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

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Reviewed, UniProtKB/Swiss-Prot Q5A3V6 (RIB3_CANAL)

Last modified November 3, 2009. Version 32. 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:
    3,4-dihydroxy-2-butanone 4-phosphate synthase
      Short name=DHBP synthase
    EC=4.1.99.12

Gene names

Name:	RIB3
ORF Names:	CaO19.5228, CaO19.12693

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length	204 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	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 By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the DHBP synthase family.
Biophysicochemical properties	Kinetic parameters: K_M=37 µM for ribulose-5-phosphate V_max=332 nmol/min/mg enzyme
Mass spectrometry	Molecular mass is 22530 Da from positions 2 - 204. Determined by ESI. Ref.2
Sequence caution	The sequence EAK97301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence EAK97301.1 differs from that shown. Reason: Frameshift at position 117.

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Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Magnesium Manganese Metal-binding
Molecular function	Lyase
Technical term	3D-structure 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 204

204

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

PRO_0000296685

Regions

Region

29 – 30

Substrate binding By similarity

Region

142 – 146

Substrate binding

Sites

Metal binding

Magnesium or manganese 1 By similarity

Metal binding

Magnesium or manganese 2 By similarity

Metal binding

145

Magnesium or manganese 2 By similarity

Binding site

Substrate

Binding site

166

Substrate By similarity

Site

128

Essential for catalytic activity By similarity

Site

166

Essential for catalytic activity

Experimental info

Mutagenesis

C → A: Increases Km for substrate 18-fold. Reduces activity by 30%.

Mutagenesis

Y → A: Increases Km for substrate 4-fold. Reduces activity by 98%. Ref.2

Mutagenesis

D → A: Loss of activity. Alters protein folding and stability. Ref.2

Mutagenesis

166

E → A: Loss of activity. Ref.2

Secondary structure

204

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q5A3V6-1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 5FEC62C3ABDA822E
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FASTA

204

22,658

        10         20         30         40         50         60 
MTNIFTPIEE ALEAYKNGEF LIVMDDEDRE NEGDLIMAAE LITQEKMAFL VRYSSGYVCV 

        70         80         90        100        110        120 
PLSEERANQL ELPPMLANRS DRHGTAYTIT CDFAEGTTTG ISAHDRALTT RSLANPNSKP 

       130        140        150        160        170        180 
QDFIKPGHIL PLRAVPGLLK KRRGHTEAAV QLSTLAGLQP AGVICELVRD EDGLMMRLDD 

       190        200 
CIQFGKKHGI KIININQLVE YISK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.
[2]	"Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans." Echt S., Bauer S., Steinbacher S., Huber R., Bacher A., Fischer M. J. Mol. Biol. 341:1085-1096(2004) [PubMed: 15328619] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-87; ASP-92 AND GLU-166, SUBUNIT.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AACQ01000070 Genomic DNA. Translation: EAK97363.1. Different initiation.
AACQ01000071 Genomic DNA. Translation: EAK97301.1. Sequence problems.

RefSeq

XP_716297.1.
XP_716359.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TKS	X-ray	1.60	A/B	1-204	[»]
1TKU	X-ray	1.66	A/B	1-204	[»]
2RIS	X-ray	1.60	A	1-204	[»]
2RIU	X-ray	1.70	A	1-204	[»]

ModBase

Search...

Genome annotation databases

GeneID

3641955.
3642062.

KEGG

cal:CaO19.12693.
cal:CaO19.5228.

Phylogenomic databases

OMA

YGSGIVC.

Enzyme and pathway databases

BRENDA

4.1.99.12. 1124.

Family and domain databases

InterPro

IPR000422. DHBP_synthase_RibB.
[Graphical view]

Pfam

PF00926. DHBP_synthase. 1 hit.
[Graphical view]

ProDom

PD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00506. ribB. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

RIB3_CANAL

Accession

Primary (citable) accession number: Q5A3V6
Secondary accession number(s): Q5A3P2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 24, 2007
Last modified:	November 3, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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