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MGAS1882_1304 3-hydroxybutyrate dehydrogenase [ Streptococcus pyogenes MGAS1882 ]

Gene ID: 12015136, discontinued on 3-Feb-2015
  • All Gene records for this genome have been discontinued due to a change in scope for prokaryotic genomes in Gene. At the time this Gene record was discontinued, the RefSeq genome was re-annotated with the following features at this location:

Summary

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Gene symbol
MGAS1882_1304
Gene description
3-hydroxybutyrate dehydrogenase
Locus tag
MGAS1882_1304
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Streptococcus pyogenes MGAS1882 (strain: MGAS1882, nat-host: Homo sapiens)
Lineage
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus
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Genomic regions, transcripts, and products

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Genomic Sequence:
NC_017053.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

General protein information

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Names
3-hydroxybutyrate dehydrogenase
YP_005412030.1
  • CDD hit: non-specific, cl9931 = d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 25 residues long, while extended SDRs are approximately 35 residues. Sequence identity between different SDR enzymes are typically in the 15-3% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-17, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_017053.1 Reference assembly

    Range
    1278479..1279258
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    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_005412030.1 3-hydroxybutyrate dehydrogenase [Streptococcus pyogenes MGAS1882]

    Status: PROVISIONAL

Nucleotide Protein
Heading Accession and Version