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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi: 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)DescriptionActionsGraphical viewLength
Metal bindingi11MagnesiumBy similarity1
Binding sitei516-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei846-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei1036-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei1676-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei2036-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

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
Ordered Locus Names:SAV0514
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001682211 – 267Dihydropteroate synthaseAdd BLAST267

Proteomic databases

PaxDbiP64141.

2D gel databases

World-2DPAGE0002:P64141.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi158878.SAV0514.

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi25 – 38Combined sources14
Beta strandi42 – 48Combined sources7
Helixi60 – 74Combined sources15
Beta strandi77 – 84Combined sources8
Helixi88 – 97Combined sources10
Beta strandi101 – 104Combined sources4
Turni105 – 108Combined sources4
Helixi114 – 120Combined sources7
Beta strandi124 – 128Combined sources5
Helixi139 – 156Combined sources18
Helixi161 – 163Combined sources3
Beta strandi164 – 167Combined sources4
Helixi176 – 183Combined sources8
Helixi186 – 190Combined sources5
Beta strandi196 – 198Combined sources3
Helixi204 – 210Combined sources7
Helixi217 – 219Combined sources3
Helixi220 – 233Combined sources14
Beta strandi237 – 241Combined sources5
Helixi243 – 262Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HB7X-ray1.95A/B1-267[»]
ProteinModelPortaliP64141.
SMRiP64141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 251Pterin-bindingPROSITE-ProRule annotationAdd BLAST251

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni239 – 2416-hydroxymethyl-7,8-dihydropterin diphosphate bindingBy similarity3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EEI. Bacteria.
COG0294. LUCA.
HOGENOMiHOG000217509.
KOiK00796.
OMAiSIDTYHA.
PhylomeDBiP64141.

Family and domain databases

CDDicd00739. DHPS. 1 hit.
Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding_dom.
[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.

P64141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTKIMGIL NVTPDSFSDG GKFNNVETAI NRVKAMIDEG ADIIDVGGVS
60 70 80 90 100
TRPGHEMVTL EEELNRVLPV 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
SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV HNVELNAKLA
260
KGIDFLKENE NARHNLS
Length:267
Mass (Da):29,533
Last modified:October 11, 2004 - v1
Checksum:iA2E41F5C5544D86C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56676.1.
RefSeqiWP_000167944.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB56676; BAB56676; SAV0514.
KEGGisav:SAV0514.
PATRICi19561650. VBIStaAur52173_0518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56676.1.
RefSeqiWP_000167944.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HB7X-ray1.95A/B1-267[»]
ProteinModelPortaliP64141.
SMRiP64141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV0514.

2D gel databases

World-2DPAGE0002:P64141.

Proteomic databases

PaxDbiP64141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB56676; BAB56676; SAV0514.
KEGGisav:SAV0514.
PATRICi19561650. VBIStaAur52173_0518.

Phylogenomic databases

eggNOGiENOG4105EEI. Bacteria.
COG0294. LUCA.
HOGENOMiHOG000217509.
KOiK00796.
OMAiSIDTYHA.
PhylomeDBiP64141.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.

Family and domain databases

CDDicd00739. DHPS. 1 hit.
Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding_dom.
[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...

Entry informationi

Entry nameiDHPS_STAAM
AccessioniPrimary (citable) accession number: P64141
Secondary accession number(s): Q99W89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 85 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, Complete proteome

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

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 one 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.