Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9JT70

- DHPS_NEIMA

UniProt

Q9JT70 - DHPS_NEIMA

Protein

Dihydropteroate synthase

Gene

folP

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

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

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi25 – 251MagnesiumBy similarity
    Binding sitei33 – 331SubstrateBy similarity
    Binding sitei99 – 991SubstrateBy similarity
    Binding sitei119 – 1191SubstrateBy similarity
    Binding sitei190 – 1901SubstrateBy similarity
    Binding sitei227 – 2271SubstrateBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Binding sitei264 – 2641SubstrateBy similarity

    GO - Molecular functioni

    1. dihydropteroate synthase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. response to antibiotic Source: UniProtKB-KW
    3. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Antibiotic resistance, Folate biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciNMEN122587:GI3Q-1793-MONOMER.
    UniPathwayiUPA00077; UER00156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteroate synthase (EC:2.5.1.15)
    Short name:
    DHPS
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    Gene namesi
    Name:folP
    Synonyms:dhpS
    Ordered Locus Names:NMA1950
    OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
    Taxonomic identifieri122587 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000626: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Dihydropteroate synthasePRO_0000168217Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi122587.NMA1950.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JT70.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 274257Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 672Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the DHPS family.Curated
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0294.
    HOGENOMiHOG000217510.
    KOiK00796.
    OMAiRIMLDPG.
    OrthoDBiEOG67T5P5.

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    InterProiIPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [Graphical view]
    PfamiPF00809. Pterin_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    TIGRFAMsiTIGR01496. DHPS. 1 hit.
    PROSITEiPS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JT70-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVGCVWQAGR FEIGLDKPKI MGIVNLTPDS LSDGGAYSQN AQTALAHAER    50
    LLKEGADILD IGGESTRPGA DYVSPEEEWA RVESVLAEVA GWGVPVSLDT 100
    RHTVVMEKAL ALGGIDIIND VAALTDEGAL ELLACQADTG ICLMHMQGLP 150
    KNMQINPKYQ DVVGEVARYL KARAAECIAA GIAPQRITLD PGFCFGKTLQ 200
    HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA ARGHGSVAAA 250
    LAAVARGAKI VRVHDVKATA DALKAWEALG INL 283
    Length:283
    Mass (Da):29,928
    Last modified:October 1, 2000 - v1
    Checksum:i89A0976A527C9E27
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 43VGC → ARH in strain: 1014 and 418.
    Natural varianti31 – 311L → F in strain: 1014 and 418.
    Natural varianti68 – 681P → L in strain: 418.
    Natural varianti75 – 751P → S in strain: 1014.
    Natural varianti84 – 841S → P in strain: 1014 and 418.
    Natural varianti87 – 871A → E in strain: 418.
    Natural varianti87 – 871A → V in strain: 1014.
    Natural varianti102 – 1021H → R in strain: 1014 and 418.
    Natural varianti105 – 1051V → I in strain: 418.
    Natural varianti115 – 1151I → V in strain: 418.
    Natural varianti125 – 1251T → N in strain: 418.
    Natural varianti130 – 1301L → V in strain: 418.
    Natural varianti135 – 1351C → R in strain: 418.
    Natural varianti147 – 1471Q → R in strain: 1014.
    Natural varianti151 – 1511K → E in strain: 1014.
    Natural varianti152 – 1521N → T in strain: 418.
    Natural varianti174 – 1741A → S in strain: 418.
    Natural varianti188 – 1881T → I in strain: 418.
    Natural varianti194 – 1941C → G in strain: 1014.
    Natural varianti194 – 1941C → GSG in strain: 418.
    Natural varianti198 – 1981T → P in strain: 418.
    Natural varianti204 – 2041T → A in strain: 1014 and 418.
    Natural varianti218 – 2181Y → F in strain: 1014 and 418.
    Natural varianti228 – 2281S → R in strain: 1014.
    Natural varianti229 – 2291M → T in strain: 418.
    Natural varianti230 – 2301I → V in strain: 1014.
    Natural varianti237 – 2382TD → AN in strain: 418.
    Natural varianti241 – 2411A → E in strain: 418.
    Natural varianti243 – 2431G → V in strain: 1014 and 418.
    Natural varianti253 – 2531A → S in strain: 1014 and 418.
    Natural varianti255 – 2551A → R in strain: 1014.
    Natural varianti259 – 2591K → Q in strain: 1014 and 418.
    Natural varianti275 – 2751A → V in strain: 1014 and 418.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68065 Genomic DNA. Translation: CAA48202.1.
    X68068 Genomic DNA. Translation: CAA48205.1.
    AL157959 Genomic DNA. Translation: CAM09062.1.
    PIRiD81823.
    S25610.
    S65838.
    RefSeqiYP_002343223.1. NC_003116.1.

    Genome annotation databases

    EnsemblBacteriaiCAM09062; CAM09062; NMA1950.
    GeneIDi907184.
    KEGGinma:NMA1950.
    PATRICi20365276. VBINeiMen132687_2326.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68065 Genomic DNA. Translation: CAA48202.1 .
    X68068 Genomic DNA. Translation: CAA48205.1 .
    AL157959 Genomic DNA. Translation: CAM09062.1 .
    PIRi D81823.
    S25610.
    S65838.
    RefSeqi YP_002343223.1. NC_003116.1.

    3D structure databases

    ProteinModelPortali Q9JT70.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 122587.NMA1950.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM09062 ; CAM09062 ; NMA1950 .
    GeneIDi 907184.
    KEGGi nma:NMA1950.
    PATRICi 20365276. VBINeiMen132687_2326.

    Phylogenomic databases

    eggNOGi COG0294.
    HOGENOMi HOG000217510.
    KOi K00796.
    OMAi RIMLDPG.
    OrthoDBi EOG67T5P5.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .
    BioCyci NMEN122587:GI3Q-1793-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    InterProi IPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [Graphical view ]
    Pfami PF00809. Pterin_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 1 hit.
    TIGRFAMsi TIGR01496. DHPS. 1 hit.
    PROSITEi PS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transformational exchanges in the dihydropteroate synthase gene of Neisseria meningitidis: a novel mechanism for acquisition of sulfonamide resistance."
      Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O., Swedberg G.
      J. Bacteriol. 174:6386-6393(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 1014 / Serogroup A / Serotype 4/21 and 418 / Serogroup A / Serotype 4/21.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Z2491.

    Entry informationi

    Entry nameiDHPS_NEIMA
    AccessioniPrimary (citable) accession number: Q9JT70
    Secondary accession number(s): A1ITE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3