Brand  (β version)

PDB ID: 3VF2

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Ligands
Code Name Style Show Link
ADP Adenosine-5'-diphosphate PoSSuM
CP Phosphoric acid mono(formamide)ester PoSSuM
FE2 Fe (II) ion PoSSuM
K Potassium ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 3VF2   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of the O-carbamoyltransferase TobZ M473I variant in complex with carbamoyl phosphate and ADP
Release Data : 2012-01-25
Compound :
mol_id molecule chains
1 O-carbamoyltransferase TobZ A
ec: 2.1.3.-
mutation: M473I
Source :
mol_id organism_scientific organism_common expression_system
1 Streptoalloteichus tenebrarius  (taxid:1933) Streptomyces tenebrarius Streptomyces lividans  (taxid:457428)
strain: DSM40770T
gene: tacA, tobZ
expression_system_strain: TK24
expression_system_vector_type: plasmid
expression_system_plasmid: pUWL201PW
Authors : Parthier, C., Stubbs, M.T., Goerlich, S., Jaenecke, F.
Keywords : antibiotic biosynthesis, substrate assisted catalysis, substrate channeling, adenylation, structural enzymology, enzyme evolution, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.900 Å )
Citation :

The O-Carbamoyltransferase TobZ Catalyzes an Ancient Enzymatic Reaction.

Parthier, C.,Gorlich, S.,Jaenecke, F.  et al.
(2012)  Angew.Chem.Int.Ed.Engl.  51 : 4046 - 4052

PubMed: 22383337
DOI: 10.1002/anie.201108896

Reaction

Chain : A
UniProt : Q70IY1 (TOBZ_STRSD)
Reaction: EC: Evidence:
Physiological Direction:
tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5' + AMP + phosphate + diphosphate + H(+) 6.1.2.2 PubMed:22383337
left-to-right
kanamycin A + carbamoyl phosphate + ATP + H2O = 6''-O- carbamoylkanamycin A + AMP + phosphate + diphosphate + H(+) 6.1.2.2 PubMed:22383337
left-to-right
carbamoyl phosphate + ATP + H2O = carbamoyl adenylate + phosphate + diphosphate - PubMed:22383337
left-to-right
tobramycin + carbamoyl adenylate = nebramycin 5' + AMP + H(+) - PubMed:22383337
left-to-right
carbamoyl adenylate + kanamycin A = 6''-O-carbamoylkanamycin A + AMP + H(+) - PubMed:22383337
left-to-right
Cofactor: Evidence: Note:
Fe(2+) ECO:0000269 | PubMed:22383337
Binds 1 Fe(2+) ion per subunit.