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Q5A3V6

- RIB3_CANAL

UniProt

Q5A3V6 - RIB3_CANAL

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
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
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    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

    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    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.
    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

    MTNIFTPIEE ALEAYKNGEF LIVMDDEDRE NEGDLIMAAE LITQEKMAFL    50
    VRYSSGYVCV PLSEERANQL ELPPMLANRS DRHGTAYTIT CDFAEGTTTG 100
    ISAHDRALTT RSLANPNSKP QDFIKPGHIL PLRAVPGLLK KRRGHTEAAV 150
    QLSTLAGLQP AGVICELVRD EDGLMMRLDD CIQFGKKHGI KIININQLVE 200
    YISK 204
    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.
    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

    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 1, 2014
    This is version 62 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