Riboflavin synthase alpha chain - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AFU8 (RISA_ECOLI)

Last modified November 3, 2009. Version 40. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Riboflavin synthase alpha chain
EC=2.5.1.9

Gene names

Name:	ribE
Synonyms:	ribC
Ordered Locus Names:	b1662, JW1654

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
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.
Sequence similarities	Contains 2 lumazine-binding repeats.

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Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Domain	Repeat
Molecular function	Transferase
Technical term	3D-structure Complete proteome
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Riboflavin synthase alpha chain

PRO_0000068166

Regions

Repeat

1 – 97

Lumazine-binding 1

Repeat

98 – 195

Lumazine-binding 2

Secondary structure

213

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AFU8-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: CD1C7E40E4AC88B6
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FASTA

213

23,445

        10         20         30         40         50         60 
MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT VTEINGNHVS 

        70         80         90        100        110        120 
FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS GHIMTTAEVA KILTSENNRQ 

       130        140        150        160        170        180 
IWFKVQDSQL MKYILYKGFI GIDGISLTVG EVTPTRFCVH LIPETLERTT LGKKKLGARV 

       190        200        210 
NIEIDPQTQA VVDTVERVLA ARENAMNQPG TEA

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli." Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A. Eur. J. Biochem. 242:712-719(1996) [PubMed: 9022701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / RR28.
[2]	"Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12." Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W. J. Bacteriol. 179:1105-1111(1997) [PubMed: 9023191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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.
[6]	"The solution structure of the N-terminal domain of riboflavin synthase." Truffault V., Coles M., Diercks T., Abelmann K., Eberhardt S., Luttgen H., Bacher A., Kessler H. J. Mol. Biol. 309:949-960(2001) [PubMed: 11399071] [Abstract] Cited for: STRUCTURE BY NMR OF 1-97.
[7]	"Crystal structure of riboflavin synthase." Liao D.I., Wawrzak Z., Calabrese J.C., Viitanen P.V., Jordan D.B. Structure 9:399-408(2001) [PubMed: 11377200] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X69109 Genomic DNA. Translation: CAA48861.1.
U68703 Genomic DNA. Translation: AAB47940.1.
U00096 Genomic DNA. Translation: AAC74734.1.
AP009048 Genomic DNA. Translation: BAA15429.1.

PIR

S28526.

RefSeq

AP_002284.1.
NP_416179.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HZE	NMR	-	A/B	1-97	[»]
1I18	NMR	-	A/B	1-97	[»]
1I8D	X-ray	2.00	A/B/C	1-213	[»]
1PKV	X-ray	2.60	A/B	1-97	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AFU8.

2-D gel databases

SWISS-2DPAGE

P0AFU8.

Genome annotation databases

GeneID

945848.

GenomeReviews

Gene locus JW1654 in contig AP009048_GR.
Gene locus b1662 in contig U00096_GR.

KEGG

ecj:JW1654.
eco:b1662.

Organism-specific databases

EchoBASE

EB1378.

EcoGene

EG11406. ribE.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AFU8.

OMA

CLTVTKI.

Enzyme and pathway databases

BioCyc

EcoCyc:RIBOFLAVIN-SYN-MON.
MetaCyc:RIBOFLAVIN-SYN-MON.

Gene expression databases

Genevestigator

P0AFU8.

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...

Other Resources

DrugBank

DB00140. Riboflavin.

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Entry information

Entry name

RISA_ECOLI

Accession

Primary (citable) accession number: P0AFU8
Secondary accession number(s): P29015

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	November 3, 2009
This is version 40 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)

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