Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - O66529 (RISB_AQUAE)

Entry version 130 (29 Sep 2021)
Sequence version 1 (01 Aug 1998)
Previous versions | rss
Add a publicationFeedback
Protein

6,7-dimethyl-8-ribityllumazine synthase

Gene

ribH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score:

Annotation score:4 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

Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.

2 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 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=10.0 µM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0)1 Publication
  2. KM=26 µM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees Celsius and pH 7.0)1 Publication
  1. Vmax=31 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)1 Publication
  2. Vmax=425 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0)1 Publication

Temperature dependencei

Extremely thermostable. Has a melting temperature of 119.9 degrees Celsius.1 Publication

<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: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil.1 Publication This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei88Proton donorSequence analysis1
<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 sitei1135-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygen1
Binding sitei1271-deoxy-L-glycero-tetrulose 4-phosphateCurated1
Binding sitei1355-amino-6-(D-ribitylamino)uracil1

<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 processRiboflavin biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		AAEO224324:G1G15-103-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.5.1.78, 396

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		O66529

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

More...UniPathwayi		UPA00275;UER00404

<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:
6,7-dimethyl-8-ribityllumazine synthase (EC:2.5.1.78)
Short name:
DMRL synthase
Short name:
LS
Short name:
Lumazine synthase
<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:ribH
Ordered Locus Names:aq_132
<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>OrganismiAquifex aeolicus (strain VF5)
<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 identifieri224324 [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 › Aquificae › Aquificales › Aquificaceae › Aquifex ›
<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
  • UP000000798 <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 location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04262, 3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid
DB04128, 5-Nitroso-6-ribityl-amino-2,4(1H,3H)-pyrimidinedione
DB02214, 6,7-dioxo-5H-8-ribitylaminolumazine

<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_00001347081 – 1546,7-dimethyl-8-ribityllumazine synthaseAdd BLAST154

<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

Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		224324.aq_132

<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

1154
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		O66529

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O66529

<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>Regioni22 – 235-amino-6-(D-ribitylamino)uracil binding2
Regioni56 – 585-amino-6-(D-ribitylamino)uracil binding3
Regioni80 – 825-amino-6-(D-ribitylamino)uracil binding3
Regioni85 – 861-deoxy-L-glycero-tetrulose 4-phosphate bindingCurated2

<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 DMRL synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0054, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_089358_1_1_0

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O66529

Identification of Orthologs from Complete Genome Data

More...OMAi		CQGVTQG

Database of Orthologous Groups

More...OrthoDBi		1680292at2

Family and domain databases

Conserved Domains Database

More...CDDi		cd09209, Lumazine_synthase-I, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.960, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00178, Lumazine_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034964, LS
IPR002180, LS/RS
IPR036467, LS/RS_sf

The PANTHER Classification System

More...PANTHERi		PTHR21058, PTHR21058, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00885, DMRL_synthase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52121, SSF52121, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00114, lumazine-synth, 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.

O66529-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQIYEGKLTA EGLRFGIVAS RFNHALVDRL VEGAIDCIVR HGGREEDITL 
        60         70         80         90        100
VRVPGSWEIP VAAGELARKE DIDAVIAIGV LIRGATPHFD YIASEVSKGL 
       110        120        130        140        150
ANLSLELRKP ITFGVITADT LEQAIERAGT KHGNKGWEAA LSAIEMANLF 

KSLR
Length:154
Mass (Da):16,705
Last modified:August 1, 1998 - 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:iA189410A16454AB7
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
AE000657 Genomic DNA Translation: AAC06489.1

Protein sequence database of the Protein Information Resource

More...PIRi		F70312

NCBI Reference Sequences

More...RefSeqi		NP_213089.1, NC_000918.1
WP_010880027.1, NC_000918.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC06489; AAC06489; aq_132

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		aae:aq_132

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224324.8.peg.111

<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
AE000657 Genomic DNA Translation: AAC06489.1
PIRiF70312
RefSeqiNP_213089.1, NC_000918.1
WP_010880027.1, NC_000918.1

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
1HQKX-ray1.60A/B/C/D/E1-154[»]
1NQUX-ray1.75A/B/C/D/E1-154[»]
1NQVX-ray2.05A/B/C/D/E1-154[»]
1NQWX-ray2.20A/B/C/D/E1-154[»]
1NQXX-ray1.82A/B/C/D/E1-154[»]
5MPPelectron microscopy3.940/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-154[»]
5MQ3electron microscopy5.40AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO1-154[»]
5MQ7electron microscopy5.200A/0B/0C/0D/0E/0X/1A/1B/1C/1D/1E/1X/2A/2B/2C/2D/2E/2X/3A/3B/3C/3D/3E/3X/4A/4B/4C/4D/4E/4X1-154[»]
7A4Felectron microscopy3.50AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ1-84[»]
7A4Gelectron microscopy4.20AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO1-84[»]
7A4Helectron microscopy4.50AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO1-84[»]
7A4Ielectron microscopy7.040A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B1-84[»]
7A4Jelectron microscopy3.040A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B1-84[»]
SMRiO66529
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_132

Chemistry databases

DrugBankiDB04262, 3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid
DB04128, 5-Nitroso-6-ribityl-amino-2,4(1H,3H)-pyrimidinedione
DB02214, 6,7-dioxo-5H-8-ribitylaminolumazine

Genome annotation databases

EnsemblBacteriaiAAC06489; AAC06489; aq_132
KEGGiaae:aq_132
PATRICifig|224324.8.peg.111

Phylogenomic databases

eggNOGiCOG0054, Bacteria
HOGENOMiCLU_089358_1_1_0
InParanoidiO66529
OMAiCQGVTQG
OrthoDBi1680292at2

Enzyme and pathway databases

UniPathwayiUPA00275;UER00404
BioCyciAAEO224324:G1G15-103-MONOMER
BRENDAi2.5.1.78, 396
SABIO-RKiO66529

Miscellaneous databases

EvolutionaryTraceiO66529

Family and domain databases

CDDicd09209, Lumazine_synthase-I, 1 hit
Gene3Di3.40.50.960, 1 hit
HAMAPiMF_00178, Lumazine_synth, 1 hit
InterProiView protein in InterPro
IPR034964, LS
IPR002180, LS/RS
IPR036467, LS/RS_sf
PANTHERiPTHR21058, PTHR21058, 1 hit
PfamiView protein in Pfam
PF00885, DMRL_synthase, 1 hit
SUPFAMiSSF52121, SSF52121, 1 hit
TIGRFAMsiTIGR00114, lumazine-synth, 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 nameiRISB_AQUAE
<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: O66529
<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: December 1, 2000
Last sequence update: August 1, 1998
Last modified: September 29, 2021
This is version 130 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
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