Riboflavin synthase - Escherichia coli (strain K12)

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P0AFU8 (RISA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Riboflavin synthase
Short name=RS
EC=2.5.1.9

Gene names

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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. Ref.1
Catalytic activity	2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. Ref.1
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
Subunit structure	Homotrimer. Unlike in B.subtilis, does not interact with 6,7-dimethyl-8-ribityllumazine synthase. Ref.1
Sequence similarities	Contains 2 lumazine-binding repeats.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Domain	Repeat
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	riboflavin biosynthetic process Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	oxidoreductase activity Inferred from electronic annotation. Source: InterPro riboflavin synthase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Riboflavin synthase

PRO_0000068166

Regions

Repeat

1 – 97

Lumazine-binding 1

Repeat

98 – 195

Lumazine-binding 2

Region

4 – 6

Substrate binding

Region

48 – 50

Substrate binding

Region

62 – 67

Substrate binding

Secondary structure

213

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AFU8 [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

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
[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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]	"The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution." Meining W., Eberhardt S., Bacher A., Ladenstein R. J. Mol. Biol. 331:1053-1063(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-97 IN COMPLEX WITH RIBOFLAVIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_416179.1. NC_000913.2.
YP_489926.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AFU8.

SMR

P0AFU8. Positions 1-206.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47865N.

IntAct

P0AFU8. 3 interactions.

STRING

511145.b1662.

2D gel databases

SWISS-2DPAGE

P0AFU8.

Proteomic databases

PaxDb

P0AFU8.

PRIDE

P0AFU8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74734; AAC74734; b1662.
BAA15429; BAA15429; BAA15429.

GeneID

12932660.
945848.

KEGG

ecj:Y75_p1639.
eco:b1662.

PATRIC

32118630. VBIEscCol129921_1735.

Organism-specific databases

EchoBASE

EB1378.

EcoGene

EG11406. ribC.

Phylogenomic databases

eggNOG

COG0307.

HOGENOM

HOG000151758.

K00793.

OMA

HILSGHV.

ProtClustDB

PRK09289.

Enzyme and pathway databases

BioCyc

EcoCyc:RIBOFLAVIN-SYN-MONOMER.
ECOL316407:JW1654-MONOMER.
MetaCyc:RIBOFLAVIN-SYN-MONOMER.

UniPathway

UPA00275; UER00405.

Gene expression databases

Genevestigator

P0AFU8.

Family and domain databases

Gene3D

2.40.30.20. 2 hits.

InterPro

IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

PANTHER

PTHR21098. PTHR21098. 1 hit.

Pfam

PF00677. Lum_binding. 2 hits.
[Graphical view]

PIRSF

PIRSF000498. Riboflavin_syn_A. 1 hit.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 2 hits.

TIGRFAMs

TIGR00187. ribE. 1 hit.

PROSITE

PS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00140. Riboflavin.

EvolutionaryTrace

P0AFU8.

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:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents