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Protein

Folylpolyglutamate synthase

Gene

fgs

Organism
Lactobacillus casei
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: tetrahydrofolylpolyglutamate biosynthesis

This protein is involved in the pathway tetrahydrofolylpolyglutamate biosynthesis, which is part of Cofactor biosynthesis.
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
Binding sitei73ATP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei73Substrate; via carbonyl oxygenCombined sources1 Publication1
Binding sitei75Folate; via amide nitrogenCombined sources1 Publication1
Binding sitei82FolateCombined sources1 Publication1
Binding sitei143ATPCombined sources1 Publication1
Binding sitei143SubstrateCombined sources1 Publication1
Binding sitei264SubstrateCombined sources1 Publication1
Binding sitei300SubstrateCombined sources1 Publication1
Binding sitei413Substrate; via amide nitrogenCombined sources1 Publication1
Binding sitei417FolateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 52ATPCombined sources1 Publication7
Nucleotide bindingi299 – 300ATPCombined sources1 Publication2
Nucleotide bindingi316 – 317ATPCombined sources1 Publication2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.2.17. 2854.
SABIO-RKP15925.
UniPathwayiUPA00850.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:fgs
OrganismiLactobacillus casei
Taxonomic identifieri1582 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi316H → A: Loss of activity. 1 Publication1
Mutagenesisi412S → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001683051 – 428Folylpolyglutamate synthaseAdd BLAST428

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Helixi23 – 31Combined sources9
Helixi35 – 37Combined sources3
Beta strandi41 – 45Combined sources5
Beta strandi47 – 49Combined sources3
Helixi50 – 63Combined sources14
Beta strandi68 – 71Combined sources4
Beta strandi76 – 78Combined sources3
Helixi79 – 82Combined sources4
Beta strandi83 – 85Combined sources3
Helixi92 – 112Combined sources21
Helixi120 – 134Combined sources15
Beta strandi138 – 143Combined sources6
Beta strandi145 – 148Combined sources4
Beta strandi159 – 163Combined sources5
Helixi168 – 170Combined sources3
Helixi171 – 174Combined sources4
Helixi178 – 185Combined sources8
Helixi186 – 188Combined sources3
Beta strandi195 – 197Combined sources3
Helixi202 – 215Combined sources14
Beta strandi219 – 221Combined sources3
Turni222 – 224Combined sources3
Beta strandi225 – 233Combined sources9
Beta strandi235 – 244Combined sources10
Beta strandi247 – 255Combined sources9
Helixi260 – 278Combined sources19
Helixi285 – 293Combined sources9
Beta strandi300 – 305Combined sources6
Turni306 – 309Combined sources4
Beta strandi310 – 313Combined sources4
Helixi318 – 331Combined sources14
Beta strandi337 – 341Combined sources5
Beta strandi343 – 345Combined sources3
Helixi348 – 358Combined sources11
Beta strandi360 – 364Combined sources5
Helixi391 – 401Combined sources11
Beta strandi407 – 412Combined sources6
Helixi413 – 423Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP15925.
SMRiP15925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15925.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 52Substrate bindingCombined sources1 Publication5
Regioni313 – 316Substrate bindingCombined sources1 Publication4

Sequence similaritiesi

Belongs to the folylpolyglutamate synthase family.Curated

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProiIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYTETVAYI HSFPRLAKTG DHRRILTLLH ALGNPQQQGR YIHVTGTNGK
60 70 80 90 100
GSAANAIAHV LEASGLTVGL YTSPFIMRFN ERIMIDHEPI PDAALVNAVA
110 120 130 140 150
FVRAALERLQ QQQADFNVTE FEFITALGYW YFRQRQVDVA VIEVGIGGDT
160 170 180 190 200
DSTNVITPVV SVLTEVALDH QKLLGHTITA IAKHKAGIIK RGIPVVTGNL
210 220 230 240 250
VPDAAAVVAA KVATTGSQWL RFDRDFSVPK AKLHGWGQRF TYEDQDGRIS
260 270 280 290 300
DLEVPLVGDY QQRNMAIAIQ TAKVYAKQTE WPLTPQNIRQ GLAASHWPAR
310 320 330 340 350
LEKISDTPLI VIDGAHNPDG INGLITALKQ LFSQPITVIA GILADKDYAA
360 370 380 390 400
MADRLTAAFS TVYLVPVPGT PRALPEAGYE ALHEGRLKDS WQEALAASLN
410 420
DVPDQPIVIT GSLYLASAVR QTLLGGKS
Length:428
Mass (Da):46,589
Last modified:April 1, 1990 - v1
Checksum:iE4B0B9ED62140181
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05221 Genomic DNA. Translation: AAA88210.1.
PIRiA35534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05221 Genomic DNA. Translation: AAA88210.1.
PIRiA35534.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP15925.
SMRiP15925.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00850.
BRENDAi6.3.2.17. 2854.
SABIO-RKP15925.

Miscellaneous databases

EvolutionaryTraceiP15925.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProiIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFOLC_LACCA
AccessioniPrimary (citable) accession number: P15925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.