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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00375
- pan locus tag?: SAUPAN001997000
- symbol: guaA
- pan gene symbol?: guaA
- synonym:
- product: GMP synthase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3919794 NCBI
- RefSeq: YP_498964 NCBI
- BioCyc: G1I0R-350 BioCyc
- MicrobesOnline: 1288858 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1501ATGGAAATGGCAAAAGAACAAGAGTTAATCCTTGTCTTAGACTTTGGTAGCCAATACAAC
CAATTAATTACACGCCGAATTCGTGAAATGGGCGTTTATAGTGAATTACACGATCATGAA
ATTTCAATTGAAGAAATTAAGAAAATGAATCCAAAAGGTATTATCTTATCAGGTGGTCCA
AATTCAGTTTATGAAGAAGGTTCATTTACAATTGATCCGGAAATATATAATTTAGGAATT
CCAGTACTTGGTATTTGTTACGGCATGCAATTAACTACTAAATTATTAGGTGGTAAAGTT
GAACGTGCCAATGAACGTGAATACGGTAAAGCAATCATTAATGCGAAGTCAGATGAGTTA
TTCGCTGGCTTACCAGCAGAACAAACTGTTTGGATGAGTCATTCTGATAAAGTTATTGAA
ATTCCAGAAGGCTTTGAAGTTATCGCTGATAGCCCAAGCACAGACTATGCAGCAATCGAA
GATAAGAAACGTCGCATTTATGGTGTTCAATTCCATCCAGAAGTACGTCATACAGAATAT
GGTAATGATTTATTAAATAATTTTGTCCGTCGTGTTTGTGATTGTAGAGGTCAATGGACA
ATGGAAAACTTTATCGAAATCGAAATTGAAAAGATTCGTCAACGCGTAGGAGACCGTCGT
GTATTATGTGCGATGAGTGGCGGCGTAGATTCATCTGTTGTAGCTGTACTATTGCATAAA
GCAATAGGTGATCAACTAACATGTATCTTTGTAGACCATGGCTTACTTCGTAAAGGTGAA
GGCGACATGGTTATGGAGCAATTCGGTGAAGGTTTCAACATGAATATTATTCGTGTTAAT
GCGAAAGATCGCTTTATGAATAAATTAAAAGGTGTTTCAGATCCTGAACAAAAACGTAAA
ATCATTGGTAATGAATTTGTATACGTATTTGATGATGAAGCATCAAAACTGAAAGGTGTA
GACTTCCTTGCGCAAGGAACACTATATACAGACGTCATCGAATCAGGTACTAAAACAGCA
CAAACAATCAAATCACACCACAATGTTGGTGGATTACCAGAAGACATGGAATTCGAATTA
ATCGAACCAATCAATACATTGTTTAAAGATGAAGTACGTAAATTAGGTATTGAGTTAGGT
ATTCCAGAACATTTAGTATGGAGACAACCATTCCCAGGACCTGGTCTTGGTATTCGTGTA
CTTGGAGAAATTACTGAAGATAAACTAGAAATCGTTAGAGAATCAGACGCGATTTTACGC
CAAGTGATTAGAGAAGAAGGTCTTGAAAGAGAAATTTGGCAATACTTCACAGTGTTACCA
AACATTCAATCAGTAGGTGTTATGGGAGACTACCGTACGTATGATCACACAGTAGGTATT
CGTGCAGTAACATCTATCGACGGTATGACAAGTGACTTCGCACGCATCGATTGGGAAGTC
TTACAAAAGATTTCTAGTCGTATCGTAAACGAAGTAGATCACGTCAACCGCGTAGTCTAT
GACATTACATCAAAACCACCAAGCACAATTGAGTGGGAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00375
- symbol: GuaA
- description: GMP synthase
- length: 513
- theoretical pI: 4.76247
- theoretical MW: 58230
- GRAVY: -0.289279
⊟Function[edit | edit source]
- reaction: EC 6.3.5.2? ExPASyGMP synthase (glutamine-hydrolyzing) ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
- TIGRFAM: Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis GMP synthase (glutamine-hydrolyzing), C-terminal domain (TIGR00884; EC 6.3.5.2; HMM-score: 508)and 13 morePurines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis GMP synthase (glutamine-hydrolyzing), N-terminal domain (TIGR00888; EC 6.3.5.2; HMM-score: 274.7)glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase (TIGR00566; HMM-score: 65.1)Amino acid biosynthesis Aromatic amino acid family anthranilate synthase (TIGR01815; EC 4.1.3.27; HMM-score: 56.2)Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, small subunit (TIGR01368; EC 6.3.5.5; HMM-score: 52.7)Amino acid biosynthesis Histidine family imidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR01855; EC 2.4.2.-; HMM-score: 35.8)Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides NAD+ synthetase (TIGR00552; EC 6.3.1.5; HMM-score: 35.6)aminodeoxychorismate synthase (TIGR01823; EC 2.6.1.85; HMM-score: 32)Hypothetical proteins Conserved TIGR00268 family protein (TIGR00268; HMM-score: 24.3)Protein synthesis tRNA and rRNA base modification tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (TIGR00420; EC 2.1.1.61; HMM-score: 20.4)Amino acid biosynthesis Aspartate family asparagine synthase (glutamine-hydrolyzing) (TIGR01536; EC 6.3.5.4; HMM-score: 17.6)Protein synthesis tRNA and rRNA base modification tRNA(Ile)-lysidine synthetase (TIGR02432; EC 6.3.4.-; HMM-score: 17.6)asparagine synthase family amidotransferase (TIGR03104; HMM-score: 14.6)Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis CTP synthase (TIGR00337; EC 6.3.4.2; HMM-score: 12.2)
- TheSEED :
- GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)
Nucleosides and Nucleotides Purines Purine conversions GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)and 1 more - PFAM: Glutaminase_I (CL0014) GATase; Glutamine amidotransferase class-I (PF00117; HMM-score: 153.3)no clan defined GMP_synt_C; GMP synthase C terminal domain (PF00958; HMM-score: 144.7)and 8 moreGlutaminase_I (CL0014) Peptidase_C26; Peptidase C26 (PF07722; HMM-score: 40.6)HUP (CL0039) NAD_synthase; NAD synthase (PF02540; HMM-score: 36.7)tRNA_Me_trans; tRNA methyl transferase (PF03054; HMM-score: 24.4)Asn_synthase; Asparagine synthase (PF00733; HMM-score: 21.4)ATP_bind_3; PP-loop family (PF01171; HMM-score: 19.3)QueC; Queuosine biosynthesis protein QueC (PF06508; HMM-score: 17.5)no clan defined LEA_6; Late embryogenesis abundant protein 18 (PF10714; HMM-score: 17)HUP (CL0039) PAPS_reduct; Phosphoadenosine phosphosulfate reductase family (PF01507; HMM-score: 12.8)
⊟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: 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): 0.00385
- TAT(Tat/SPI): 0.00072
- LIPO(Sec/SPII): 0.000338
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MEMAKEQELILVLDFGSQYNQLITRRIREMGVYSELHDHEISIEEIKKMNPKGIILSGGPNSVYEEGSFTIDPEIYNLGIPVLGICYGMQLTTKLLGGKVERANEREYGKAIINAKSDELFAGLPAEQTVWMSHSDKVIEIPEGFEVIADSPSTDYAAIEDKKRRIYGVQFHPEVRHTEYGNDLLNNFVRRVCDCRGQWTMENFIEIEIEKIRQRVGDRRVLCAMSGGVDSSVVAVLLHKAIGDQLTCIFVDHGLLRKGEGDMVMEQFGEGFNMNIIRVNAKDRFMNKLKGVSDPEQKRKIIGNEFVYVFDDEASKLKGVDFLAQGTLYTDVIESGTKTAQTIKSHHNVGGLPEDMEFELIEPINTLFKDEVRKLGIELGIPEHLVWRQPFPGPGLGIRVLGEITEDKLEIVRESDAILRQVIREEGLEREIWQYFTVLPNIQSVGVMGDYRTYDHTVGIRAVTSIDGMTSDFARIDWEVLQKISSRIVNEVDHVNRVVYDITSKPPSTIEWE
⊟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_00519 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00878 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_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: G-box (transcription termination) regulon
G-box (5' cis-acting region) important in Purine metabolism; transcription unit transferred from N315 data RegPrecise
⊟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 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)