENOM	HOG000028966.
KO	K01520.
OMA	KVCLINH.
ProtClustDB	PRK00601.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-1882-MONOMER.
UniPathway	UPA00610; UER00666.
Family and domain databases
HAMAP	MF_00116. dUTPase_bact.
InterPro	IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view]
PANTHER	PTHR11241. PTHR11241. 1 hit.
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00576. dut. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DUT_CORGL

Accession

Primary (citable) accession number: Q8NPA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program