C2VYQ4 (C2VYQ4_BACCE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
6,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
Short name=DMRL synthase HAMAP MF_00178
Short name=Lumazine synthase HAMAP MF_00178
EC=2.5.1.9 HAMAP MF_00178

Alternative name(s):
Riboflavin synthase beta chain HAMAP MF_00178

Gene names

Name:	ribH HAMAP MF_00178
ORF Names:	bcere0021_39100 EMBL EEL43943.1

Organism

Bacillus cereus Rock3-42 EMBL EEL43943.1

Taxonomic identifier

526985 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Protein existence	Inferred 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 RuleBase RU003795
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 RuleBase RU003795
Sequence similarities	Belongs to the DMRL synthase family. HAMAP MF_00178 RuleBase RU003795

Ontologies

Keywords
Biological process	Riboflavin biosynthesis HAMAP MF_00178 RuleBase RU003795
Molecular function	Transferase HAMAP MF_00178 RuleBase RU003795
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...

Sequences

	Sequence		Length	Mass (Da)
	C2VYQ4 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: AA5386484EA66839	FASTA	153	16,246
	10 20 30 40 50 60 MVFEGHLVGT GLKVGVVVGR FNEFITSKLL GGALDGLKRH GVEENDIDVA WVPGAFEIPL 70 80 90 100 110 120 IAKKMANSGK YDAVITLGTV IRGATTHYDY VCNEVAKGVA SLSLQTDIPV IFGVLTTETI 130 140 150 EQAIERAGTK AGNKGYESAV AAIEMAHLSK QWA

References

[1]

"Annotation of the Bacillus cereus Rock3-42 genome." Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E. Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Rock3-42 EMBL EEL43943.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACMK01000117 Genomic DNA. Translation: EEL43943.1.
3D structure databases
ProteinModelPortal	C2VYQ4.
SMR	C2VYQ4. Positions 2-152.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000408761; EBBACP00000401524; EBBACG00000409328.
PATRIC	25068533. VBIBacCer34651_0615.
Family and domain databases
HAMAP	MF_00178. Lumazine_synth. [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]
SUPFAM	SSF52121. DMRL_synthase. 1 hit.
TIGRFAMs	TIGR00114. Lumazine-synth. 1 hit.
ProtoNet	Search...

Entry information

Entry name

C2VYQ4_BACCE

Accession

Primary (citable) accession number: C2VYQ4

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)