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Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, 7,8-dihydromonapterin and 7,8-dihydroxanthopterin, respectively, in equal quantities. After longer incubation times the only product is 6-hydroxymethyl-7,8-dihydropterin.1 Publication

Miscellaneous

Was identified as a high-confidence drug target.

Catalytic activityi

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.1 Publication
7,8-dihydroneopterin = 7,8-dihydromonapterin.1 Publication
7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde.1 Publication

Kineticsi

kcat is 0.0054 sec(-1) for the aldolase reaction with 7,8-dihydroneopterin as substrate. kcat is 0.006 sec(-1) for the aldolase reaction with 7,8-dihydromonapterin as substrate. kcat is 0.0015 sec(-1) for the epimerization of 7,8-dihydroneopterin. kcat is 0.0011 sec(-1) for the oxygenation reaction of 7,8-dihydroneopterin.1 Publication
  1. KM=0.165 µM for 7,8-dihydroneopterin in the aldolase reaction1 Publication
  2. KM=0.154 µM for 7,8-dihydromonapterin in the aldolase reaction1 Publication
  3. KM=0.154 µM for 7,8-dihydroneopterin in the epimerase reaction1 Publication
  4. KM=0.154 µM for 7,8-dihydroneopterin in the oxygenase reaction1 Publication

    Pathwayi: tetrahydrofolate biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. no protein annotated in this organism
    3. Dihydroneopterin aldolase (folB), 7,8-dihydroneopterin aldolase (LH57_19660)
    4. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (folK)
    This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei22SubstrateCombined sources1 Publication1
    Binding sitei54SubstrateCombined sources1 Publication1
    Active sitei99Proton donor/acceptorBy similarityCurated1

    GO - Molecular functioni

    GO - Biological processi

    • folic acid biosynthetic process Source: UniProtKB-KW
    • growth Source: MTBBASE
    • tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywordsi

    Molecular functionIsomerase, Lyase, Oxidoreductase
    Biological processFolate biosynthesis

    Enzyme and pathway databases

    BRENDAi4.1.2.25. 3445.
    UniPathwayiUPA00077; UER00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydroneopterin aldolase1 Publication (EC:4.1.2.251 Publication)
    Short name:
    DHNA1 Publication
    Alternative name(s):
    7,8-dihydroneopterin 2'-epimerase
    7,8-dihydroneopterin aldolase1 Publication
    7,8-dihydroneopterin epimerase (EC:5.1.99.81 Publication)
    7,8-dihydroneopterin hydroxylase (EC:1.13.11.811 Publication)
    Dihydroneopterin epimerase
    Dihydroneopterin hydroxylase
    Gene namesi
    Name:folB1 Publication
    Ordered Locus Names:Rv3607c
    ORF Names:MTCY07H7B.15
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv3607c.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001682751 – 133Dihydroneopterin aldolaseAdd BLAST133

    Proteomic databases

    PaxDbiP9WNC5.

    Interactioni

    Subunit structurei

    Homotetramer in the absence of substrate. Homooctamer in the presence of substrate.2 Publications

    Protein-protein interaction databases

    STRINGi83332.Rv3607c.

    Structurei

    Secondary structure

    1133
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 14Combined sources11
    Helixi22 – 25Combined sources4
    Beta strandi27 – 36Combined sources10
    Helixi40 – 45Combined sources6
    Helixi48 – 50Combined sources3
    Helixi54 – 66Combined sources13
    Beta strandi67 – 69Combined sources3
    Helixi73 – 85Combined sources13
    Beta strandi92 – 98Combined sources7
    Beta strandi105 – 107Combined sources3
    Beta strandi109 – 118Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NBUX-ray1.60A/B/C/D/E/F/G/H1-119[»]
    1Z9WX-ray2.50A1-133[»]
    ProteinModelPortaliP9WNC5.
    SMRiP9WNC5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni73 – 74Substrate bindingCombined sources1 Publication2

    Sequence similaritiesi

    Belongs to the DHNA family.Curated

    Phylogenomic databases

    eggNOGiENOG4105KRF. Bacteria.
    COG1539. LUCA.
    KOiK01633.
    OMAiFYAYHGV.
    PhylomeDBiP9WNC5.

    Family and domain databases

    CDDicd00534. DHNA_DHNTPE. 1 hit.
    InterProiView protein in InterPro
    IPR006156. Dihydroneopterin_aldolase.
    IPR006157. FolB_dom.
    PfamiView protein in Pfam
    PF02152. FolB. 1 hit.
    SMARTiView protein in SMART
    SM00905. FolB. 1 hit.
    TIGRFAMsiTIGR00525. folB. 1 hit.
    TIGR00526. folB_dom. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P9WNC5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MADRIELRGL TVHGRHGVYD HERVAGQRFV IDVTVWIDLA EAANSDDLAD
    60 70 80 90 100
    TYDYVRLASR AAEIVAGPPR KLIETVGAEI ADHVMDDQRV HAVEVAVHKP
    110 120 130
    QAPIPQTFDD VAVVIRRSRR GGRGWVVPAG GAV
    Length:133
    Mass (Da):14,552
    Last modified:April 16, 2014 - v1
    Checksum:iB7BD7CD0D71AFB54
    GO

    Mass spectrometryi

    Molecular mass is 16585 Da from positions 2 - 133. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46430.1.
    PIRiH70955.
    RefSeqiWP_003419537.1. NZ_KK339374.1.
    YP_177996.1. NC_000962.3.

    Genome annotation databases

    EnsemblBacteriaiCCP46430; CCP46430; Rv3607c.
    GeneIDi885345.
    KEGGimtu:Rv3607c.

    Similar proteinsi

    Entry informationi

    Entry nameiFOLB_MYCTU
    AccessioniPrimary (citable) accession number: P9WNC5
    Secondary accession number(s): L0TG79, O06275, P0A580
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: June 7, 2017
    This is version 21 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: 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