Reviewed, UniProtKB/Swiss-Prot P61714 (RISB_ECOLI)

Names and origin

Protein names

Recommended 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
Synonyms:	ribE, ybaF
Ordered Locus Names:	b0415, JW0405

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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
Subunit structure	Oligomer of 60 beta subunits forming an icosahedral capsid. The core of the capsid does not contain alpha subunits. HAMAP MF_00178
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	riboflavin synthase activity Inferred from electronic annotation. Source: HAMAP
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 MF_00178		PRO_0000134754

Sequences

	Sequence		Length	Mass (Da)
	P61714-1 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 1F8504B2892195C7	FASTA	156	16,157
	10 20 30 40 50 60 MNIIEANVAT PDARVAITIA RFNNFINDSL LEGAIDALKR IGQVKDENIT VVWVPGAYEL 70 80 90 100 110 120 PLAAGALAKT GKYDAVIALG TVIRGGTAHF EYVAGGASNG LAHVAQDSEI PVAFGVLTTE 130 140 150 SIEQAIERAG TKAGNKGAEA ALTALEMINV LKAIKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation." Taura T., Ueguchi C., Shiba K., Ito K. Mol. Gen. Genet. 234:429-432(1992) [PubMed: 1406588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli." Moertl S., Fischer M., Richter G., Tack J., Weinkauf S., Bacher A. J. Biol. Chem. 271:33201-33207(1996) [PubMed: 8969176] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64395 Genomic DNA. Translation: CAA45736.1. U82664 Genomic DNA. Translation: AAB40171.1. U00096 Genomic DNA. Translation: AAC73518.1. AP009048 Genomic DNA. Translation: BAE76195.1.
PIR	S26202.
RefSeq	AP_001065.1. NP_414949.1.
3D structure databases
HSSP	HSSP built from PDB template 1RVV based on UniProtKB P11998.
ModBase	Search...
Protein-protein interaction databases
STRING	P61714.
2-D gel databases
SWISS-2DPAGE	P61714.
Genome annotation databases
GeneID	946453.
GenomeReviews	Gene locus JW0405 in contig AP009048_GR. Gene locus b0415 in contig U00096_GR.
KEGG	ecj:JW0405. eco:b0415.
Organism-specific databases
EchoBASE	EB1298.
EcoGene	EG11322. ribH.
CMR	Search...
Phylogenomic databases
HOGENOM	P61714.
OMA	LTTDTMQ.
Enzyme and pathway databases
BioCyc	EcoCyc:LUMAZINESYN-MON. MetaCyc:LUMAZINESYN-MON.
BRENDA	2.5.1.9. 246.
Gene expression databases
Genevestigator	P61714.
Family and domain databases
HAMAP	MF_00178. [Tree]
InterPro	IPR002180. DMRL_synthase. [Graphical view]
Gene3D	G3DSA:3.40.50.960. DMRL_synthase. 1 hit.
PANTHER	PTHR21058. DMRL_synthase. 1 hit.
Pfam	PF00885. DMRL_synthase. 1 hit. [Graphical view]
ProDom	PD003664. DMRL_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00114. lumazine-synth. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RISB_ECOLI

Accession

Primary (citable) accession number: P61714
Secondary accession number(s): P25540, P77114, Q2MC11

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)