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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus aureus (strain COL)
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

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl 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

Pathwayi

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

BioCyciSAUR93062:GCEP-548-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:SACOL0558
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000530 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Dihydropteroate synthasePRO_0000168220Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi93062.SACOL0558.

Structurei

3D structure databases

ProteinModelPortaliQ5HIG1.
SMRiQ5HIG1. 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

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.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5HIG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTKIMGIL NVTPDSFSDG GKFNNVESAI NRVKAMIDEG ADIIDVGGVS
60 70 80 90 100
MRPGHEMVSL EEEMNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD
110 120 130 140 150
MINDQWAGLY DHRMFQIVAK YDAEIILMHN GNGNRDEPVV EEMLTSLLAQ
160 170 180 190 200
AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA EVMARLDELV ATEYPVLLAT
210 220 230 240 250
SRKRFTKKMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV HNVELNAKLA
260
KGIDFLKENE NARHNLS
Length:267
Mass (Da):29,552
Last modified:February 15, 2005 - v1
Checksum:i12A65C8540EC223C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW37670.1.
RefSeqiWP_000167922.1. NC_002951.2.
YP_185446.1. NC_002951.2.

Genome annotation databases

EnsemblBacteriaiAAW37670; AAW37670; SACOL0558.
KEGGisac:SACOL0558.
PATRICi19527362. VBIStaAur112458_0543.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW37670.1.
RefSeqiWP_000167922.1. NC_002951.2.
YP_185446.1. NC_002951.2.

3D structure databases

ProteinModelPortaliQ5HIG1.
SMRiQ5HIG1. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0558.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW37670; AAW37670; SACOL0558.
KEGGisac:SACOL0558.
PATRICi19527362. VBIStaAur112458_0543.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217509.
KOiK00796.
OMAiSIDTYHA.
OrthoDBiEOG67T5P5.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BioCyciSAUR93062:GCEP-548-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.
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: COL.

Entry informationi

Entry nameiDHPS_STAAC
AccessioniPrimary (citable) accession number: Q5HIG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: May 27, 2015
This is version 72 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

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.