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Q54YD9 (FOL1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Folic acid synthesis protein FOL1

Including the following 3 domains:

  1. Dihydroneopterin aldolase
    Short name=DHNA
    EC=4.1.2.25
  2. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
    EC=2.7.6.3
    Alternative name(s):
    6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
    Short name=PPPK
    7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
    Short name=HPPK
  3. Dihydropteroate synthase
    Short name=DHPS
    EC=2.5.1.15
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
Gene names
Name:fol1
ORF Names:DDB_G0278283
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes three sequential steps of tetrahydrofolate biosynthesis By similarity.

Catalytic activity

2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.

ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.

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

Cofactor

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

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.

Sequence similarities

In the N-terminal section; belongs to the DHNA family.

In the central section; belongs to the HPPK family.

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

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Folic acid synthesis protein FOL1
PRO_0000328111

Regions

Domain333 – 641309Pterin-binding
Region1 – 116116DHNA
Region149 – 274126HPPK
Region325 – 657333DHPS
Region380 – 3812Substrate binding By similarity
Compositional bias303 – 3064Poly-Pro
Compositional bias462 – 51655Asn-rich
Compositional bias485 – 50925Poly-Asn

Sites

Metal binding3401Magnesium By similarity
Binding site3481Substrate By similarity
Binding site4161Substrate By similarity
Binding site4351Substrate By similarity
Binding site5471Substrate By similarity
Binding site5831Substrate By similarity
Binding site6291Substrate By similarity
Binding site6311Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54YD9 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: C1CA4397EE959845

FASTA65773,720
        10         20         30         40         50         60 
MDKIIIKDLL IQAVIGVNPG ERIIKQNIII SVTAYKDLSK CGSSDNVIDT VSYSSLSKSI 

        70         80         90        100        110        120 
CSYSESSHHY TLEALATGVA KICCLGFGIE RVKVLVQKPG AIKLAKWPGV QIERTLDYFK 

       130        140        150        160        170        180 
SNSFVEIPSK LINNNKNSNN SNAGNNIVYL AFGSNLGDKF QNILNSFKRL EKQCFIQSTS 

       190        200        210        220        230        240 
FMYESSPQYY REQDSFYNCA CKVSTDLKPH DLLKFIKQIE NDMGRVETFR NGPRVIDIDI 

       250        260        270        280        290        300 
IYYNGLIIKT DDLEIPHPLM WERDFVLLPL SDIAPNFIHP TLHITTNRMK LNLPNGGNIH 

       310        320        330        340        350        360 
NIPPPPTATT TCNNIIEKVI RIGNLNYNWN DKTFIMGILN VTPDSFVDGG KFNTLEKSIQ 

       370        380        390        400        410        420 
QATALIEQGA DIIDIGGQST YPGAQQISIE EEINRVVPTI KKIREVLGND IPLSIDTLHH 

       430        440        450        460        470        480 
QVAKEAILAG CNIINDVSGE FRVPIILNHS QPTTQYLQQK QNEQYLNNSN DSNSNSSINT 

       490        500        510        520        530        540 
NGEDNNNNNN NNNNNNNNNN NNNNNNNNND DNDNDNRSKI KQKIDLSSPK IETCTKLGLF 

       550        560        570        580        590        600 
RWQIILDPGL GFYKTYEQSI EILQRGKELM GLGFPVLIGP SRKGFIANTI ANAEKDKSLP 

       610        620        630        640        650 
PPSPKSERRL WGTIACCCIG SMWGANIIRI HDIPEIRDAM LISDSVNKPQ RRYQIQK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000023 Genomic DNA. Translation: EAL68314.1.

3D structure databases

ProteinModelPortalQ54YD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0230139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0230139; DDB0230139; DDB_G0278283.
KEGGddi:DDB_G0278283.

Organism-specific databases

dictyBaseDDB_G0278283. fol1.

Phylogenomic databases

eggNOGCOG0294.
KOK13939.
OMAWQIILDP.
PhylomeDBQ54YD9.
ProtClustDBCLSZ2729110.

Enzyme and pathway databases

UniPathwayUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProIPR011005. Dihydropteroate_synth-like.
IPR006157. FolB_dom.
IPR000550. Hppk.
IPR000489. Pterin-binding.
[Graphical view]
PfamPF02152. FolB. 1 hit.
PF01288. HPPK. 1 hit.
PF00809. Pterin_bind. 1 hit.
[Graphical view]
SMARTSM00905. FolB. 1 hit.
[Graphical view]
SUPFAMSSF51717. SSF51717. 2 hits.
SSF55083. SSF55083. 1 hit.
TIGRFAMsTIGR00526. folB_dom. 1 hit.
TIGR01498. folK. 1 hit.
PROSITEPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS00794. HPPK. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOL1_DICDI
AccessionPrimary (citable) accession number: Q54YD9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase