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SSUBM407_0242 MutT/NUDIX hydrolase family protein [ Streptococcus suis BM407 ]

Gene ID: 8154483, updated on 7-Oct-2015

Summary

Gene symbol
SSUBM407_0242
Gene description
MutT/NUDIX hydrolase family protein
Locus tag
SSUBM407_0242
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Streptococcus suis BM407 (strain: BM407)
Lineage
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus

Genomic context

Sequence:
NC_012926.1 (259490..260098)

NC_012926.1Genomic Context describing neighboring genes Neighboring gene glycerol facilitator-aquaporin Neighboring gene hypothetical protein Neighboring gene hypothetical protein Neighboring gene surface-anchored protein

Bibliography

Related articles in PubMed

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

General gene information

Miscellaneous features

  • Loc: 259637-259888 HMMPfam hit to PF00293, NUDIX, score 1.4e-15 inference = protein motif:HMMPfam:PF00293
  • Loc: 259661-259726 ScanRegExp hit to PS00893, NUDIX, score 8e-5 inference = protein motif:Prosite:PS00893

General protein information

Names
MutT/NUDIX hydrolase family protein
YP_003028018.1
  • Orthologue of S. suis P17 (AM946016) SSU0251

NCBI Reference Sequences (RefSeq)

Genome Annotation

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

Reference assembly

Genomic

  1. NC_012926.1 Reference assembly

    Range
    259490..260098
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_003028018.1 MutT/NUDIX hydrolase family protein [Streptococcus suis BM407]

    See identical proteins and their annotated locations for YP_003028018.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A0H3MT74
    Conserved Domains (1) summary
    cd03426
    Location:21193
    CoAse; Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative ...
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