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Q81R22

- Q81R22_BACAN

UniProt

Q81R22 - Q81R22_BACAN

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Protein

Dihydrofolate reductase

Gene

dfrA

Organism
Bacillus anthracis
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
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
Complete GO annotation...

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
Synonyms:dfrDImported
Ordered Locus Names:BA_2237Imported, BAS2083Imported, GBAA_2237Imported
ORF Names:DH23_2166Imported, DJ42_799Imported, DJ43_1447Imported, DJ44_442Imported, DJ45_3684Imported, DJ48_2031Imported, DJ49_2771Imported, HYU01_11160Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_2237.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

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

        10         20         30         40         50
MIVSFMVAMD ENRVIGKDNN LPWRLPSELQ YVKKTTMGHP LIMGRKNYEA
60 70 80 90 100
IGRPLPGRRN IIVTRNEGYH VEGCEVAHSV EEVFELCKNE EEIFIFGGAQ
110 120 130 140 150
IYDLFLPYVD KLYITKIHHA FEGDTFFPEM DMTNWKEVFV EKGLTDEKNP
160
YTYYYHVYEK QQ
Length:162
Mass (Da):19,125
Last modified:June 1, 2003 - v1
Checksum:i4259925DD9A1365A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CP008846 Genomic DNA. Translation: AIF56465.1.
CP007660 Genomic DNA. Translation: AIK08291.1.
CP007618 Genomic DNA. Translation: AIK33852.1.
CP008752 Genomic DNA. Translation: AIK54032.1.
CP007704 Genomic DNA. Translation: AIK57700.1.
JNOD01000013 Genomic DNA. Translation: KFJ81276.1.
JMPV01000008 Genomic DNA. Translation: KFL65433.1.
JMPU01000016 Genomic DNA. Translation: KFL69605.1.
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:
EMBLi
GenBanki
DDBJi
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 .
CP008846 Genomic DNA. Translation: AIF56465.1 .
CP007660 Genomic DNA. Translation: AIK08291.1 .
CP007618 Genomic DNA. Translation: AIK33852.1 .
CP008752 Genomic DNA. Translation: AIK54032.1 .
CP007704 Genomic DNA. Translation: AIK57700.1 .
JNOD01000013 Genomic DNA. Translation: KFJ81276.1 .
JMPV01000008 Genomic DNA. Translation: KFL65433.1 .
JMPU01000016 Genomic DNA. Translation: KFL69605.1 .
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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 and Ames / isolate PortonImported.
  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].
    Strain: SterneImported.
  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 ancestorImported and Ames AncestorImported.
  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).
  16. "Complete Genome Sequence of Bacillus anthracis HYU01, Isolated from Soil Samples in the Korean Peninsula."
    Kim S.K., Chung W.H., Kim S.H., Jung K.H., Kim N., Chai Y.G.
    Genome Announc. 2:e00769-14(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HYU01Imported.
  17. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2000031021Imported, A.Br.003Imported, Smith 1013Imported and Zimbabwe 89Imported.
  18. "Draft Genome Sequence of Bacillus anthracis STI."
    Okinaka R.T., Challacombe J.F., Drees K., Birdsell D.N., Janke N., Naumann A., Seymour M., O'Neill H.H., Schupp J., Sahl J., Foster J.T., Pearson T., Keim P.
    Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: STI-1Imported.
  19. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BFVImported.
  20. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Delta SterneImported.

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: November 26, 2014
This is version 108 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