Jump to navigation
Jump to search
NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01007
- pan locus tag?: SAUPAN003276000
- symbol: SAOUHSC_01007
- pan gene symbol?: folD
- synonym:
- product: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920405 NCBI
- RefSeq: YP_499557 NCBI
- BioCyc: G1I0R-947 BioCyc
- MicrobesOnline: 1289470 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
61
121
181
241
301
361
421
481
541
601
661
721
781
841ATGGTTGCTAAAATTTTAGATGGTAAACAAATTGCCAAAGACTACAGACAGGGGTTACAA
GATCAAGTTGAAGCGCTAAAAGAAAAGGGTTTTACACCTAAATTATCCGTTATATTAGTT
GGTAATGATGGCGCTAGTCAAAGTTATGTTAGATCAAAAAAGAAAGCAGCTGAAAAAATT
GGTATGATTTCAGAAATCGTACATTTGGAAGAAACAGCTACTGAAGAAGAAGTATTAAAC
GAACTAAATAGACTAAATAATGATGATTCTGTAAGTGGTATTTTGGTACAAGTACCATTA
CCAAAACAAGTTAGCGAACAGAAAATATTAGAAGCAATCAATCCTGAAAAAGATGTGGAC
GGTTTTCATCCAATAAATATAGGGAAATTATATATCGATGAACAAACTTTTGTACCTTGC
ACACCGCTCGGCATCATGGAAATATTAAAACATGCTGATATTGATTTAGAAGGTAAAAAT
GCAGTTGTAATTGGACGAAGTCATATTGTCGGACAACCAGTTTCTAAGTTACTACTTCAA
AAAAATGCATCAGTAACAATCTTACATTCTCGTTCAAAAGATATGGCATCATATTTAAAA
GATGCTGATGTCATTGTCAGTGCAGTTGGTAAGCCTGGTTTAGTAACAAAAGATGTGGTC
AAAGAAGGAGCAGTAATTATCGATGTTGGCAATACGCCAGATGAAAATGGCAAATTAAAA
GGTGACGTTGATTATGATGCGGTTAAAGAAATTGCTGGAGCTATTACACCAGTTCCTGGT
GGCGTTGGTCCATTAACAATTACTATGGTATTAAATAATACTTTGCTTGCAGAAAAAATG
CGTCGAGGTATTGATTCGTAA60
120
180
240
300
360
420
480
540
600
660
720
780
840
861
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01007
- symbol: SAOUHSC_01007
- description: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
- length: 286
- theoretical pI: 5.24534
- theoretical MW: 30843.3
- GRAVY: -0.127972
⊟Function[edit | edit source]
- reaction: EC 1.5.1.5? ExPASyMethylenetetrahydrofolate dehydrogenase (NADP+) 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPHEC 3.5.4.9? ExPASyMethenyltetrahydrofolate cyclohydrolase 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate
- TIGRFAM: Unknown function General putative RNA-binding protein, YhbY family (TIGR00253; HMM-score: 11.1)
- TheSEED :
- Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)
- Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)
Carbohydrates One-carbon Metabolism One-carbon metabolism by tetrahydropterines Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)and 4 moreCarbohydrates One-carbon Metabolism One-carbon metabolism by tetrahydropterines Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)Carbohydrates One-carbon Metabolism Serine-glyoxylate cycle Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) - PFAM: NADP_Rossmann (CL0063) THF_DHG_CYH_C; Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain (PF02882; HMM-score: 222.8)and 3 moreAA_dh_N (CL0603) THF_DHG_CYH; Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain (PF00763; HMM-score: 139.6)NADP_Rossmann (CL0063) AlaDh_PNT_C; Alanine dehydrogenase/PNT, C-terminal domain (PF01262; HMM-score: 17)Shikimate_DH; Shikimate / quinate 5-dehydrogenase (PF01488; HMM-score: 13.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 7.5
- Cytoplasmic Membrane Score: 1.15
- Cellwall Score: 0.62
- Extracellular Score: 0.73
- 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): 0.003408
- TAT(Tat/SPI): 0.000272
- LIPO(Sec/SPII): 0.000481
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [2] [3]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [4] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [4] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [4] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [4] (data from MRSA252) SAOUHSC_00132 aldehyde dehydrogenase [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00346 GTP-dependent nucleic acid-binding protein EngD [4] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00742 ribonucleotide-diphosphate reductase subunit alpha [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_00906 hypothetical protein [4] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [4] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [4] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [4] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_01909 S-adenosylmethionine synthetase [4] (data from MRSA252) SAOUHSC_02241 hypothetical protein [4] (data from MRSA252) SAOUHSC_02243 hypothetical protein [4] (data from MRSA252) SAOUHSC_02366 fructose-bisphosphate aldolase [4] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252) SAOUHSC_02965 carbamate kinase [4] (data from MRSA252) SAOUHSC_02969 arginine deiminase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- predicted SigA promoter [5] : SAOUHSC_01005 < S409 < S410 < S411 < SAOUHSC_01007 < S412
⊟Regulation[edit | edit source]
- data available for N315
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] 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]
- ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
BMC Genomics: 2009, 10;291
[PubMed:19570206] [WorldCat.org] [DOI] (I e) - ↑ 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) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 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) - ↑ 5.0 5.1 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)