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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
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:itetrahydrofolate 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 sitei89 – 891SubstrateBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Binding sitei172 – 1721SubstrateBy similarity
Binding sitei208 – 2081SubstrateBy similarity
Binding sitei244 – 2441SubstrateBy similarity
Binding sitei246 – 2461SubstrateBy 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

BioCyciSEPI176279:GJJB-157-MONOMER.
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
Ordered Locus Names:SERP0153
OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Taxonomic identifieri176279 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000531 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Dihydropteroate synthasePRO_0000168228Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi176279.SERP0153.

Structurei

3D structure databases

ProteinModelPortaliQ5HRP0.
SMRiQ5HRP0. Positions 3-270.
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

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217509.
KOiK00796.
OMAiSIDTYHA.
OrthoDBiEOG67T5P5.

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.

Q5HRP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKTKIMGIL NVTPDSFSDG GQYHSVDQAV KRAKEMIDEG VDIIDVGGVS
60 70 80 90 100
TRPGHKEVSH KEVSLKEEMN RVLPVVESIV KYDVQISVDT FRSEVAEACL
110 120 130 140 150
KLGVSMINDQ WAGLFDSNMF NVVSQYGAEI VLMHNGDGHR DKPVVEEMLV
160 170 180 190 200
SLLAQANKAE LAGIPHNKIW LDPGIGFAKT REEENEVMAR LDELVATEYP
210 220 230 240 250
VLLATSRKRY IKEMMNQDSS PSDRDEATAA TTAYGIMKGV RGVRVHNVLL
260 270
NTRLAQSMDF LKENEYERHH LS
Length:272
Mass (Da):30,373
Last modified:February 15, 2005 - v1
Checksum:i5A9CE9F3822019B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000029 Genomic DNA. Translation: AAW53522.1.
RefSeqiWP_002457105.1. NC_002976.3.

Genome annotation databases

EnsemblBacteriaiAAW53522; AAW53522; SERP0153.
KEGGiser:SERP0153.
PATRICi19611163. VBIStaEpi130894_0144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000029 Genomic DNA. Translation: AAW53522.1.
RefSeqiWP_002457105.1. NC_002976.3.

3D structure databases

ProteinModelPortaliQ5HRP0.
SMRiQ5HRP0. Positions 3-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176279.SERP0153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW53522; AAW53522; SERP0153.
KEGGiser:SERP0153.
PATRICi19611163. VBIStaEpi130894_0144.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217509.
KOiK00796.
OMAiSIDTYHA.
OrthoDBiEOG67T5P5.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BioCyciSEPI176279:GJJB-157-MONOMER.

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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
    Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
    , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
    J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35984 / RP62A.

Entry informationi

Entry nameiDHPS_STAEQ
AccessioniPrimary (citable) accession number: Q5HRP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: July 22, 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

Keywords - Technical termi

Complete proteome, Reference proteome

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.