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P37672

- DLGD_ECOLI

UniProt

P37672 - DLGD_ECOLI

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Protein
2,3-diketo-L-gulonate reductase
Gene
dlgD, yiaK, b3575, JW3547
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.1 Publication

Catalytic activityi

3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H.UniRule annotation

Enzyme regulationi

The enzyme is inhibited by tartrate and D-malate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441Proton donor Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1747NADUniRule annotation
Nucleotide bindingi224 – 2252NADUniRule annotation
Nucleotide bindingi304 – 3063NADUniRule annotation

GO - Molecular functioni

  1. 3-dehydro-L-gulonate 2-dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD+ binding Source: InterPro
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: EcoCyc
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12279-MONOMER.
    ECOL316407:JW3547-MONOMER.
    MetaCyc:EG12279-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-diketo-L-gulonate reductase (EC:1.1.1.130)
    Short name:
    2,3-DKG reductase
    Alternative name(s):
    3-dehydro-L-gulonate 2-dehydrogenase
    Gene namesi
    Name:dlgD
    Synonyms:yiaK
    Ordered Locus Names:b3575, JW3547
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12279. dlgD.

    Subcellular locationi

    Cytoplasm Reviewed prediction UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3323322,3-diketo-L-gulonate reductaseUniRule annotation
    PRO_0000083830Add
    BLAST

    Proteomic databases

    PRIDEiP37672.

    Expressioni

    Gene expression databases

    GenevestigatoriP37672.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi511145.b3575.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1814
    Helixi23 – 3816
    Turni43 – 453
    Helixi46 – 483
    Helixi49 – 579
    Beta strandi68 – 736
    Beta strandi76 – 805
    Helixi86 – 10419
    Beta strandi105 – 11410
    Helixi121 – 1299
    Beta strandi133 – 1386
    Beta strandi149 – 1513
    Beta strandi159 – 1635
    Beta strandi169 – 1735
    Beta strandi175 – 1784
    Helixi180 – 1889
    Beta strandi203 – 2064
    Helixi209 – 2157
    Turni221 – 2233
    Helixi224 – 24118
    Helixi246 – 2527
    Beta strandi254 – 2563
    Beta strandi258 – 2669
    Turni269 – 2713
    Helixi274 – 28916
    Beta strandi293 – 2953
    Turni303 – 3053
    Helixi306 – 31712
    Helixi323 – 3319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NXUX-ray1.80A/B1-332[»]
    1S20X-ray2.20A/B/C/D/E/F/G/H1-332[»]
    ProteinModelPortaliP37672.
    SMRiP37672. Positions 1-332.

    Miscellaneous databases

    EvolutionaryTraceiP37672.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2055.
    HOGENOMiHOG000249660.
    KOiK08092.
    OMAiGHEFTTI.
    OrthoDBiEOG6QK4PJ.
    PhylomeDBiP37672.

    Family and domain databases

    HAMAPiMF_00820. Diketo_gul_reduc.
    InterProiIPR023689. Diketo_gul_Rdtase.
    IPR003767. Malate/L-lactate_DH.
    [Graphical view]
    PANTHERiPTHR11091. PTHR11091. 1 hit.
    PfamiPF02615. Ldh_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF89733. SSF89733. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37672-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTFEQLKA AFNRVLISRG VDSETADACA EMFARTTESG VYSHGVNRFP    50
    RFIQQLENGD IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL 100
    AADHGIGLVA LRNANHWMRG GSYGWQAAEK GYIGICWTNS IAVMPPWGAK 150
    ECRIGTNPLI VAIPSTPITM VDMSMSMFSY GMLEVNRLAG RQLPVDGGFD 200
    DEGNLTKEPG VIEKNRRILP MGYWKGSGMS IVLDMIATLL SDGASVAEVT 250
    QDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTS AERADENQAI 300
    RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL 332
    Length:332
    Mass (Da):36,573
    Last modified:November 1, 1997 - v2
    Checksum:iA411EB14D5C03DF7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00039 Genomic DNA. Translation: AAB18552.1.
    U00096 Genomic DNA. Translation: AAC76599.1.
    AP009048 Genomic DNA. Translation: BAE77718.1.
    AJ223475 Genomic DNA. Translation: CAA11398.1.
    PIRiA65157.
    RefSeqiNP_418032.1. NC_000913.3.
    YP_491859.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76599; AAC76599; b3575.
    BAE77718; BAE77718; BAE77718.
    GeneIDi12933552.
    948096.
    KEGGiecj:Y75_p3600.
    eco:b3575.
    PATRICi32122626. VBIEscCol129921_3690.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00039 Genomic DNA. Translation: AAB18552.1 .
    U00096 Genomic DNA. Translation: AAC76599.1 .
    AP009048 Genomic DNA. Translation: BAE77718.1 .
    AJ223475 Genomic DNA. Translation: CAA11398.1 .
    PIRi A65157.
    RefSeqi NP_418032.1. NC_000913.3.
    YP_491859.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NXU X-ray 1.80 A/B 1-332 [» ]
    1S20 X-ray 2.20 A/B/C/D/E/F/G/H 1-332 [» ]
    ProteinModelPortali P37672.
    SMRi P37672. Positions 1-332.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 511145.b3575.

    Proteomic databases

    PRIDEi P37672.

    Protocols and materials databases

    DNASUi 948096.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76599 ; AAC76599 ; b3575 .
    BAE77718 ; BAE77718 ; BAE77718 .
    GeneIDi 12933552.
    948096.
    KEGGi ecj:Y75_p3600.
    eco:b3575.
    PATRICi 32122626. VBIEscCol129921_3690.

    Organism-specific databases

    EchoBASEi EB2187.
    EcoGenei EG12279. dlgD.

    Phylogenomic databases

    eggNOGi COG2055.
    HOGENOMi HOG000249660.
    KOi K08092.
    OMAi GHEFTTI.
    OrthoDBi EOG6QK4PJ.
    PhylomeDBi P37672.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12279-MONOMER.
    ECOL316407:JW3547-MONOMER.
    MetaCyc:EG12279-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P37672.
    PROi P37672.

    Gene expression databases

    Genevestigatori P37672.

    Family and domain databases

    HAMAPi MF_00820. Diketo_gul_reduc.
    InterProi IPR023689. Diketo_gul_Rdtase.
    IPR003767. Malate/L-lactate_DH.
    [Graphical view ]
    PANTHERi PTHR11091. PTHR11091. 1 hit.
    Pfami PF02615. Ldh_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89733. SSF89733. 1 hit.
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "A rare 920-kilobase chromosomal inversion mediated by IS1 transposition causes constitutive expression of the yiaK-S operon for carbohydrate utilization in Escherichia coli."
      Badia J., Ibanez E., Sabate M., Baldoma L., Aguilar J.
      J. Biol. Chem. 273:8376-8381(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
    5. "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons."
      Yew W.S., Gerlt J.A.
      J. Bacteriol. 184:302-306(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12 / MG1655 / ATCC 47076.
    6. "A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)."
      Forouhar F., Lee I., Benach J., Kulkarni K., Xiao R., Acton T.B., Montelione G.T., Tong L.
      J. Biol. Chem. 279:13148-13155(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH NAD AND TARTRATE, SUBUNIT.

    Entry informationi

    Entry nameiDLGD_ECOLI
    AccessioniPrimary (citable) accession number: P37672
    Secondary accession number(s): P76716, Q2M7N8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 1, 1997
    Last modified: May 14, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3

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