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P24186

- FOLD_ECOLI

UniProt

P24186 - FOLD_ECOLI

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Protein

Bifunctional protein FolD

Gene

folD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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. This enzyme is specific for NADP.1 PublicationUniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei232 – 2321NADP; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi166 – 1683NADPUniRule annotation

GO - Molecular functioni

  1. methenyltetrahydrofolate cyclohydrolase activity Source: EcoCyc
  2. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: RefGenome

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. histidine biosynthetic process Source: UniProtKB-KW
  3. methionine biosynthetic process Source: UniProtKB-KW
  4. one-carbon metabolic process Source: RefGenome
  5. purine nucleotide biosynthetic process Source: UniProtKB-KW
  6. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
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

BioCyciEcoCyc:FOLD-MONOMER.
ECOL316407:JW0518-MONOMER.
MetaCyc:FOLD-MONOMER.
SABIO-RKP24186.
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
Synonyms:ads
Ordered Locus Names:b0529, JW0518
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10328. folD.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RefGenome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 288287Bifunctional protein FolDPRO_0000199306Add
BLAST

Proteomic databases

PaxDbiP24186.
PRIDEiP24186.

Expressioni

Gene expression databases

GenevestigatoriP24186.

Interactioni

Subunit structurei

Homodimer.2 PublicationsUniRule annotation

Protein-protein interaction databases

DIPiDIP-9675N.
IntActiP24186. 4 interactions.
STRINGi511145.b0529.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2821Combined sources
Beta strandi35 – 428Combined sources
Helixi45 – 6117Combined sources
Beta strandi68 – 703Combined sources
Helixi76 – 8712Combined sources
Beta strandi94 – 974Combined sources
Helixi107 – 1115Combined sources
Turni116 – 1183Combined sources
Helixi125 – 1328Combined sources
Helixi141 – 15212Combined sources
Beta strandi161 – 1655Combined sources
Turni169 – 1713Combined sources
Helixi172 – 1809Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1895Combined sources
Helixi196 – 2027Combined sources
Beta strandi204 – 2085Combined sources
Turni218 – 2203Combined sources
Beta strandi226 – 2294Combined sources
Helixi246 – 2527Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi259 – 2635Combined sources
Helixi264 – 28118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0AX-ray2.56A1-288[»]
ProteinModelPortaliP24186.
SMRiP24186. Positions 2-288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24186.

Family & Domainsi

Sequence similaritiesi

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0190.
HOGENOMiHOG000218242.
InParanoidiP24186.
KOiK01491.
OMAiCHSKSIY.
OrthoDBiEOG6K6VBB.
PhylomeDBiP24186.

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.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24186-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKIIDGKT IAQQVRSEVA QKVQARIAAG LRAPGLAVVL VGSNPASQIY
60 70 80 90 100
VASKRKACEE VGFVSRSYDL PETTSEAELL ELIDTLNADN TIDGILVQLP
110 120 130 140 150
LPAGIDNVKV LERIHPDKDV DGFHPYNVGR LCQRAPRLRP CTPRGIVTLL
160 170 180 190 200
ERYNIDTFGL NAVVIGASNI VGRPMSMELL LAGCTTTVTH RFTKNLRHHV
210 220 230 240 250
ENADLLIVAV GKPGFIPGDW IKEGAIVIDV GINRLENGKV VGDVVFEDAA
260 270 280
KRASYITPVP GGVGPMTVAT LIENTLQACV EYHDPQDE
Length:288
Mass (Da):31,044
Last modified:January 23, 2007 - v4
Checksum:i028039D7C611085D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471S → L in AAB40282. 1 PublicationCurated
Sequence conflicti200 – 2001V → L in AAA23803. (PubMed:1748668)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH64784. JS0662.
RefSeqiNP_415062.1. NC_000913.3.
YP_488818.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73631; AAC73631; b0529.
BAE76306; BAE76306; BAE76306.
GeneIDi12933825.
945221.
KEGGiecj:Y75_p0515.
eco:b0529.
PATRICi32116218. VBIEscCol129921_0550.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi H64784. JS0662.
RefSeqi NP_415062.1. NC_000913.3.
YP_488818.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B0A X-ray 2.56 A 1-288 [» ]
ProteinModelPortali P24186.
SMRi P24186. Positions 2-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9675N.
IntActi P24186. 4 interactions.
STRINGi 511145.b0529.

Proteomic databases

PaxDbi P24186.
PRIDEi P24186.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73631 ; AAC73631 ; b0529 .
BAE76306 ; BAE76306 ; BAE76306 .
GeneIDi 12933825.
945221.
KEGGi ecj:Y75_p0515.
eco:b0529.
PATRICi 32116218. VBIEscCol129921_0550.

Organism-specific databases

EchoBASEi EB0324.
EcoGenei EG10328. folD.

Phylogenomic databases

eggNOGi COG0190.
HOGENOMi HOG000218242.
InParanoidi P24186.
KOi K01491.
OMAi CHSKSIY.
OrthoDBi EOG6K6VBB.
PhylomeDBi P24186.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci EcoCyc:FOLD-MONOMER.
ECOL316407:JW0518-MONOMER.
MetaCyc:FOLD-MONOMER.
SABIO-RK P24186.

Miscellaneous databases

EvolutionaryTracei P24186.
PROi P24186.

Gene expression databases

Genevestigatori P24186.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01576. THF_DHG_CYH.
InterProi IPR016040. 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 ]
Pfami PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
PROSITEi PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiFOLD_ECOLI
AccessioniPrimary (citable) accession number: P24186
Secondary accession number(s): P77132, Q2MBQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3