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Protein

6,7-dimethyl-8-ribityllumazine synthase 2

Gene

ribH2

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate.

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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 6,7-dimethyl-8-ribityllumazine synthase 1 (ribH1), 6,7-dimethyl-8-ribityllumazine synthase 2 (ribH2)
  2. no protein annotated in this organism
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 2015-amino-6-(D-ribitylamino)uracilBy similarity
Active sitei86 – 861Proton donorSequence analysis
Binding sitei111 – 11115-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei125 – 12511-deoxy-L-glycero-tetrulose 4-phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404.

Names & Taxonomyi

Protein namesi
Recommended name:
6,7-dimethyl-8-ribityllumazine synthase 2 (EC:2.5.1.78)
Short name:
DMRL synthase 2
Short name:
LS 2
Short name:
Lumazine synthase 2
Alternative name(s):
Type II lumazine synthase
Gene namesi
Name:ribH2
Ordered Locus Names:BMEII0589
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1581586,7-dimethyl-8-ribityllumazine synthase 2PRO_0000134727Add
BLAST

Proteomic databases

PRIDEiP61712.

Expressioni

Inductioni

The two ribH genes may be differentially expressed during the Brucella infection cycle. Brucella would use RibH1 for flavin biosynthesis during the extracellular phase and RibH2 during intracellular growth (By similarity).By similarity

Interactioni

Subunit structurei

Homodecamer, arranged as a dimer of pentamers.By similarity

Protein-protein interaction databases

STRINGi224914.BAWG_1983.

Structurei

3D structure databases

ProteinModelPortaliP61712.
SMRiP61712. Positions 8-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 5635-amino-6-(D-ribitylamino)uracil bindingBy similarity
Regioni78 – 8035-amino-6-(D-ribitylamino)uracil bindingBy similarity

Sequence similaritiesi

Belongs to the DMRL synthase family.Curated

Phylogenomic databases

eggNOGiENOG410908U. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229252.
KOiK00794.
OMAiRRYTAIV.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth. 1 hit.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.

Sequencei

Sequence statusi: Complete.

P61712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD
60 70 80 90 100
VPGAYEIPLH AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ
110 120 130 140 150
VQLETEVPVL SVVLTPHHFH ESKEHHDFFH AHFKVKGVEA AHAALQIVSE

RSRIAALV
Length:158
Mass (Da):17,356
Last modified:June 7, 2004 - v1
Checksum:iEE59C2C815E53A2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008918 Genomic DNA. Translation: AAL53831.1.
PIRiAD3583.
RefSeqiWP_002965946.1. NZ_GG703779.1.

Genome annotation databases

EnsemblBacteriaiAAL53831; AAL53831; BMEII0589.
GeneIDi23672548.
KEGGibme:BMEII0589.
bmel:DK63_2656.
PATRICi17799922. VBIBruMel146950_2295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008918 Genomic DNA. Translation: AAL53831.1.
PIRiAD3583.
RefSeqiWP_002965946.1. NZ_GG703779.1.

3D structure databases

ProteinModelPortaliP61712.
SMRiP61712. Positions 8-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BAWG_1983.

Proteomic databases

PRIDEiP61712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL53831; AAL53831; BMEII0589.
GeneIDi23672548.
KEGGibme:BMEII0589.
bmel:DK63_2656.
PATRICi17799922. VBIBruMel146950_2295.

Phylogenomic databases

eggNOGiENOG410908U. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229252.
KOiK00794.
OMAiRRYTAIV.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth. 1 hit.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRISB2_BRUME
AccessioniPrimary (citable) accession number: P61712
Secondary accession number(s): Q44668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 7, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.