Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05382

- DHPS_STRPN

UniProt

P05382 - DHPS_STRPN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dihydropteroate synthase

Gene

sulA

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - 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

Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate (By similarity).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.
OMAiDMFYVAA.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U16156 Genomic DNA. Translation: AAB63944.1 .
AE005672 Genomic DNA. Translation: AAK74467.1 .
PIRi A43661.
B95034.
B97905.
RefSeqi NP_344827.1. NC_003028.3.
WP_001855229.1. NC_003028.3.

3D structure databases

ProteinModelPortali P05382.
SMRi P05382. Positions 7-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P05382. 3 interactions.
STRINGi 170187.SP_0289.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK74467 ; AAK74467 ; SP_0289 .
GeneIDi 930100.
KEGGi spn:SP_0289.
PATRICi 19704915. VBIStrPne105772_0303.

Phylogenomic databases

eggNOGi COG0294.
HOGENOMi HOG000217509.
KOi K00796.
OMAi DMFYVAA.
OrthoDBi EOG67T5P5.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00156 .
BioCyci SPNE170187:GHGN-295-MONOMER.
SABIO-RK P05382.

Family and domain databases

Gene3Di 3.20.20.20. 1 hit.
InterProi IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view ]
Pfami PF00809. Pterin_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF51717. SSF51717. 1 hit.
TIGRFAMsi TIGR01496. DHPS. 1 hit.
PROSITEi PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 118 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