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Q5A3V6

- RIB3_CANAL

UniProt

Q5A3V6 - RIB3_CANAL

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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: 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

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.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: CGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. riboflavin biosynthetic process Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Riboflavin biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

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: 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 – 169
Beta strandi21 – 277
Beta strandi34 – 385
Helixi39 – 413
Helixi44 – 529
Beta strandi59 – 635
Helixi64 – 696
Beta strandi91 – 944
Beta strandi98 – 1003
Helixi103 – 11412
Helixi120 – 1223
Beta strandi123 – 13412
Helixi138 – 1403
Helixi145 – 15511
Beta strandi160 – 1689
Turni170 – 1723
Helixi178 – 18811
Beta strandi192 – 1943
Helixi195 – 2028

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 24, 2007 - v2
Checksum:i5FEC62C3ABDA822E
GO

Sequence cautioni

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

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000070 Genomic DNA. Translation: EAK97363.1 . Different initiation.
AACQ01000071 Genomic DNA. Translation: EAK97301.1 . Sequence problems.
RefSeqi XP_716297.1. XM_711204.1.
XP_716359.1. XM_711266.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q5A3V6.
SMRi Q5A3V6. Positions 3-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5476.CAL0003526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3641955.
3642062.
KEGGi cal:CaO19.12693.
cal:CaO19.5228.

Phylogenomic databases

eggNOGi COG0108.
InParanoidi Q5A3V6.
KOi K02858.
OrthoDBi EOG76TB2T.

Enzyme and pathway databases

UniPathwayi UPA00275 ; UER00399 .

Miscellaneous databases

EvolutionaryTracei Q5A3V6.

Family and domain databases

Gene3Di 3.90.870.10. 1 hit.
HAMAPi MF_00180. RibB.
InterProi IPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view ]
Pfami PF00926. DHBP_synthase. 1 hit.
[Graphical view ]
SUPFAMi SSF55821. SSF55821. 1 hit.
TIGRFAMsi TIGR00506. ribB. 1 hit.
ProtoNeti Search...

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(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.

Entry informationi

Entry nameiRIB3_CANAL
AccessioniPrimary (citable) accession number: Q5A3V6
Secondary accession number(s): Q5A3P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: October 29, 2014
This is version 63 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