Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AC16

- FOLB_ECOLI

UniProt

P0AC16 - FOLB_ECOLI

Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity.

    Catalytic activityi

    2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.

    Pathwayi

    GO - Molecular functioni

    1. dihydroneopterin aldolase activity Source: EcoCyc

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Folate biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:H2NEOPTERINALDOL-MONOMER.
    ECOL316407:JW3030-MONOMER.
    MetaCyc:H2NEOPTERINALDOL-MONOMER.
    UniPathwayiUPA00077; UER00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydroneopterin aldolase (EC:4.1.2.25)
    Short name:
    DHNA
    Gene namesi
    Name:folB
    Synonyms:ygiG
    Ordered Locus Names:b3058, JW3030
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11673. folB.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 122122Dihydroneopterin aldolasePRO_0000168269Add
    BLAST

    Proteomic databases

    PaxDbiP0AC16.
    PRIDEiP0AC16.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AC16.

    Interactioni

    Subunit structurei

    Homooctamer.

    Protein-protein interaction databases

    DIPiDIP-36044N.
    IntActiP0AC16. 2 interactions.
    STRINGi511145.b3058.

    Structurei

    Secondary structure

    1
    122
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1514
    Helixi19 – 235
    Beta strandi26 – 3611
    Helixi39 – 446
    Helixi47 – 493
    Helixi53 – 6412
    Beta strandi68 – 703
    Helixi72 – 8615
    Beta strandi92 – 976
    Beta strandi109 – 1146

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O90X-ray1.07A1-122[»]
    ProteinModelPortaliP0AC16.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AC16.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DHNA family.Curated

    Phylogenomic databases

    eggNOGiCOG1539.
    HOGENOMiHOG000217627.
    KOiK01633.
    OMAiERGKIRY.
    OrthoDBiEOG6ND0KG.
    PhylomeDBiP0AC16.

    Family and domain databases

    InterProiIPR006156. Dihydroneopterin_aldolase.
    IPR006157. FolB_dom.
    [Graphical view]
    PfamiPF02152. FolB. 1 hit.
    [Graphical view]
    SMARTiSM00905. FolB. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00525. folB. 1 hit.
    TIGR00526. folB_dom. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AC16-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC    50
    LSYADIAETV VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG 100
    AVARAANVGV IIERGNNLKE NN 122
    Length:122
    Mass (Da):13,620
    Last modified:November 8, 2005 - v1
    Checksum:iBEA82C1E0AA38A55
    GO

    Sequence cautioni

    The sequence AAA89138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 822EL → DV in L12966. (PubMed:8389741)Curated
    Sequence conflicti100 – 12223GAVAR…LKENN → ASGAGGECWRNH in L12966. (PubMed:8389741)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12966 Genomic DNA. No translation available.
    U28379 Genomic DNA. Translation: AAA89138.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76094.2.
    AP009048 Genomic DNA. Translation: BAE77109.1.
    PIRiH65093.
    RefSeqiNP_417530.2. NC_000913.3.
    YP_491250.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76094; AAC76094; b3058.
    BAE77109; BAE77109; BAE77109.
    GeneIDi12930262.
    947544.
    KEGGiecj:Y75_p2984.
    eco:b3058.
    PATRICi32121528. VBIEscCol129921_3151.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12966 Genomic DNA. No translation available.
    U28379 Genomic DNA. Translation: AAA89138.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC76094.2 .
    AP009048 Genomic DNA. Translation: BAE77109.1 .
    PIRi H65093.
    RefSeqi NP_417530.2. NC_000913.3.
    YP_491250.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O90 X-ray 1.07 A 1-122 [» ]
    ProteinModelPortali P0AC16.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36044N.
    IntActi P0AC16. 2 interactions.
    STRINGi 511145.b3058.

    Proteomic databases

    PaxDbi P0AC16.
    PRIDEi P0AC16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76094 ; AAC76094 ; b3058 .
    BAE77109 ; BAE77109 ; BAE77109 .
    GeneIDi 12930262.
    947544.
    KEGGi ecj:Y75_p2984.
    eco:b3058.
    PATRICi 32121528. VBIEscCol129921_3151.

    Organism-specific databases

    EchoBASEi EB1624.
    EcoGenei EG11673. folB.

    Phylogenomic databases

    eggNOGi COG1539.
    HOGENOMi HOG000217627.
    KOi K01633.
    OMAi ERGKIRY.
    OrthoDBi EOG6ND0KG.
    PhylomeDBi P0AC16.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00154 .
    BioCyci EcoCyc:H2NEOPTERINALDOL-MONOMER.
    ECOL316407:JW3030-MONOMER.
    MetaCyc:H2NEOPTERINALDOL-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AC16.
    PROi P0AC16.

    Gene expression databases

    Genevestigatori P0AC16.

    Family and domain databases

    InterProi IPR006156. Dihydroneopterin_aldolase.
    IPR006157. FolB_dom.
    [Graphical view ]
    Pfami PF02152. FolB. 1 hit.
    [Graphical view ]
    SMARTi SM00905. FolB. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00525. folB. 1 hit.
    TIGR00526. folB_dom. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Amplification of the bacA gene confers bacitracin resistance to Escherichia coli."
      Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M.
      J. Bacteriol. 175:3784-3789(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / ATCC 35607 / JM83.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase."
      Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.
      J. Biol. Chem. 273:17418-17424(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiFOLB_ECOLI
    AccessioniPrimary (citable) accession number: P0AC16
    Secondary accession number(s): P31055, P76659, Q2M9E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 77 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, 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