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Reviewed, UniProtKB/Swiss-Prot P15925 (FOLC_LACCA)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Folylpolyglutamate synthase
    EC=6.3.2.17
Alternative name(s):
    Folylpoly-gamma-glutamate synthetase
      Short name=FPGS
    Tetrahydrofolylpolyglutamate synthase
      Short name=Tetrahydrofolate synthase
Gene names
Name: fgs
OrganismLactobacillus casei
Taxonomic identifier1582 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Conversion of folates to polyglutamate derivatives. It preferes 5,10-methylenetetrahydrofolate, rather than 10-formyltetrahydrofolate as folate substrate.

Catalytic activity

ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).

Pathway

Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.

Subunit structure

Monomer.

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Folylpolyglutamate synthase
PRO_0000168305

Regions

Nucleotide binding46 – 527ATP

Secondary structure

.............................................................. 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15925-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E4B0B9ED62140181

FASTA42846,589
        10         20         30         40         50         60 
MNYTETVAYI HSFPRLAKTG DHRRILTLLH ALGNPQQQGR YIHVTGTNGK GSAANAIAHV 

        70         80         90        100        110        120 
LEASGLTVGL YTSPFIMRFN ERIMIDHEPI PDAALVNAVA FVRAALERLQ QQQADFNVTE 

       130        140        150        160        170        180 
FEFITALGYW YFRQRQVDVA VIEVGIGGDT DSTNVITPVV SVLTEVALDH QKLLGHTITA 

       190        200        210        220        230        240 
IAKHKAGIIK RGIPVVTGNL VPDAAAVVAA KVATTGSQWL RFDRDFSVPK AKLHGWGQRF 

       250        260        270        280        290        300 
TYEDQDGRIS DLEVPLVGDY QQRNMAIAIQ TAKVYAKQTE WPLTPQNIRQ GLAASHWPAR 

       310        320        330        340        350        360 
LEKISDTPLI VIDGAHNPDG INGLITALKQ LFSQPITVIA GILADKDYAA MADRLTAAFS 

       370        380        390        400        410        420 
TVYLVPVPGT PRALPEAGYE ALHEGRLKDS WQEALAASLN DVPDQPIVIT GSLYLASAVR 


QTLLGGKS 

« Hide

References

[1]"Cloning and expression of the gene encoding Lactobacillus casei folylpoly-gamma-glutamate synthetase in Escherichia coli and determination of its primary structure."
Toy J., Bognar A.L.
J. Biol. Chem. 265:2492-2499(1990) [PubMed: 2105929] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase."
Sun X., Bognar A.L., Baker E.N., Smith C.A.
Proc. Natl. Acad. Sci. U.S.A. 95:6647-6652(1998) [PubMed: 9618466] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

J05221 Genomic DNA. Translation: AAA88210.1.
PIRA35534.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FGSX-ray2.40A1-428[»]
1JBVX-ray1.95A1-428[»]
1JBWX-ray1.85A1-428[»]
2GC5X-ray1.85A1-428[»]
2GC6X-ray1.90A1-428[»]
2GCAX-ray2.40A1-428[»]
2GCBX-ray2.30A1-428[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.3.2.17. 610.

Family and domain databases

InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR001645. Fpolygl_synthtse.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
Gene3DG3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
PANTHERPTHR11136. Fpolygl_synthtse. 1 hit.
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01499. folC. 1 hit.
PROSITEPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOLC_LACCA
AccessionPrimary (citable) accession number: P15925
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents