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O05701

- DHPS_STAAU

UniProt

O05701 - DHPS_STAAU

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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide.1 Publication

Catalytic activityi

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

Cofactori

Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Magnesium
Binding sitei19 – 191Substrate
Binding sitei84 – 841Substrate
Binding sitei103 – 1031Substrate
Binding sitei167 – 1671Substrate
Binding sitei203 – 2031Substrate
Binding sitei239 – 2391Substrate
Binding sitei241 – 2411Substrate

GO - Molecular functioni

  1. dihydropteroate synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. response to antibiotic Source: UniProtKB-KW
  3. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic resistance, Folate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteroate synthase (EC:2.5.1.15)
Short name:
DHPS
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene namesi
Name:folP
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Dihydropteroate synthasePRO_0000168225Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi14 – 163Combined sources
Turni20 – 234Combined sources
Helixi26 – 3813Combined sources
Beta strandi42 – 487Combined sources
Helixi60 – 7415Combined sources
Beta strandi77 – 848Combined sources
Helixi88 – 969Combined sources
Beta strandi101 – 1044Combined sources
Turni105 – 1084Combined sources
Helixi114 – 1207Combined sources
Beta strandi124 – 1285Combined sources
Helixi139 – 15618Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1674Combined sources
Helixi176 – 1849Combined sources
Helixi186 – 1905Combined sources
Beta strandi196 – 1983Combined sources
Helixi204 – 2074Combined sources
Beta strandi210 – 2123Combined sources
Helixi216 – 2194Combined sources
Helixi220 – 23314Combined sources
Beta strandi237 – 2415Combined sources
Helixi243 – 26220Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD1X-ray2.20A/B2-267[»]
1AD4X-ray2.40A/B2-267[»]
ProteinModelPortaliO05701.
SMRiO05701. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO05701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 251251Pterin-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 522Substrate binding

Sequence similaritiesi

Belongs to the DHPS family.Curated
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0294.

Family and domain databases

Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamiPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMiSSF51717. SSF51717. 1 hit.
TIGRFAMsiTIGR01496. DHPS. 1 hit.
PROSITEiPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O05701-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKTKIMGIL NVTPDSFSDG GKFNNVESAV TRVKAMMDEG ADIIDVGGVS
60 70 80 90 100
TRPGHEMITV EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD
110 120 130 140 150
IINDQWAGLY DHRMFQVVAK YDAEIVLMHN GNGNRDEPVV EEMLTSLLAQ
160 170 180 190 200
AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA EVMARLDELV ATEYPVLLAT
210 220 230 240 250
SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV HNVELNAKLA
260
KGIDFLKENE NARHNFS
Length:267
Mass (Da):29,498
Last modified:July 1, 1997 - v1
Checksum:iF9FB01B1EAFBC275
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z84573 Genomic DNA. Translation: CAB06539.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z84573 Genomic DNA. Translation: CAB06539.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AD1 X-ray 2.20 A/B 2-267 [» ]
1AD4 X-ray 2.40 A/B 2-267 [» ]
ProteinModelPortali O05701.
SMRi O05701. Positions 2-265.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0294.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00156 .

Miscellaneous databases

EvolutionaryTracei O05701.

Family and domain databases

Gene3Di 3.20.20.20. 1 hit.
InterProi IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view ]
Pfami PF00809. Pterin_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF51717. SSF51717. 1 hit.
TIGRFAMsi TIGR01496. DHPS. 1 hit.
PROSITEi PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure and function of the dihydropteroate synthase from Staphylococcus aureus."
    Hampele I.C., D'Arcy A., Dale G.E., Kostrewa D., Nielsen J., Oefner C., Page M.G.P., Schoenfeld H.-J., Stueber D., Then R.L.
    J. Mol. Biol. 268:21-30(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS; HYDROXYMETHYLPTERIN PYROPHOSPHATE, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.

Entry informationi

Entry nameiDHPS_STAAU
AccessioniPrimary (citable) accession number: O05701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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