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P28822 (DHPS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Short name=DHPS
EC=2.5.1.15
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene names
Name:sul
Ordered Locus Names:BSU00770
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length285 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.

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.

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Dihydropteroate synthase
PRO_0000168205

Regions

Domain25 – 271247Pterin-binding
Region72 – 732Substrate binding By similarity

Sites

Metal binding321Magnesium By similarity
Binding site401Substrate By similarity
Binding site1061Substrate By similarity
Binding site1251Substrate By similarity
Binding site1891Substrate By similarity
Binding site2251Substrate By similarity
Binding site2591Substrate By similarity
Binding site2611Substrate By similarity

Experimental info

Sequence conflict1951A → P in AAA22697. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28822 [UniParc].

Last modified August 4, 2003. Version 2.
Checksum: F2878DEC3D9000D6

FASTA28531,002
        10         20         30         40         50         60 
MAQHTIDQTQ VIHTKPSALS YKEKTLVMGI LNVTPDSFSD GGKYDSLDKA LLHAKEMIDD 

        70         80         90        100        110        120 
GAHIIDIGGE STRPGAECVS EDEEMSRVIP VIERITKELG VPISVDTYKA SVADEAVKAG 

       130        140        150        160        170        180 
ASIINDIWGA KHDPKMASVA AEHNVPIVLM HNRPERNYND LLPDMLSDLM ESVKIAVEAG 

       190        200        210        220        230        240 
VDEKNIILDP GIGFAKTYHD NLAVMNKLEI FSGLGYPVLL ATSRKRFIGR VLDLPPEERA 

       250        260        270        280 
EGTGATVCLG IQKGCDIVRV HDVKQIARMA KMMDAMLNKG GVHHG 

« Hide

References

« Hide 'large scale' references
[1]"An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene."
Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.
J. Bacteriol. 172:7211-7226(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ASB342.
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34053 Genomic DNA. Translation: AAA22697.1.
D26185 Genomic DNA. Translation: BAA05312.1.
AL009126 Genomic DNA. Translation: CAB11853.1.
PIRG69719.
RefSeqNP_387958.1. NC_000964.3.

3D structure databases

ProteinModelPortalP28822.
SMRP28822. Positions 19-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU00770.

Proteomic databases

PaxDbP28822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11853; CAB11853; BSU00770.
GeneID936256.
KEGGbsu:BSU00770.
PATRIC18971629. VBIBacSub10457_0078.

Organism-specific databases

GenoListBSU00770. [Micado]

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217509.
KOK00796.
OMADCWISVD.
OrthoDBEOG67T5P5.
PhylomeDBP28822.

Enzyme and pathway databases

BioCycBSUB:BSU00770-MONOMER.
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 nameDHPS_BACSU
AccessionPrimary (citable) accession number: P28822
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: August 4, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 2 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList