Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -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. 7,8-dihydroneopterin aldolase (LH57_19660), Dihydroneopterin aldolase (folB)
    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

    Keywordsi

    Molecular functionIsomerase, Lyase, Oxidoreductase
    Biological processFolate biosynthesis

    Enzyme and pathway databases

    BRENDAi4.1.2.25 3445
    UniPathwayi
    UPA00077;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

    3D structure databases

    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

    Cross-referencesi

    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

    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...

    Protein-protein interaction databases

    STRINGi83332.Rv3607c

    Proteomic databases

    PaxDbiP9WNC5

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP46430; CCP46430; Rv3607c
    GeneIDi885345
    KEGGimtu:Rv3607c

    Organism-specific databases

    TubercuListiRv3607c

    Phylogenomic databases

    eggNOGiENOG4105KRF Bacteria
    COG1539 LUCA
    KOiK01633
    OMAiFYAYHGV
    PhylomeDBiP9WNC5

    Enzyme and pathway databases

    UniPathwayi
    UPA00077;UER00154

    BRENDAi4.1.2.25 3445

    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
    ProtoNetiSearch...

    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: September 12, 2018
    This is version 23 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again