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P24186 (FOLD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Bifunctional protein FolD

Including the following 2 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
Gene names
Name:folD
Synonyms:ads
Ordered Locus Names:b0529, JW0518
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP. Ref.1

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01576

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01576

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01576

Subunit structure

Homodimer. Ref.1 Ref.6

Sequence similarities

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 288287Bifunctional protein FolD HAMAP-Rule MF_01576
PRO_0000199306

Regions

Nucleotide binding166 – 1683NADP By similarity

Sites

Binding site2321NADP; via amide nitrogen By similarity

Experimental info

Sequence conflict471S → L in AAB40282. Ref.3
Sequence conflict2001V → L in AAA23803. Ref.1

Secondary structure

............................................ 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24186 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 028039D7C611085D

FASTA28831,044
        10         20         30         40         50         60 
MAAKIIDGKT IAQQVRSEVA QKVQARIAAG LRAPGLAVVL VGSNPASQIY VASKRKACEE 

        70         80         90        100        110        120 
VGFVSRSYDL PETTSEAELL ELIDTLNADN TIDGILVQLP LPAGIDNVKV LERIHPDKDV 

       130        140        150        160        170        180 
DGFHPYNVGR LCQRAPRLRP CTPRGIVTLL ERYNIDTFGL NAVVIGASNI VGRPMSMELL 

       190        200        210        220        230        240 
LAGCTTTVTH RFTKNLRHHV ENADLLIVAV GKPGFIPGDW IKEGAIVIDV GINRLENGKV 

       250        260        270        280 
VGDVVFEDAA KRASYITPVP GGVGPMTVAT LIENTLQACV EYHDPQDE 

« Hide

References

« Hide 'large scale' references
[1]"Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli."
D'Ari L., Rabinowitz J.C.
J. Biol. Chem. 266:23953-23958(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-36, FUNCTION, SUBUNIT.
[2]"Cloning and nucleotide sequence analysis of a novel adenine-sensitive mutation of Escherichia coli strain K-12 W3110."
Yonetani Y., Sanpei G., Mizobuchi K.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase."
Shen B.W., Dyer D.H., Huang J.-Y., D'Ari L., Rabinowitz J., Stoddard B.L.
Protein Sci. 8:1342-1349(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74789 Genomic DNA. Translation: AAA23803.1.
D10588 Genomic DNA. Translation: BAA01445.1.
U82664 Genomic DNA. Translation: AAB40282.1.
U00096 Genomic DNA. Translation: AAC73631.1.
AP009048 Genomic DNA. Translation: BAE76306.1.
PIRJS0662. H64784.
RefSeqNP_415062.1. NC_000913.3.
YP_488818.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0AX-ray2.56A1-288[»]
ProteinModelPortalP24186.
SMRP24186. Positions 2-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9675N.
IntActP24186. 4 interactions.
STRING511145.b0529.

Proteomic databases

PaxDbP24186.
PRIDEP24186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73631; AAC73631; b0529.
BAE76306; BAE76306; BAE76306.
GeneID12933825.
945221.
KEGGecj:Y75_p0515.
eco:b0529.
PATRIC32116218. VBIEscCol129921_0550.

Organism-specific databases

EchoBASEEB0324.
EcoGeneEG10328. folD.

Phylogenomic databases

eggNOGCOG0190.
HOGENOMHOG000218242.
KOK01491.
OMACHSKSIY.
OrthoDBEOG6K6VBB.
PhylomeDBP24186.

Enzyme and pathway databases

BioCycEcoCyc:FOLD-MONOMER.
ECOL316407:JW0518-MONOMER.
MetaCyc:FOLD-MONOMER.
SABIO-RKP24186.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorP24186.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01576. THF_DHG_CYH.
InterProIPR016040. 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]
PfamPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
PROSITEPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24186.
PROP24186.

Entry information

Entry nameFOLD_ECOLI
AccessionPrimary (citable) accession number: P24186
Secondary accession number(s): P77132, Q2MBQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 4 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene