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Protein

Bifunctional protein FolD

Gene

folD

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311NADP; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1673NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-909-MONOMER.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein FolDUniRule annotation
Including the following 2 domains:
Methylenetetrahydrofolate dehydrogenaseUniRule annotation (EC:1.5.1.5UniRule annotation)
Methenyltetrahydrofolate cyclohydrolaseUniRule annotation (EC:3.5.4.9UniRule annotation)
Gene namesi
Name:folDUniRule annotation
Ordered Locus Names:FTT_0892
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Bifunctional protein FolDPRO_0000268352Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ5NGF3. 1 interaction.
STRINGi177416.FTT_0892.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2823Combined sources
Beta strandi33 – 408Combined sources
Helixi43 – 5816Combined sources
Beta strandi62 – 687Combined sources
Helixi74 – 8512Combined sources
Beta strandi92 – 954Combined sources
Helixi105 – 1117Combined sources
Helixi114 – 1163Combined sources
Helixi123 – 1319Combined sources
Helixi140 – 15112Combined sources
Beta strandi160 – 1645Combined sources
Turni168 – 1703Combined sources
Helixi171 – 18010Combined sources
Beta strandi184 – 1885Combined sources
Helixi195 – 1995Combined sources
Beta strandi203 – 2075Combined sources
Helixi217 – 2193Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi237 – 2393Combined sources
Helixi244 – 2474Combined sources
Turni248 – 2503Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi257 – 2615Combined sources
Helixi264 – 27916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L07X-ray1.88A/B1-282[»]
ProteinModelPortaliQ5NGF3.
SMRiQ5NGF3. Positions 2-280.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5NGF3.

Family & Domainsi

Sequence similaritiesi

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CN0. Bacteria.
COG0190. LUCA.
HOGENOMiHOG000218242.
KOiK01491.
OMAiLMFNTIK.
OrthoDBiEOG6K6VBB.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5NGF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILIDGKSLS KDLKERLATQ VQEYKHHTAI TPKLVAIIVG NDPASKTYVA
60 70 80 90 100
SKEKACAQVG IDSQVITLPE HTTESELLEL IDQLNNDSSV HAILVQLPLP
110 120 130 140 150
AHINKNNVIY SIKPEKDVDG FHPTNVGRLQ LRDKKCLESC TPKGIMTMLR
160 170 180 190 200
EYGIKTEGAY AVVVGASNVV GKPVSQLLLN AKATVTTCHR FTTDLKSHTT
210 220 230 240 250
KADILIVAVG KPNFITADMV KEGAVVIDVG INHVDGKIVG DVDFAAVKDK
260 270 280
VAAITPVPGG VGPMTITELL YNTFQCAQEL NR
Length:282
Mass (Da):30,454
Last modified:February 1, 2005 - v1
Checksum:i0DD0F5FEF81CEF09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45525.1.
RefSeqiWP_003020886.1. NZ_CP010290.1.
YP_169889.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45525; CAG45525; FTT_0892.
GeneIDi3191934.
KEGGiftu:FTT_0892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45525.1.
RefSeqiWP_003020886.1. NZ_CP010290.1.
YP_169889.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L07X-ray1.88A/B1-282[»]
ProteinModelPortaliQ5NGF3.
SMRiQ5NGF3. Positions 2-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5NGF3. 1 interaction.
STRINGi177416.FTT_0892.

Protocols and materials databases

DNASUi3191934.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45525; CAG45525; FTT_0892.
GeneIDi3191934.
KEGGiftu:FTT_0892.

Phylogenomic databases

eggNOGiENOG4105CN0. Bacteria.
COG0190. LUCA.
HOGENOMiHOG000218242.
KOiK01491.
OMAiLMFNTIK.
OrthoDBiEOG6K6VBB.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciFTUL177416:GNBP-909-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5NGF3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCHU S4 / Schu 4.
  2. "X-ray crystal structure of methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative bifunctional protein FolD from Francisella tularensis."
    Center for structural genomics of infectious diseases (CSGID)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, SUBUNIT.

Entry informationi

Entry nameiFOLD_FRATT
AccessioniPrimary (citable) accession number: Q5NGF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 1, 2005
Last modified: December 9, 2015
This is version 73 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, Complete proteome, Multifunctional enzyme, Reference proteome

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.