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P15925

- FOLC_LACCA

UniProt

P15925 - FOLC_LACCA

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Protein

Folylpolyglutamate synthase

Gene
fgs
Organism
Lactobacillus casei
Status
Reviewed - Annotation score: 4 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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 527ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. tetrahydrofolylpolyglutamate synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Folylpolyglutamate synthasePRO_0000168305Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108
Helixi23 – 319
Helixi35 – 373
Beta strandi41 – 455
Beta strandi47 – 493
Helixi50 – 6314
Beta strandi68 – 714
Beta strandi76 – 783
Helixi79 – 824
Beta strandi83 – 853
Helixi92 – 11221
Helixi120 – 13415
Beta strandi138 – 1436
Beta strandi145 – 1484
Beta strandi159 – 1635
Helixi168 – 1703
Helixi171 – 1744
Helixi178 – 1858
Helixi186 – 1883
Beta strandi195 – 1973
Helixi202 – 21514
Beta strandi219 – 2213
Turni222 – 2243
Beta strandi225 – 2339
Beta strandi235 – 24410
Beta strandi247 – 2559
Helixi260 – 27819
Helixi285 – 2939
Beta strandi300 – 3056
Turni306 – 3094
Beta strandi310 – 3134
Helixi318 – 33114
Beta strandi337 – 3415
Beta strandi343 – 3453
Helixi348 – 35811
Beta strandi360 – 3645
Helixi391 – 40111
Beta strandi407 – 4126
Helixi413 – 42311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-425.

Miscellaneous databases

EvolutionaryTraceiP15925.

Family & Domainsi

Sequence similaritiesi

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

MNYTETVAYI HSFPRLAKTG DHRRILTLLH ALGNPQQQGR YIHVTGTNGK    50
GSAANAIAHV LEASGLTVGL YTSPFIMRFN ERIMIDHEPI PDAALVNAVA 100
FVRAALERLQ QQQADFNVTE FEFITALGYW YFRQRQVDVA VIEVGIGGDT 150
DSTNVITPVV SVLTEVALDH QKLLGHTITA IAKHKAGIIK RGIPVVTGNL 200
VPDAAAVVAA KVATTGSQWL RFDRDFSVPK AKLHGWGQRF TYEDQDGRIS 250
DLEVPLVGDY QQRNMAIAIQ TAKVYAKQTE WPLTPQNIRQ GLAASHWPAR 300
LEKISDTPLI VIDGAHNPDG INGLITALKQ LFSQPITVIA GILADKDYAA 350
MADRLTAAFS TVYLVPVPGT PRALPEAGYE ALHEGRLKDS WQEALAASLN 400
DVPDQPIVIT GSLYLASAVR QTLLGGKS 428
Length:428
Mass (Da):46,589
Last modified:April 1, 1990 - v1
Checksum:iE4B0B9ED62140181
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05221 Genomic DNA. Translation: AAA88210.1.
PIRiA35534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05221 Genomic DNA. Translation: AAA88210.1 .
PIRi A35534.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FGS X-ray 2.40 A 1-428 [» ]
1JBV X-ray 1.95 A 1-428 [» ]
1JBW X-ray 1.85 A 1-428 [» ]
2GC5 X-ray 1.85 A 1-428 [» ]
2GC6 X-ray 1.90 A 1-428 [» ]
2GCA X-ray 2.40 A 1-428 [» ]
2GCB X-ray 2.30 A 1-428 [» ]
ProteinModelPortali P15925.
SMRi P15925. Positions 1-425.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00850 .
SABIO-RK P15925.

Miscellaneous databases

EvolutionaryTracei P15925.

Family and domain databases

Gene3Di 3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProi IPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view ]
PANTHERi PTHR11136. PTHR11136. 1 hit.
Pfami PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view ]
PIRSFi PIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMi SSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsi TIGR01499. folC. 1 hit.
PROSITEi PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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: October 16, 2013
This is version 94 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

External Data

Dasty 3

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