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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus haemolyticus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.By similarity

Pathway: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (folP)
  2. no protein annotated in this organism
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

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

GO - Molecular functioni

GO - Biological processi

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 haemolyticus
Taxonomic identifieri1283 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Dihydropteroate synthasePRO_0000168229Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ59919.
SMRiQ59919. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity

Sequence similaritiesi

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

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.

Q59919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTKIIGIL NVTPDSFSDG GKYNSVDKAI ARAKEMIDEG VDIIDVGGVS
60 70 80 90 100
TRPGHTEVSL EEEMERVVPV VEQLVKLDVQ ISVDTYRSEV AEACLKLGAT
110 120 130 140 150
MINDQWAGLY DPKIFDVVSD YNAEIVLMHN GDGQREQPVV EEMLLSLLTQ
160 170 180 190 200
ANKAEMAGIE KGNIWLDPGI GFAKSRSEEK EVMARLDELV ATEYPVLLAT
210 220 230 240 250
SRKRFIKEMI GKETTPAERD EATAATTVYG IMKGIQAVRV HNVDLNVKLA
260
QSIDFLKENE HERHHLS
Length:267
Mass (Da):29,613
Last modified:November 1, 1996 - v1
Checksum:i87807DFB3FBA8CBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40768 Genomic DNA. Translation: AAC43583.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40768 Genomic DNA. Translation: AAC43583.1.

3D structure databases

ProteinModelPortaliQ59919.
SMRiQ59919. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.

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]
ProtoNetiSearch...

Publicationsi

  1. "Functional cloning of the dihydropteroate synthase gene of Staphylococcus haemolyticus."
    Kellam P., Dallas W.S., Ballantine S.P., Delves C.J.
    FEMS Microbiol. Lett. 134:165-169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDHPS_STAHA
AccessioniPrimary (citable) accession number: Q59919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.