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Protein

Dihydropteroate synthase

Gene

folP

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.By similarity

Catalytic activityi

6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.By similarity

Cofactori

Mg2+By similarity

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (folP)
  2. no protein annotated in this organism
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi25MagnesiumBy similarity1
Binding sitei666-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei996-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei1196-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei1906-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei2276-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Folate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

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
Proteomesi
  • UP000000626 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001682171 – 283Dihydropteroate synthaseAdd BLAST283

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ9JT70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 274Pterin-bindingPROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni262 – 2646-hydroxymethyl-7,8-dihydropterin diphosphate bindingBy similarity3

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000217510.
KOiK00796.
OMAiSIDTYHA.

Family and domain databases

CDDicd00739. DHPS. 1 hit.
Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding_dom.
[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

        10         20         30         40         50
MVGCVWQAGR FEIGLDKPKI MGIVNLTPDS LSDGGAYSQN AQTALAHAER
60 70 80 90 100
LLKEGADILD IGGESTRPGA DYVSPEEEWA RVESVLAEVA GWGVPVSLDT
110 120 130 140 150
RHTVVMEKAL ALGGIDIIND VAALTDEGAL ELLACQADTG ICLMHMQGLP
160 170 180 190 200
KNMQINPKYQ DVVGEVARYL KARAAECIAA GIAPQRITLD PGFCFGKTLQ
210 220 230 240 250
HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA ARGHGSVAAA
260 270 280
LAAVARGAKI VRVHDVKATA DALKAWEALG INL
Length:283
Mass (Da):29,928
Last modified:October 1, 2000 - v1
Checksum:i89A0976A527C9E27
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2 – 4VGC → ARH in strain: 1014 and 418. 3
Natural varianti31L → F in strain: 1014 and 418. 1
Natural varianti68P → L in strain: 418. 1
Natural varianti75P → S in strain: 1014. 1
Natural varianti84S → P in strain: 1014 and 418. 1
Natural varianti87A → E in strain: 418. 1
Natural varianti87A → V in strain: 1014. 1
Natural varianti102H → R in strain: 1014 and 418. 1
Natural varianti105V → I in strain: 418. 1
Natural varianti115I → V in strain: 418. 1
Natural varianti125T → N in strain: 418. 1
Natural varianti130L → V in strain: 418. 1
Natural varianti135C → R in strain: 418. 1
Natural varianti147Q → R in strain: 1014. 1
Natural varianti151K → E in strain: 1014. 1
Natural varianti152N → T in strain: 418. 1
Natural varianti174A → S in strain: 418. 1
Natural varianti188T → I in strain: 418. 1
Natural varianti194C → G in strain: 1014. 1
Natural varianti194C → GSG in strain: 418. 1
Natural varianti198T → P in strain: 418. 1
Natural varianti204T → A in strain: 1014 and 418. 1
Natural varianti218Y → F in strain: 1014 and 418. 1
Natural varianti228S → R in strain: 1014. 1
Natural varianti229M → T in strain: 418. 1
Natural varianti230I → V in strain: 1014. 1
Natural varianti237 – 238TD → AN in strain: 418. 2
Natural varianti241A → E in strain: 418. 1
Natural varianti243G → V in strain: 1014 and 418. 1
Natural varianti253A → S in strain: 1014 and 418. 1
Natural varianti255A → R in strain: 1014. 1
Natural varianti259K → Q in strain: 1014 and 418. 1
Natural varianti275A → V in strain: 1014 and 418. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68065 Genomic DNA. Translation: CAA48202.1.
X68068 Genomic DNA. Translation: CAA48205.1.
AL157959 Genomic DNA. Translation: CAM09062.1.
PIRiD81823.
S25610.
S65838.
RefSeqiWP_002248109.1. NC_003116.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68065 Genomic DNA. Translation: CAA48202.1.
X68068 Genomic DNA. Translation: CAA48205.1.
AL157959 Genomic DNA. Translation: CAM09062.1.
PIRiD81823.
S25610.
S65838.
RefSeqiWP_002248109.1. NC_003116.1.

3D structure databases

ProteinModelPortaliQ9JT70.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000217510.
KOiK00796.
OMAiSIDTYHA.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.

Family and domain databases

CDDicd00739. DHPS. 1 hit.
Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding_dom.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.