| Glutamate 5-kinase, putative [Q4Q8S0] | |
|---|---|
| Systematic Name | LmjF.26.2710 [Leishmania major] |
| Gene Name | LMJF_26_2710 |
| Molecular Weight | 29085 Da |
| Protein Sequence Size | 264 |
| Function | Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline |
| Charge | 2.5 |
| Isoelectric Point | 6.9 pH |
| Description | Glutamate 5-kinase, putative (EC 2.7.2.11). |
| Subcellular Location | cytoplasm[Predict] |
| E. C. Number | 2.7.2.11 |
| Sequence | >tr|Q4Q8S0|Q4Q8S0_LEIMA Glutamate 5-kinase, putative (EC 2.7.2.11) - Leishmania major ADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCKFIADLQTKYEVILVTSGAVAAGYTQ KEMDKAYVPNKQALASMGQPLLMHMYYTQLQKHGILCAQMLLAAYDLDSRKRTMNAHNTI EVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYTENPRA STDAKIRSVVHELSPDDLVAEATPNNPFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEK AREFLFGGSHEIGTLFYPRGSSS |
| DNA Sequence | >LmjF26.2710 |||glutamate 5-kinase, putative|Leishmania major|chr 26|||Manual ATGGCGGACA TCTTGAAGTC GGTGAAGCGC ATCGTGGTGA AAGTGGGCTC CTCGATCCTTGTGGACAATC AGGAGATCGC CGCGCACCGG ATCGAGGCGC TATGCAAGTT TATCGCCGACCTCCAGACGA AGTATGAAGT GATCCTTGTC ACCTCCGGCG CAGTAGCCGC GGGGTACACACAAAAAGAGA TGGACAAGGC ATATGTGCCG AACAAGCAGG CACTTGCGTC GATGGGGCAGCCACTGCTCA TGCACATGTA CTACACTCAG CTCCAAAAGC ACGGCATCCT GTGCGCGCAGATGCTGCTTG CTGCCTATGA TCTGGACTCG CGGAAACGTA CGATGAACGC CCACAATACCATTGAGGTAC TCATCAGCCA CAAGGTGATC CCGATCATCA ACGAAAACGA CGCGACGGCGCTGCACGAGC TGGTCTTTGG TGACAATGAC CGTCTGTCCG CGCTTGTCGC GCACCACTTCAAGGCGGACC TACTTGTCAT TCTCAGCGAC ATCGACGGCT ACTACACCGA AAATCCTCGCGCCTCCACCG ATGCCAAGAT ACGCTCTGTC GTCCACGAAC TTAGCCCTGA CGATCTTGTGGCGGAGGCCA CGCCGAACAA TCCGTTCGCG ACGGGTGGGA TCGTAACGAA GCTGCAGGCTGCTCAATTCC TCCTAGAGAG GGGAGGAAAG ATGTACCTCT CGAGCGGATT CCACTTGGAGAAGGCGCGCG AGTTCCTTTT CGGCGGCTCG CACGAGATTG GTACCCTGTT TTATCCAAGGGGCTCCTCGT CTTGA |
| Glutamate 5-kinase, putative Q4Q8S0] | |
|---|---|
| Metabolite Information | |
| Molecular Function | glutamate 5-kinase activity |
| Biochemical Pathway | amino acid biosynthesis; proline biosynthesis |
| Regulatory Pathway | |
| KEGG Pathways | K00931 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | pyrroline-5-carboxylate synthetase isoform 1 [Homo sapiens] | 28 | 3e-23 | 105 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| proB gamma-glutamyl kinase | Mycobacterium tuberculosis H37Rv | 36% | 9e-31 | 127 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00701 | Glutamate 5-kinase signature | 207-224; | PS00902 | |
| Acylation | N-myristoylation site | 53-58; 95-100; 212-217; | PS00008 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 111-114; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 43-46; 60-63; 169-172; 195-198; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 7-9; 60-62; 110-112; 126-128; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 62-68; | PS00007 | |
| Sulfation | Tyrosine sulfation site | 167-181; 168-182; | PS00003 | |
| Glutamate 5-kinase, putative [Q4Q8S0] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2akoD | |
| Percent Identity | 49% | |
| Target Region | 9-258 | |
| Template Region | 2-241 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 58-64-0 | ADENOSINE-5'-DIPHOSPHATE | 507.181 | C10 H16 N5 O13 P3 | O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O | 2ako |
| Mutational Information | ||
|---|---|---|
| Residue | Feature | Description |
|
|
|
| Modeled Protein | Template Structure |
|
|
+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/639672/Q4Q8S0.pdb 2.0 250 = residues | | = | | Ramachandran plot: 94.7% core 5.3% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 4 labelled residues (out of 248) = | +| Chi1-chi2 plots: 1 labelled residues (out of 155) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 11.4 Bad contacts: = 0 | *| Bond len/angle: 9.8 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.13 Covalent: -0.20 Overall: = 0.00 | | = | *| M/c bond lengths: 98.9% within limits 1.1% highlighted 1 off = graph | *| M/c bond angles: 93.6% within limits 6.4% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |