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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01451
- pan locus tag?: SAUPAN003892000
- symbol: SAOUHSC_01451
- pan gene symbol?: ilvA1
- synonym:
- product: threonine dehydratase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01451
- symbol: SAOUHSC_01451
- product: threonine dehydratase
- replicon: chromosome
- strand: -
- coordinates: 1407997..1409037
- length: 1041
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3920228 NCBI
- RefSeq: YP_499972 NCBI
- BioCyc: G1I0R-1349 BioCyc
- MicrobesOnline: 1289886 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1021ATGACAACCAACACAGTTACATTACAAACAGCACATATTGTAAGTTTAGGAGATATCGAA
GAAGCTAAAGCAAGCATTAAACCATTTATTCGTCGAACACCTCTAATTAAATCAATGTAT
TTAAGCCAAAGTATAACTAAAGGGAATGTATTTCTAAAATTAGAAAATATGCAATTCACA
GGATCTTTTAAATTTAGAGGCGCTAGCAATAAAATTAATCACTTAACAGATGAACAAAAA
GAAAAAGGCATTATCGCAGCATCTGCTGGGAACCATGCACAAGGTGTTGCTTTAACAGCT
AAATTATTAGGCATTGATGCAACGATTGTAATGCCTGAAACAGCACCACAAGCGAAACAA
CAAGCAACAAAAGGCTATGGGGCAAAGGTTATTTTAAAAGGTAAAAACTTTAACGAAACT
AGACTTTATATGGAAGAATTAGCGAAAGAAAATGGCATGACAATCGTTCATCCATATGAC
GATAAGTTTGTAATGGCAGGCCAAGGAACAATTGGTTTAGAAATTTTAGATGATATTTGG
AATGTGAATACAGTCATCGTACCAGTTGGCGGTGGAGGATTAATTGCAGGTATTGCCACC
GCATTAAAATCATTTAACCCTTCAATTCATATTATCGGTGTTCAATCTGAGAATGTTCAT
GGTATGGCTGAGTCTTTCTATAAGAGAGATTTAACTGAACATCGAGTGGATAGCACAATA
GCAGATGGTTGTGATGTAAAAGTTCCTGGTGAACAAACATATGAAGTAGTTAAACATTTA
GTAGATGAATTTATTCTTGTTACTGAAGAAGAAATTGAACATGCTATGAAAGATTTAATG
CAGCGTGCCAAAATTATTACTGAAGGTGCAGGCGCATTACCAACAGCTGCAATTTTAAGT
GGAAAAATAAACAATAAATGGCTTGAAGATAAAAATGTTGTTGCATTAGTTTCAGGCGGG
AATGTTGACTTAACTAGAGTTTCAGGTGTCATTGAACATGGACTGAATATTGCAGATACA
AGCAAGGGTGTGGTAGGTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01451
- symbol: SAOUHSC_01451
- description: threonine dehydratase
- length: 346
- theoretical pI: 6.51894
- theoretical MW: 37305.6
- GRAVY: -0.0575145
⊟Function[edit | edit source]
- ⊞reaction: EC 4.3.1.19? ExPASy
- ⊞TIGRFAM: Amino acid biosynthesis Pyruvate family threonine ammonia-lyase (TIGR01127; EC 4.3.1.19; HMM-score: 395.5)and 16 more
- ⊞TheSEED :
- L-serine dehydratase, (PLP)-dependent (EC 4.3.1.17)
- Threonine dehydratase, catabolic (EC 4.3.1.19)
Amino Acids and Derivatives Alanine, serine, and glycine Glycine and Serine Utilization Threonine dehydratase, catabolic (EC 4.3.1.19)and 2 more - PFAM: NADP_Rossmann (CL0063) PALP; Pyridoxal-phosphate dependent enzyme (PF00291; HMM-score: 279)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: pyridoxal 5'-phosphate
- effectors:
⊟Localization[edit | edit source]
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTTNTVTLQTAHIVSLGDIEEAKASIKPFIRRTPLIKSMYLSQSITKGNVFLKLENMQFTGSFKFRGASNKINHLTDEQKEKGIIAASAGNHAQGVALTAKLLGIDATIVMPETAPQAKQQATKGYGAKVILKGKNFNETRLYMEELAKENGMTIVHPYDDKFVMAGQGTIGLEILDDIWNVNTVIVPVGGGGLIAGIATALKSFNPSIHIIGVQSENVHGMAESFYKRDLTEHRVDSTIADGCDVKVPGEQTYEVVKHLVDEFILVTEEEIEHAMKDLMQRAKIITEGAGALPTAAILSGKINNKWLEDKNVVALVSGGNVDLTRVSGVIEHGLNIADTSKGVVG
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization:
- quantitative data / protein copy number per cell:
- ⊟interaction partners:
SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01909 S-adenosylmethionine synthetase [3] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_01450 < SAOUHSC_01451 < SAOUHSC_01452predicted SigA promoter [4] : SAOUHSC_01448 < S605 < SAOUHSC_01450 < SAOUHSC_01451 < S606 < SAOUHSC_01452
⊟Regulation[edit | edit source]
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] ⊟Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟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]
⊟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) - ↑ Jump up to: 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p) - ↑ Jump up to: 4.0 4.1 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)