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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: 3 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 – 108Combined sources
Helixi23 – 319Combined sources
Helixi35 – 373Combined sources
Beta strandi41 – 455Combined sources
Beta strandi47 – 493Combined sources
Helixi50 – 6314Combined sources
Beta strandi68 – 714Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 824Combined sources
Beta strandi83 – 853Combined sources
Helixi92 – 11221Combined sources
Helixi120 – 13415Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi159 – 1635Combined sources
Helixi168 – 1703Combined sources
Helixi171 – 1744Combined sources
Helixi178 – 1858Combined sources
Helixi186 – 1883Combined sources
Beta strandi195 – 1973Combined sources
Helixi202 – 21514Combined sources
Beta strandi219 – 2213Combined sources
Turni222 – 2243Combined sources
Beta strandi225 – 2339Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi247 – 2559Combined sources
Helixi260 – 27819Combined sources
Helixi285 – 2939Combined sources
Beta strandi300 – 3056Combined sources
Turni306 – 3094Combined sources
Beta strandi310 – 3134Combined sources
Helixi318 – 33114Combined sources
Beta strandi337 – 3415Combined sources
Beta strandi343 – 3453Combined sources
Helixi348 – 35811Combined sources
Beta strandi360 – 3645Combined sources
Helixi391 – 40111Combined sources
Beta strandi407 – 4126Combined sources
Helixi413 – 42311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15925.

Family & Domainsi

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 .
PIRi A35534.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 96 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