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P0C0X1 (DHPS1_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropteroate synthase 1

Short name=DHPS 1
EC=2.5.1.15
Alternative name(s):
Dihydropteroate pyrophosphorylase 1
Gene names
Name:folP1
Synonyms:folP
Ordered Locus Names:ML0224
ORF Names:MLCB2548.07c
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide By similarity.

Catalytic activity

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.

Cofactor

Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate By similarity.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Dihydropteroate synthase 1
PRO_0000168213

Regions

Domain6 – 265260Pterin-binding
Region53 – 542Substrate binding By similarity

Sites

Metal binding131Magnesium By similarity
Binding site211Substrate By similarity
Binding site861Substrate By similarity
Binding site1051Substrate By similarity
Binding site1771Substrate By similarity
Binding site2131Substrate By similarity
Binding site2531Substrate By similarity
Binding site2551Substrate By similarity

Experimental info

Sequence conflict531T → A in BAA84081. Ref.1
Sequence conflict531T → I in BAA84080. Ref.1
Sequence conflict531T → I in BAA84079. Ref.1
Sequence conflict551P → L in BAA84078. Ref.1
Sequence conflict551P → L in BAA84077. Ref.1
Sequence conflict551P → L in BAA84076. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0C0X1 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: A576FF46C16AC826

FASTA28429,448
        10         20         30         40         50         60 
MSLAPVQVIG VLNVTDNSFS DGGRYLDPDD AVQHGLAMVA EGAAIVDVGG ESTRPGAIRT 

        70         80         90        100        110        120 
DPRVELSRIV PVVKELAAQG ITVSIDTTRA DVARAALQSG ARIVNDVSGG RADPAMAPLV 

       130        140        150        160        170        180 
AEAGVAWVLM HWRLMSAERP YEAPNYRDVV AEVRADLLAG VDQAVAAGVD PGSLVIDPGL 

       190        200        210        220        230        240 
GFAKTGQHNW ALLNALPELV ATGVPILLGA SRKRFLGRLL AGADGAVRPP DGRETATAVI 

       250        260        270        280 
SALAALHGAW GVRVHDVRAS VDALKVVGAW LHAGPQIEKV RCDG 

« Hide

References

« Hide 'large scale' references
[1]"Diaminodiphenylsulfone resistance of Mycobacterium leprae due to mutations in the dihydropteroate synthase gene."
Kai M., Matsuoka M., Nakata N., Maeda S., Gidoh M., Maeda Y., Hashimoto K., Kobayashi K., Kashiwabara Y.
FEMS Microbiol. Lett. 177:231-235(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli."
Nopponpunth V., Sirawaraporn W., Greene P.J., Santi D.V.
J. Bacteriol. 181:6814-6821(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Massive gene decay in the leprosy bacillus."
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. expand/collapse author list , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G.
Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028658 Genomic DNA. Translation: BAA84076.1.
AB028659 Genomic DNA. Translation: BAA84077.1.
AB028660 Genomic DNA. Translation: BAA84078.1.
AB028661 Genomic DNA. Translation: BAA84079.1.
AB028662 Genomic DNA. Translation: BAA84080.1.
AB028663 Genomic DNA. Translation: BAA84081.1.
AB028656 Genomic DNA. Translation: BAA84074.1.
AB028657 Genomic DNA. Translation: BAA84075.1.
AF117618 Genomic DNA. Translation: AAF06725.1.
AL023093 Genomic DNA. Translation: CAA18794.1.
AL583917 Genomic DNA. Translation: CAC29732.1.
PIRH86936.
RefSeqNP_301284.1. NC_002677.1.

3D structure databases

ProteinModelPortalP0C0X1.
SMRP0C0X1. Positions 5-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML0224.

Chemistry

ChEMBLCHEMBL2362993.
DrugBankDB00250. Dapsone.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC29732; CAC29732; CAC29732.
GeneID908646.
KEGGmle:ML0224.
PATRIC18050810. VBIMycLep78757_0356.

Organism-specific databases

LepromaML0224.
CMRSearch...

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217509.
KOK00796.
OMASIDTYHA.
OrthoDBEOG67T5P5.
ProtClustDBCLSK799350.

Enzyme and pathway databases

UniPathwayUPA00077; UER00156.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
InterProIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMSSF51717. SSF51717. 1 hit.
TIGRFAMsTIGR01496. DHPS. 1 hit.
PROSITEPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHPS1_MYCLE
AccessionPrimary (citable) accession number: P0C0X1
Secondary accession number(s): O69530 expand/collapse secondary AC list , P46812, Q9R2Q6, Q9R2U9, Q9S0T0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: December 11, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways