Q9UVT8 (RIB4_MAGO7) Reviewed, UniProtKB/Swiss-Prot

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

ORF Names:

MGG_04626

Organism

Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]

Taxonomic identifier

242507 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydroxy-2-butanone 4-phosphate to produce 6,7-dimethyl-8-(1-D-ribityl)lumazine.
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; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
Subunit structure	Homopentamer.
Sequence similarities	Belongs to the DMRL synthase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	riboflavin synthase complex Inferred from electronic annotation. Source: InterPro
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 – 200

200

6,7-dimethyl-8-ribityllumazine synthase

PRO_0000134855

Secondary structure

1

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200

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Helix

27 – 43

17

Helix

48 – 50

3

Beta strand

51 – 58

8

Helix

61 – 75

15

Beta strand

112 – 121

10

Helix

127 – 146

20

Beta strand

150 – 159

10

Helix

160 – 166

7

Helix

176 – 195

20

Sequences

	Sequence		Length	Mass (Da)
	Q9UVT8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E079F049D32271B5	FASTA	200	21,072
	10 20 30 40 50 60 MHTKGPTPQQ HDGSALRIGI VHARWNETII EPLLAGTKAK LLACGVKESN IVVQSVPGSW 70 80 90 100 110 120 ELPIAVQRLY SASQLQTPSS GPSLSAGDLL GSSTTDLTAL PTTTASSTGP FDALIAIGVL 130 140 150 160 170 180 IKGETMHFEY IADSVSHGLM RVQLDTGVPV IFGVLTVLTD DQAKARAGVI EGSHNHGEDW 190 200 GLAAVEMGVR RRDWAAGKTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Crystal structure analysis of a pentameric fungal and an icosahedral plant lumazine synthase reveals the structural basis for differences in assembly." Persson K., Schneider G., Jordan D.B., Viitanen P.V., Sandalova T. Protein Sci. 8:2355-2365(1999) [PubMed: 10595538] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[2]	"The genome sequence of the rice blast fungus Magnaporthe grisea." Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M. , Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W. Nature 434:980-986(2005) [PubMed: 15846337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF148449 mRNA. Translation: AAD55372.1.
CM001231 Genomic DNA. Translation: EHA58265.1.

RefSeq

XP_362181.1. XM_362181.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C41	X-ray	3.10	A/B/C/D/E/F/G/H/I/J	1-200	[»]

ProteinModelPortal

Q9UVT8.

SMR

Q9UVT8. Positions 5-199.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UVT8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2677942.

KEGG

mgr:MGG_04626.

NMPDR

fig|242507.1.peg.3921.

Phylogenomic databases

OrthoDB

EOG49S9GR.

Family and domain databases

InterPro

IPR002180. DMRL_synthase.
[Graphical view]

Gene3D

G3DSA:3.40.50.960. DMRL_synthase. 1 hit.

KO

K00794.

PANTHER

PTHR21058. DMRL_synthase. 1 hit.

Pfam

PF00885. DMRL_synthase. 2 hits.
[Graphical view]

SUPFAM

SSF52121. DMRL_synthase. 1 hit.

TIGRFAMs

TIGR00114. Lumazine-synth. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RIB4_MAGO7

Accession

Primary (citable) accession number: Q9UVT8
Secondary accession number(s): A4QVB0, G4MRQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program