Q57679 (NTPA_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-canonical purine NTP pyrophosphatase
EC=3.6.1.19

Alternative name(s):
Non-standard purine NTP pyrophosphatase
Nucleoside-triphosphate diphosphatase
Nucleoside-triphosphate pyrophosphatase
Short name=NTPase

Gene names

Ordered Locus Names:

MJ0226

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective monophosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. Ref.2
Catalytic activity	A nucleoside triphosphate + H2O = a nucleotide + diphosphate. Ref.2
Cofactor	Binds 1 divalent cation ion per subunit; can use either magnesium or manganese. Ref.2
Subunit structure	Homodimer. Ref.2
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. XDP or GDP are not hydrolyzed to XMP or GMP, suggesting that Mj0226 is a pyrophosphate-releasing NTPase. HAMAP-Rule MF_01405
Sequence similarities	Belongs to the HAM1 NTPase family.
Biophysicochemical properties	Kinetic parameters: KM=0.10 mM for XTP Ref.2 KM=0.15 mM for ITP KM=1.11 mM for GTP KM=1.13 mM for dGTP Temperature dependence: Optimum temperature is 80 degrees Celsius.
Sequence caution	The sequence AAB98211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleoside triphosphate catabolic process Inferred from electronic annotation. Source: InterPro purine nucleotide metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro nucleoside-triphosphate diphosphatase activity Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 185

185

Non-canonical purine NTP pyrophosphatase HAMAP-Rule MF_01405

PRO_0000178274

Regions

Region

7 – 12

6

Substrate binding By similarity

Region

65 – 66

2

Substrate binding By similarity

Sites

Metal binding

37

1

Manganese or magnesium By similarity

Metal binding

65

1

Manganese or magnesium By similarity

Binding site

144

1

Substrate By similarity

Binding site

164

1

Substrate By similarity

Binding site

170

1

Substrate By similarity

Secondary structure

1

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185

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Helix

10 – 19

10

Turn

20 – 22

3

Beta strand

28 – 31

4

Beta strand

38 – 40

3

Helix

42 – 57

16

Beta strand

61 – 70

10

Helix

71 – 73

3

Helix

81 – 87

7

Helix

89 – 97

9

Beta strand

104 – 115

12

Beta strand

118 – 130

13

Helix

142 – 145

4

Beta strand

146 – 149

4

Helix

156 – 158

3

Helix

161 – 164

4

Turn

165 – 167

3

Helix

169 – 182

14

Sequences

	Sequence		Length	Mass (Da)
	Q57679 [UniParc]. Last modified June 28, 2011. Version 2. Checksum: 97EC2DA5C0D21D67	FASTA	185	21,273
	10 20 30 40 50 60 MKIYFATGNP NKIKEANIIL KDLKDVEIEQ IKISYPEIQG TLEEVAEFGA KWVYNILKKP 70 80 90 100 110 120 VIVEDSGFFV EALNGFPGTY SKFVQETIGN EGILKLLEGK DNRNAYFKTV IGYCDENGVR 130 140 150 160 170 180 LFKGIVKGRV SEEIRSKGYG FAYDSIFIPE EEERTFAEMT TEEKSQISHR KKAFEEFKKF LLDRI

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB98211.1. Different initiation.

PIR

C64328.

RefSeq

NP_247195.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B78	X-ray	2.20	A/B	1-185	[»]
2MJP	X-ray	2.20	A/B	1-185	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

243232.MJ0226.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB98211; AAB98211; MJ_0226.

GeneID

1451077.

KEGG

mja:MJ_0226.

Phylogenomic databases

eggNOG

COG0127.

KO

K02428.

ProtClustDB

PRK14821.

Family and domain databases

HAMAP

MF_01405. Non_canon_purine_NTPase.

InterPro

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

PANTHER

PTHR11067. PTHR11067. 1 hit.

Pfam

PF01725. Ham1p_like. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00042. TIGR00042. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q57679.

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:	June 28, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program