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P0A017

- DYR_STAAU

UniProt

P0A017 - DYR_STAAU

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Protein

Dihydrofolate reductase

Gene

folA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Substrate
Binding sitei58 – 581Substrate
Binding sitei101 – 1011NADP1 Publication
Binding sitei112 – 1121Substrate
Binding sitei122 – 1221NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 82NADP1 Publication
Nucleotide bindingi15 – 206NADP1 Publication
Nucleotide bindingi44 – 474NADP1 Publication
Nucleotide bindingi63 – 664NADP1 Publication
Nucleotide bindingi93 – 986NADP1 Publication

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. 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

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Short name:
DHFR
Gene namesi
Name:folA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 159158Dihydrofolate reductasePRO_0000186411Add
BLAST

Proteomic databases

PRIDEiP0A017.

Interactioni

Structurei

Secondary structure

1
159
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi14 – 174
Helixi26 – 3611
Beta strandi39 – 446
Helixi45 – 517
Beta strandi58 – 636
Beta strandi75 – 773
Helixi80 – 856
Beta strandi90 – 945
Helixi96 – 1027
Turni103 – 1053
Beta strandi107 – 1148
Beta strandi121 – 1233
Turni129 – 1313
Beta strandi132 – 1398
Beta strandi150 – 1578

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W9GX-ray1.95A1-159[»]
2W9HX-ray1.48A1-159[»]
3FRAX-ray2.35X2-159[»]
3FRBX-ray2.00X2-159[»]
3FRDX-ray2.10X2-159[»]
3FREX-ray2.20X2-159[»]
3FRFX-ray2.20X2-159[»]
3FY8X-ray2.20X2-159[»]
3FY9X-ray2.25X2-159[»]
3FYVX-ray2.20X2-159[»]
3FYWX-ray2.10X2-159[»]
3I8AX-ray2.41X2-158[»]
3LG4X-ray3.15A/B1-158[»]
3M08X-ray2.01A2-158[»]
3M09X-ray2.01A2-158[»]
3SGYX-ray2.60A/B2-158[»]
3SH2X-ray3.00A/B2-158[»]
3SQYX-ray1.50X1-159[»]
3SR5X-ray1.68X2-159[»]
3SRQX-ray1.69X1-159[»]
3SRRX-ray1.70X1-159[»]
3SRSX-ray1.70X1-159[»]
3SRUX-ray1.70X1-159[»]
3SRWX-ray1.70X1-159[»]
4FGGX-ray2.30A1-159[»]
4FGHX-ray2.50A1-159[»]
4LAEX-ray1.69X1-159[»]
4LAGX-ray1.70X1-159[»]
4LAHX-ray1.88X1-159[»]
4LEKX-ray1.70X1-159[»]
ProteinModelPortaliP0A017.
SMRiP0A017. Positions 2-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156DHFRPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0262.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A017 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES
60 70 80 90 100
IGKPLPNRRN VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE
110 120 130 140 150
EMIDKVDDMY ITVIEGKFRG DTFFPPYTFE DWEVASSVEG KLDEKNTIPH

TFLHLIRKK
Length:159
Mass (Da):18,251
Last modified:January 23, 2007 - v2
Checksum:i811898409FEAFAAB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z16422 Genomic DNA. Translation: CAA78910.1.
PIRiS32014.
RefSeqiWP_000175746.1. NZ_JJOP01000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z16422 Genomic DNA. Translation: CAA78910.1 .
PIRi S32014.
RefSeqi WP_000175746.1. NZ_JJOP01000008.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2W9G X-ray 1.95 A 1-159 [» ]
2W9H X-ray 1.48 A 1-159 [» ]
3FRA X-ray 2.35 X 2-159 [» ]
3FRB X-ray 2.00 X 2-159 [» ]
3FRD X-ray 2.10 X 2-159 [» ]
3FRE X-ray 2.20 X 2-159 [» ]
3FRF X-ray 2.20 X 2-159 [» ]
3FY8 X-ray 2.20 X 2-159 [» ]
3FY9 X-ray 2.25 X 2-159 [» ]
3FYV X-ray 2.20 X 2-159 [» ]
3FYW X-ray 2.10 X 2-159 [» ]
3I8A X-ray 2.41 X 2-158 [» ]
3LG4 X-ray 3.15 A/B 1-158 [» ]
3M08 X-ray 2.01 A 2-158 [» ]
3M09 X-ray 2.01 A 2-158 [» ]
3SGY X-ray 2.60 A/B 2-158 [» ]
3SH2 X-ray 3.00 A/B 2-158 [» ]
3SQY X-ray 1.50 X 1-159 [» ]
3SR5 X-ray 1.68 X 2-159 [» ]
3SRQ X-ray 1.69 X 1-159 [» ]
3SRR X-ray 1.70 X 1-159 [» ]
3SRS X-ray 1.70 X 1-159 [» ]
3SRU X-ray 1.70 X 1-159 [» ]
3SRW X-ray 1.70 X 1-159 [» ]
4FGG X-ray 2.30 A 1-159 [» ]
4FGH X-ray 2.50 A 1-159 [» ]
4LAE X-ray 1.69 X 1-159 [» ]
4LAG X-ray 1.70 X 1-159 [» ]
4LAH X-ray 1.88 X 1-159 [» ]
4LEK X-ray 1.70 X 1-159 [» ]
ProteinModelPortali P0A017.
SMRi P0A017. Positions 2-158.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P0A017.
ChEMBLi CHEMBL1681620.

Proteomic databases

PRIDEi P0A017.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0262.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Miscellaneous databases

EvolutionaryTracei P0A017.

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. "Characterization of the gene for chromosomal trimethoprim-sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923."
    Dale G.E., Then R.L., Stueber D.
    Antimicrob. Agents Chemother. 37:1400-1405(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
  2. "N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus."
    Hartman P.G., Stahli M., Kocher H.P., Then R.L.
    FEBS Lett. 242:157-160(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
    Strain: 157/4696.
  3. "Inhibitory properties and X-ray crystallographic study of the binding of AR-101, AR-102 and iclaprim in ternary complexes with NADPH and dihydrofolate reductase from Staphylococcus aureus."
    Oefner C., Parisi S., Schulz H., Lociuro S., Dale G.E.
    Acta Crystallogr. D 65:751-757(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-159.
  4. "Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim."
    Heaslet H., Harris M., Fahnoe K., Sarver R., Putz H., Chang J., Subramanyam C., Barreiro G., Miller J.R.
    Proteins 76:706-717(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH NADPH AND TRIMETHOPRIM.

Entry informationi

Entry nameiDYR_STAAU
AccessioniPrimary (citable) accession number: P0A017
Secondary accession number(s): P10167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two DhfR isozymes in S.aureus, this one is chromosomal and is sensitive to trimethoprim.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3