UniProtKB - Q75UV1 (NDX1_THETH)
Protein
Diadenosine hexaphosphate hydrolase
Gene
ndx1
Organism
Thermus thermophilus
Status
Functioni
Specifically hydrolyzes (di)adenosine polyphosphates but not ATP or diadenosine triphosphate, generating ATP as the product. Diadenosine hexaphosphate (Ap6A) is the preferred substrate and hydrolysis yields 2 ATP. It is the only enzyme that symmetrically hydrolyzes Ap6A. It also hydrolyzes diadenosine pentaphosphate (Ap5A), diadenosine tetraphosphate (Ap4A) and adenosine tetraphosphate (p4A).1 Publication
Catalytic activityi
Cofactori
Mg2+1 PublicationNote: Also able to use Mn2+ and Zn2+, but the activity is less than that obtained with Mg2+ ions.1 Publication
Activity regulationi
Strongly inhibited by fluoride ions.1 Publication
Kineticsi
Kcat is 4.1 sec(-1) with Ap6A (at 25 degrees Celsius). Kcat is 1.4 sec(-1) with p4A (at 25 degrees Celsius). Kcat is 0.52 sec(-1) with Ap5A (at 25 degrees Celsius). Kcat is 0.27 sec(-1) with Ap4A (at 25 degrees Celsius).
- KM=1 µM for p4A (at 25 degrees Celsius)1 Publication
- KM=1.1 µM for Ap4A (at 25 degrees Celsius)1 Publication
- KM=1.1 µM for Ap5A (at 25 degrees Celsius)1 Publication
- KM=1.4 µM for Ap6A (at 25 degrees Celsius)1 Publication
- KM=1.4 µM for diguanosine pentaphosphate (Gp5G) (at 25 degrees Celsius)1 Publication
- KM=9.3 µM for diguanosine tetraphosphate (Gp4G) (at 25 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 8.1 Publication
Temperature dependencei
Optimum temperature is 70 degrees Celsius. Ndx1 is stable up to 95 degrees Celsius at pH 7.5.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 46 | Magnesium1 Publication | 1 | |
Metal bindingi | 50 | Magnesium1 Publication | 1 | |
Binding sitei | 74 | Substrate1 Publication | 1 | |
Binding sitei | 112 | Substrate1 Publication | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 3.6.1.61, 2305 |
Names & Taxonomyi
Protein namesi | Recommended name: Diadenosine hexaphosphate hydrolase1 Publication (EC:3.6.1.611 Publication)Short name: Ap6A hydrolase1 Publication Alternative name(s): ATP-generating (di)nucleotide polyphosphate hydrolase1 Publication ATP-generating Ap6A hydrolase1 Publication Nudix protein1 Publication |
Gene namesi | Name:ndx11 Publication |
Organismi | Thermus thermophilus |
Taxonomic identifieri | 274 [NCBI] |
Taxonomic lineagei | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 26 | W → A: Strong decrease of the affinity for Ap6A. 1 Publication | 1 | |
Mutagenesisi | 46 | E → Q: Strong decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 49 | E → Q: Very little effect on hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 50 | E → Q: Strong decrease in catalytic efficiency. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB02738, Adenosine-5'-Pentaphosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000422740 | 1 – 126 | Diadenosine hexaphosphate hydrolaseAdd BLAST | 126 |
Interactioni
Subunit structurei
Monomer.
1 Publication1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q75UV1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q75UV1 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 121 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 121 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 21 – 23 | Substrate binding1 Publication | 3 | |
Regioni | 30 – 32 | Substrate binding1 Publication | 3 | |
Regioni | 66 – 68 | Substrate binding1 Publication | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 31 – 52 | Nudix boxPROSITE-ProRule annotationAdd BLAST | 22 |
Sequence similaritiesi
Belongs to the Nudix hydrolase family.Curated
Family and domain databases
InterProi | View protein in InterPro IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
Q75UV1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MELGAGGVVF NAKREVLLLR DRMGFWVFPK GHPEPGESLE EAAVREVWEE
60 70 80 90 100
TGVRAEVLLP LYPTRYVNPK GVEREVHWFL MRGEGAPRLE EGMTGAGWFS
110 120
PEEARALLAF PEDLGLLEVA LERLPL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB125632 Genomic DNA Translation: BAD18071.1 |
RefSeqi | WP_011228981.1, NZ_AP019801.1 YP_145146.1, NC_006461.1 |
Genome annotation databases
GeneIDi | 3169127 |
KEGGi | ttj:TTHA1880 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB125632 Genomic DNA Translation: BAD18071.1 |
RefSeqi | WP_011228981.1, NZ_AP019801.1 YP_145146.1, NC_006461.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1VC8 | X-ray | 2.00 | A/B | 1-126 | [»] | |
1VC9 | X-ray | 2.30 | A/B | 1-126 | [»] | |
1VCD | X-ray | 1.70 | A/B | 1-126 | [»] | |
SMRi | Q75UV1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB02738, Adenosine-5'-Pentaphosphate |
Genome annotation databases
GeneIDi | 3169127 |
KEGGi | ttj:TTHA1880 |
Enzyme and pathway databases
BRENDAi | 3.6.1.61, 2305 |
Miscellaneous databases
EvolutionaryTracei | Q75UV1 |
Family and domain databases
InterProi | View protein in InterPro IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NDX1_THETH | |
Accessioni | Q75UV1Primary (citable) accession number: Q75UV1 Secondary accession number(s): F6DFL8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 26, 2013 |
Last sequence update: | July 5, 2004 | |
Last modified: | December 2, 2020 | |
This is version 93 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families