Reviewed, UniProtKB/Swiss-Prot Q8TG90 (RIB3_MAGGR)

Names and origin

Protein names

Recommended name:
    3,4-dihydroxy-2-butanone 4-phosphate synthase
      Short name=DHBP synthase
    EC=4.1.99.12

Gene names

Name:	RIB3
ORF Names:	MGG_01049

Organism

Magnaporthe grisea (Rice blast fungus) (Pyricularia grisea) [Complete proteome]

Taxonomic identifier

148305 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity.
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese. Ref.1
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Subunit structure	Homodimer. Ref.3
Sequence similarities	Belongs to the DHBP synthase family.
Mass spectrometry	Molecular mass is 24870.7 Da from positions 2 - 233. Determined by ESI. Ref.1

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Magnesium Manganese Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 233

233

3,4-dihydroxy-2-butanone 4-phosphate synthase

PRO_0000296686

Regions

Region

36 – 37

2

Substrate binding By similarity

Region

150 – 154

5

Substrate binding

Sites

Metal binding

37

1

Magnesium or manganese 1

Metal binding

37

1

Magnesium or manganese 2

Metal binding

153

1

Magnesium or manganese 2

Binding site

41

1

Substrate By similarity

Binding site

174

1

Substrate By similarity

Site

136

1

Essential for catalytic activity By similarity

Site

174

1

Essential for catalytic activity By similarity

Secondary structure

1

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233

Helix Strand Turn

Details...

Helix

15 – 23

9

Beta strand

28 – 31

4

Turn

34 – 37

4

Beta strand

40 – 45

6

Helix

46 – 48

3

Helix

51 – 60

10

Beta strand

66 – 69

4

Helix

71 – 76

6

Beta strand

98 – 100

3

Beta strand

106 – 108

3

Helix

111 – 122

12

Helix

128 – 130

3

Beta strand

131 – 141

11

Helix

146 – 149

4

Helix

153 – 163

11

Beta strand

168 – 177

10

Beta strand

188 – 190

3

Helix

196 – 205

10

Beta strand

209 – 212

4

Helix

213 – 224

12

Sequences

	Sequence		Length	Mass (Da)
	Q8TG90-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 5C83AA5C49DFD07E	FASTA	233	25,003
	10 20 30 40 50 60 MPSTDSIPKS NFDAIPDVIQ AFKNGEFVVV LDDPSRENEA DLIIAAESVT TEQMAFMVRH 70 80 90 100 110 120 SSGLICAPLT PERTTALDLP QMVTHNADPR GTAYTVSVDA EHPSTTTGIS AHDRALACRM 130 140 150 160 170 180 LAAPDAQPSH FRRPGHVFPL RAVAGGVRAR RGHTEAGVEL CRLAGKRPVA VISEIVDDGQ 190 200 210 220 230 EVEGRAVRAA PGMLRGDECV AFARRWGLKV CTIEDMIAHV EKTEGKLETN GSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe grisea." Liao D.-I., Viitanen P.V., Jordan D.B. Acta Crystallogr. D 56:1495-1497(2000) [PubMed: 11053863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17, CHARACTERIZATION, COFACTOR, MASS SPECTROMETRY.
[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 / FGSC 8958.
[3]	"Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase." Liao D.-I., Zheng Y.-J., Viitanen P.V., Jordan D.B. Biochemistry 41:1795-1806(2002) [PubMed: 11827524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) IN COMPLEXES WITH DIVALENT METAL CATIONS AND SUBSTRATE ANALOGS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF430214 mRNA. Translation: AAL84175.1.
CH476836 Genomic DNA. Translation: EDK02274.1.

RefSeq

XP_368195.1.

UniGene

Mgr.4599

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K49	X-ray	1.50	A	1-233	[»]
1K4I	X-ray	0.98	A	1-233	[»]
1K4L	X-ray	1.60	A	1-233	[»]
1K4O	X-ray	1.10	A	1-233	[»]
1K4P	X-ray	1.00	A	1-233	[»]

ModBase

Search...

Genome annotation databases

GeneID

2674307.

KEGG

mgr:MGG_01049.

NMPDR

fig|242507.1.peg.113.

Phylogenomic databases

OMA

RGHTEAT.

OrthoDB

EOG9W3V4Z.

PhylomeDB

Q8TG90.

Enzyme and pathway databases

BRENDA

4.1.99.12. 5953.

Family and domain databases

InterPro

IPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]

Gene3D

G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.

Pfam

PF00926. DHBP_synthase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00506. ribB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RIB3_MAGGR

Accession

Primary (citable) accession number: Q8TG90

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)