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P24186

- FOLD_ECOLI

UniProt

P24186 - FOLD_ECOLI

Protein

Bifunctional protein FolD

Gene

folD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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 – 2821
    Beta strandi35 – 428
    Helixi45 – 6117
    Beta strandi68 – 703
    Helixi76 – 8712
    Beta strandi94 – 974
    Helixi107 – 1115
    Turni116 – 1183
    Helixi125 – 1328
    Helixi141 – 15212
    Beta strandi161 – 1655
    Turni169 – 1713
    Helixi172 – 1809
    Turni181 – 1833
    Beta strandi185 – 1895
    Helixi196 – 2027
    Beta strandi204 – 2085
    Turni218 – 2203
    Beta strandi226 – 2294
    Helixi246 – 2527
    Beta strandi254 – 2563
    Beta strandi259 – 2635
    Helixi264 – 28118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MAAKIIDGKT IAQQVRSEVA QKVQARIAAG LRAPGLAVVL VGSNPASQIY    50
    VASKRKACEE VGFVSRSYDL PETTSEAELL ELIDTLNADN TIDGILVQLP 100
    LPAGIDNVKV LERIHPDKDV DGFHPYNVGR LCQRAPRLRP CTPRGIVTLL 150
    ERYNIDTFGL NAVVIGASNI VGRPMSMELL LAGCTTTVTH RFTKNLRHHV 200
    ENADLLIVAV GKPGFIPGDW IKEGAIVIDV GINRLENGKV VGDVVFEDAA 250
    KRASYITPVP GGVGPMTVAT LIENTLQACV EYHDPQDE 288
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 119 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