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Q5A3V6 (RIB3_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:CaO19.12693, CaO19.5228
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
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. HAMAP-Rule MF_00180

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP-Rule MF_00180

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. HAMAP-Rule MF_00180

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the DHBP synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=37 µM for ribulose-5-phosphate Ref.2

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.

The sequence EAK97363.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2042043,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP-Rule MF_00180
PRO_0000296685

Regions

Region29 – 302Substrate binding By similarity
Region142 – 1465Substrate binding HAMAP-Rule MF_00180

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 [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] [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.
RefSeqXP_716297.1. XM_711204.1.
XP_716359.1. XM_711266.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TKSX-ray1.60A/B1-204[»]
1TKUX-ray1.66A/B1-204[»]
2RISX-ray1.60A1-204[»]
2RIUX-ray1.70A1-204[»]
ProteinModelPortalQ5A3V6.
SMRQ5A3V6. Positions 3-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0003526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGCOG0108.
KOK02858.
OrthoDBEOG76TB2T.

Enzyme and pathway databases

UniPathwayUPA00275; UER00399.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
HAMAPMF_00180. RibB.
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMSSF55821. SSF55821. 1 hit.
TIGRFAMsTIGR00506. ribB. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ5A3V6.

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: February 19, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names