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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0660 [new locus tag: SACOL_RS03415 ]
- pan locus tag?: SAUPAN002470000
- symbol: adhP
- pan gene symbol?: adh1
- synonym:
- product: alcohol dehydrogenase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0660 [new locus tag: SACOL_RS03415 ]
- symbol: adhP
- product: alcohol dehydrogenase
- replicon: chromosome
- strand: +
- coordinates: 688943..689953
- length: 1011
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238251 NCBI
- RefSeq: YP_185544 NCBI
- BioCyc: see SACOL_RS03415
- MicrobesOnline: 912140 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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961ATGAGAGCAGCAGTTGTAACGAAAGATCACAAAGTAAGTATTGAGGACAAAAAGTTAAGA
GCTTTAAAACCTGGTGAAGCGTTGGTACAAACGGAATATTGTGGCGTTTGTCATACCGAT
TTACATGTTAAGAATGCTGATTTTGGTGATGTTACAGGCGTTACTTTAGGTCATGAAGGT
ATTGGTAAAGTCATCGAAGTTGCGGAAGATGTAGAATCATTAAAAATTGGAGACCGTGTG
TCTATCGCTTGGATGTTCGAAAGCTGTGGAAGATGTGAATATTGTACAACAGGTCGTGAA
ACACTTTGCCGTAGTGTGAAAAATGCTGGTTATACAGTAGATGGTGCAATGGCTGAACAA
GTTATTGTTACTGCAGACTATGCTGTGAAAGTACCTGAAAAATTAGATCCAGCAGCAGCG
TCTTCTATTACATGCGCAGGTGTGACAACTTATAAAGCTGTAAAAGTAAGTAATGTAAAA
CCTGGACAATGGTTAGGTGTTTTTGGTATAGGTGGTTTAGGTAACCTAGCTTTACAATAT
GCTAAAAACGTTATGGGGGCTAAAATTGTTGCCTTCGACATCAATGATGATAAATTAGCA
TTCGCGAAAGAATTAGGTGCTGATGCTATTATTAATTCTAAAGATGTTGATCCAGTTGCA
GAAGTTATGAAATTAACTGATAACAAAGGATTAGATGCAACAGTGGTAACTTCAGTTGCT
AAGACGCCATTTAACCAAGCGGTTGATGTTGTAAAAGCTGGTGCAAGAGTTGTTGCCGTT
GGTTTACCTGTTGATAAAATGAACTTAGATATCCCAAGATTAGTGCTTGATGGTATTGAA
GTAGTAGGTTCACTTGTTGGTACAAGACAAGACTTACGTGAAGCGTTTGAATTTGCTGCT
GAAAATAAAGTAACACCTAAAGTTCAATTAAGAAAATTAGAAGAAATCAATGATATTTTT
GAAGAAATGGAAAATGGTACTATAACTGGTAGAATGGTTATTAAATTTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0660 [new locus tag: SACOL_RS03415 ]
- symbol: AdhP
- description: alcohol dehydrogenase
- length: 336
- theoretical pI: 5.15171
- theoretical MW: 36047.3
- GRAVY: 0.0455357
⊟Function[edit | edit source]
- ⊞reaction: EC 1.1.1.1? ExPASy
- ⊞TIGRFAM: Energy metabolism Fermentation zinc-binding alcohol dehydrogenase family protein (TIGR02822; EC 1.-.-.-; HMM-score: 156.6)Cellular processes Detoxification S-(hydroxymethyl)mycothiol dehydrogenase (TIGR03451; EC 1.1.1.306; HMM-score: 152.2)Energy metabolism Amino acids and amines L-threonine 3-dehydrogenase (TIGR00692; EC 1.1.1.103; HMM-score: 144)Unknown function Enzymes of unknown specificity NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family (TIGR03989; EC 1.1.99.36; HMM-score: 137.4)6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase (TIGR03201; EC 1.1.1.-; HMM-score: 135.5)and 12 more
- ⊞TheSEED :
- Alcohol dehydrogenase (EC 1.1.1.1)
and 2 more - ⊞PFAM: NADP_Rossmann (CL0063) ADH_zinc_N; Zinc-binding dehydrogenase (PF00107; HMM-score: 111.5)GroES (CL0296) ADH_N; Alcohol dehydrogenase GroES-like domain (PF08240; HMM-score: 95.1)and 6 more
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Zn2+
- effectors:
⊟Localization[edit | edit source]
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MRAAVVTKDHKVSIEDKKLRALKPGEALVQTEYCGVCHTDLHVKNADFGDVTGVTLGHEGIGKVIEVAEDVESLKIGDRVSIAWMFESCGRCEYCTTGRETLCRSVKNAGYTVDGAMAEQVIVTADYAVKVPEKLDPAAASSITCAGVTTYKAVKVSNVKPGQWLGVFGIGGLGNLALQYAKNVMGAKIVAFDINDDKLAFAKELGADAIINSKDVDPVAEVMKLTDNKGLDATVVTSVAKTPFNQAVDVVKAGARVVAVGLPVDKMNLDIPRLVLDGIEVVGSLVGTRQDLREAFEFAAENKVTPKVQLRKLEEINDIFEEMENGTITGRMVIKF
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell:
- ⊟interaction partners:
SACOL1513 (hup) DNA-binding protein HU [4] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [4] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [4] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [4] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [4] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [4] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [4] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [4] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [4] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [4] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [4] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [4] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [4] (data from MRSA252) SACOL0426 acetyl-CoA acetyltransferase [4] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [4] (data from MRSA252) SACOL0944 NADH dehydrogenase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟Regulation[edit | edit source]
⊟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]
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Jump up to: 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 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)