3,4-dihydroxy-2-butanone 4-phosphate synthase - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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Q5A3V6 (RIB3_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 58. 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:
3,4-dihydroxy-2-butanone 4-phosphate synthase
Short name=DHBP synthase
EC=4.1.99.12

Gene names

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

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	204 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 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 Ref.2 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. The sequence EAK97363.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Magnesium Manganese Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	riboflavin biosynthetic process Inferred from direct assay Ref.2. Source: CGD
Molecular_function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from direct assay Ref.2. Source: CGD metal 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 – 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...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5A3V6 [UniParc].

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

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

« Hide

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.
[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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

RefSeq

XP_716297.1. XM_711204.1.
XP_716359.1. XM_711266.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q5A3V6.

SMR

Q5A3V6. Positions 3-204.

ModBase

Search...

Protein-protein interaction databases

STRING

5476.CAL0003526.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3641955.
3642062.

KEGG

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

Phylogenomic databases

eggNOG

COG0108.

K02858.

Enzyme and pathway databases

UniPathway

UPA00275; UER00399.

Family and domain databases

Gene3D

3.90.870.10. 1 hit.

InterPro

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

Pfam

PF00926. DHBP_synthase. 1 hit.
[Graphical view]

SUPFAM

SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.

TIGRFAMs

TIGR00506. ribB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q5A3V6.

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:	April 3, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

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

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents