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Protein

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

Gene

RIB3

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 divalent metal cations per subunit. Magnesium or manganese.By similarity

Kineticsi

  1. KM=37 µM for ribulose-5-phosphate1 Publication

Vmax=332 nmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301Magnesium or manganese 1By similarity
Metal bindingi30 – 301Magnesium or manganese 2By similarity
Binding sitei34 – 341Substrate1 Publication
Sitei128 – 1281Essential for catalytic activityBy similarity
Metal bindingi145 – 1451Magnesium or manganese 2By similarity
Binding sitei166 – 1661SubstrateBy similarity
Sitei166 – 1661Essential for catalytic activity

GO - Molecular functioni

  1. 3,4-dihydroxy-2-butanone-4-phosphate synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Riboflavin biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.99.12. 1096.
UniPathwayiUPA00275; UER00399.

Names & Taxonomyi

Protein namesi
Recommended name:
3,4-dihydroxy-2-butanone 4-phosphate synthase (EC:4.1.99.12)
Short name:
DHBP synthase
Gene namesi
Name:RIB3
ORF Names:CaO19.12693, CaO19.5228
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591C → A: Increases Km for substrate 18-fold. Reduces activity by 30%.
Mutagenesisi87 – 871Y → A: Increases Km for substrate 4-fold. Reduces activity by 98%. 1 Publication
Mutagenesisi92 – 921D → A: Loss of activity. Alters protein folding and stability. 1 Publication
Mutagenesisi166 – 1661E → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2042043,4-dihydroxy-2-butanone 4-phosphate synthasePRO_0000296685Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi5476.CAL0003526.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Beta strandi21 – 277Combined sources
Beta strandi34 – 385Combined sources
Helixi39 – 413Combined sources
Helixi44 – 529Combined sources
Beta strandi59 – 635Combined sources
Helixi64 – 696Combined sources
Beta strandi91 – 944Combined sources
Beta strandi98 – 1003Combined sources
Helixi103 – 11412Combined sources
Helixi120 – 1223Combined sources
Beta strandi123 – 13412Combined sources
Helixi138 – 1403Combined sources
Helixi145 – 15511Combined sources
Beta strandi160 – 1689Combined sources
Turni170 – 1723Combined sources
Helixi178 – 18811Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 2028Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TKSX-ray1.60A/B1-204[»]
1TKUX-ray1.66A/B1-204[»]
2RISX-ray1.60A1-204[»]
2RIUX-ray1.70A1-204[»]
ProteinModelPortaliQ5A3V6.
SMRiQ5A3V6. Positions 3-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5A3V6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 302Substrate bindingBy similarity
Regioni142 – 1465Substrate binding

Sequence similaritiesi

Belongs to the DHBP synthase family.Curated

Phylogenomic databases

eggNOGiCOG0108.
InParanoidiQ5A3V6.
KOiK02858.
OrthoDBiEOG76TB2T.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00180. RibB.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00506. ribB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5A3V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNIFTPIEE ALEAYKNGEF LIVMDDEDRE NEGDLIMAAE LITQEKMAFL
60 70 80 90 100
VRYSSGYVCV PLSEERANQL ELPPMLANRS DRHGTAYTIT CDFAEGTTTG
110 120 130 140 150
ISAHDRALTT RSLANPNSKP QDFIKPGHIL PLRAVPGLLK KRRGHTEAAV
160 170 180 190 200
QLSTLAGLQP AGVICELVRD EDGLMMRLDD CIQFGKKHGI KIININQLVE

YISK
Length:204
Mass (Da):22,658
Last modified:July 23, 2007 - v2
Checksum:i5FEC62C3ABDA822E
GO

Sequence cautioni

The sequence EAK97301.1 differs from that shown. Reason: Frameshift at position 117. Curated
The sequence EAK97301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAK97363.1 differs from that shown. Reason: Erroneous initiation. Curated

Mass spectrometryi

Molecular mass is 22530 Da from positions 2 - 204. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000070 Genomic DNA. Translation: EAK97363.1. Different initiation.
AACQ01000071 Genomic DNA. Translation: EAK97301.1. Sequence problems.
RefSeqiXP_716297.1. XM_711204.1.
XP_716359.1. XM_711266.1.

Genome annotation databases

GeneIDi3641955.
3642062.
KEGGical:CaO19.12693.
cal:CaO19.5228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000070 Genomic DNA. Translation: EAK97363.1. Different initiation.
AACQ01000071 Genomic DNA. Translation: EAK97301.1. Sequence problems.
RefSeqiXP_716297.1. XM_711204.1.
XP_716359.1. XM_711266.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TKSX-ray1.60A/B1-204[»]
1TKUX-ray1.66A/B1-204[»]
2RISX-ray1.60A1-204[»]
2RIUX-ray1.70A1-204[»]
ProteinModelPortaliQ5A3V6.
SMRiQ5A3V6. Positions 3-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5476.CAL0003526.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3641955.
3642062.
KEGGical:CaO19.12693.
cal:CaO19.5228.

Phylogenomic databases

eggNOGiCOG0108.
InParanoidiQ5A3V6.
KOiK02858.
OrthoDBiEOG76TB2T.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00399.
BRENDAi4.1.99.12. 1096.

Miscellaneous databases

EvolutionaryTraceiQ5A3V6.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00180. RibB.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00506. ribB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(2003) [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.

Entry informationi

Entry nameiRIB3_CANAL
AccessioniPrimary (citable) accession number: Q5A3V6
Secondary accession number(s): Q5A3P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 23, 2007
Last sequence update: July 23, 2007
Last modified: March 31, 2015
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.