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Protein

Dihydropteroate synthase

Gene

sulA

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: -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

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

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

Keywordsi

Molecular functionTransferase
Biological processAntibiotic resistance, Folate biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciSPNE171101:G1FZH-289-MONOMER
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

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

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

Proteomic databases

PRIDEiP59655

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

Phylogenomic databases

eggNOGiENOG4105EEI Bacteria
COG0294 LUCA
HOGENOMiHOG000217509
KOiK00796
OMAiWAVRVHD

Family and domain databases

CDDicd00739 DHPS, 1 hit
Gene3Di3.20.20.20, 1 hit
InterProiView protein in InterPro
IPR006390 DHP_synth
IPR011005 Dihydropteroate_synth-like
IPR000489 Pterin-binding_dom
PfamiView protein in Pfam
PF00809 Pterin_bind, 1 hit
SUPFAMiSSF51717 SSF51717, 1 hit
TIGRFAMsiTIGR01496 DHPS, 1 hit
PROSITEiView protein in PROSITE
PS00792 DHPS_1, 1 hit
PS00793 DHPS_2, 1 hit
PS50972 PTERIN_BINDING, 1 hit

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
PATRICifig|171101.6.peg.303

Similar proteinsi

Entry informationi

Entry nameiDHPS_STRR6
AccessioniPrimary (citable) accession number: P59655
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: May 23, 2018
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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