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Entry version 115 (29 Sep 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Bifunctional dihydropteroate synthase/dihydropteroate reductase

Gene

folP

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Bifunctional enzyme that catalyzes the formation of dihydropteroate, the immediate precursor of folic acid and the reduction of dihydropteroate to tetrahydropteroate.

2 Publications

Miscellaneous

FolP can complement an E.coli strain in which the two distinct genes encoding dihydrofolate reductases folA and folM are deleted.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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. 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi126MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2026-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei2216-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei2896-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei3256-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFolate biosynthesis
LigandFAD, Flavoprotein, FMN, Magnesium, Metal-binding, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
HPY:HP1232-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00077;UER00156

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional dihydropteroate synthase/dihydropteroate reductase
Including the following 2 domains:
Dihydropteroate reductase1 Publication (EC:1.5.8.-1 Publication)
Short name:
DHPR1 Publication
Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
Short name:
DHPS1 Publication
Alternative name(s):
Dihydropteroate pyrophosphorylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:folP1 Publication
Ordered Locus Names:C694_06360, HP_1232
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri85962 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000429 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi28M → A: Unable to bind FMN. 1 Publication1
Mutagenesisi31K → A: Unable to bind FMN. 1 Publication1
Mutagenesisi51K → A: Unstable protein. 1 Publication1
Mutagenesisi58G → A: No effect. 1 Publication1
Mutagenesisi92K → E: Unable to bind FMN. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004286751 – 380Bifunctional dihydropteroate synthase/dihydropteroate reductaseAdd BLAST380

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O25830

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-3693N

Protein interaction database and analysis system

More...
IntActi
O25830, 1 interactor

Molecular INTeraction database

More...
MINTi
O25830

STRING: functional protein association networks

More...
STRINGi
85962.C694_06360

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O25830

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini119 – 371Pterin-bindingPROSITE-ProRule annotationAdd BLAST253

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 104Dihydropteroate reductaseAdd BLAST104
Regioni105 – 380Dihydropteroate synthaseAdd BLAST276
Regioni359 – 3616-hydroxymethyl-7,8-dihydropterin diphosphate bindingBy similarity3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal extension of FolP is essential for the reducing activity and binds FMN.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the C-terminal section; belongs to the DHPS family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0294, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_008023_1_0_7

Identification of Orthologs from Complete Genome Data

More...
OMAi
VGASRKN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O25830

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00739, DHPS, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006390, DHP_synth_dom
IPR011005, Dihydropteroate_synth-like
IPR016227, Dihydropteroate_synthase_prd
IPR000489, Pterin-binding_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00809, Pterin_bind, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000501, DHPS_Campy_prd, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51717, SSF51717, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01496, DHPS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50972, PTERIN_BINDING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O25830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVKRLNPDA LKNALQKIGP EKIAQDRMHQ KGVSFVFEIQ HLPLSATLIL
60 70 80 90 100
KQEAISVGGD FATPRDCILA KEPFYDGVLI ASAKQLERLI VKCHSQPFGL
110 120 130 140 150
KHLAQELKSH LKAPKPNTPQ IMAVLNLTPD SFYEKSRFDS KKALEEIYQW
160 170 180 190 200
LEKGITLIDI GAASSRPESE IIDPKIEQDR LKEILLEIKS QKLYQCAKFS
210 220 230 240 250
IDTYHATTAQ MALEHYFSIL NDVSGFNSAE MLEVAKDYKP TCILMHTQKT
260 270 280 290 300
PKDMQENVFY HNLFDEMDRF FKEKLEVLEK YVLQDIILDI GFGFAKLKEH
310 320 330 340 350
NLALIKHLSH FLKFKKPLLV GASRKNTIGL ITGREVQDRL AGTLSLHLMA
360 370 380
LQNGASVLRV HDIDEHIDLI KVFKSLEETD
Length:380
Mass (Da):43,275
Last modified:January 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i618C39DFDA39B174
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE000511 Genomic DNA Translation: AAD08276.1
CP003904 Genomic DNA Translation: AFV42447.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H64673

NCBI Reference Sequences

More...
RefSeqi
NP_208024.1, NC_000915.1
WP_000636048.1, NC_018939.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAD08276; AAD08276; HP_1232

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
heo:C694_06360
hpy:HP1232

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|85962.47.peg.1320

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA Translation: AAD08276.1
CP003904 Genomic DNA Translation: AFV42447.1
PIRiH64673
RefSeqiNP_208024.1, NC_000915.1
WP_000636048.1, NC_018939.1

3D structure databases

SMRiO25830
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-3693N
IntActiO25830, 1 interactor
MINTiO25830
STRINGi85962.C694_06360

Proteomic databases

PaxDbiO25830

Genome annotation databases

EnsemblBacteriaiAAD08276; AAD08276; HP_1232
KEGGiheo:C694_06360
hpy:HP1232
PATRICifig|85962.47.peg.1320

Phylogenomic databases

eggNOGiCOG0294, Bacteria
HOGENOMiCLU_008023_1_0_7
OMAiVGASRKN
PhylomeDBiO25830

Enzyme and pathway databases

UniPathwayiUPA00077;UER00156
BioCyciHPY:HP1232-MONOMER

Family and domain databases

CDDicd00739, DHPS, 1 hit
Gene3Di3.20.20.20, 1 hit
InterProiView protein in InterPro
IPR006390, DHP_synth_dom
IPR011005, Dihydropteroate_synth-like
IPR016227, Dihydropteroate_synthase_prd
IPR000489, Pterin-binding_dom
PfamiView protein in Pfam
PF00809, Pterin_bind, 1 hit
PIRSFiPIRSF000501, DHPS_Campy_prd, 1 hit
SUPFAMiSSF51717, SSF51717, 1 hit
TIGRFAMsiTIGR01496, DHPS, 1 hit
PROSITEiView protein in PROSITE
PS50972, PTERIN_BINDING, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHPRS_HELPY
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O25830
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: January 1, 1998
Last modified: September 29, 2021
This is version 115 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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