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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0111 [new locus tag: SACOL_RS00555 ]
- pan locus tag?: SAUPAN000932000
- symbol: SACOL0111
- pan gene symbol?: butA
- synonym:
- product: acetoin reductase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0111 [new locus tag: SACOL_RS00555 ]
- symbol: SACOL0111
- product: acetoin reductase
- replicon: chromosome
- strand: +
- coordinates: 126369..127145
- length: 777
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236834 NCBI
- RefSeq: YP_185015 NCBI
- BioCyc: see SACOL_RS00555
- MicrobesOnline: 911590 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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721ATGACAAACAACAAAGTAGCATTAGTAACTGGCGGAGCACAAGGGATTGGTTTTAAAATT
GCAGAACGTTTAGTGGAAGATGGTTTCAAAGTAGCAGTTGTTGATTTCAATGAAGAAGGG
GCAAAAGCAGCTGCACTTAAATTATCAAGTGATGGTACAAAAGCTATTGCTATCAAAGCA
GATGTATCAAACCGTGATGATGTATTTAACGCAGTAAGACAAACTGCCGCGCAATTTGGC
GATTTCCATGTCATGGTTAACAATGCCGGCCTTGGACCAACAACACCAATCGATACAATT
ACTGAAGAACAGTTTAAAACAGTATATGGCGTGAACGTTGCAGGTGTGCTATGGGGTATT
CAAGCCGCACATGAACAATTTAAAAAATTCAATCATGGCGGTAAAATTATCAATGCAACA
TCTCAAGCAGGCGTTGAGGGTAACCCAGGCTTGTCTTTATATTGCAGTACAAAATTCGCA
GTGCGAGGTTTAACACAAGTAGCCGCACAAGATTTAGCGTCTGAAGGTATTACTGTGAAT
GCATTCGCACCTGGTATCGTTCAAACACCAATGATGGAAAGTATCGCAGTGGCAACAGCC
GAAGAAGCAGGTAAACCTGAAGCATGGGGTTGGGAACAATTTACAAGTCAGATTGCTTTG
GGCAGAGTTTCTCAACCAGAAGATGTTTCAAATGTAGTGAGCTTCTTAGCTGGTAAAGAC
TCTGATTACATTACTGGACAAACAATTATTGTAGATGGTGGTATGAGATTCCGTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0111 [new locus tag: SACOL_RS00555 ]
- symbol: SACOL0111
- description: acetoin reductase
- length: 258
- theoretical pI: 4.79367
- theoretical MW: 27215.5
- GRAVY: -0.0108527
⊟Function[edit | edit source]
- reaction: EC 1.1.1.304? ExPASyDiacetyl reductase ((S)-acetoin forming) (S)-acetoin + NAD+ = diacetyl + NADH
- TIGRFAM: Energy metabolism Fermentation acetoin reductases (TIGR02415; EC 1.1.1.-; HMM-score: 418.5)and 19 moreFatty acid and phospholipid metabolism Biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (TIGR01830; EC 1.1.1.100; HMM-score: 190.3)3-hydroxybutyrate dehydrogenase (TIGR01963; HMM-score: 184.5)Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR03971; EC 1.1.99.-; HMM-score: 170.7)acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 155.2)2-hydroxycyclohexanecarboxyl-CoA dehydrogenase (TIGR03206; EC 1.1.1.-; HMM-score: 153.3)2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (TIGR04316; EC 1.3.1.28; HMM-score: 151.9)Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR04504; EC 1.1.99.-; HMM-score: 132.1)Energy metabolism Biosynthesis and degradation of polysaccharides 2-deoxy-D-gluconate 3-dehydrogenase (TIGR01832; EC 1.1.1.125; HMM-score: 128.7)rhamnulose-1-phosphate aldolase/alcohol dehydrogenase (TIGR02632; EC 1.1.1.1,4.1.2.19; HMM-score: 128.2)Fatty acid and phospholipid metabolism Biosynthesis putative 3-oxoacyl-(acyl-carrier-protein) reductase (TIGR01831; HMM-score: 127.3)cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (TIGR03325; EC 1.3.1.56; HMM-score: 101.2)pteridine reductase (TIGR02685; EC 1.5.1.33; HMM-score: 92.3)sepiapterin reductase (TIGR01500; EC 1.1.1.153; HMM-score: 42.2)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll light-dependent protochlorophyllide reductase (TIGR01289; EC 1.3.1.33; HMM-score: 18.5)polyketide-type polyunsaturated fatty acid synthase PfaA (TIGR02813; HMM-score: 16.8)Energy metabolism Sugars UDP-glucose 4-epimerase GalE (TIGR01179; EC 5.1.3.2; HMM-score: 16)NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family (TIGR04180; HMM-score: 14.5)Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides dTDP-glucose 4,6-dehydratase (TIGR01181; EC 4.2.1.46; HMM-score: 14.1)Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides ADP-glyceromanno-heptose 6-epimerase (TIGR02197; EC 5.1.3.20; HMM-score: 12.1)
- TheSEED :
- 2,3-butanediol dehydrogenase, S-alcohol forming, (R)-acetoin-specific (EC 1.1.1.4)
- Diacetyl reductase [(S)-acetoin forming] (EC 1.1.1.304)
Carbohydrates Fermentation Acetoin, butanediol metabolism 2,3-butanediol dehydrogenase, S-alcohol forming, (R)-acetoin-specific (EC 1.1.1.4)and 1 more - PFAM: NADP_Rossmann (CL0063) adh_short_C2; Enoyl-(Acyl carrier protein) reductase (PF13561; HMM-score: 196.9)adh_short; short chain dehydrogenase (PF00106; HMM-score: 187.2)and 11 moreKR; KR domain (PF08659; HMM-score: 56)3Beta_HSD; 3-beta hydroxysteroid dehydrogenase/isomerase family (PF01073; HMM-score: 16.8)Sacchrp_dh_NADP; Saccharopine dehydrogenase NADP binding domain (PF03435; HMM-score: 16.4)TrkA_N; TrkA-N domain (PF02254; HMM-score: 15.7)3HCDH_N; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain (PF02737; HMM-score: 15.1)Epimerase; NAD dependent epimerase/dehydratase family (PF01370; HMM-score: 15)Ubie_methyltran; ubiE/COQ5 methyltransferase family (PF01209; HMM-score: 14.7)no clan defined Dynein_attach_N; Dynein attachment factor N-terminus (PF15867; HMM-score: 14.6)Pec_lyase-like (CL0268) Pertactin; Pertactin (PF03212; HMM-score: 12.6)NADP_Rossmann (CL0063) GDP_Man_Dehyd; GDP-mannose 4,6 dehydratase (PF16363; HMM-score: 11.6)NmrA; NmrA-like family (PF05368; HMM-score: 10.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.005476
- TAT(Tat/SPI): 0.000558
- LIPO(Sec/SPII): 0.000737
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTNNKVALVTGGAQGIGFKIAERLVEDGFKVAVVDFNEEGAKAAALKLSSDGTKAIAIKADVSNRDDVFNAVRQTAAQFGDFHVMVNNAGLGPTTPIDTITEEQFKTVYGVNVAGVLWGIQAAHEQFKKFNHGGKIINATSQAGVEGNPGLSLYCSTKFAVRGLTQVAAQDLASEGITVNAFAPGIVQTPMMESIAVATAEEAGKPEAWGWEQFTSQIALGRVSQPEDVSNVVSFLAGKDSDYITGQTIIVDGGMRFR
⊟Experimental data[edit | edit source]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟Regulation[edit | edit source]
- regulator: CodY (repression) regulon
CodY (TF) important in Amino acid metabolism; RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e)