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Protein

Dihydropteroate synthase

Gene

sulA

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 bindingi17 – 171MagnesiumBy similarity
Binding sitei25 – 251SubstrateBy similarity
Binding sitei91 – 911SubstrateBy similarity
Binding sitei110 – 1101SubstrateBy similarity
Binding sitei201 – 2011SubstrateBy similarity
Binding sitei237 – 2371SubstrateBy similarity
Binding sitei282 – 2821SubstrateBy similarity
Binding sitei284 – 2841SubstrateBy similarity

GO - Molecular functioni

  1. dihydropteroate synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. response to antibiotic Source: UniProtKB-KW
  3. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic resistance, Folate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-295-MONOMER.
SABIO-RKP05382.
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:sulA
Ordered Locus Names:SP_0289
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000585: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Dihydropteroate synthasePRO_0000168230Add
BLAST

Interactioni

Subunit structurei

Homodimer or homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
groSQ97NV32EBI-2206997,EBI-2206949
malRP0A4T12EBI-2206997,EBI-2207435
SP_1069Q97QX54EBI-2206997,EBI-6472250

Protein-protein interaction databases

IntActiP05382. 3 interactions.
STRINGi170187.SP_0289.

Structurei

3D structure databases

ProteinModelPortaliP05382.
SMRiP05382. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 294285Pterin-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 582Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217509.
KOiK00796.
OMAiVAVGKMA.
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.

P05382-1 [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 MAYVVAEARA KVVIMFNPVM ARPQHPSSLI
160 170 180 190 200
FPHFGFGQTF TEKELADFET LPIEDLMVAF 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):34,403
Last modified:September 26, 2001 - v2
Checksum:iF2F20D9A782083FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1232AY → PH in AAB63944. (PubMed:3114239)Curated
Sequence conflicti131 – 1311K → Q in AAB63944. (PubMed:3114239)Curated
Sequence conflicti159 – 1591T → A in AAB63944. (PubMed:3114239)Curated
Sequence conflicti163 – 1631K → E in AAB63944. (PubMed:3114239)Curated
Sequence conflicti175 – 1751D → E in AAB63944. (PubMed:3114239)Curated
Sequence conflicti178 – 1781V → E in AAB63944. (PubMed:3114239)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671E → EIE in mutant SUL-D.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16156 Genomic DNA. Translation: AAB63944.1.
AE005672 Genomic DNA. Translation: AAK74467.1.
PIRiA43661.
B95034.
B97905.
RefSeqiNP_344827.1. NC_003028.3.
WP_001855229.1. NC_003028.3.

Genome annotation databases

EnsemblBacteriaiAAK74467; AAK74467; SP_0289.
GeneIDi930100.
KEGGispn:SP_0289.
PATRICi19704915. VBIStrPne105772_0303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16156 Genomic DNA. Translation: AAB63944.1.
AE005672 Genomic DNA. Translation: AAK74467.1.
PIRiA43661.
B95034.
B97905.
RefSeqiNP_344827.1. NC_003028.3.
WP_001855229.1. NC_003028.3.

3D structure databases

ProteinModelPortaliP05382.
SMRiP05382. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP05382. 3 interactions.
STRINGi170187.SP_0289.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK74467; AAK74467; SP_0289.
GeneIDi930100.
KEGGispn:SP_0289.
PATRICi19704915. VBIStrPne105772_0303.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217509.
KOiK00796.
OMAiVAVGKMA.
OrthoDBiEOG67T5P5.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BioCyciSPNE170187:GHGN-295-MONOMER.
SABIO-RKP05382.

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

« Hide 'large scale' publications
  1. "Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the gene encoding dihydropteroate synthase and characterization of the enzyme."
    Lopez P., Espinosa M., Greenberg B., Lacks S.A.
    J. Bacteriol. 169:4320-4326(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 772.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.

Entry informationi

Entry nameiDHPS_STRPN
AccessioniPrimary (citable) accession number: P05382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: September 26, 2001
Last modified: January 7, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown here is that of sul-s (wild-type). The protein of the spontaneous mutation to sulfonamide resistance (sul-d) has an insert of 2 AA.

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.