UniProt functional annotation for Q70IY1



	UniProt functional annotation for Q70IY1

UniProt code: Q70IY1.

Organism: Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1) (Streptomyces tenebrarius).

Taxonomy: Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; Streptoalloteichus.

Function: TobZ is involved in the biosynthesis of the 2- deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O- carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. {ECO:0000269|PubMed:20936279, ECO:0000269|PubMed:22383337}.

Catalytic activity: Reaction=ATP + carbamoyl phosphate + H2O + tobramycin = AMP + diphosphate + H(+) + nebramycin 5' + phosphate; Xref=Rhea:RHEA:42096, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:73678, ChEBI:CHEBI:73679, ChEBI:CHEBI:456215; EC=6.1.2.2; Evidence={ECO:0000269|PubMed:22383337};

Catalytic activity: Reaction=ATP + carbamoyl phosphate + H2O + kanamycin A = 6''-O- carbamoylkanamycin A + AMP + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:42100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58214, ChEBI:CHEBI:58228, ChEBI:CHEBI:73675, ChEBI:CHEBI:456215; EC=6.1.2.2; Evidence={ECO:0000269|PubMed:22383337};

Cofactor: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:22383337}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:22383337};

Activity regulation: ADP inhibits the formation of nebramycin 5. {ECO:0000269|PubMed:22383337}.

Pathway: Antibiotic biosynthesis; kanamycin biosynthesis.

Pathway: Antibiotic biosynthesis; tobramycin biosynthesis.

Domain: Consists of two major domains: the N-terminal domain (Kae1- like) is involved in the transfer of carbamoyl from O- carbamoyladenylate to tobramycin or kanamycin; the C-terminal domain (YrdC-like) is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP.

Disruption phenotype: Cells lacking this gene accumulate kanamycin. {ECO:0000269|PubMed:20936279}.

Miscellaneous: It seems that TobZ plays a solely passive role in the adenylation reaction: all functional groups appear to be provided by the substrates themselves, representing an extreme form of substrate- assisted catalysis. The role of the iron in catalysis remains unclear (PubMed:22383337). {ECO:0000305|PubMed:22383337}.

Similarity: Belongs to the NodU/CmcH family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1) (Streptomyces tenebrarius).
Taxonomy:		Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; Streptoalloteichus.



Function:		TobZ is involved in the biosynthesis of the 2- deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O- carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. {ECO:0000269\|PubMed:20936279, ECO:0000269\|PubMed:22383337}.


Catalytic activity:		Reaction=ATP + carbamoyl phosphate + H2O + tobramycin = AMP + diphosphate + H(+) + nebramycin 5' + phosphate; Xref=Rhea:RHEA:42096, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:73678, ChEBI:CHEBI:73679, ChEBI:CHEBI:456215; EC=6.1.2.2; Evidence={ECO:0000269\|PubMed:22383337};
Catalytic activity:		Reaction=ATP + carbamoyl phosphate + H2O + kanamycin A = 6''-O- carbamoylkanamycin A + AMP + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:42100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58214, ChEBI:CHEBI:58228, ChEBI:CHEBI:73675, ChEBI:CHEBI:456215; EC=6.1.2.2; Evidence={ECO:0000269\|PubMed:22383337};
Cofactor:		Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269\|PubMed:22383337}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269\|PubMed:22383337};
Activity regulation:		ADP inhibits the formation of nebramycin 5. {ECO:0000269\|PubMed:22383337}.
Pathway:		Antibiotic biosynthesis; kanamycin biosynthesis.
Pathway:		Antibiotic biosynthesis; tobramycin biosynthesis.
Domain:		Consists of two major domains: the N-terminal domain (Kae1- like) is involved in the transfer of carbamoyl from O- carbamoyladenylate to tobramycin or kanamycin; the C-terminal domain (YrdC-like) is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP.
Disruption phenotype:		Cells lacking this gene accumulate kanamycin. {ECO:0000269\|PubMed:20936279}.
Miscellaneous:		It seems that TobZ plays a solely passive role in the adenylation reaction: all functional groups appear to be provided by the substrates themselves, representing an extreme form of substrate- assisted catalysis. The role of the iron in catalysis remains unclear (PubMed:22383337). {ECO:0000305\|PubMed:22383337}.
Similarity:		Belongs to the NodU/CmcH family. {ECO:0000305}.