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UniProtKB - O66529 (RISB_AQUAE)
Protein
6,7-dimethyl-8-ribityllumazine synthase
Gene
ribH
Organism
Aquifex aeolicus (strain VF5)
Status
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 PublicationsCatalytic activityi
- (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H+ + 2 H2O + phosphate2 PublicationsEC:2.5.1.782 Publications
Kineticsi
- KM=10.0 µM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0)1 Publication
- KM=26 µM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees Celsius and pH 7.0)1 Publication
- Vmax=31 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)1 Publication
- 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
: riboflavin biosynthesis Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 88 | Proton donorSequence analysis | 1 | |
Binding sitei | 113 | 5-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygen | 1 | |
Binding sitei | 127 | 1-deoxy-L-glycero-tetrulose 4-phosphateCurated | 1 | |
Binding sitei | 135 | 5-amino-6-(D-ribitylamino)uracil | 1 |
GO - Molecular functioni
- 6,7-dimethyl-8-ribityllumazine synthase activity Source: GO_Central
GO - Biological processi
- riboflavin biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Riboflavin biosynthesis |
Enzyme and pathway databases
BioCyci | AAEO224324:G1G15-103-MONOMER |
BRENDAi | 2.5.1.78, 396 |
SABIO-RKi | O66529 |
UniPathwayi | UPA00275;UER00404 |
Names & Taxonomyi
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 |
Gene namesi | Name:ribH Ordered Locus Names:aq_132 |
Organismi | Aquifex aeolicus (strain VF5) |
Taxonomic identifieri | 224324 [NCBI] |
Taxonomic lineagei | Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: GO_Central
Other locations
- riboflavin synthase complex Source: InterPro
Pathology & Biotechi
Chemistry databases
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 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000134708 | 1 – 154 | 6,7-dimethyl-8-ribityllumazine synthaseAdd BLAST | 154 |
Interactioni
Subunit structurei
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.
1 PublicationProtein-protein interaction databases
STRINGi | 224324.aq_132 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O66529 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O66529 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 22 – 23 | 5-amino-6-(D-ribitylamino)uracil binding | 2 | |
Regioni | 56 – 58 | 5-amino-6-(D-ribitylamino)uracil binding | 3 | |
Regioni | 80 – 82 | 5-amino-6-(D-ribitylamino)uracil binding | 3 | |
Regioni | 85 – 86 | 1-deoxy-L-glycero-tetrulose 4-phosphate bindingCurated | 2 |
Sequence similaritiesi
Belongs to the DMRL synthase family.Curated
Phylogenomic databases
eggNOGi | COG0054, Bacteria |
HOGENOMi | CLU_089358_1_1_0 |
InParanoidi | O66529 |
OMAi | CQGVTQG |
OrthoDBi | 1680292at2 |
Family and domain databases
CDDi | cd09209, Lumazine_synthase-I, 1 hit |
Gene3Di | 3.40.50.960, 1 hit |
HAMAPi | MF_00178, Lumazine_synth, 1 hit |
InterProi | View protein in InterPro IPR034964, LS IPR002180, LS/RS IPR036467, LS/RS_sf |
PANTHERi | PTHR21058, PTHR21058, 1 hit |
Pfami | View protein in Pfam PF00885, DMRL_synthase, 1 hit |
SUPFAMi | SSF52121, SSF52121, 1 hit |
TIGRFAMsi | TIGR00114, lumazine-synth, 1 hit |
i Sequence
Sequence statusi: Complete.
O66529-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000657 Genomic DNA Translation: AAC06489.1 |
PIRi | F70312 |
RefSeqi | NP_213089.1, NC_000918.1 WP_010880027.1, NC_000918.1 |
Genome annotation databases
EnsemblBacteriai | AAC06489; AAC06489; aq_132 |
KEGGi | aae:aq_132 |
PATRICi | fig|224324.8.peg.111 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000657 Genomic DNA Translation: AAC06489.1 |
PIRi | F70312 |
RefSeqi | NP_213089.1, NC_000918.1 WP_010880027.1, NC_000918.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1HQK | X-ray | 1.60 | A/B/C/D/E | 1-154 | [»] | |
1NQU | X-ray | 1.75 | A/B/C/D/E | 1-154 | [»] | |
1NQV | X-ray | 2.05 | A/B/C/D/E | 1-154 | [»] | |
1NQW | X-ray | 2.20 | A/B/C/D/E | 1-154 | [»] | |
1NQX | X-ray | 1.82 | A/B/C/D/E | 1-154 | [»] | |
5MPP | electron microscopy | 3.94 | 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T | 1-154 | [»] | |
5MQ3 | electron microscopy | 5.40 | AA/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/BO | 1-154 | [»] | |
5MQ7 | electron microscopy | 5.20 | 0A/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/4X | 1-154 | [»] | |
7A4F | electron microscopy | 3.50 | AA/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/CJ | 1-84 | [»] | |
7A4G | electron microscopy | 4.20 | AA/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/BO | 1-84 | [»] | |
7A4H | electron microscopy | 4.50 | AA/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/BO | 1-84 | [»] | |
7A4I | electron microscopy | 7.04 | 0A/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/7B | 1-84 | [»] | |
7A4J | electron microscopy | 3.04 | 0A/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/7B | 1-84 | [»] | |
SMRi | O66529 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224324.aq_132 |
Chemistry databases
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 |
Genome annotation databases
EnsemblBacteriai | AAC06489; AAC06489; aq_132 |
KEGGi | aae:aq_132 |
PATRICi | fig|224324.8.peg.111 |
Phylogenomic databases
eggNOGi | COG0054, Bacteria |
HOGENOMi | CLU_089358_1_1_0 |
InParanoidi | O66529 |
OMAi | CQGVTQG |
OrthoDBi | 1680292at2 |
Enzyme and pathway databases
UniPathwayi | UPA00275;UER00404 |
BioCyci | AAEO224324:G1G15-103-MONOMER |
BRENDAi | 2.5.1.78, 396 |
SABIO-RKi | O66529 |
Miscellaneous databases
EvolutionaryTracei | O66529 |
Family and domain databases
CDDi | cd09209, Lumazine_synthase-I, 1 hit |
Gene3Di | 3.40.50.960, 1 hit |
HAMAPi | MF_00178, Lumazine_synth, 1 hit |
InterProi | View protein in InterPro IPR034964, LS IPR002180, LS/RS IPR036467, LS/RS_sf |
PANTHERi | PTHR21058, PTHR21058, 1 hit |
Pfami | View protein in Pfam PF00885, DMRL_synthase, 1 hit |
SUPFAMi | SSF52121, SSF52121, 1 hit |
TIGRFAMsi | TIGR00114, lumazine-synth, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RISB_AQUAE | |
Accessioni | O66529Primary (citable) accession number: O66529 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families