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A3DLT5 (RISB_STAMF) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 31. 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:Smar_0487
OrganismStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]
Taxonomic identifier399550 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus

Protein attributes

Sequence length150 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 – 1501506,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_1000040525

Sequences

Sequence LengthMass (Da)Tools
A3DLT5 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 7E5061EDC50180AF

FASTA15016,577
        10         20         30         40         50         60 
MARIGIVVSE FNYDITYLML QKAISHARFL GLEITYVFKV PGTYEIPFAV ANLLKRNDVD 

        70         80         90        100        110        120 
GVVALGAVIK GATKHDELVA SQTARKLMDL MIQYGKPVGL GIIGPGATRM QALERVEDYA 

       130        140        150 
RRAVEAVAKM INRSKSLEEK KFAGETVFIE 

« Hide

References

[1]"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota."
Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.
BMC Genomics 10:145-145(2009) [PubMed: 19341479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.
[2]"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1."
Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C.
Stand. Genomic Sci. 1:183-188(2009)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000575 Genomic DNA. Translation: ABN69595.1.
RefSeqYP_001040503.1. NC_009033.1.

3D structure databases

ProteinModelPortalA3DLT5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3DLT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4908000.
GenomeReviewsGene locus Smar_0487 in contig CP000575_GR.
KEGGsmr:Smar_0487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG09975.
HOGENOMHBG311126.
OMAIQGATKH.
ProtClustDBCLSK2785935.

Enzyme and pathway databases

BioCycSMAR399550:SMAR_0487-MONOMER.

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_STAMF
AccessionPrimary (citable) accession number: A3DLT5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: November 16, 2011
This is version 31 of the entry and version 1 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