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ARTAU:Q6SJY7

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Species (Taxon ID) Arthrobacter aurescens. (43663)
Gene Name(s) No Information Provided.
Protein Name(s) Triazine hydrolase (ECO:0000313 with EMBL:AAS20185.1)
External Links
UniProt Q6SJY7
EMBL AY456696
PDB 3LS9
3LSB
3LSC
4L9X
4LH8
PDBsum 3LS9
3LSB
3LSC
4L9X
4LH8
ProteinModelPortal Q6SJY7
EvolutionaryTrace Q6SJY7
GO GO:0004040
GO:0046872
GO:0008152
Gene3D 2.30.40.10
InterPro IPR006680
IPR011059
Pfam PF01979
SUPFAM SSF51338

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004040

amidase activity

PMID:16885454[1]

ECO:0000314

F

Figure 5 demonstrates the activity of Zn(II) and Co(II) trzN with selected s-triazines as substrates.

Figure 4 shows the effect of metal addition on ametryn hydrolysis activity of native TrzN purified from recombinant cells grown on 500M zinc and metal-depleted TrzN.

complete
CACAO 7543

enables

GO:0004040

amidase activity

PMID:16885454[1]

ECO:0000314

direct assay evidence used in manual assertion

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:IPR006680

F

Seeded From UniProt

complete

enables

GO:0016810

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011059

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Shapir, N et al. (2006) TrzN from Arthrobacter aurescens TC1 Is a zinc amidohydrolase. J. Bacteriol. 188 5859-64 PubMed GONUTS page