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P15925 (FOLC_LACCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 94. 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:
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 lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of folates to polyglutamate derivatives. It prefers 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.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolylpolyglutamate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05221 Genomic DNA. Translation: AAA88210.1.
PIRA35534.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP15925.
SMRP15925. Positions 1-425.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP15925.
UniPathwayUPA00850.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERPTHR11136. PTHR11136. 1 hit.
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsTIGR01499. folC. 1 hit.
PROSITEPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15925.

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: October 16, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways