Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 54 (02 Jun 2021)
Sequence version 1 (05 Jul 2004)
Previous versions | rss
Add a publicationFeedback
Protein

nebramycin 5' synthase

Gene

tobZ

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

2 Publications

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).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ADP inhibits the formation of nebramycin 5.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: kanamycin biosynthesis

This protein is involved in the pathway kanamycin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway kanamycin biosynthesis and in Antibiotic biosynthesis.

Pathwayi: tobramycin biosynthesis

This protein is involved in the pathway tobramycin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway tobramycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei12Tobramycin1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei14Proton acceptor1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi114Iron1
Metal bindingi118Iron1
Metal bindingi137Iron1
Binding sitei139O-carbamoyladenylate1
Binding sitei168O-carbamoyladenylate; via carbonyl oxygen1
Binding sitei172O-carbamoyladenylate1
Binding sitei172Tobramycin1
Binding sitei228Tobramycin1
Binding sitei230Tobramycin1
Binding sitei310O-carbamoyladenylate; via amide nitrogen1
Binding sitei314O-carbamoyladenylate1
Metal bindingi338Iron1
Binding sitei418ATP1 Publication1
Binding sitei449ATP1 Publication1
Binding sitei496ATP1 Publication1
Binding sitei498Carbamoyl phosphate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi443 – 445ATP1 Publication3
Nucleotide bindingi530 – 535ATP1 Publication6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Ligase
Biological processAntibiotic biosynthesis
LigandATP-binding, Iron, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17235

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00965
UPA00971

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
nebramycin 5' synthase (EC:6.1.2.2)
Alternative name(s):
Kanamycin A carbamoyltransferase
Tobramycin carbamoyltransferase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tobZ
Synonyms:tacA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1) (Streptomyces tenebrarius)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1933 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeStreptoalloteichus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene accumulate kanamycin.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14H → N: Shows negligible tobramycin carbamoylation activity. 1 Publication1
Mutagenesisi443K → A: The nucleotide binds in a similar fashion to ACP in wild-type, but the positions of the beta- and gamma-phosphorus atoms are shifted, so that the magnesium ion no longer coordinates the gamma-phosphate and the mutant is unable to catalyze the adenylation. 1 Publication1
Mutagenesisi473M → I: Binds carbamoyl phosphate, but not nucleotide, so that the mutant is unable to catalyze the adenylation. 1 Publication1
Mutagenesisi530S → A: Binds carbamoyl phosphate, but not nucleotide, so that the mutant is unable to catalyze the adenylation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004258061 – 570nebramycin 5' synthaseAdd BLAST570

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q70IY1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1570
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q70IY1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 354Kae1-likeAdd BLAST354
Regioni367 – 570YrdC-likeAdd BLAST204
Regioni418 – 419Carbamoyl phosphate binding2
Regioni528 – 530Carbamoyl phosphate binding3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NodU/CmcH family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.870.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043129, ATPase_NBD
IPR031730, Carbam_trans_C
IPR038152, Carbam_trans_C_sf
IPR003696, Carbtransf_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16861, Carbam_trans_C, 1 hit
PF02543, Carbam_trans_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53067, SSF53067, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q70IY1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVLGLNGWP RDFHDASAAL LVDGRIAAFA EEERFTRKKH GYNTAPVQAA
60 70 80 90 100
AFCLAQAGLT VDDLDAVAFG WDLPAMYRER LGGWPHSDSE ALDILLPRDV
110 120 130 140 150
FPRRTDPPLH FVQHHLAHAA SAYYFSGEDR GAVLIVDGQG EEECVTLAHA
160 170 180 190 200
EGGKITVLDT VPGAWSLGFF YEHVSEYTGL GGDNPGKLMG LAAHGTTVDE
210 220 230 240 250
TLSAFAFDSD GYRLNLIDPQ ARDPEDWDEY SVTERAWFAH LERIYRLPPN
260 270 280 290 300
EFVRRYDPAK GRVVRDTRRD PYEYRDLAAT AQAALERAVF GLADSVLART
310 320 330 340 350
GERTLFVAGG VGLNATMNGK LLTRSTVDKM FVPPVASDIG VSLGAAAAVA
360 370 380 390 400
VELGDRIAPM GDTAAWGPEF SPDQVRAALD RTGLAYREPA NLEREVAALI
410 420 430 440 450
ASGKVVGWAQ GRGEVGPRAL GQRSLLGSAH SPTMRDHINL RVKDREWWRP
460 470 480 490 500
FAPSMLRSVS DQVLEVDADF PYMIMTTKVR AAYAERLPSV VHEDWSTRPQ
510 520 530 540 550
TVTEASNPRY HRMLTELGDL VGDPVCLNTS FNDRGEPIVS SPADALLTFS
560 570
RLPIDALAVG PYLVTKDLRH
Length:570
Mass (Da):62,547
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i88C6B6E44CC00546
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ579650 Genomic RNA Translation: CAE22473.1
AJ810851 Genomic DNA Translation: CAH18554.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAE22473

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ579650 Genomic RNA Translation: CAE22473.1
AJ810851 Genomic DNA Translation: CAH18554.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VENX-ray1.57A1-570[»]
3VEOX-ray2.19A1-570[»]
3VERX-ray2.34A1-570[»]
3VESX-ray2.23A1-570[»]
3VETX-ray2.20A1-570[»]
3VEWX-ray2.35A1-570[»]
3VEXX-ray1.90A1-570[»]
3VEZX-ray2.40A1-570[»]
3VF2X-ray2.90A1-570[»]
3VF4X-ray2.40A1-570[»]
SMRiQ70IY1
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiQ70IY1

Genome annotation databases

KEGGiag:CAE22473

Enzyme and pathway databases

UniPathwayiUPA00965
UPA00971
BioCyciMetaCyc:MONOMER-17235

Family and domain databases

Gene3Di3.90.870.20, 1 hit
InterProiView protein in InterPro
IPR043129, ATPase_NBD
IPR031730, Carbam_trans_C
IPR038152, Carbam_trans_C_sf
IPR003696, Carbtransf_dom
PfamiView protein in Pfam
PF16861, Carbam_trans_C, 1 hit
PF02543, Carbam_trans_N, 1 hit
SUPFAMiSSF53067, SSF53067, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTOBZ_STRSD
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q70IY1
Secondary accession number(s): Q2MF18
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: July 5, 2004
Last modified: June 2, 2021
This is version 54 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again