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Protein

Dihydropteroate synthase

Gene

sulA

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: Annotation score: 5 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, the immediate precursor of folate derivatives.1 Publication
Is the target for the sulfonamide group of antimicrobial drugs. Sulfonamide drugs act as pABA analogs, they inhibit the reaction by acting as alternative substrates, leading to a "dead end" sulfa-pterin product.2 Publications

Catalytic activityi

6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Is potently inhibited by sulfonamides, with Ki values between 25 nM and 850 nM.1 Publication

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 (sulA)
  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 bindingi17MagnesiumBy similarity1
Binding sitei916-hydroxymethyl-7,8-dihydropterin diphosphate1 Publication1
Binding sitei1106-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
Binding sitei2016-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
Binding sitei2376-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1

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

BRENDAi2.5.1.15. 1960.
UniPathwayiUPA00077; UER00156.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
Short name:
DHPS1 Publication
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene namesi
Name:sulA
Ordered Locus Names:spr0266
OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
Taxonomic identifieri171101 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000586 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001682311 – 314Dihydropteroate synthaseAdd BLAST314

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi171101.spr0266.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 17Combined sources7
Helixi31 – 44Combined sources14
Beta strandi48 – 53Combined sources6
Helixi63 – 83Combined sources21
Beta strandi87 – 91Combined sources5
Helixi95 – 103Combined sources9
Beta strandi108 – 111Combined sources4
Turni112 – 115Combined sources4
Helixi121 – 128Combined sources8
Beta strandi131 – 135Combined sources5
Helixi138 – 141Combined sources4
Turni146 – 150Combined sources5
Helixi166 – 170Combined sources5
Helixi173 – 191Combined sources19
Helixi195 – 197Combined sources3
Beta strandi198 – 201Combined sources4
Helixi210 – 218Combined sources9
Helixi220 – 224Combined sources5
Turni225 – 227Combined sources3
Beta strandi230 – 233Combined sources4
Helixi238 – 246Combined sources9
Helixi256 – 275Combined sources20
Beta strandi279 – 284Combined sources6
Helixi286 – 300Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VEFX-ray1.80A/B1-314[»]
2VEGX-ray2.40A/B1-314[»]
ProteinModelPortaliP59655.
SMRiP59655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59655.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 294Pterin-bindingPROSITE-ProRule annotationAdd BLAST285

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni282 – 2846-hydroxymethyl-7,8-dihydropterin diphosphate bindingCombined sources1 Publication3

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.

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.

P59655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKANHAKT VICGIINVTP DSFSDGGQFF ALEQALQQAR KLIAEGASML
60 70 80 90 100
DIGGESTRPG SSYVEIEEEI QRVVPVIKAI RKESDVLISI DTWKSQVAEA
110 120 130 140 150
ALAAGADLVN DITGLMGDEK MPHVVAEARA QVVIMFNPVM ARPQHPSSLI
160 170 180 190 200
FPHFGFGQAF TEEELADFET LPIEELMEAF FERALARAAE AGIAPENILL
210 220 230 240 250
DPGIGFGLTK KENLLLLRDL DKLHQKGYPI FLGVSRKRFV INILEENGFE
260 270 280 290 300
VNPETELGFR NRDTASAHVT SIAARQGVEV VRVHDVASHR MAVEIASAIR
310
LADEAENLDL KQYK
Length:314
Mass (Da):34,418
Last modified:April 30, 2003 - v1
Checksum:iC7CEDD0C2EDAA061
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007317 Genomic DNA. Translation: AAK99070.1.
RefSeqiNP_357860.1. NC_003098.1.
WP_010976411.1. NC_003098.1.

Genome annotation databases

EnsemblBacteriaiAAK99070; AAK99070; spr0266.
GeneIDi934662.
KEGGispr:spr0266.
PATRICi19700365. VBIStrPne107296_0303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007317 Genomic DNA. Translation: AAK99070.1.
RefSeqiNP_357860.1. NC_003098.1.
WP_010976411.1. NC_003098.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VEFX-ray1.80A/B1-314[»]
2VEGX-ray2.40A/B1-314[»]
ProteinModelPortaliP59655.
SMRiP59655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi171101.spr0266.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK99070; AAK99070; spr0266.
GeneIDi934662.
KEGGispr:spr0266.
PATRICi19700365. VBIStrPne107296_0303.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BRENDAi2.5.1.15. 1960.

Miscellaneous databases

EvolutionaryTraceiP59655.

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_STRR6
AccessioniPrimary (citable) accession number: P59655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: November 30, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Reaction proceeds via an ordered binding mechanism, with DHPPP binding to the enzyme first, inducing a structural change which forms the pABA-binding site.2 Publications
One or two residue insertions within this gene are responsible for sulfonamide resistance in streptococcal clinical isolates. Sulfonamide-resistance mutations in the second loop region have a drastic effect on pABA binding.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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.