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Protein

6,7-dimethyl-8-ribityllumazine synthase

Gene

ribH

Organism
Edwardsiella ictaluri (strain 93-146)
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

Pathway: 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 sitei22 – 2215-amino-6-(D-ribitylamino)uracilUniRule annotation
Active sitei89 – 891Proton donorUniRule annotation
Binding sitei114 – 11415-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei128 – 12811-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

BioCyciEICT634503:GCMY-1046-MONOMER.
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
Ordered Locus Names:NT01EI_1057
OrganismiEdwardsiella ictaluri (strain 93-146)
Taxonomic identifieri634503 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella
ProteomesiUP000001485 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1561566,7-dimethyl-8-ribityllumazine synthasePRO_1000203790Add
BLAST

Proteomic databases

PRIDEiC5BCH5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi634503.NT01EI_1057.

Structurei

3D structure databases

ProteinModelPortaliC5BCH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 5935-amino-6-(D-ribitylamino)uracil bindingUniRule annotation
Regioni81 – 8335-amino-6-(D-ribitylamino)uracil bindingUniRule annotation
Regioni86 – 8721-deoxy-L-glycero-tetrulose 4-phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the DMRL synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0054.
HOGENOMiHOG000229250.
KOiK00794.
OMAiSHVAMNS.
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.

C5BCH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTIQGVVAA PQARVAIAIS RFNHFINDSL LEGAIDALKR IGQVSDENIT
60 70 80 90 100
VVWVPGAYEL PLTVRALASS GRYDAVVALG TVIRGGTAHF EFVAGECSSG
110 120 130 140 150
LASVALNTDV PVAFGVLTTE TIEQAIDRAG AKAGNKGAEA ALTALEMINV

LKAIKA
Length:156
Mass (Da):16,147
Last modified:July 28, 2009 - v1
Checksum:iEDD1FEFA5894EF20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001600 Genomic DNA. Translation: ACR68269.1.
RefSeqiWP_015870450.1. NC_012779.2.
YP_002932504.1. NC_012779.2.

Genome annotation databases

EnsemblBacteriaiACR68269; ACR68269; NT01EI_1057.
GeneIDi7959440.
KEGGieic:NT01EI_1057.
PATRICi21835282. VBIEdwIct114273_0957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001600 Genomic DNA. Translation: ACR68269.1.
RefSeqiWP_015870450.1. NC_012779.2.
YP_002932504.1. NC_012779.2.

3D structure databases

ProteinModelPortaliC5BCH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi634503.NT01EI_1057.

Proteomic databases

PRIDEiC5BCH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR68269; ACR68269; NT01EI_1057.
GeneIDi7959440.
KEGGieic:NT01EI_1057.
PATRICi21835282. VBIEdwIct114273_0957.

Phylogenomic databases

eggNOGiCOG0054.
HOGENOMiHOG000229250.
KOiK00794.
OMAiSHVAMNS.
OrthoDBiEOG6RC3WC.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404.
BioCyciEICT634503:GCMY-1046-MONOMER.

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

  1. "Complete genome sequence of Edwardsiella ictaluri 93-146."
    Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 93-146.

Entry informationi

Entry nameiRISB_EDWI9
AccessioniPrimary (citable) accession number: C5BCH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 27, 2015
This is version 43 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.