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NCBI: 02-MAR-2017
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus N315
- locus tag: SA_RS05190 [old locus tag: SA0915 ]
- pan locus tag?: SAUPAN003276000
- symbol: SA_RS05190
- pan gene symbol?: folD
- synonym:
- product: bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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841ATGGTTGCTAAAATTTTAGATGGTAAACAAATTGCCAAAGACTACAGACAGGGGTTACAA
GATCAAGTTGAAGCGCTAAAAGAAAAGGGTTTTACACCTAAATTATCCGTTATATTAGTT
GGTAATGATGGCGCTAGTCAAAGTTATGTTAGATCAAAAAAGAAAGCAGCTGAAAAAATT
GGTATGATTTCAGAAATCGTACATTTGGAAGAAACAGCTACTGAAGAAGAAGTATTAAAC
GAACTAAATAGACTAAATAATGATGATTCTGTAAGTGGTATTTTGGTACAAGTACCATTA
CCAAAACAAGTTAGCGAACAGAAAATATTAGAAGCAATCAATCCTGAAAAAGATGTGGAC
GGATTTCATCCAATAAATATAGGGAAATTATATATCGATGAACAAACTTTTGTACCTTGC
ACACCGCTCGGCATCATGGAAATATTAAAACATGCTGATATTGATTTAGAAGCTAAAAAT
GCAGTTGTAATTGGACGAAGTCATATTGTCGGACAACCAGTTTCTAAGTTACTACTTCAA
AAAAATGCATCAGTAACAATCTTACATTCTCGTTCAAAAGATATGGCATCATATTTAAAA
GATGCTGATGTCATTGTCAGTGCAGTTGGTAAGCCTAGTTTAGTAACAAAAGATGTGGTC
AAAGAAGGAGCAGTAATTATCGATGTTGGCAATACGCCAGATGAAAATGGCAAATTAAAA
GGTGACGTTGATTATGATGCGGTTAAAGAAATTGCTGGAGCTATTACACCAGTTCCTGGT
GGCGTTGGTCCATTAACAATTACTATGGTATTAAATAATACTTTGCTTGCAGAAAAAATG
CGTCGAGGTATTGATTCGTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SA_RS05190 [old locus tag: SA0915 ]
- symbol: SA_RS05190
- description: bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
- length: 286
- theoretical pI: 5.24534
- theoretical MW: 30887.4
- GRAVY: -0.121678
⊟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:
- TheSEED: see SA0915
- PFAM: NADP_Rossmann (CL0063) THF_DHG_CYH_C; Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain (PF02882; HMM-score: 219.8)and 4 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: 14.8)Phosphatase (CL0031) PTS_IIB; PTS system, Lactose/Cellobiose specific IIB subunit (PF02302; HMM-score: 13.8)
⊟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:
- 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]
- MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEAKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPSLVTKDVVKEGAVIIDVGNTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS
⊟Experimental data[edit | edit source]
- experimentally validated: data available for COL, NCTC8325
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SA_RS11130 (deoA) pyrimidine-nucleoside phosphorylase [1] (data from MRSA252) SA_RS00980 aldehyde dehydrogenase [1] (data from MRSA252) SA_RS01275 formate acetyltransferase [1] (data from MRSA252) SA_RS02005 GTP-binding protein YchF [1] (data from MRSA252) SA_RS02910 50S ribosomal protein L1 [1] (data from MRSA252) SA_RS02915 50S ribosomal protein L10 [1] (data from MRSA252) SA_RS02920 50S ribosomal protein L7/L12 [1] (data from MRSA252) SA_RS02935 DNA-directed RNA polymerase subunit beta' [1] (data from MRSA252) SA_RS02955 elongation factor G [1] (data from MRSA252) SA_RS02960 elongation factor Tu [1] (data from MRSA252) SA_RS03910 ribonucleotide-diphosphate reductase subunit alpha [1] (data from MRSA252) SA_RS04575 NADH dehydrogenase [1] (data from MRSA252) SA_RS04710 hypothetical protein [1] (data from MRSA252) SA_RS05350 pyruvate dehydrogenase E1 component subunit alpha [1] (data from MRSA252) SA_RS05355 pyruvate dehydrogenase E1 component subunit beta [1] (data from MRSA252) SA_RS05360 dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex [1] (data from MRSA252) SA_RS05365 dihydrolipoyl dehydrogenase [1] (data from MRSA252) SA_RS06140 50S ribosomal protein L19 [1] (data from MRSA252) SA_RS06225 30S ribosomal protein S2 [1] (data from MRSA252) SA_RS07060 dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex [1] (data from MRSA252) SA_RS07385 DNA-binding protein HU [1] (data from MRSA252) SA_RS07955 molecular chaperone DnaK [1] (data from MRSA252) SA_RS08295 50S ribosomal protein L21 [1] (data from MRSA252) SA_RS08545 isocitrate dehydrogenase (NADP(+)) [1] (data from MRSA252) SA_RS08560 pyruvate kinase [1] (data from MRSA252) SA_RS08625 universal stress protein UspA [1] (data from MRSA252) SA_RS08675 30S ribosomal protein S4 [1] (data from MRSA252) SA_RS09055 S-adenosylmethionine synthase [1] (data from MRSA252) SA_RS10410 gamma-hemolysin subunit B [1] (data from MRSA252) SA_RS10415 succinyl-diaminopimelate desuccinylase [1] (data from MRSA252) SA_RS11075 fructose-bisphosphate aldolase [1] (data from MRSA252) SA_RS11430 Asp23/Gls24 family envelope stress response protein [1] (data from MRSA252) SA_RS11600 30S ribosomal protein S9 [1] (data from MRSA252) SA_RS11640 30S ribosomal protein S11 [1] (data from MRSA252) SA_RS11670 50S ribosomal protein L15 [1] (data from MRSA252) SA_RS11680 30S ribosomal protein S5 [1] (data from MRSA252) SA_RS11690 50S ribosomal protein L6 [1] (data from MRSA252) SA_RS11705 50S ribosomal protein L5 [1] (data from MRSA252) SA_RS11735 30S ribosomal protein S3 [1] (data from MRSA252) SA_RS11740 50S ribosomal protein L22 [1] (data from MRSA252) SA_RS11745 30S ribosomal protein S19 [1] (data from MRSA252) SA_RS11750 50S ribosomal protein L2 [1] (data from MRSA252) SA_RS13905 carbamate kinase 2 [1] (data from MRSA252) SA_RS13920 arginine deiminase [1] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: PurR see SA0915
⊟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]
- ↑ 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 1.41 1.42 1.43 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)