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Q8KAW4 (RISB_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:CT2037
OrganismChlorobium tepidum
Taxonomic identifier1097 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length155 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
Reference 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 – 1551556,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134740

Sequences

Sequence LengthMass (Da)Tools
Q8KAW4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 912EC24A91BF7675

FASTA15516,308
        10         20         30         40         50         60 
MQVQNIEGSL NASGLKFALV VSRFNDFIGQ KLVEGAIDCI VRHGGSADEI TVIRCPGAFE 

        70         80         90        100        110        120 
LPSVTRKAML SGKYDAIVTL GVIIRGSTPH FDVIAAEATK GIAQVGMEAA IPVSFGVLTT 

       130        140        150 
ENLEQAIERA GTKAGNKGFD AALAAIEMAN LYKQL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM73254.1.
RefSeqNP_662912.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KAW4.
SMRQ8KAW4. Positions 4-155.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1007523.
GenomeReviewsGene locus CT2037 in contig AE006470_GR.
KEGGcte:CT2037.
NMPDRfig|194439.1.peg.2006.
PATRIC21401887. VBIChlTep116050_1846.
TIGRCT2037.

Phylogenomic databases

HOGENOMHBG311126.
OMADYVCNEA.
ProtClustDBPRK00061.

Enzyme and pathway databases

BioCycCTEP194439:CT_2037-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_CHLTE
AccessionPrimary (citable) accession number: Q8KAW4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 50 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