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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0154 [new locus tag: SACOL_RS00780 ]
- pan locus tag?: SAUPAN001003000
- symbol: aldA1
- pan gene symbol?: aldA
- synonym:
- product: aldehyde dehydrogenase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0154 [new locus tag: SACOL_RS00780 ]
- symbol: aldA1
- product: aldehyde dehydrogenase
- replicon: chromosome
- strand: +
- coordinates: 171181..172668
- length: 1488
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238707 NCBI
- RefSeq: YP_185054 NCBI
- BioCyc: see SACOL_RS00780
- MicrobesOnline: 911631 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1441ATGGCAGTAAACGTTCGAGATTATATTGCAGAGAATTATGGTTTATTTATCAATGGGGAA
TTTGTTAAAGGTAGCAGTGACGAAACAATCGAAGTGACTAATCCAGCAACTGGAGAAACA
CTATCACATATTACAAGAGCAAAAGATAAAGATGTCGATCATGCAGTCAAAGTGGCGCAA
GAGGCATTTGAATCATGGTCATTAACTTCTAAATCAGAACGTGCACAAATGTTGCGTGAT
ATTGGTGATAAATTAATGGCACAAAAAGATAAAATTGCAATGATTGAAACATTAAATAAT
GGTAAACCGATTCGTGAGACAACAGCAATTGATATTCCATTTGCTGCAAGACATTTCCAT
TATTTCGCAAGTGTTATTGAAACAGAAGAAGGTACAGTGAATGATATCGATAAAGACACA
ATGAGTATCGTACGACATGAGCCGATTGGCGTCGTAGGTGCTGTTGTTGCTTGGAACTTC
CCAATGCTATTAGCTGCATGGAAGATTGCGCCAGCCATTGCTGCAGGTAATACAATTGTG
ATTCAACCTTCGTCTTCAACACCATTAAGTTTATTGGAAGTTGCTAAAATTTTCCAAGAG
GTATTACCTAAAGGTGTTGTCAATATACTAACGGGTAAAGGTTCAGAATCAGGTAATGCA
ATTTTCAATCATGATGGTGTAGATAAATTATCATTTACGGGCTCAACTGATGTAGGTTAT
CAAGTTGCCGAAGCTGCAGCAAAACATCTAGTACCCGCTACATTAGAGCTTGGTGGTAAA
AGCGCCAATATCATATTAGATGATGCTAATTTAGACCTTGCAGTTGAAGGTATTCAGTTA
GGTATTTTATTCAACCAAGGTGAAGTATGTAGTGCAGGTTCTCGATTATTAGTTCATGAA
AAAATTTATGATCAATTGGTGCCACGTTTACAAGAGGCATTTTCAAATATTAAAGTTGGA
AATCCACAAGATGAAGCTACACAAATGGGTAGTCAAACTGGTAAGGATCAATTAGATAAA
ATTCAATCATATATTGATGCAGCAAAAGAATCAGATGCACAAATTTTAGCAGGCGGTCAT
CGCTTAACTGAAAATGGATTAGATAAAGGGTTCTTCTTTGAGCCGACATTAATTGCTGTG
CCAGACAATCATCACAAATTAGCACAAGAAGAAATATTTGGACCAGTGTTAACAGTGATT
AAAGTGAAGGACGATCAAGAAGCAATTGATATAGCTAATGATTCTGAGTATGGTTTAGCA
GGCGGTGTATTTTCTCAAAATATCACACGTGCATTAAATATTGCTAAAGCTGTACGTACA
GGACGTATTTGGATTAACACTTACAACCAAGTACCAGAAGGCGCACCATTTGGTGGTTAT
AAAAAATCAGGTATCGGTCGAGAAACTTATAAAGGTGCGTTAAGTAACTATCAACAAGTT
AAAAATATTTATATTGATACAAGCAATGCTTTAAAAGGTTTGTACTAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0154 [new locus tag: SACOL_RS00780 ]
- symbol: AldA1
- description: aldehyde dehydrogenase
- length: 495
- theoretical pI: 4.90708
- theoretical MW: 53658.2
- GRAVY: -0.171717
⊟Function[edit | edit source]
- reaction: EC 1.2.1.3? ExPASyAldehyde dehydrogenase (NAD+) An aldehyde + NAD+ + H2O = a carboxylate + NADH
- TIGRFAM: Cellular processes Adaptations to atypical conditions betaine-aldehyde dehydrogenase (TIGR01804; EC 1.2.1.8; HMM-score: 518.9)5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase (TIGR02299; EC 1.2.1.60; HMM-score: 439.6)and 14 moreEnergy metabolism Other 2-hydroxymuconic semialdehyde dehydrogenase (TIGR03216; EC 1.2.1.-; HMM-score: 379.4)Central intermediary metabolism Other succinate-semialdehyde dehydrogenase (TIGR01780; EC 1.2.1.-; HMM-score: 369.5)1-pyrroline dehydrogenase (TIGR03374; EC 1.2.1.19; HMM-score: 367.9)Unknown function Enzymes of unknown specificity aldehyde dehydrogenase, Rv0768 family (TIGR04284; EC 1.2.1.-; HMM-score: 349.7)Energy metabolism Amino acids and amines putative delta-1-pyrroline-5-carboxylate dehydrogenase (TIGR01237; EC 1.2.1.88; HMM-score: 308.7)Energy metabolism Amino acids and amines methylmalonate-semialdehyde dehydrogenase (acylating) (TIGR01722; EC 1.2.1.27; HMM-score: 248.5)putative phosphonoacetaldehyde dehydrogenase (TIGR03250; EC 1.2.1.-; HMM-score: 234.3)Energy metabolism Amino acids and amines succinylglutamate-semialdehyde dehydrogenase (TIGR03240; EC 1.2.1.71; HMM-score: 226.9)Energy metabolism Amino acids and amines delta-1-pyrroline-5-carboxylate dehydrogenase (TIGR01238; EC 1.2.1.88; HMM-score: 192.6)Energy metabolism Amino acids and amines 1-pyrroline-5-carboxylate dehydrogenase (TIGR01236; EC 1.2.1.88; HMM-score: 183.5)phenylacetic acid degradation protein paaN (TIGR02278; HMM-score: 122.3)acetaldehyde dehydrogenase (acetylating) (TIGR02518; EC 1.2.1.10; HMM-score: 42.7)phenylacetic acid degradation protein paaN (TIGR02288; HMM-score: 30.3)Amino acid biosynthesis Glutamate family glutamate-5-semialdehyde dehydrogenase (TIGR00407; EC 1.2.1.41; HMM-score: 26.5)
- TheSEED :
- Aldehyde dehydrogenase B (EC 1.2.1.22)
Carbohydrates Central carbohydrate metabolism Methylglyoxal Metabolism Aldehyde dehydrogenase B (EC 1.2.1.22)and 1 more - PFAM: ALDH-like (CL0099) Aldedh; Aldehyde dehydrogenase family (PF00171; HMM-score: 575.7)and 1 moreLuxC; Acyl-CoA reductase (LuxC) (PF05893; HMM-score: 11.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- 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): 0.006878
- TAT(Tat/SPI): 0.000512
- LIPO(Sec/SPII): 0.001159
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MAVNVRDYIAENYGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVKVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDTSNALKGLY
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4]
- quantitative data / protein copy number per cell:
- interaction partners:
SACOL1760 (ackA) acetate kinase [5] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [5] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL2618 (ldh2) L-lactate dehydrogenase [5] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [5] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [5] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [5] (data from MRSA252) SACOL2212 (rplQ) 50S ribosomal protein L17 [5] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [5] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [5] (data from MRSA252) SACOL2112 (rpmE2) 50S ribosomal protein L31 [5] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [5] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [5] (data from MRSA252) SACOL1831 (tal) translaldolase [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL2104 (upp) uracil phosphoribosyltransferase [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟Regulation[edit | edit source]
- regulator: CcpA regulon
CcpA (TF) important in Carbon catabolism; 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]
- ↑ 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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ 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) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 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)