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Entry version 102 (17 Jun 2020)
Sequence version 1 (01 Dec 1992)
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Protein

Folic acid synthesis protein fol1

Gene

fol1

Organism
Pneumocystis carinii
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

Catalyzes three sequential steps of tetrahydrofolate biosynthesis.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.3 µM for 7,8-dihydroneopterin2 Publications
  2. KM=3.6 µM for 6-hydroxymethyl-7,8-dihydropterin2 Publications
  1. Vmax=36 nmol/min/mg enzyme for 7,8-dihydroneopterin2 Publications

pH dependencei

Optimum pH is 8.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 3 and 4 of the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Folic acid synthesis protein fol1 (fol1)
  4. Folic acid synthesis protein fol1 (fol1)
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 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

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. Folic acid synthesis protein fol1 (fol1)
  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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi478MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei5176-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei5526-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei5716-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei6436-hydroxymethyl-7,8-dihydropterin diphosphateBy similarity1
Binding sitei6836-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 functionKinase, Lyase, Multifunctional enzyme, Transferase
Biological processFolate biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P29251

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

More...
UniPathwayi
UPA00077;UER00154
UPA00077;UER00155
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%5Fand%5Ftaxonomy%5Fsection">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:
Folic acid synthesis protein fol1
Including the following 3 domains:
Dihydroneopterin aldolase1 Publication (EC:4.1.2.252 Publications)
Short name:
DHNA1 Publication
Alternative name(s):
7,8-dihydroneopterin aldolase
FasA1 Publication
FasB1 Publication
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase1 Publication (EC:2.7.6.32 Publications)
Short name:
HPPK
Alternative name(s):
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
Short name:
PPPK1 Publication
Dihydropterin pyrophosphokinase1 Publication
FasC1 Publication
Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
Short name:
DHPS1 Publication
Alternative name(s):
Dihydropteroate pyrophosphorylase
FasD1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:fol1
Synonyms:fas1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPneumocystis carinii
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri4754 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi39D → E: Abolishes DHNA activity. 1 Publication1
Mutagenesisi53G → A: Reduces DHNA activity 11-fold. 1 Publication1
Mutagenesisi63Q → N: Reduces DHNA activity 16-fold. 1 Publication1
Mutagenesisi161D → E: No effect. 1 Publication1
Mutagenesisi175G → A: Abolishes DHNA activity. 1 Publication1
Mutagenesisi185Q → N: Reduces DHNA activity 24-fold. 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_00001682421 – 740Folic acid synthesis protein fol1Add BLAST740

<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
P29251

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%5Fand%5Fdomains%5Fsection">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>Domaini471 – 730Pterin-bindingPROSITE-ProRule annotationAdd BLAST260

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>Regioni39 – 160DHNA 1Add BLAST122
Regioni161 – 280DHNA 2Add BLAST120
Regioni291 – 449HPPKAdd BLAST159
Regioni473 – 740DHPSAdd BLAST268
Regioni718 – 7206-hydroxymethyl-7,8-dihydropterin diphosphate bindingBy similarity3

<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 N-terminal section; belongs to the DHNA family.Curated
In the central section; belongs to the HPPK family.Curated
In the C-terminal section; belongs to the DHPS family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00534, DHNA_DHNTPE, 2 hits
cd00739, DHPS, 1 hit
cd00483, HPPK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.20, 1 hit
3.30.1130.10, 2 hits
3.30.70.560, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006390, DHP_synth
IPR011005, Dihydropteroate_synth-like
IPR006157, FolB_dom
IPR016261, Folic_acid_synth
IPR043133, GTP-CH-I_C/QueF
IPR000550, Hppk
IPR035907, Hppk_sf
IPR000489, Pterin-binding_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02152, FolB, 2 hits
PF01288, HPPK, 1 hit
PF00809, Pterin_bind, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000741, Folic_acid_synth, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00905, FolB, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51717, SSF51717, 1 hit
SSF55083, SSF55083, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01496, DHPS, 1 hit
TIGR00526, folB_dom, 2 hits
TIGR01498, folK, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00792, DHPS_1, 1 hit
PS00793, DHPS_2, 1 hit
PS00794, HPPK, 1 hit
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P29251-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIFKSLKIFP FYQIYGFRFL KGMIFKKKIH LSKLNKNHDL IHIHSLTLKS
60 70 80 90 100
IVGKNSWAQR LLQPVVLTLS MGINASLSGN MDDLSYSIDY ATVYKEVFKL
110 120 130 140 150
VENSKFENLL DLSDKISKVV LGDKCKGNWV KVIAETPKGH LLAETGLQII
160 170 180 190 200
RRKDGIREID DQFFIKNLSL YTIIGINPEE RVNKQNIIID LILFKSSINL
210 220 230 240 250
ECKDDFIINT YNIEKLLKEI VKHVEESTFK TIEALALSIA RISCISHNIE
260 270 280 290 300
KIIVKVKKSC ALAFAESAGV EIVRSRSCFS SNNYIKSENS IDNEAVYISL
310 320 330 340 350
GSNLGNRIKF ILDAIEKMSI KGIKVLKTSM LYESKPMYFK DQPAFYNAVC
360 370 380 390 400
KVQTSLHPEQ LLFELQLIEK ELGRVKVIDK GPRCIDLDIV FYGRKIINSE
410 420 430 440 450
SLIIPHPRVL ERSFVLKPLL DISGDLVHPV TGLSIASYFE KIVDHDIKPV
460 470 480 490 500
LPFLYKNKSI DFSFRSYKAP TYIMAILNLT PDSFFDGGIH SYDSVLIDVE
510 520 530 540 550
KFINAGATII DIGGQSTRPG SYIIPLEEEI FRVIPAIKYL QKTYPDILIS
560 570 580 590 600
IDTFRSEVAE QAVKAGASLV NDISGGRYDP KMFNTVARLK VPICIMHMRG
610 620 630 640 650
NFLNMDNLTD YGTDIIEQIT IELEKLLNSA EKSGIPRWNI ILDPGLGFSK
660 670 680 690 700
TLHQNIELLR RFNELKSKNC FNGLPWLLGP SRKRFTGFIT GDNMPKDRIW
710 720 730 740
GTVAAVVASI SGGCDIIRVH DVYEMYKISK MSDAIWKEIY
Length:740
Mass (Da):83,962
Last modified:December 1, 1992 - 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:i328F6EB91B4499EB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M86602 Genomic DNA Translation: AAA33790.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S28666

<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
M86602 Genomic DNA Translation: AAA33790.1
PIRiS28666

3D structure databases

SMRiP29251
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00077;UER00154
UPA00077;UER00155
UPA00077;UER00156
SABIO-RKiP29251

Family and domain databases

CDDicd00534, DHNA_DHNTPE, 2 hits
cd00739, DHPS, 1 hit
cd00483, HPPK, 1 hit
Gene3Di3.20.20.20, 1 hit
3.30.1130.10, 2 hits
3.30.70.560, 1 hit
InterProiView protein in InterPro
IPR006390, DHP_synth
IPR011005, Dihydropteroate_synth-like
IPR006157, FolB_dom
IPR016261, Folic_acid_synth
IPR043133, GTP-CH-I_C/QueF
IPR000550, Hppk
IPR035907, Hppk_sf
IPR000489, Pterin-binding_dom
PfamiView protein in Pfam
PF02152, FolB, 2 hits
PF01288, HPPK, 1 hit
PF00809, Pterin_bind, 1 hit
PIRSFiPIRSF000741, Folic_acid_synth, 1 hit
SMARTiView protein in SMART
SM00905, FolB, 2 hits
SUPFAMiSSF51717, SSF51717, 1 hit
SSF55083, SSF55083, 1 hit
TIGRFAMsiTIGR01496, DHPS, 1 hit
TIGR00526, folB_dom, 2 hits
TIGR01498, folK, 1 hit
PROSITEiView protein in PROSITE
PS00792, DHPS_1, 1 hit
PS00793, DHPS_2, 1 hit
PS00794, HPPK, 1 hit
PS50972, PTERIN_BINDING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiFOL1_PNECA
<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: P29251
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 17, 2020
This is version 102 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 programFungal 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

Direct protein sequencing

Documents

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