Skip Header

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

P0C0G0

- DHPS_STRPY

UniProt

P0C0G0 - DHPS_STRPY

(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

folP

Organism
Streptococcus pyogenes
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 bindingi19 – 191MagnesiumBy similarity
Binding sitei27 – 271SubstrateBy similarity
Binding sitei93 – 931SubstrateBy similarity
Binding sitei112 – 1121SubstrateBy similarity
Binding sitei176 – 1761SubstrateBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Binding sitei248 – 2481SubstrateBy similarity
Binding sitei250 – 2501SubstrateBy 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

SABIO-RKP0C0G0.
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
OrganismiStreptococcus pyogenes
Taxonomic identifieri1314 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Dihydropteroate synthasePRO_0000168232Add
BLAST

Interactioni

Subunit structurei

Homodimer or homotrimer.

Structurei

3D structure databases

ProteinModelPortaliP0C0G0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 260249Pterin-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 602Substrate bindingBy similarity

Sequence similaritiesi

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

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.

P0C0G0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIGKFVIDG NAAIMGILNV TPDSFSDGGS YTTVQKVLQQ VDQLIAGGAK
60 70 80 90 100
IIDVGGESTR PGYQFVSAAD EIERVVPMIK AIKAKYDVLI SIDTYKTETA
110 120 130 140 150
RAALEAGADI LNDVRAGLYD GEMLALAAEY DVPIILMHNQ KEEVYQDVTQ
160 170 180 190 200
DVCDFLSARA QAAIDAGVPK DNIWIDPGFG FPKSVQHNME LLKGLDHVCQ
210 220 230 240 250
LGYPVLFGIS RKGVVDALLG GNTKAKERDG ATAALSAYAL GKGCQLVRVH
260
DVKANQEIVA VLSQLM
Length:266
Mass (Da):28,515
Last modified:September 13, 2005 - v1
Checksum:iC6BC402F07CFDF36
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000685 Genomic DNA. Translation: CAA04238.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000685 Genomic DNA. Translation: CAA04238.1 .

3D structure databases

ProteinModelPortali P0C0G0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00156 .
SABIO-RK P0C0G0.

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

  1. "Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of its chromosomal dihydropteroate synthase."
    Swedberg G., Ringertz S., Skoeld O.
    Antimicrob. Agents Chemother. 42:1062-1067(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G56.
  2. "Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance."
    Swedberg G., Fermer C., Skoeld O.
    Adv. Exp. Med. Biol. 338:555-558(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G56.

Entry informationi

Entry nameiDHPS_STRPY
AccessioniPrimary (citable) accession number: P0C0G0
Secondary accession number(s): O33724
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: October 1, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3