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Reviewed, UniProtKB/Swiss-Prot Q01994 (RIB1_PHOLE)

Last modified September 22, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    6,7-dimethyl-8-ribityllumazine synthase
      Short name=DMRL synthase
      Short name=Lumazine synthase
    EC=2.5.1.9
Alternative name(s):
    Riboflavin synthase beta chain
Gene names
Name: ribH
OrganismPhotobacterium leiognathi
Taxonomic identifier553611 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length144 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine. HAMAP MF_00178

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil and riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine: step 1/1. HAMAP MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   Molecular functionTransferase
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›144›1446,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134779

Experimental info

Non-terminal residue1441

Sequences

Sequence LengthMass (Da)Tools
Q01994-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 4A4E4820CD960359

FASTA14415,181
        10         20         30         40         50         60 
MKLLKGVDCT SCCIAIVIAR FNSFINENLL SGAINALQRK GQVKAENITV IRCPGAYELP 

        70         80         90        100        110        120 
LAAQQIAKQG NYDAIIAIGA VIRGGTPHFD FVAGECNKGL AQVALEYQTP VAFGVLTVDS 

       130        140 
IEQAIERAGT KMGNKGEEAA LSAL 

« Hide

References

[1]"The lux genes in Photobacterium leiognathi are closely linked with genes corresponding in sequence to riboflavin synthesis genes."
Lee C.Y., Meighen E.A.
Biochem. Biophys. Res. Commun. 186:690-697(1992) [PubMed: 1339274] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25521 / L1 / CIP 665.

Cross-references

Sequence databases

M90094 Genomic DNA. Translation: AAA73230.1.
PIRPC1110.

3D structure databases

HSSPHSSP built from PDB template 1RVV based on UniProtKB P11998.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.9. 349.

Family and domain databases

HAMAPMF_00178.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
ProDomPD003664. DMRL_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00114. lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIB1_PHOLE
AccessionPrimary (citable) accession number: Q01994
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 22, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents