| Dihydrolipoamide dehydrogenase, putative [Q4Q4U1] | |
|---|---|
| Systematic Name | LmjF.32.3310 [Leishmania major] |
| Gene Name | GCVL-2 |
| Molecular Weight | 50578 Da |
| Protein Sequence Size | 476 |
| Function | |
| Charge | 3 |
| Isoelectric Point | 6.8681 pH |
| Description | Dihydrolipoamide dehydrogenase, putative (EC 1.8.1.4). |
| Subcellular Location | cytoplasm[Predict] |
| E. C. Number | 1.8.1.4 |
| Sequence | >tr|Q4Q4U1|Q4Q4U1_LEIMA Dihydrolipoamide dehydrogenase, putative (EC 1.8.1.4) - Leishmania major. FRRNIAHLASYDVTVIGGGPGGYVAAIKAAQLGLKTACIEKRGALGGTCLNVGCIPSKAL LHATHLYHDAHANFAQYGLRGGENVTMDVSAMQAQKGKGVKALTGGVEYLFKKNKVTYYK GEGSFVNPNTIKVKGLDGKEETLESKKTIVATGSEPTELPFLPFDEKVVMSSTGALDLDH VPKKMIVVGGGVIGLELGSVWARLGAEVTVVEFASRCAATTDADVSKALTDALVKHEKMK IMTNTKVVSGTNNGSSVTIEVEDKDGKHQTLEADALLCSVGRRPHTTGLNAEAINLQMER GFICINDHFETNVPNVYAIGDVVNKGPMLAHKAEEEGVACAEILAGKPGHVNYSVIPGVI YTNPEVAQVGETEEQVKKRGIDYKVGKFPFSANSRAKAVGTEDGFVKVVTDKKTDRILGV QIVCTAAGEMIAEPTLAMEYGASSEDLGRTCHAHPTMSEAVKEACMACFAQTINF |
| DNA Sequence | >LmjF32.3310 |||dihydrolipoamide dehydrogenase, putative|Leishmania major|chr 32|||Manual ATGTTCCGCA GGAACATAGC GCACCTGGCG TCCTACGACG TGACGGTGAT CGGCGGTGGTCCTGGCGGGT ACGTGGCGGC CATCAAGGCC GCCCAGCTTG GCCTCAAGAC CGCCTGCATCGAGAAGCGCG GTGCTCTTGG CGGCACCTGC CTGAATGTCG GCTGCATCCC GTCAAAGGCGCTGCTGCACG CGACGCACCT GTACCACGAC GCCCACGCCA ACTTTGCCCA GTATGGCCTGCGCGGCGGGG AAAACGTGAC GATGGATGTG TCTGCGATGC AGGCGCAGAA GGGGAAGGGGGTGAAGGCGC TGACGGGCGG CGTCGAGTAC CTCTTCAAGA AGAACAAGGT CACATACTACAAGGGCGAGG GCAGCTTCGT GAACCCCAAC ACGATCAAGG TGAAGGGTCT TGACGGCAAGGAGGAGACGC TCGAGTCGAA GAAGACGATT GTGGCCACTG GCAGCGAGCC GACGGAGCTGCCGTTCCTGC CCTTCGACGA GAAGGTTGTG ATGTCCTCCA CCGGCGCCCT CGACCTCGACCACGTGCCCA AGAAGATGAT CGTGGTTGGC GGAGGCGTGA TTGGGCTGGA GCTTGGTAGCGTGTGGGCCC GCCTCGGTGC TGAGGTGACC GTGGTGGAGT TTGCCTCTCG CTGCGCCGCCACCACCGACG CCGACGTGTC CAAGGCGCTC ACGGATGCGC TGGTGAAGCA CGAGAAGATGAAAATCATGA CCAACACGAA GGTCGTTAGC GGGACGAACA ACGGTAGCAG CGTGACGATCGAGGTGGAGG ACAAGGATGG AAAGCATCAG ACGCTCGAGG CGGACGCGCT GCTGTGCTCCGTGGGCCGCC GCCCGCACAC GACCGGGCTG AACGCCGAGG CCATCAACCT CCAAATGGAGCGCGGTTTTA TCTGCATCAA CGACCACTTC GAGACGAACG TGCCGAACGT ATACGCGATCGGCGACGTCG TGAACAAGGG CCCGATGCTA GCGCACAAGG CCGAGGAGGA AGGCGTCGCGTGCGCGGAGA TACTGGCTGG CAAGCCCGGG CACGTGAACT ACAGCGTCAT CCCCGGCGTCATCTACACCA ACCCCGAGGT CGCGCAGGTG GGCGAGACGG AAGAGCAGGT GAAGAAGAGGGGCATCGACT ACAAGGTTGG CAAGTTCCCC TTCAGCGCCA ACTCGCGCGC CAAGGCCGTCGGCACCGAGG ACGGCTTTGT GAAGGTGGTG ACGGACAAGA AGACGGACCG CATCCTTGGCGTGCAGATTG TGTGCACGGC TGCTGGCGAG ATGATCGCGG AGCCGACGCT GGCGATGGAGTACGGCGCAA GCTCCGAGGA TTTGGGCCGC ACCTGCCACG CTCACCCAAC GATGTCCGAGGCGGTGAAGG AGGCGTGCAT GGCGTGCTTT GCGCAGACGA TCAACTTCTA A |
| Dihydrolipoamide dehydrogenase, putative Q4Q4U1] | |
|---|---|
| Metabolite Information | electron transport; regulation of cell redox homeostasis |
| Molecular Function | |
| Biochemical Pathway | |
| Regulatory Pathway | |
| KEGG Pathways | K00382 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | dihydrolipoamide dehydrogenase precursor [Homo sapiens] | 51 | 1e-127 | 452 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| lpdA dihydrolipoamide-dehydrogenase | Salmonella typhimurium | 40% | 2e-92 | 333 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00595 | Formate--tetrahydrofolate ligase signatures | 85-88; 254-257; 353-356; | PS00722 | |
| PDOC00073 | Pyridine nucleotide-disulphide oxidoreductases class-I active site | 47-57; | PS00076 | |
| Acylation | N-myristoylation site | 18-23; 19-24; 22-27; 34-39; 44-49; 48-53; 54-59; 79-84; 154-159; 191-196; 195-200; 199-204; 206-211; 251-256; 255-260; 338-343; 359-364; 401-406; | PS00008 | |
| Amidation | Amidation site | 281-284; | PS00009 | |
| Phosphorylation | Casein kinase II phosphorylation site | 153-156; 210-213; 222-225; 363-366; 444-447; 457-460; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 131-133; 146-148; 411-413; 415-417; | PS00005 | |
| Dihydrolipoamide dehydrogenase, putative [Q4Q4U1] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1dxlD | |
| Percent Identity | 56% | |
| Target Region | 1-476 | |
| Template Region | 4-467 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| CYS | 50 | Unknown |
| CYS | 55 | Unknown |
| HIS | 455 | Unknown |
| GLU | 460 | Unknown |
| Co-Factor | |
|---|---|
| Metal | Description |
| FAD | Binds 1 FAD per subunit |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 16426-55-4 | FLAVIN-ADENINE DINUCLEOTIDE | 785.55 | C27 H33 N9 O15 P2 | O=C2C3=Nc1cc(c(cc1N(C3=NC(=O)N2)CC(O)C(O)C(O)COP(=O)(O)OP(=O)(O)OCC6OC(n5cnc4c(ncnc45)N)C(O)C6O)C)C | 1dxl |
| Mutational Information | ||
|---|---|---|
| Residue | Feature | Description |
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| Modeled Protein | Template Structure |
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+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/2319360/Q4Q4U1.pdb 2.0 476 = residues | | = | *| Ramachandran plot: 89.0% core 9.6% allow 1.0% gener 0.5% = disall | | = | *| All Ramachandrans: 17 labelled residues (out of 474) = | +| Chi1-chi2 plots: 5 labelled residues (out of 240) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.1 Bad contacts: = 11 | *| Bond len/angle: 8.1 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: -0.07 Covalent: -0.28 Overall: = -0.14 | | = | | M/c bond lengths: 99.0% within limits 1.0% highlighted = | *| M/c bond angles: 91.0% within limits 9.0% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |