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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1477 [new locus tag: SACOL_RS07525 ]
- pan locus tag?: SAUPAN003892000
- symbol: ilvA1
- 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: SACOL1477 [new locus tag: SACOL_RS07525 ]
- symbol: ilvA1
- product: threonine dehydratase
- replicon: chromosome
- strand: -
- coordinates: 1514662..1515702
- length: 1041
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236081 NCBI
- RefSeq: YP_186322 NCBI
- BioCyc: see SACOL_RS07525
- MicrobesOnline: 912930 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: SACOL1477 [new locus tag: SACOL_RS07525 ]
- symbol: IlvA1
- 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? ExPASyThreonine ammonia-lyase L-threonine = 2-oxobutanoate + NH3
- TIGRFAM: Amino acid biosynthesis Pyruvate family threonine ammonia-lyase (TIGR01127; EC 4.3.1.19; HMM-score: 395.5)and 16 moreAmino acid biosynthesis Pyruvate family threonine ammonia-lyase, biosynthetic (TIGR01124; EC 4.3.1.19; HMM-score: 301.5)Amino acid biosynthesis Pyruvate family threonine dehydratase (TIGR02079; EC 4.3.1.19; HMM-score: 266.5)ectoine utilization protein EutB (TIGR02991; HMM-score: 263.4)Amino acid biosynthesis Serine family cysteine synthase (TIGR01136; EC 2.5.1.47; HMM-score: 94.6)Amino acid biosynthesis Serine family cysteine synthase A (TIGR01139; EC 2.5.1.47; HMM-score: 81.6)Amino acid biosynthesis Aspartate family threonine synthase (TIGR00260; EC 4.2.3.1; HMM-score: 74.2)Amino acid biosynthesis Serine family cysteine synthase B (TIGR01138; EC 2.5.1.47; HMM-score: 71.9)Cellular processes Biosynthesis of natural products 2,3-diaminopropionate biosynthesis protein SbnA (TIGR03945; HMM-score: 68.5)Amino acid biosynthesis Serine family cystathionine beta-synthase (TIGR01137; EC 4.2.1.22; HMM-score: 60.9)diaminopropionate ammonia-lyase (TIGR03528; EC 4.3.1.15; HMM-score: 56)Energy metabolism Other diaminopropionate ammonia-lyase family (TIGR01747; EC 4.3.1.15; HMM-score: 49.7)Amino acid biosynthesis Aromatic amino acid family tryptophan synthase, beta subunit (TIGR00263; EC 4.2.1.20; HMM-score: 30.7)pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family (TIGR01275; HMM-score: 29.8)Unknown function Enzymes of unknown specificity pyridoxal-phosphate dependent TrpB-like enzyme (TIGR01415; HMM-score: 28.5)Biosynthesis of cofactors, prosthetic groups, and carriers Other cysteate synthase (TIGR03844; EC 2.5.1.76; HMM-score: 22.9)Energy metabolism Methanogenesis cysteate synthase (TIGR03844; EC 2.5.1.76; HMM-score: 22.9)
- 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: no clan defined PALP; Pyridoxal-phosphate dependent enzyme (PF00291; HMM-score: 275.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: pyridoxal 5'-phosphate
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic Membrane
- Cytoplasmic Score: 1.78
- Cytoplasmic Membrane Score: 8.16
- Cellwall Score: 0.06
- Extracellular Score: 0.01
- 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): 0.016412
- TAT(Tat/SPI): 0.000648
- LIPO(Sec/SPII): 0.001021
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTTNTVTLQTAHIVSLGDIEEAKASIKPFIRRTPLIKSMYLSQSITKGNVFLKLENMQFTGSFKFRGASNKINHLTDEQKEKGIIAASAGNHAQGVALTAKLLGIDATIVMPETAPQAKQQATKGYGAKVILKGKNFNETRLYMEELAKENGMTIVHPYDDKFVMAGQGTIGLEILDDIWNVNTVIVPVGGGGLIAGIATALKSFNPSIHIIGVQSENVHGMAESFYKRDLTEHRVDSTIADGCDVKVPGEQTYEVVKHLVDEFILVTEEEIEHAMKDLMQRAKIITEGAGALPTAAILSGKINNKWLEDKNVVALVSGGNVDLTRVSGVIEHGLNIADTSKGVVG
⊟Experimental data[edit | edit source]
- experimentally validated: data available for NCTC8325
- protein localization:
- quantitative data / protein copy number per cell:
- interaction partners:
SACOL0452 (ahpC) alkyl hydroperoxide reductase subunit C [1] (data from MRSA252) SACOL2657 (arcA) arginine deiminase [1] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [1] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [1] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [1] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [1] (data from MRSA252) SACOL1837 (metK) S-adenosylmethionine synthetase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [1] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [1] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [1] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [1] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [1] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [1] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [1] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [1] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [1] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [1] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [1] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [1] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [1] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [1] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [1] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [1] (data from MRSA252) SACOL0944 NADH dehydrogenase [1] (data from MRSA252) SACOL1759 universal stress protein [1] (data from MRSA252) SACOL2173 alkaline shock protein 23 [1] (data from MRSA252) SACOL2561 hydroxymethylglutaryl-CoA synthase [1] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SACOL1476 < ilvA1 < ald1
⊟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]
- 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]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 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)