B4EU19 (RISB_PROMH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6,7-dimethyl-8-ribityllumazine synthase
Short name=DMRL synthase
Short name=LS
Short name=Lumazine synthase
EC=2.5.1.78

Gene names

Name:	ribH
Ordered Locus Names:	PMI0082

Organism

Proteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]

Taxonomic identifier

529507 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus › Proteus mirabilis

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_00178
Catalytic activity	1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate. HAMAP-Rule MF_00178
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. HAMAP-Rule MF_00178
Subunit structure	Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers By similarity.
Sequence similarities	Belongs to the DMRL synthase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	riboflavin synthase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	6,7-dimethyl-8-ribityllumazine synthase activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 156	156	6,7-dimethyl-8-ribityllumazine synthase HAMAP-Rule MF_00178		PRO_1000098219
Regions
	Region	57 – 59	3	5-amino-6-(D-ribitylamino)uracil binding By similarity
	Region	81 – 83	3	5-amino-6-(D-ribitylamino)uracil binding By similarity
	Region	86 – 87	2	1-deoxy-L-glycero-tetrulose 4-phosphate binding By similarity
Sites
	Active site	89	1	Proton donor Potential
	Binding site	22	1	5-amino-6-(D-ribitylamino)uracil By similarity
	Binding site	114	1	5-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	128	1	1-deoxy-L-glycero-tetrulose 4-phosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4EU19 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 019F4B5A30525F81	FASTA	156	16,315
	10 20 30 40 50 60 MNVIKGVVAA PNARVAIAIA RFNNFINDSL LEGAVDALER IGQVSSENIT VVWVPGAYEL 70 80 90 100 110 120 PLTVKALVES DKYDAVIALG TVIRGGTAHF EYVAGECSSG LSHVAMQSEI PVTFGVLTTE 130 140 150 SIEQAIERAG TKAGNKGAEA AMTALEMINV LKAIKG

References

[1]

"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility." Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T. J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HI4320.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM942759 Genomic DNA. Translation: CAR40327.1.
RefSeq	YP_002149867.1. NC_010554.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	529507.PMI0082.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR40327; CAR40327; PMI0082.
GeneID	6802412.
KEGG	pmr:PMI0082.
PATRIC	20514841. VBIProMir120933_0082.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0054.
HOGENOM	HOG000229250.
KO	K00794.
OMA	TALEMVS.
ProtClustDB	PRK00061.
Enzyme and pathway databases
BioCyc	PMIR529507:GJIW-81-MONOMER.
UniPathway	UPA00275; UER00404.
Family and domain databases
Gene3D	3.40.50.960. 1 hit.
HAMAP	MF_00178. Lumazine_synth.
InterPro	IPR002180. DMRL_synthase. [Graphical view]
PANTHER	PTHR21058. PTHR21058. 1 hit.
Pfam	PF00885. DMRL_synthase. 1 hit. [Graphical view]
SUPFAM	SSF52121. DMRL_synthase. 1 hit.
TIGRFAMs	TIGR00114. lumazine-synth. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RISB_PROMH

Accession

Primary (citable) accession number: B4EU19

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program