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P0AC15 (DHPS_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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

Short name=DHPS
EC=2.5.1.15
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene names
Name:folP
Ordered Locus Names:SF3217, S3435
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length282 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 caution

The sequence AAN44683.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAP18497.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Dihydropteroate synthase
PRO_0000168209

Regions

Domain15 – 267253Pterin-binding
Region62 – 632Substrate binding By similarity

Sites

Metal binding221Magnesium By similarity
Binding site301Substrate By similarity
Binding site961Substrate By similarity
Binding site1151Substrate By similarity
Binding site1851Substrate By similarity
Binding site2211Substrate By similarity
Binding site2551Substrate By similarity
Binding site2571Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AC15 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 6230C8883796F59E

FASTA28230,615
        10         20         30         40         50         60 
MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA GATIIDVGGE 

        70         80         90        100        110        120 
STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP EVIRESAKVG AHIINDIRSL 

       130        140        150        160        170        180 
SEPGALEAAA ETGLPVCLMH MQGNPKTMQE APKYDDVFAE VNRYFIEQIA RCEQAGIAKE 

       190        200        210        220        230        240 
KLLLDPGFGF GKNLSHNYSL LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL 

       250        260        270        280 
ACAVIAAMQG AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN44683.2. Different initiation.
AE014073 Genomic DNA. Translation: AAP18497.1. Different initiation.
RefSeqNP_708976.4. NC_004337.2.
NP_838686.2. NC_004741.1.

3D structure databases

ProteinModelPortalP0AC15.
SMRP0AC15. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF3217.

Proteomic databases

PaxDbP0AC15.
PRIDEP0AC15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN44683; AAN44683; SF3217.
AAP18497; AAP18497; S3435.
GeneID1027106.
1079671.
KEGGsfl:SF3217.
sfx:S3435.
PATRIC18708619. VBIShiFle31049_3755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217510.
KOK00796.
OrthoDBEOG67T5P5.

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 nameDHPS_SHIFL
AccessionPrimary (citable) accession number: P0AC15
Secondary accession number(s): P26282, P78110
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 63 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