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ECOLI:NUDB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) nudB (synonyms: ntpA)
Protein Name(s) Dihydroneopterin triphosphate pyrophosphatase

dATP pyrophosphohydrolase

External Links
UniProt P0AFC0
EMBL X59551
D10165
U00096
AP009048
PIR B38113
RefSeq NP_416379.1
YP_490127.1
PDB 2O1C
2O5W
PDBsum 2O1C
2O5W
ProteinModelPortal P0AFC0
SMR P0AFC0
DIP DIP-10372N
IntAct P0AFC0
STRING 511145.b1865
EnsemblBacteria AAC74935
BAA15676
GeneID 12931354
946383
KEGG ecj:Y75_p1841
eco:b1865
PATRIC 32119053
EchoBASE EB1128
EcoGene EG11138
eggNOG COG0494
HOGENOM HOG000264405
InParanoid P0AFC0
KO K08310
OMA VTRNTEH
OrthoDB EOG69WFKW
BioCyc EcoCyc:H2NEOPTERINP3PYROPHOSPHOHYDRO-MONOMER
ECOL316407:JW1854-MONOMER
MetaCyc:H2NEOPTERINP3PYROPHOSPHOHYDRO-MONOMER
EvolutionaryTrace P0AFC0
PRO PR:P0AFC0
Proteomes UP000000318
UP000000625
Genevestigator P0AFC0
GO GO:0008828
GO:0019177
GO:0000287
GO:0006281
GO:0046656
GO:0046654
Gene3D 3.90.79.10
InterPro IPR003564
IPR020084
IPR000086
IPR015797
Pfam PF00293
PRINTS PR01404
SUPFAM SSF55811
PROSITE PS51462
PS00893

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0046656

folic acid biosynthetic process

PMID:17698004[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

PMID:17698004[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0019177

dihydroneopterin triphosphate pyrophosphohydrolase activity

PMID:17698004[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008828

dATP pyrophosphohydrolase activity

PMID:17698004[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:4362677[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008828

dATP pyrophosphohydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003564

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000086
InterPro:IPR015797
InterPro:IPR020084

F

Seeded From UniProt

complete

enables

GO:0019177

dihydroneopterin triphosphate pyrophosphohydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003564

F

Seeded From UniProt

complete

involved_in

GO:0046656

folic acid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003564

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0046656

folic acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0289

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Gabelli, SB et al. (2007) Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15 1014-22 PubMed GONUTS page
  2. Suzuki, Y & Brown, GM (1974) The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J. Biol. Chem. 249 2405-10 PubMed GONUTS page