O05701 (DHPS_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydropteroate synthase
Short name=DHPS
EC=2.5.1.15

Alternative name(s):
Dihydropteroate pyrophosphorylase

Gene names

Name:

folP

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide. Ref.1
Catalytic activity	(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. Ref.1
Cofactor	Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Subunit structure	Homodimer. Ref.1
Sequence similarities	Belongs to the DHPS family. Contains 1 pterin-binding domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Folate biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dihydropteroate synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Dihydropteroate synthase

PRO_0000168225

Regions

Domain

1 – 251

251

Pterin-binding

Region

51 – 52

2

Substrate binding

Sites

Metal binding

11

1

Magnesium

Binding site

19

1

Substrate

Binding site

84

1

Substrate

Binding site

103

1

Substrate

Binding site

167

1

Substrate

Binding site

203

1

Substrate

Binding site

239

1

Substrate

Binding site

241

1

Substrate

Secondary structure

1

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267

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

14 – 16

3

Turn

20 – 23

4

Helix

26 – 38

13

Beta strand

42 – 48

7

Helix

60 – 74

15

Beta strand

77 – 84

8

Helix

88 – 96

9

Beta strand

101 – 104

4

Turn

105 – 108

4

Helix

114 – 120

7

Beta strand

124 – 128

5

Helix

139 – 156

18

Helix

161 – 163

3

Beta strand

164 – 167

4

Helix

176 – 184

9

Helix

186 – 190

5

Beta strand

196 – 198

3

Helix

204 – 207

4

Beta strand

210 – 212

3

Helix

216 – 219

4

Helix

220 – 233

14

Beta strand

237 – 241

5

Helix

243 – 262

20

Sequences

	Sequence		Length	Mass (Da)
	O05701 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: F9FB01B1EAFBC275	FASTA	267	29,498
	10 20 30 40 50 60 MTKTKIMGIL NVTPDSFSDG GKFNNVESAV TRVKAMMDEG ADIIDVGGVS TRPGHEMITV 70 80 90 100 110 120 EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD IINDQWAGLY DHRMFQVVAK 130 140 150 160 170 180 YDAEIVLMHN GNGNRDEPVV EEMLTSLLAQ AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA 190 200 210 220 230 240 EVMARLDELV ATEYPVLLAT SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV 250 260 HNVELNAKLA KGIDFLKENE NARHNFS

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z84573 Genomic DNA. Translation: CAB06539.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O05701.

SMR

O05701. Positions 2-265.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG0294.

Enzyme and pathway databases

UniPathway

UPA00077; UER00156.

Family and domain databases

Gene3D

3.20.20.20. 1 hit.

InterPro

IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]

Pfam

PF00809. Pterin_bind. 1 hit.
[Graphical view]

SUPFAM

SSF51717. DHP_synth_like. 1 hit.

TIGRFAMs

TIGR01496. DHPS. 1 hit.

PROSITE

PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O05701.

Entry information

Entry name

DHPS_STAAU

Accession

Primary (citable) accession number: O05701

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program