CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydropteroate synthase 
Protein Synonyms/Alias
 DHPS; Dihydropteroate pyrophosphorylase 
Gene Name
 folP 
Gene Synonyms/Alias
 dhpS; b3177; JW3144 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
153KTMQEAPKYDDVFAEacetylation[1]
181QAGIAKEKLLLDPGFacetylation[1]
260IIRVHDVKETVEAMRacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide. 
Sequence Annotation
 DOMAIN 15 267 Pterin-binding.
 REGION 62 63 Substrate binding.
 METAL 22 22 Magnesium.
 BINDING 30 30 Substrate.
 BINDING 96 96 Substrate.
 BINDING 115 115 Substrate.
 BINDING 185 185 Substrate.
 BINDING 221 221 Substrate.
 BINDING 255 255 Substrate.
 BINDING 257 257 Substrate.  
Keyword
 3D-structure; Antibiotic resistance; Complete proteome; Direct protein sequencing; Folate biosynthesis; Magnesium; Metal-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 282 AA 
Protein Sequence
MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA GATIIDVGGE 60
STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP EVIRESAKVG AHIINDIRSL 120
SEPGALEAAA ETGLPVCLMH MQGNPKTMQE APKYDDVFAE VNRYFIEQIA RCEQAGIAKE 180
KLLLDPGFGF GKNLSHNYSL LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL 240
ACAVIAAMQG AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE 282 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoCyc.
 GO:0004156; F:dihydropteroate synthase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0046656; P:folic acid biosynthetic process; IMP:EcoCyc.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0042493; P:response to drug; IMP:EcoliWiki.
 GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006390; DHP_synth.
 IPR011005; Dihydropteroate_synth-like.
 IPR000489; Pterin-binding. 
Pfam
 PF00809; Pterin_bind 
SMART
  
PROSITE
 PS00792; DHPS_1
 PS00793; DHPS_2
 PS50972; PTERIN_BINDING 
PRINTS