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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02284
- pan locus tag?: SAUPAN005306000
- symbol: SAOUHSC_02284
- pan gene symbol?: ilvC
- synonym:
- product: ketol-acid reductoisomerase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_02284
- symbol: SAOUHSC_02284
- product: ketol-acid reductoisomerase
- replicon: chromosome
- strand: +
- coordinates: 2115682..2116686
- length: 1005
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3919159 NCBI
- RefSeq: YP_500766 NCBI
- BioCyc: G1I0R-2156 BioCyc
- MicrobesOnline: 1290722 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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961ATGACAACAGTTTATTATGATCAAGATGTAAAAACGGACGCTTTACAAGGCAAAAAAATT
GCAGTAGTAGGTTATGGATCACAAGGTCACGCGCATGCACAAAACTTAAAAGACAATGGA
TATGATGTAGTCATCGGCATTCGCCCAGGTCGTTCTTTTGACAAAGCTAAAGAAGATGGA
TTTGATGTGTTCCCTGTTGCAGAAGCAGTTAAGCAAGCTGATGTAATTATGGTGCTATTA
CCTGATGAAATTCAAGGTGATGTATACAAAAACGAAATTGAACCAAATTTAGAAAAACAT
AATGCGCTTGCATTTGCTCATGGCTTTAACATTCATTTTGGTGTTATTCAACCACCAGCT
GATGTTGATGTATTTTTAGTAGCTCCTAAAGGACCGGGTCATTTAGTTAGACGTACATTT
GTTGAAGGTTCTGCTGTACCATCACTATTTGGTATTCAACAAGGCGCTTCAGGTCAAGCA
CGTAATATTGCTTTAAGTTATGCAAAAGGTATTGGTGCAACTCGTGCAGGTGTTATTGAA
ACAACATTTAAAGAAGAAACTGAGACAGATTTATTTGGTGAACAAGCAGTACTTTGCGGT
GGTGTATCGAAATTAATTCAAAGTGGCTTTGAAACATTAGTAGAAGCGGGTTATCAACCA
GAATTAGCTTATTTTGAAGTATTACATGAAATGAAATTAATCGTTGATTTGATGTATGAA
GGCGGTATGGAAAATGTACGTTACTCAATTTCAAATACTGCTGAATTTGGTGACTATGTT
TCAGGACCACGTGTTATCACACCAGATGTTAAAGAAAATATGAAAGCTGTATTAACTGAT
ATCCAAAATGGTAACTTCAGTAATCGCTTTATCGAAGACAATAAAAATGGATTCAAAGAA
TTTTATAAATTACGCGAAGAACAACATGGTCATCAAATTGAAAAAGTTGGTCGTGAATTA
CGCGAAATGATGCCTTTTATTAAATCTAAAAGCATTGAAAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02284
- symbol: SAOUHSC_02284
- description: ketol-acid reductoisomerase
- length: 334
- theoretical pI: 5.04028
- theoretical MW: 36955.6
- GRAVY: -0.29491
⊟Function[edit | edit source]
- reaction: EC 1.1.1.86? ExPASyKetol-acid reductoisomerase (NADP+) (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH
- TIGRFAM: Amino acid biosynthesis Pyruvate family ketol-acid reductoisomerase (TIGR00465; EC 1.1.1.86; HMM-score: 436.7)and 7 moreEnergy metabolism Amino acids and amines adenosylhomocysteinase (TIGR00936; EC 3.3.1.1; HMM-score: 31.9)2-hydroxy-3-oxopropionate reductase (TIGR01505; EC 1.1.1.60; HMM-score: 17.5)Cellular processes Sporulation and germination dipicolinic acid synthetase, A subunit (TIGR02853; HMM-score: 15.6)Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A 2-dehydropantoate 2-reductase (TIGR00745; EC 1.1.1.-; HMM-score: 15.3)Energy metabolism Amino acids and amines 3-hydroxyisobutyrate dehydrogenase (TIGR01692; EC 1.1.1.31; HMM-score: 14.5)Energy metabolism Pentose phosphate pathway 6-phosphogluconate dehydrogenase (decarboxylating) (TIGR00872; EC 1.1.1.44; HMM-score: 12.7)glutamate synthase, NADH/NADPH, small subunit (TIGR01317; EC 1.4.1.-; HMM-score: 12.4)
- TheSEED :
- Ketol-acid reductoisomerase (EC 1.1.1.86)
Amino Acids and Derivatives Branched-chain amino acids Branched-Chain Amino Acid Biosynthesis Ketol-acid reductoisomerase (EC 1.1.1.86)and 1 more - PFAM: NADP_Rossmann (CL0063) IlvN; Acetohydroxy acid isomeroreductase, NADPH-binding domain (PF07991; HMM-score: 250)6PGD_C (CL0106) IlvC; Acetohydroxy acid isomeroreductase, catalytic domain (PF01450; HMM-score: 218.6)and 12 moreNADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 31.6)F420_oxidored; NADP oxidoreductase coenzyme F420-dependent (PF03807; HMM-score: 30.6)AdoHcyase_NAD; S-adenosyl-L-homocysteine hydrolase, NAD binding domain (PF00670; HMM-score: 27.6)NAD_binding_2; NAD binding domain of 6-phosphogluconate dehydrogenase (PF03446; HMM-score: 27.5)NAD_Gly3P_dh_N; NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus (PF01210; HMM-score: 18.3)CoA_binding; CoA binding domain (PF02629; HMM-score: 16.5)ApbA; Ketopantoate reductase PanE/ApbA (PF02558; HMM-score: 15.6)CoA_binding_2; CoA binding domain (PF13380; HMM-score: 13.5)Chelatase (CL0043) Oxidored_nitro; Nitrogenase component 1 type Oxidoreductase (PF00148; HMM-score: 12.7)NADP_Rossmann (CL0063) Mur_ligase; Mur ligase family, catalytic domain (PF01225; HMM-score: 12.7)Shikimate_DH; Shikimate / quinate 5-dehydrogenase (PF01488; HMM-score: 12.7)NAD_binding_7; Putative NAD(P)-binding (PF13241; HMM-score: 12.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Mg2+
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- 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): 0.059023
- TAT(Tat/SPI): 0.00266
- LIPO(Sec/SPII): 0.005356
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTTVYYDQDVKTDALQGKKIAVVGYGSQGHAHAQNLKDNGYDVVIGIRPGRSFDKAKEDGFDVFPVAEAVKQADVIMVLLPDEIQGDVYKNEIEPNLEKHNALAFAHGFNIHFGVIQPPADVDVFLVAPKGPGHLVRRTFVEGSAVPSLFGIQQGASGQARNIALSYAKGIGATRAGVIETTFKEETETDLFGEQAVLCGGVSKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMENVRYSISNTAEFGDYVSGPRVITPDVKENMKAVLTDIQNGNFSNRFIEDNKNGFKEFYKLREEQHGHQIEKVGRELREMMPFIKSKSIEK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- predicted SigA promoter [3] : S883 > S884 > SAOUHSC_02281 > SAOUHSC_02282 > SAOUHSC_02283 > S885 > SAOUHSC_02284 > SAOUHSC_02285 > SAOUHSC_02286 > SAOUHSC_02287 > leuD > SAOUHSC_02289
⊟Regulation[edit | edit source]
- regulator: CodY* (repression) regulon
CodY* (TF) important in Amino acid metabolism; RegPrecise transcription unit transferred from N315 data RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [3] Multi-gene expression profiles
⊟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]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.0 3.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e) - ↑ Charlotte D Majerczyk, Paul M Dunman, Thanh T Luong, Chia Y Lee, Marat R Sadykov, Greg A Somerville, Kip Bodi, Abraham L Sonenshein
Direct targets of CodY in Staphylococcus aureus.
J Bacteriol: 2010, 192(11);2861-77
[PubMed:20363936] [WorldCat.org] [DOI] (I p)