Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydropteroate synthase

Gene

folP

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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.UniRule annotation

Cofactori

Mg2+UniRule annotation

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.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (ADK18_00325), Dihydropteroate synthase, Dihydropteroate synthase (ABW01_27475), Dihydropteroate synthase (sul), 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationImported

Keywords - Biological processi

Folate biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciANTHRA:FOLP-MONOMER.
BANT260799:GJAJ-80-MONOMER.
BANT261594:GJ7F-82-MONOMER.
BRENDAi2.5.1.15. 634.
UniPathwayiUPA00077; UER00156.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteroate synthaseUniRule annotation (EC:2.5.1.15UniRule annotation)
Short name:
DHPSUniRule annotation
Alternative name(s):
Dihydropteroate pyrophosphorylaseUniRule annotation
Gene namesi
Name:folPImported
Ordered Locus Names:GBAA_0071Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075045.

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_0071.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TWSX-ray2.00A/B5-280[»]
1TWWX-ray2.50A/B5-280[»]
1TWZX-ray2.75A/B5-280[»]
1TX0X-ray2.15A/B5-280[»]
1TX2X-ray1.83A/B5-280[»]
3H21X-ray2.32A/B5-280[»]
3H22X-ray2.40A/B5-280[»]
3H23X-ray2.20A/B5-280[»]
3H24X-ray2.50A/B5-280[»]
3H26X-ray2.50A/B5-280[»]
3H2AX-ray2.40A/B5-280[»]
3H2CX-ray2.60A/B5-280[»]
3H2EX-ray2.00A/B5-280[»]
3H2FX-ray2.20A/B5-280[»]
3H2MX-ray2.31A/B5-280[»]
3H2NX-ray2.40A/B5-280[»]
3H2OX-ray2.70A/B5-280[»]
3TYAX-ray2.61A/B5-280[»]
3TYBX-ray2.60A/B5-280[»]
3TYCX-ray2.30A/B5-280[»]
3TYDX-ray2.50A/B5-280[»]
3TYEX-ray2.30A/B5-280[»]
4D8AX-ray2.18A/B5-280[»]
4D8ZX-ray2.20A/B5-280[»]
4D9PX-ray2.26A/B5-280[»]
4DAFX-ray2.50A/B5-280[»]
4DAIX-ray2.50A/B5-280[»]
4DB7X-ray2.50A/B5-280[»]
4NHVX-ray1.99A/B5-280[»]
4NILX-ray2.18A/B5-280[»]
4NIRX-ray1.77A/B5-280[»]
4NL1X-ray2.30A/B5-280[»]
SMRiQ81VW8. Positions 5-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 269247Pterin-bindingInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the DHPS family.UniRule annotation
Contains 1 pterin-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EEI. Bacteria.
COG0294. LUCA.
KOiK00796.
OMAiSIDTYHA.

Family and domain databases

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.

Q81VW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCSLKWDYDL RCGEYTLNLN EKTLIMGILN VTPDSFSDGG SYNEVDAAVR
60 70 80 90 100
HAKEMRDEGA HIIDIGGEST RPGFAKVSVE EEIKRVVPMI QAVSKEVKLP
110 120 130 140 150
ISIDTYKAEV AKQAIEAGAH IINDIWGAKA EPKIAEVAAH YDVPIILMHN
160 170 180 190 200
RDNMNYRNLM ADMIADLYDS IKIAKDAGVR DENIILDPGI GFAKTPEQNL
210 220 230 240 250
EAMRNLEQLN VLGYPVLLGT SRKSFIGHVL DLPVEERLEG TGATVCLGIE
260 270 280
KGCEFVRVHD VKEMSRMAKM MDAMIGKGVK
Length:280
Mass (Da):30,976
Last modified:June 1, 2003 - v1
Checksum:iACEB54F50658A69B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29149.1.
DQ139876 Genomic DNA. Translation: AAZ65853.1.

Genome annotation databases

EnsemblBacteriaiAAT29149; AAT29149; GBAA_0071.
KEGGibar:GBAA_0071.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29149.1.
DQ139876 Genomic DNA. Translation: AAZ65853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TWSX-ray2.00A/B5-280[»]
1TWWX-ray2.50A/B5-280[»]
1TWZX-ray2.75A/B5-280[»]
1TX0X-ray2.15A/B5-280[»]
1TX2X-ray1.83A/B5-280[»]
3H21X-ray2.32A/B5-280[»]
3H22X-ray2.40A/B5-280[»]
3H23X-ray2.20A/B5-280[»]
3H24X-ray2.50A/B5-280[»]
3H26X-ray2.50A/B5-280[»]
3H2AX-ray2.40A/B5-280[»]
3H2CX-ray2.60A/B5-280[»]
3H2EX-ray2.00A/B5-280[»]
3H2FX-ray2.20A/B5-280[»]
3H2MX-ray2.31A/B5-280[»]
3H2NX-ray2.40A/B5-280[»]
3H2OX-ray2.70A/B5-280[»]
3TYAX-ray2.61A/B5-280[»]
3TYBX-ray2.60A/B5-280[»]
3TYCX-ray2.30A/B5-280[»]
3TYDX-ray2.50A/B5-280[»]
3TYEX-ray2.30A/B5-280[»]
4D8AX-ray2.18A/B5-280[»]
4D8ZX-ray2.20A/B5-280[»]
4D9PX-ray2.26A/B5-280[»]
4DAFX-ray2.50A/B5-280[»]
4DAIX-ray2.50A/B5-280[»]
4DB7X-ray2.50A/B5-280[»]
4NHVX-ray1.99A/B5-280[»]
4NILX-ray2.18A/B5-280[»]
4NIRX-ray1.77A/B5-280[»]
4NL1X-ray2.30A/B5-280[»]
SMRiQ81VW8. Positions 5-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_0071.

Chemistry

ChEMBLiCHEMBL1075045.

Protocols and materials databases

DNASUi1083704.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT29149; AAT29149; GBAA_0071.
KEGGibar:GBAA_0071.

Phylogenomic databases

eggNOGiENOG4105EEI. Bacteria.
COG0294. LUCA.
KOiK00796.
OMAiSIDTYHA.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BioCyciANTHRA:FOLP-MONOMER.
BANT260799:GJAJ-80-MONOMER.
BANT261594:GJ7F-82-MONOMER.
BRENDAi2.5.1.15. 634.

Family and domain databases

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 nameiQ81VW8_BACAN
AccessioniPrimary (citable) accession number: Q81VW8
Secondary accession number(s): E9QTW3
, E9QTW4, E9QTW5, Q2QCA4, Q6I4X2, Q6KYL6
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: September 7, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.