P0C0X1 (DHPS1_MYCLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydropteroate synthase 1 Short name=DHPS 1 EC=2.5.1.15 Alternative name(s): Dihydropteroate pyrophosphorylase 1 | ||||||||
| Gene names |
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| Organism | Mycobacterium leprae [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1769 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 284 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 | |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the DHPS family. Contains 1 pterin-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance Folate biosynthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to antibioticInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | dihydropteroate synthase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 284 | 284 | Dihydropteroate synthase 1 | PRO_0000168213 | |||||
Regions | |||||||||
| Domain | 6 – 265 | 260 | Pterin-binding | ||||||
| Region | 53 – 54 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 13 | 1 | Magnesium By similarity | ||||||
| Binding site | 21 | 1 | Substrate By similarity | ||||||
| Binding site | 86 | 1 | Substrate By similarity | ||||||
| Binding site | 105 | 1 | Substrate By similarity | ||||||
| Binding site | 177 | 1 | Substrate By similarity | ||||||
| Binding site | 213 | 1 | Substrate By similarity | ||||||
| Binding site | 253 | 1 | Substrate By similarity | ||||||
| Binding site | 255 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 53 | 1 | T → A in BAA84081. Ref.1 | ||||||
| Sequence conflict | 53 | 1 | T → I in BAA84080. Ref.1 | ||||||
| Sequence conflict | 53 | 1 | T → I in BAA84079. Ref.1 | ||||||
| Sequence conflict | 55 | 1 | P → L in BAA84078. Ref.1 | ||||||
| Sequence conflict | 55 | 1 | P → L in BAA84077. Ref.1 | ||||||
| Sequence conflict | 55 | 1 | P → L in BAA84076. Ref.1 | ||||||
Sequences
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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: 10474189] [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: 10542185] [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. Barrell B.G.Nature 409:1007-1011(2001) [PubMed: 11234002] [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. |
| PIR | H86936. |
| RefSeq | NP_301284.1. NC_002677.1. |
3D structure databases | |
| ProteinModelPortal | P0C0X1. |
| SMR | P0C0X1. Positions 5-273. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000028197; EBMYCP00000027803; EBMYCG00000028192. |
| GeneID | 908646. |
| GenomeReviews | Gene locus ML0224 in contig AL450380_GR. |
| KEGG | mle:ML0224. |
| NMPDR | fig|272631.1.peg.156. |
| PATRIC | 18050810. VBIMycLep78757_0356. |
Organism-specific databases | |
| Leproma | ML0224. |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000015914. |
| HOGENOM | HBG754410. |
| OMA | VVMHWRG. |
| ProtClustDB | CLSK799350. |
Enzyme and pathway databases | |
| BioCyc | MLEP272631:ML0224-MONOMER. |
Family and domain databases | |
| InterPro | IPR006390. DHP_synth. IPR011005. Dihydropteroate_synth-like. IPR000489. Pterin-binding. [Graphical view] |
| Gene3D | G3DSA:3.20.20.20. Dhdropt_synth. 1 hit. |
| KO | K00796. |
| Pfam | PF00809. Pterin_bind. 1 hit. [Graphical view] |
| SUPFAM | SSF51717. DHP_synth_like. 1 hit. |
| TIGRFAMs | TIGR01496. DHPS. 1 hit. |
| PROSITE | PS00792. DHPS_1. 1 hit. PS00793. DHPS_2. 1 hit. PS50972. PTERIN_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00250. Dapsone. |
Entry information
| Entry name | DHPS1_MYCLE | ||||||||
| Accession | Primary (citable) accession number: P0C0X1 Secondary accession number(s): O69530 Q9S0T0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with