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A3MA34 (RISB_ACIBT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Ordered Locus Names:A1S_3389
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
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 By similarity. 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; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. HAMAP MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1561566,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_1000098155

Sequences

Sequence LengthMass (Da)Tools
A3MA34 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: AE8164D59C6BE50E

FASTA15616,493
        10         20         30         40         50         60 
MAIRRIEGLL HLASEGRYAI LVGRFNSFVV EHLLEGAIDT LKRHGVNEDN ITVIHAPGAW 

        70         80         90        100        110        120 
ELPIVAKKLA TSNQFDAIIA LGAVIRGSTP HFDFVAGECA KGLGVVALES SLPVINGVLT 

       130        140        150 
TDSIEQAIER SGTKAGNKGS EAALTAIEMV NLLKAI 

« Hide

References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000521 Genomic DNA. Translation: ABO13778.2.
RefSeqYP_001086380.1. NC_009085.1.

3D structure databases

ProteinModelPortalA3MA34.
SMRA3MA34. Positions 4-156.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MA34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4917253.
GenomeReviewsGene locus A1S_3389 in contig CP000521_GR.
KEGGacb:A1S_3389.
NMPDRfig|400667.4.peg.3495.
PATRIC20723120. VBIAciBau103176_3419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0054.
HOGENOMHBG311126.
ProtClustDBPRK00061.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KOK00794.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
TIGRFAMsTIGR00114. Lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB_ACIBT
AccessionPrimary (citable) accession number: A3MA34
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: December 14, 2011
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families