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Q81R22

- Q81R22_BACAN

UniProt

Q81R22 - Q81R22_BACAN

Protein

Dihydrofolate reductase

Gene

dfrA

Organism
Bacillus anthracis
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.UniRule annotation

    Catalytic activityi

    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81NADP; via amide nitrogen and carbonyl oxygenImported
    Binding sitei15 – 151NADP; via carbonyl oxygenImported
    Binding sitei79 – 791NADP
    Binding sitei96 – 961Trimethoprim 2
    Metal bindingi108 – 1081Calcium; via carbonyl oxygenImported
    Metal bindingi110 – 1101CalciumImported
    Metal bindingi147 – 1471CalciumImported

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 202NADPImported
    Nucleotide bindingi45 – 473NADPImported
    Nucleotide bindingi63 – 653NADPImported
    Nucleotide bindingi98 – 1014NADPImported

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. NADP binding Source: InterPro

    GO - Biological processi

    1. glycine biosynthetic process Source: InterPro
    2. nucleotide biosynthetic process Source: InterPro
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    OxidoreductaseUniRule annotationImported

    Keywords - Biological processi

    One-carbon metabolismUniRule annotation

    Keywords - Ligandi

    CalciumImported, Metal-bindingImported, NADPUniRule annotationImported, Nucleotide-bindingImported

    Enzyme and pathway databases

    BioCyciANTHRA:DFRA-MONOMER.
    BANT260799:GJAJ-2151-MONOMER.
    BANT261594:GJ7F-2226-MONOMER.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductaseUniRule annotation (EC:1.5.1.3UniRule annotation)
    Gene namesi
    Name:dfrAImported
    Ordered Locus Names:BA_2237Imported, BAS2083Imported, GBAA_2237Imported
    OrganismiBacillus anthracisImported
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000427: Chromosome, UP000005639: Chromosome, UP000000594: Chromosome

    Interactioni

    Protein-protein interaction databases

    STRINGi198094.BA_2237.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KGKNMR-A1-162[»]
    2QK8X-ray2.40A1-162[»]
    3DATX-ray2.30A1-162[»]
    3E0BX-ray2.25A/B1-162[»]
    3FL8X-ray2.29A/B/C/D/E/F/G/H1-162[»]
    3FL9X-ray2.40A/B/C/D/E/F/G/H1-162[»]
    3JVXX-ray2.25A/B1-162[»]
    3JW3X-ray2.57A/B1-162[»]
    3JW5X-ray2.89A/B1-162[»]
    3JWCX-ray2.57A/B1-162[»]
    3JWFX-ray2.57A/B1-162[»]
    3JWKX-ray2.08A/B1-162[»]
    3JWMX-ray2.57A/B1-162[»]
    3S9UX-ray1.90A/B1-162[»]
    3SA1X-ray2.50A/B1-162[»]
    3SA2X-ray2.25A/B1-162[»]
    3SAIX-ray2.25A/B1-162[»]
    4ELBX-ray2.60A/B/C/D/E/F/G/H1-162[»]
    4ELEX-ray2.35A/B/C/D/E/F/G/H1-162[»]
    4ELFX-ray2.30A/B/C/D/E/F/G/H1-162[»]
    4ELGX-ray2.10A/B/C/D/E/F/G/H1-162[»]
    4ELHX-ray2.10A/B/C/D/E/F/G/H1-162[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81R22.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 83Trimethoprim 2 binding

    Sequence similaritiesi

    Belongs to the dihydrofolate reductase family.UniRule annotation

    Phylogenomic databases

    KOiK00287.
    OMAiFKALTMG.
    OrthoDBiEOG6KT2V2.

    Family and domain databases

    Gene3Di3.40.430.10. 1 hit.
    InterProiIPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view]
    PfamiPF00186. DHFR_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000194. DHFR. 1 hit.
    PRINTSiPR00070. DHFR.
    SUPFAMiSSF53597. SSF53597. 1 hit.
    PROSITEiPS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q81R22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVSFMVAMD ENRVIGKDNN LPWRLPSELQ YVKKTTMGHP LIMGRKNYEA    50
    IGRPLPGRRN IIVTRNEGYH VEGCEVAHSV EEVFELCKNE EEIFIFGGAQ 100
    IYDLFLPYVD KLYITKIHHA FEGDTFFPEM DMTNWKEVFV EKGLTDEKNP 150
    YTYYYHVYEK QQ 162
    Length:162
    Mass (Da):19,125
    Last modified:June 1, 2003 - v1
    Checksum:i4259925DD9A1365A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP26114.1.
    AE017334 Genomic DNA. Translation: AAT31357.1.
    AY569129 Genomic DNA. Translation: AAT40581.1.
    AE017225 Genomic DNA. Translation: AAT54397.1.
    RefSeqiNP_844628.1. NC_003997.3.
    YP_018882.1. NC_007530.2.
    YP_028346.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP26114; AAP26114; BA_2237.
    AAT31357; AAT31357; GBAA_2237.
    AAT54397; AAT54397; BAS2083.
    GeneIDi1085515.
    2814627.
    2849969.
    KEGGiban:BA_2237.
    bar:GBAA_2237.
    bat:BAS2083.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP26114.1 .
    AE017334 Genomic DNA. Translation: AAT31357.1 .
    AY569129 Genomic DNA. Translation: AAT40581.1 .
    AE017225 Genomic DNA. Translation: AAT54397.1 .
    RefSeqi NP_844628.1. NC_003997.3.
    YP_018882.1. NC_007530.2.
    YP_028346.1. NC_005945.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KGK NMR - A 1-162 [» ]
    2QK8 X-ray 2.40 A 1-162 [» ]
    3DAT X-ray 2.30 A 1-162 [» ]
    3E0B X-ray 2.25 A/B 1-162 [» ]
    3FL8 X-ray 2.29 A/B/C/D/E/F/G/H 1-162 [» ]
    3FL9 X-ray 2.40 A/B/C/D/E/F/G/H 1-162 [» ]
    3JVX X-ray 2.25 A/B 1-162 [» ]
    3JW3 X-ray 2.57 A/B 1-162 [» ]
    3JW5 X-ray 2.89 A/B 1-162 [» ]
    3JWC X-ray 2.57 A/B 1-162 [» ]
    3JWF X-ray 2.57 A/B 1-162 [» ]
    3JWK X-ray 2.08 A/B 1-162 [» ]
    3JWM X-ray 2.57 A/B 1-162 [» ]
    3S9U X-ray 1.90 A/B 1-162 [» ]
    3SA1 X-ray 2.50 A/B 1-162 [» ]
    3SA2 X-ray 2.25 A/B 1-162 [» ]
    3SAI X-ray 2.25 A/B 1-162 [» ]
    4ELB X-ray 2.60 A/B/C/D/E/F/G/H 1-162 [» ]
    4ELE X-ray 2.35 A/B/C/D/E/F/G/H 1-162 [» ]
    4ELF X-ray 2.30 A/B/C/D/E/F/G/H 1-162 [» ]
    4ELG X-ray 2.10 A/B/C/D/E/F/G/H 1-162 [» ]
    4ELH X-ray 2.10 A/B/C/D/E/F/G/H 1-162 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198094.BA_2237.

    Chemistry

    ChEMBLi CHEMBL5270.

    Protocols and materials databases

    DNASUi 1085515.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP26114 ; AAP26114 ; BA_2237 .
    AAT31357 ; AAT31357 ; GBAA_2237 .
    AAT54397 ; AAT54397 ; BAS2083 .
    GeneIDi 1085515.
    2814627.
    2849969.
    KEGGi ban:BA_2237.
    bar:GBAA_2237.
    bat:BAS2083.

    Phylogenomic databases

    KOi K00287.
    OMAi FKALTMG.
    OrthoDBi EOG6KT2V2.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci ANTHRA:DFRA-MONOMER.
    BANT260799:GJAJ-2151-MONOMER.
    BANT261594:GJ7F-2226-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q81R22.

    Family and domain databases

    Gene3Di 3.40.430.10. 1 hit.
    InterProi IPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view ]
    Pfami PF00186. DHFR_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000194. DHFR. 1 hit.
    PRINTSi PR00070. DHFR.
    SUPFAMi SSF53597. SSF53597. 1 hit.
    PROSITEi PS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AmesImported, Ames ancestor and Sterne.
    2. "Functional cloning of Bacillus anthracis dihydrofolate reductase and confirmation of natural resistance to trimethoprim."
      Barrow E.W., Bourne P.C., Barrow W.W.
      Antimicrob. Agents Chemother. 48:4643-4649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: SterneImported.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase."
      Bennett B.C., Xu H., Simmerman R.F., Lee R.E., Dealwis C.G.
      J. Med. Chem. 50:4374-4381(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
    5. "Synthetic and crystallographic studies of a new inhibitor series targeting Bacillus anthracis dihydrofolate reductase."
      Beierlein J.M., Frey K.M., Bolstad D.B., Pelphrey P.M., Joska T.M., Smith A.E., Priestley N.D., Wright D.L., Anderson A.C.
      J. Med. Chem. 51:7532-7540(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP.
    6. "Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity."
      Bourne C.R., Bunce R.A., Bourne P.C., Berlin K.D., Barrow E.W., Barrow W.W.
      Antimicrob. Agents Chemother. 53:3065-3073(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH CALCIUM.
    7. "The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors."
      Beierlein J.M., Deshmukh L., Frey K.M., Vinogradova O., Anderson A.C.
      Biochemistry 48:4100-4108(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH NADP.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate PortonImported, Ames AncestorImported, Ames ancestorImported and SterneImported.
    9. "X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design."
      Bennett B.C., Wan Q., Ahmad M.F., Langan P., Dealwis C.G.
      J. Struct. Biol. 166:162-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NADP.
    10. "Mutational Studies into Trimethoprim Resistance in Bacillus anthracis Dihydrofolate Reductase."
      Beierlein J.M., Karri N.G., Anderson A.C.
      Submitted (SEP-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH NADP.
    11. Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., Sutton G.
      Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: AmesImported.
    12. "SAR studies of heterocyclic propargyl-linked TMP analogs targeting Bacillus dihydrofolate reductase."
      Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
      Submitted (JUN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP.
    13. "SAR studies of heterocyclic propargyl-linked TMP analogs to Bacillus dihydrofolate reductase."
      Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
      Submitted (JUN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP.
    14. "Structure-Activity Studies of Heterocyclic Propargyl-linked TMP Analogs Targeting Bacillus anthracis Dihydrofolate Reductase."
      Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
      Submitted (JUN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP.
    15. "Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase."
      Bourne C.R., Wakeham N., Nammalwar B., Tseitin V., Bourne P.C., Barrow E.W., Mylvaganam S., Ramnarayan K., Bunce R.A., Berlin K.D., Barrow W.W.
      Biochim. Biophys. Acta 1834:46-52(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).

    Entry informationi

    Entry nameiQ81R22_BACAN
    AccessioniPrimary (citable) accession number: Q81R22
    Secondary accession number(s): E9R6R2
    , E9R6R3, E9R6R4, Q68SA0, Q6HZ92, Q6KT86
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 1, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3