Reviewed, UniProtKB/Swiss-Prot Q57679 (NTPA_METJA)

Names and origin

Protein names

Recommended name:
    Nucleoside-triphosphatase
    EC=3.6.1.15
Alternative name(s):
    Nucleoside triphosphate phosphohydrolase
      Short name=NTPase

Gene names

Ordered Locus Names:

MJ0226

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes non-standard nucleotides such as XTP and ITP to nucleotide monophosphate and pyrophosphate. Probably excludes non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions. HAMAP MF_01405
Catalytic activity	NTP + H2O = NDP + phosphate. Ref.2
Cofactor	Magnesium or manganese. Ref.2
Subunit structure	Homodimer. HAMAP MF_01405
Miscellaneous	XTP is the best substrate, followed by ITP, GTP or dGTP, both of which are hydrolyzed 100-fold less efficiently than XTP, and finally ATP, CTP and TTP which are hydrolyzed the least well. HAMAP MF_01405
Sequence similarities	Belongs to the HAM1 NTPase family.
Biophysicochemical properties	Kinetic parameters: KM=0.10 mM for XTP HAMAP MF_01405 KM=0.15 mM for ITP KM=1.11 mM for GTP Temperature dependence: Optimum temperature is 80 degrees Celsius.

Ontologies

Keywords
Ligand	Magnesium Manganese
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity 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 – 193

193

Nucleoside-triphosphatase HAMAP MF_01405

PRO_0000178274

Secondary structure

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193

Helix Strand Turn

Details...

Beta strand

11 – 14

4

Helix

18 – 27

10

Turn

28 – 30

3

Beta strand

36 – 39

4

Beta strand

46 – 48

3

Helix

50 – 65

16

Beta strand

69 – 78

10

Helix

79 – 81

3

Helix

89 – 95

7

Helix

97 – 105

9

Beta strand

112 – 123

12

Beta strand

126 – 138

13

Helix

150 – 153

4

Beta strand

154 – 157

4

Helix

164 – 166

3

Helix

169 – 172

4

Turn

173 – 175

3

Helix

177 – 190

14

Sequences

	Sequence		Length	Mass (Da)
	Q57679-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3570565E007D3DAC	FASTA	193	22,202
	10 20 30 40 50 60 MQRTLGEIMK IYFATGNPNK IKEANIILKD LKDVEIEQIK ISYPEIQGTL EEVAEFGAKW 70 80 90 100 110 120 VYNILKKPVI VEDSGFFVEA LNGFPGTYSK FVQETIGNEG ILKLLEGKDN RNAYFKTVIG 130 140 150 160 170 180 YCDENGVRLF KGIVKGRVSE EIRSKGYGFA YDSIFIPEEE ERTFAEMTTE EKSQISHRKK 190 AFEEFKKFLL DRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Structure-based identification of a novel NTPase from Methanococcus jannaschii." Hwang K.Y., Chung J.H., Kim S.-H., Han Y.S., Cho Y. Nat. Struct. Biol. 6:691-696(1999) [PubMed: 10404228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB98211.1.

PIR

C64328.

RefSeq

NP_247195.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B78	X-ray	2.20	A/B	1-193	[»]
2MJP	X-ray	2.20	A/B	1-193	[»]

ModBase

Search...

Genome annotation databases

GeneID

1451077.

GenomeReviews

Gene locus MJ0226 in contig L77117_GR.

KEGG

mja:MJ0226.

NMPDR

fig|243232.1.peg.232.

TIGR

MJ0226.

Phylogenomic databases

HOGENOM

HBG697237.

OMA

FAYDSIF.

Enzyme and pathway databases

BRENDA

3.6.1.15. 256362.

Family and domain databases

HAMAP

MF_01405. Nucleoside_triphosp. Divergent sequence.
[Tree]

InterPro

IPR002637. Ham1p-like.
IPR020922. Nucleoside-triphosphatase.
[Graphical view]

PANTHER

PTHR11067. Ham1p_like. 1 hit.

Pfam

PF01725. Ham1p_like. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00042. Ham1p_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

NTPA_METJA

Accession

Primary (citable) accession number: Q57679

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)