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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00894
- pan locus tag?: SAUPAN003059000
- symbol: rocD
- pan gene symbol?: rocD
- synonym:
- product: ornithine--oxo-acid transaminase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00894
- symbol: rocD
- product: ornithine--oxo-acid transaminase
- replicon: chromosome
- strand: +
- coordinates: 857718..858908
- length: 1191
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921740 NCBI
- RefSeq: YP_499447 NCBI
- BioCyc: G1I0R-837 BioCyc
- MicrobesOnline: 1289358 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1141ATGACTAAATCTGAAAAAATTATTGAGTTAACAAATCATTACGGAGCACATAATTATTTA
CCATTGCCAATTGTCATTTCAGAAGCTGAAGGGGTATGGGTTAAAGATCCTGAAGGCAAT
AAATATATGGATATGTTATCTGCATATTCCGCTGTTAACCAAGGTCATAGACATCCGAAA
ATTATTCAAGCATTAAAAGATCAAGCTGATAAAGTGACTTTAGTTTCACGTGCTTTTCAT
AGTGATAACTTAGGTGAATGGTACGAAAAAATTTGTAAACTGGCAGGTAAAGATAAAGCT
TTACCAATGAATACAGGTGCTGAAGCAGTAGAAACAGCTTTGAAAGCAGCACGACGCTGG
GCATACGATGTTAAAGGAATTGAGCCAAATAAAGCAGAAATCATTGCATTTAATGGTAAC
TTCCATGGTCGAACAATGGCGCCAGTTTCATTATCTTCAGAAGCAGAATACCAACGTGGT
TATGGTCCGTTATTAGATGGATTTAGAAAAGTTGATTTTGGAGATGTAGATGCATTGAAA
GCTGCAATTAATGAAAATACTGCAGCAGTTTTAGTAGAACCAATTCAAGGTGAAGCGGGT
ATAAATATACCGCCAGAAGGATATTTGAAAGCAATTAGAGAATTATGTGATGAACATAAT
GTCTTATTTATTGCTGACGAAATCCAAGCAGGATTAGGTCGTTCGGGTAAATTATTTGCT
ACGGATTGGGATAATGTAAAACCTGATGTCTATATTTTAGGTAAAGCACTAGGTGGTGGA
GTCTTCCCAATTTCTGTTGTATTAGCAGATAAAGAAGTATTAGATGTCTTTACACCTGGC
TCACATGGTTCAACATTTGGTGGTAATCCACTTGCTTGTGCTGCATCAATTGCTGCATTA
GATGTTATCGTTGATGAGGATTTACCAGGCCGCTCTTTAGAATTAGGAGATTATTTTAAA
GAACAATTAAAGCAAATTGATCATCCATCAATTAAAGAAGTCCGTGGACGTGGTTTGTTT
ATAGGTGTGGAACTTAATGAAAGTGCTAGACCATATTGTGAAGCTTTGAAAGAAGAAGGC
TTATTATGTAAAGAAACGCATGATACTGTCATTCGTTTTGCACCACCATTAATTATTACT
AAAGAAGAATTGGACCTTGCACTTGAAAAAATAAGACATGTATTTCAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00894
- symbol: RocD
- description: ornithine--oxo-acid transaminase
- length: 396
- theoretical pI: 5.02774
- theoretical MW: 43417.2
- GRAVY: -0.183333
⊟Function[edit | edit source]
- reaction: EC 2.6.1.13? ExPASyOrnithine aminotransferase L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid
- TIGRFAM: ornithine--oxo-acid transaminase (TIGR01885; EC 2.6.1.13; HMM-score: 538.4)and 16 moretransaminase, acetylornithine/succinylornithine family (TIGR00707; HMM-score: 402)Energy metabolism Amino acids and amines succinylornithine transaminase family (TIGR03246; EC 2.6.1.81; HMM-score: 310.5)Central intermediary metabolism Polyamine biosynthesis putrescine aminotransferase (TIGR03372; EC 2.6.1.82; HMM-score: 256.2)Biosynthesis of cofactors, prosthetic groups, and carriers Biotin adenosylmethionine-8-amino-7-oxononanoate transaminase (TIGR00508; EC 2.6.1.62; HMM-score: 249.2)Central intermediary metabolism Other 4-aminobutyrate transaminase (TIGR00700; EC 2.6.1.19; HMM-score: 248.1)Central intermediary metabolism Other 2,4-diaminobutyrate 4-transaminase (TIGR00709; EC 2.6.1.-; HMM-score: 209.8)Cellular processes Adaptations to atypical conditions diaminobutyrate--2-oxoglutarate aminotransferase (TIGR02407; EC 2.6.1.76; HMM-score: 188.8)L-lysine 6-transaminase (TIGR03251; EC 2.6.1.36; HMM-score: 155.7)Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713; EC 5.4.3.8; HMM-score: 143.3)Central intermediary metabolism Other 4-aminobutyrate aminotransferase (TIGR00699; EC 2.6.1.19; HMM-score: 107)Protein synthesis tRNA and rRNA base modification cysteine desulfurase IscS (TIGR02006; EC 2.8.1.7; HMM-score: 16.4)Biosynthesis of cofactors, prosthetic groups, and carriers Other cysteine desulfurase IscS (TIGR02006; EC 2.8.1.7; HMM-score: 16.4)cysteine desulfurase, NifS family (TIGR03403; EC 2.8.1.7; HMM-score: 15.6)Energy metabolism Amino acids and amines tyrosine aminotransferase (TIGR01264; EC 2.6.1.5; HMM-score: 15.1)tyrosine/nicotianamine family aminotransferase (TIGR01265; HMM-score: 15)cysteine desulfurase NifS (TIGR03402; EC 2.8.1.7; HMM-score: 11.8)
- TheSEED :
- Ornithine aminotransferase (EC 2.6.1.13)
- PFAM: PLP_aminotran (CL0061) Aminotran_3; Aminotransferase class-III (PF00202; HMM-score: 446.1)and 4 moreAminotran_1_2; Aminotransferase class I and II (PF00155; HMM-score: 24.2)DegT_DnrJ_EryC1; DegT/DnrJ/EryC1/StrS aminotransferase family (PF01041; HMM-score: 23)Beta_elim_lyase; Beta-eliminating lyase (PF01212; HMM-score: 14.9)Aminotran_5; Aminotransferase class-V (PF00266; HMM-score: 12.1)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: pyridoxal 5'-phosphate
- 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): 0.007347
- TAT(Tat/SPI): 0.00029
- LIPO(Sec/SPII): 0.000678
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTKSEKIIELTNHYGAHNYLPLPIVISEAEGVWVKDPEGNKYMDMLSAYSAVNQGHRHPKIIQALKDQADKVTLVSRAFHSDNLGEWYEKICKLAGKDKALPMNTGAEAVETALKAARRWAYDVKGIEPNKAEIIAFNGNFHGRTMAPVSLSSEAEYQRGYGPLLDGFRKVDFGDVDALKAAINENTAAVLVEPIQGEAGINIPPEGYLKAIRELCDEHNVLFIADEIQAGLGRSGKLFATDWDNVKPDVYILGKALGGGVFPISVVLADKEVLDVFTPGSHGSTFGGNPLACAASIAALDVIVDEDLPGRSLELGDYFKEQLKQIDHPSIKEVRGRGLFIGVELNESARPYCEALKEEGLLCKETHDTVIRFAPPLIITKEELDLALEKIRHVFQ
⊟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:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_02703 (gpmA) 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [3] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [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_02500 (rplE) 50S ribosomal protein L5 [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_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_01755 (rpmA) 50S ribosomal protein L27 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [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_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [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_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulators: ArgR/AhrC* (repression) regulon, CcpA* regulon
ArgR/AhrC* (TF) important in Arginine biosynthesis, Arginine degradation; RegPrecise CcpA* (TF) important in Carbon catabolism; RegPrecise
⊟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]
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) - ↑ 3.00 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 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) - ↑ 4.0 4.1 4.2 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)