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UniProtKB - K4REZ6 (ROSB_STRDJ)

Entry version 44 (11 Dec 2019)
Sequence version 1 (09 Jan 2013)
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Protein

8-demethyl-8-aminoriboflavin-5'-phosphate synthase

Gene

rosB

Organism
Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
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

Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin) (PubMed:27062037). Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined oxidation, decarboxylation and transamination reaction (PubMed:27062037, PubMed:27331868, PubMed:27981706). The catalysis is initiated by an oxidation step in which the C-8 methyl group on the dimethylbenzene ring of FMN is converted to a formyl group to yield the 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) intermediate (PubMed:27062037). In the presence of thiamine, the formyl group is oxidized into a carboxyl group to yield the 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate (PubMed:27062037). Finally, in the presence of L-glutamate as an amino donor, decarboxylation and aminotransfer occur, resulting in production of 8-demethyl-8-aminoriboflavin-5'-phosphate (PubMed:27062037). Addition of NAD (but not NADP) to the reaction increases the yield 1.7-fold (PubMed:27062037). The reaction also proceeds without the addition of any electron acceptor, and it is possible that molecular oxygen serves this role (PubMed:27062037).3 Publications

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

This protein is involved in Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei13Important to position the amino-group donor glutamate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei240FMN1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi11 – 13FMNCombined sources1 Publication3
Nucleotide bindingi19 – 21FMNCombined sources1 Publication3
Nucleotide bindingi91 – 94FMNCombined sources1 Publication4
Nucleotide bindingi132 – 136FMNCombined sources1 Publication5

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionTransferase
Biological processAntibiotic biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-20150
SDAV1214101:G13G5-8070-MONOMER

<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_and_taxonomy_section">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:
8-demethyl-8-aminoriboflavin-5'-phosphate synthase1 Publication (EC:2.6.1.1141 Publication2 Publications)
Short name:
AFP synthase1 Publication
Alternative name(s):
8-amino-flavin synthase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:rosB1 Publication
Synonyms:Orf79891 Publication
ORF Names:BN159_7989Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiStreptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri1214101 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008043 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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 are unable to produce 8-demethyl-8-aminoriboflavin (AF).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi11T → A: Loss of synthase activity due to the absence of substrate binding. 1 Publication1
Mutagenesisi13R → A: Loss of synthase activity due to the reduced ability to catalyze the introduction of an amino group and predominantly to synthesize 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate. 1 Publication1
Mutagenesisi19S → A: Loss of synthase activity due to the absence of substrate binding. 1 Publication1
Mutagenesisi21T → A: Strong decrease of synthase activity. 1 Publication1
Mutagenesisi53Y → A: Loss of synthase activity. 1 Publication1
Mutagenesisi55D → A: Loss of synthase activity due to the absence of substrate binding. 1 Publication1
Mutagenesisi94N → A: Loss of synthase activity due to the absence of substrate binding. 1 Publication1
Mutagenesisi240Y → A: Loss of synthase activity due to the absence of substrate binding. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004444751 – 2578-demethyl-8-aminoriboflavin-5'-phosphate synthaseAdd BLAST257

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		1214101.BN159_7989

<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

1257
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		K4REZ6

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

<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 SsuE family.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K22598

Identification of Orthologs from Complete Genome Data

More...OMAi		SHDCVAN

Database of Orthologous Groups

More...OrthoDBi		796211at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.360, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029039 Flavoprotein-like_sf
IPR005025 FMN_Rdtase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03358 FMN_red, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52218 SSF52218, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

K4REZ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALKALILNT TLRRSPSRSQ TQGLIDKAVP LYEKEGIETE VVRVIDHDIE 
        60         70         80         90        100
QEYWDDYDDW NAGEKARRED EWPWLLEKIR EADILVIATP ITLNMCTSAA 
       110        120        130        140        150
HVILEKLNLM DELNGDTKQF PLYNKVAGLL MCGNEDGAHH VAGTVLNNLG 
       160        170        180        190        200
RLGYSVPPNA AAYWLGPAGT GPGYIEGKGD RHFHTNKLIR FMVANTSHLA 
       210        220        230        240        250
RMLQETPYTT DLEACAQAAR EESDDVFAIR VNVNTPAIRY KRFQKLGEVK 

VEESQLG
Length:257
Mass (Da):28,865
Last modified:January 9, 2013 - 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:iF92673D1CC9EC343
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
HE971709 Genomic DNA Translation: CCK32368.1

NCBI Reference Sequences

More...RefSeqi		WP_015662694.1, NC_020504.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CCK32368; CCK32368; BN159_7989

Database of genes from NCBI RefSeq genomes

More...GeneIDi		31229912

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sdv:BN159_7989

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1214101.3.peg.8085

<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
HE971709 Genomic DNA Translation: CCK32368.1
RefSeqiWP_015662694.1, NC_020504.1

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
5MJIX-ray2.00A1-257[»]
5MLDX-ray1.70A/B/C/D/E/F/G/H1-257[»]
SMRiK4REZ6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1214101.BN159_7989

Genome annotation databases

EnsemblBacteriaiCCK32368; CCK32368; BN159_7989
GeneIDi31229912
KEGGisdv:BN159_7989
PATRICifig|1214101.3.peg.8085

Phylogenomic databases

KOiK22598
OMAiSHDCVAN
OrthoDBi796211at2

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-20150
SDAV1214101:G13G5-8070-MONOMER

Family and domain databases

Gene3Di3.40.50.360, 1 hit
InterProiView protein in InterPro
IPR029039 Flavoprotein-like_sf
IPR005025 FMN_Rdtase-like
PfamiView protein in Pfam
PF03358 FMN_red, 1 hit
SUPFAMiSSF52218 SSF52218, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiROSB_STRDJ
<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: K4REZ6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2018
Last sequence update: January 9, 2013
Last modified: December 11, 2019
This is version 44 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, Reference proteome

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
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