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Reviewed, UniProtKB/Swiss-Prot Q5A3V6 (RIB3_CANAL)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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:

KM=37 µM for ribulose-5-phosphate

Vmax=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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2042043,4-dihydroxy-2-butanone 4-phosphate synthase
PRO_0000296685

Regions

Region29 – 302Substrate binding By similarity
Region142 – 1465Substrate binding

Sites

Metal binding301Magnesium or manganese 1 By similarity
Metal binding301Magnesium or manganese 2 By similarity
Metal binding1451Magnesium or manganese 2 By similarity
Binding site341Substrate
Binding site1661Substrate By similarity
Site1281Essential for catalytic activity By similarity
Site1661Essential for catalytic activity

Experimental info

Mutagenesis591C → A: Increases Km for substrate 18-fold. Reduces activity by 30%.
Mutagenesis871Y → A: Increases Km for substrate 4-fold. Reduces activity by 98%. Ref.2
Mutagenesis921D → A: Loss of activity. Alters protein folding and stability. Ref.2
Mutagenesis1661E → A: Loss of activity. Ref.2

Secondary structure

................................... 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5A3V6-1 [UniParc].

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

FASTA20422,658
        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' 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.

Cross-references

Sequence databases

AACQ01000070 Genomic DNA. Translation: EAK97363.1. Different initiation.
AACQ01000071 Genomic DNA. Translation: EAK97301.1. Sequence problems.
RefSeqXP_716297.1.
XP_716359.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TKSX-ray1.60A/B1-204[»]
1TKUX-ray1.66A/B1-204[»]
2RISX-ray1.60A1-204[»]
2RIUX-ray1.70A1-204[»]
ModBaseSearch...

Genome annotation databases

GeneID3641955.
3642062.
KEGGcal:CaO19.12693.
cal:CaO19.5228.

Phylogenomic databases

OMAYGSGIVC.

Enzyme and pathway databases

BRENDA4.1.99.12. 1124.

Family and domain databases

InterProIPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamPF00926. DHBP_synthase. 1 hit.
[Graphical view]
ProDomPD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIB3_CANAL
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents