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Protein

Dihydrofolate synthase/folylpolyglutamate synthase

Gene

folC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives.By similarity

Catalytic activityi

ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate.By similarity
ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).By similarity

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (sul)
  2. Dihydrofolate synthase/folylpolyglutamate synthase (folC)
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.

Pathwayi: tetrahydrofolylpolyglutamate biosynthesis

This protein is involved in the pathway tetrahydrofolylpolyglutamate biosynthesis, which is part of Cofactor biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolylpolyglutamate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi75Magnesium 1By similarity1
Metal bindingi145Magnesium 1By similarity1
Metal bindingi172Magnesium 2By similarity1
Binding sitei263ATPBy similarity1
Binding sitei302ATPBy similarity1
Binding sitei315ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi51 – 54ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processFolate biosynthesis, One-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU28080-MONOMER.
UniPathwayiUPA00077; UER00157.
UPA00850.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate synthase/folylpolyglutamate synthase (EC:6.3.2.12, EC:6.3.2.17)
Short name:
DHFS / FPGS
Alternative name(s):
Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase
Folylpolyglutamate synthetase
Tetrahydrofolylpolyglutamate synthase
Gene namesi
Name:folC
Ordered Locus Names:BSU28080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001682991 – 430Dihydrofolate synthase/folylpolyglutamate synthaseAdd BLAST430

Proteomic databases

PaxDbiQ05865.
PRIDEiQ05865.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015346.

Structurei

3D structure databases

ProteinModelPortaliQ05865.
SMRiQ05865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 1177,8-dihydropteroate bindingBy similarity4
Regioni152 – 1547,8-dihydropteroate bindingBy similarity3

Sequence similaritiesi

Belongs to the folylpolyglutamate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105DPM. Bacteria.
COG0285. LUCA.
HOGENOMiHOG000019981.
InParanoidiQ05865.
KOiK11754.
OMAiVVTENSW.
PhylomeDBiQ05865.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
InterProiView protein in InterPro
IPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiView protein in Pfam
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiView protein in PROSITE
PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05865-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTAYQDARS WIHGRLKFGV KPGLGRMKQL MARLGHPEKK IRAFHVAGTN
60 70 80 90 100
GKGSTVAFIR SMLQEAGYTV GTFTSPYIIT FNERISVNGI PISDEEWTAL
110 120 130 140 150
VNQMKPHVEA LDQTEYGQPT EFEIMTACAF LYFAEFHKVD FVIFETGLGG
160 170 180 190 200
RFDSTNVVEP LLTVITSIGH DHMNILGNTI EEIAGEKAGI IKEGIPIVTA
210 220 230 240 250
VTQPEALQVI RHEAERHAAP FQSLHDACVI FNEEALPAGE QFSFKTEEKC
260 270 280 290 300
YEDIRTSLIG THQRQNAALS ILAAEWLNKE NIAHISDEAL RSGLVKAAWP
310 320 330 340 350
GRLELVQEHP PVYLDGAHNE EGVEKLAETM KQRFANSRIS VVFSALKDKP
360 370 380 390 400
YQNMIKRLET IAHAIHFASF DFPRASLAKD LYDASEISNK SWSEDPDDVI
410 420 430
KFIESKKGSN EIVLITGSLY FISDIRKRLK
Length:430
Mass (Da):48,165
Last modified:October 1, 1994 - v2
Checksum:i8AD1DF9151D51160
GO

Sequence cautioni

The sequence AAA83364 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti295V → M in AAA83364 (PubMed:9384377).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04520 Genomic DNA. Translation: AAB59021.1.
AL009126 Genomic DNA. Translation: CAB14768.1.
M30805 Genomic DNA. Translation: AAA83364.1. Different initiation.
PIRiB40646.
RefSeqiNP_390686.1. NC_000964.3.
WP_003229640.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14768; CAB14768; BSU28080.
GeneIDi936327.
KEGGibsu:BSU28080.
PATRICi18977490. VBIBacSub10457_2934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04520 Genomic DNA. Translation: AAB59021.1.
AL009126 Genomic DNA. Translation: CAB14768.1.
M30805 Genomic DNA. Translation: AAA83364.1. Different initiation.
PIRiB40646.
RefSeqiNP_390686.1. NC_000964.3.
WP_003229640.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliQ05865.
SMRiQ05865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015346.

Proteomic databases

PaxDbiQ05865.
PRIDEiQ05865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14768; CAB14768; BSU28080.
GeneIDi936327.
KEGGibsu:BSU28080.
PATRICi18977490. VBIBacSub10457_2934.

Phylogenomic databases

eggNOGiENOG4105DPM. Bacteria.
COG0285. LUCA.
HOGENOMiHOG000019981.
InParanoidiQ05865.
KOiK11754.
OMAiVVTENSW.
PhylomeDBiQ05865.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00157.
UPA00850.
BioCyciBSUB:BSU28080-MONOMER.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
InterProiView protein in InterPro
IPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiView protein in Pfam
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiView protein in PROSITE
PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFOLC_BACSU
AccessioniPrimary (citable) accession number: Q05865
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1994
Last modified: May 10, 2017
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.