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Protein

6,7-dimethyl-8-ribityllumazine synthase

Gene

ribH

Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
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.UniRule annotation

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.UniRule annotation

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.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 6,7-dimethyl-8-ribityllumazine synthase (ribH)
  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 sitei18 – 1815-amino-6-(D-ribitylamino)uracilUniRule annotation
Active sitei83 – 831Proton donorUniRule annotation
Binding sitei108 – 10815-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei122 – 12211-deoxy-L-glycero-tetrulose 4-phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

BioCyciBHEN283166:GIVZ-757-MONOMER.
BRENDAi2.5.1.78. 7854.
UniPathwayiUPA00275; UER00404.

Names & Taxonomyi

Protein namesi
Recommended name:
6,7-dimethyl-8-ribityllumazine synthaseUniRule annotation (EC:2.5.1.78UniRule annotation)
Short name:
DMRL synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lumazine synthaseUniRule annotation
Gene namesi
Name:ribHUniRule annotation
Synonyms:ribE
Ordered Locus Names:BH07580
OrganismiBartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
Taxonomic identifieri283166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000000421 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1551556,7-dimethyl-8-ribityllumazine synthasePRO_0000134717Add
BLAST

Proteomic databases

PaxDbiQ9REF4.

Interactioni

Protein-protein interaction databases

STRINGi283166.BH07580.

Structurei

3D structure databases

ProteinModelPortaliQ9REF4.
SMRiQ9REF4. Positions 10-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 5135-amino-6-(D-ribitylamino)uracil bindingUniRule annotation
Regioni75 – 7735-amino-6-(D-ribitylamino)uracil bindingUniRule annotation
Regioni80 – 8121-deoxy-L-glycero-tetrulose 4-phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the DMRL synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108UTT. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229250.
KOiK00794.
OMAiTVCNDSS.
OrthoDBiEOG6RC3WC.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.
TIGRFAMsiTIGR00114. lumazine-synth. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9REF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIEICKKLH VLIVEARFYD GISDALLTGA VSTLQKAEAT YDIVTVPGAL
60 70 80 90 100
EIPGAIAFAE KNSKIYYDGY VALGCVIRGE TYHFEIVAND SCRALMDLTI
110 120 130 140 150
HKHLAIGNGI LTVENEKQAW ARAKQDEKNK GGFAAQAALC MIALKKRFGE

IIKYG
Length:155
Mass (Da):16,953
Last modified:August 31, 2004 - v2
Checksum:i26590561428BC2AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951L → S in CAB63092 (PubMed:10488170).Curated
Sequence conflicti126 – 1261D → A in CAB63092 (PubMed:10488170).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132928 Genomic DNA. Translation: CAB63092.1.
BX897699 Genomic DNA. Translation: CAF27559.1.
RefSeqiWP_011180660.1. NZ_LRIJ01000002.1.

Genome annotation databases

EnsemblBacteriaiCAF27559; CAF27559; BH07580.
KEGGibhe:BH07580.
PATRICi20545332. VBIBarHen29080_0811.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132928 Genomic DNA. Translation: CAB63092.1.
BX897699 Genomic DNA. Translation: CAF27559.1.
RefSeqiWP_011180660.1. NZ_LRIJ01000002.1.

3D structure databases

ProteinModelPortaliQ9REF4.
SMRiQ9REF4. Positions 10-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283166.BH07580.

Proteomic databases

PaxDbiQ9REF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF27559; CAF27559; BH07580.
KEGGibhe:BH07580.
PATRICi20545332. VBIBarHen29080_0811.

Phylogenomic databases

eggNOGiENOG4108UTT. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229250.
KOiK00794.
OMAiTVCNDSS.
OrthoDBiEOG6RC3WC.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404.
BioCyciBHEN283166:GIVZ-757-MONOMER.
BRENDAi2.5.1.78. 7854.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.
TIGRFAMsiTIGR00114. lumazine-synth. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of riboflavin synthesis genes in Bartonella henselae and use of the ribC gene for differentiation of Bartonella species by PCR."
    Bereswill S., Hinkelmann S., Kist M., Sander A.
    J. Clin. Microbiol. 37:3159-3166(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 49882 / DSM 28221 / Houston 1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49882 / DSM 28221 / Houston 1.

Entry informationi

Entry nameiRISB_BARHE
AccessioniPrimary (citable) accession number: Q9REF4
Secondary accession number(s): Q6G3K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: August 31, 2004
Last modified: May 11, 2016
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.