Reviewed, UniProtKB/Swiss-Prot Q44680 (RISA_BACAM)

Names and origin

Protein names

Recommended name:
    Riboflavin synthase alpha chain
    EC=2.5.1.9

Gene names

Name:	ribE
Synonyms:	ribB

Organism

Bacillus amyloliquefaciens

Taxonomic identifier

1390 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione By similarity.
Catalytic activity	2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.
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.
Subunit structure	Oligomer that consist of 3 alpha subunits and 60 beta subunits By similarity.
Sequence similarities	Contains 2 lumazine-binding repeats.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Domain	Repeat
Molecular function	Transferase
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	riboflavin synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 215	215	Riboflavin synthase alpha chain		PRO_0000068158
Regions
	Repeat	1 – 96	96	Lumazine-binding 1
	Repeat	97 – 193	97	Lumazine-binding 2

Sequences

	Sequence		Length	Mass (Da)
	Q44680-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5A5174315DFE0033	FASTA	215	23,089
	10 20 30 40 50 60 MFTGIVEETG TIQAIKKTGL SMALTIAASK VTSDVRLGDS IAVNGICLTV TGFSDNQFTV 70 80 90 100 110 120 DVMPETVKAT SLNGLSKGSK VNLERAMSAN GRFGGHFVSG HVDGTAEITR IEKKSNAVYY 130 140 150 160 170 180 DLKLSPELTK TLVLKGSITV DGVSSTIFGL SDESVTVSVI PHTISETIFR TKAVGSIVNI 190 200 210 ECDMIGKYLY RFLHKTEQTK SNQTITEAFF SENGF

References

[1]

"Riboflavin biosynthetic genes in Bacillus amyloliquefaciens: primary structure, organization and regulation of activity." Gusarov I.I., Kreneva R.A., Podcharniaev D.A., Iomantas I.U.V., Abalakina E.G., Stoinova N.V., Perumov D.A., Kozlov I.U.I. Mol. Biol. (Mosk.) 31:446-453(1997) [PubMed: 9297088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A 50.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X95955 Genomic DNA. Translation: CAA65190.1.
PIR	T50542.
3D structure databases
HSSP	HSSP built from PDB template 1KZL based on UniProtKB Q9Y7P0.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.9. 1130.
Family and domain databases
InterPro	IPR001783. Lumazine_bd. [Graphical view]
PANTHER	PTHR21098. Lumazine_bd. 1 hit.
Pfam	PF00677. Lum_binding. 2 hits. [Graphical view]
PIRSF	PIRSF000498. Riboflavin_syn_A. 1 hit.
ProDom	PD004110. Lum_binding. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00187. ribE. 1 hit.
PROSITE	PS51177. LUMAZINE_BIND. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RISA_BACAM

Accession

Primary (citable) accession number: Q44680

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	September 22, 2009
This is version 47 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)