Trypanothione reductase [Q4QJG7] | |
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Systematic Name | LmjF.05.0350 [Leishmania major] |
Gene Name | TRYR |
Molecular Weight | 53144 Da |
Protein Sequence Size | 491 |
Function | |
Charge | -3 |
Isoelectric Point | 6.1 pH |
Description | Trypanothione reductase (EC 1.8.1.12). |
Subcellular Location | cytoplasm[Predict] |
E. C. Number | 1.8.1.12 |
Sequence | >tr|Q4QJG7|Q4QJG7_LEIMA Trypanothione reductase (EC 1.8.1.12) - Leishmania major. SRAYDLVVLGAGSGGLEAGWNAAATYKKKVAVVDVQATHGPPFFAALGGTCVNVGCVPKK LMVTGAQYMDLIRESGGFGWEMNRESLCPNWKTLIAAKNKVVNGINESYKSMFADTEGLS FHMGFGALQDAHTVLVRKSEDPNSDVLETLDTEYILIATGSWPTRLGVPGDEFCITSNEA FYLEDAPKRMLCVGGGYIAVEFAGIFNGYKPRGGYVDLCYRGDLILRGFDTEVRKSLTKQ LGANGIRVRTNLNPTKITKNEDGSNHVHFNDGTEEDYDQVMLAIGRVPRSQTLQLDKAGV QTAKNGAVQVDAYSKTSVDNIYAIGDVTNRVMLTPVAINEGAAFAETVFGGKPRATDHTK VACAVFSIPPIGTCGMTEEEAAKNHETVAVYESCFTPLMHNISGSKHKEFMIRIITDQPS GEVLGVHMLGDSAPEIIQSVGICMKMGAKISDFHNTIGVHPTSAEELCSMRTPAYFYENG KRVEKLSSNL |
DNA Sequence | >LmjF05.0350 |TRYR||trypanothione reductase|Leishmania major|chr 5|||Manual ATGTCCCGCG CGTACGACCT CGTGGTGCTT GGCGCCGGAT CTGGAGGTCT GGAGGCGGGATGGAACGCGG CCGCCACGTA CAAGAAGAAG GTGGCCGTCG TCGATGTGCA GGCGACGCACGGTCCGCCGT TTTTCGCCGC GCTCGGCGGC ACGTGCGTGA ACGTCGGCTG CGTCCCTAAGAAACTCATGG TGACAGGTGC CCAGTACATG GACCTGATCC GCGAGTCTGG CGGCTTCGGATGGGAGATGA ACCGCGAATC GCTCTGCCCC AATTGGAAGA CGCTCATCGC CGCGAAGAACAAGGTGGTGA ACGGCATCAA CGAGAGCTAC AAGAGCATGT TTGCTGATAC GGAGGGCCTCAGCTTTCACA TGGGCTTCGG CGCCCTTCAG GACGCTCACA CGGTGCTGGT GCGCAAGTCGGAAGACCCAA ACAGCGACGT GCTGGAGACC CTCGACACGG AGTACATCCT CATTGCTACCGGCTCCTGGC CGACGCGCCT TGGAGTCCCC GGCGATGAGT TCTGCATCAC GAGCAACGAGGCCTTCTACC TCGAAGATGC CCCCAAGCGG ATGCTGTGCG TCGGCGGCGG CTACATCGCCGTCGAGTTTG CCGGCATCTT CAACGGCTAC AAGCCCCGCG GTGGTTATGT AGACCTGTGCTACCGCGGCG ATCTTATTTT GCGCGGCTTC GACACAGAGG TGCGCAAGAG CCTGACTAAGCAGCTGGGGG CGAACGGCAT ACGAGTGCGC ACCAACTTGA ACCCGACAAA AATTACGAAGAACGAGGACG GCTCGAATCA CGTTCACTTC AACGATGGCA CGGAGGAGGA CTACGATCAGGTCATGCTCG CGATCGGTCG CGTGCCGCGC TCGCAGACGC TGCAGCTCGA CAAGGCCGGCGTTCAAACAG CAAAGAACGG CGCCGTGCAG GTCGACGCGT ACTCGAAGAC TTCGGTGGACAACATCTACG CCATCGGTGA CGTGACGAAC CGCGTGATGT TGACGCCGGT GGCCATCAACGAAGGCGCCG CCTTCGCCGA AACCGTCTTC GGCGGCAAGC CTCGCGCCAC CGACCACACGAAGGTCGCGT GCGCCGTGTT CTCCATACCG CCGATCGGCA CGTGCGGCAT GACGGAGGAGGAGGCGGCGA AGAACCACGA AACTGTCGCC GTGTACGAGA GCTGCTTCAC GCCCCTTATGCACAACATCA GCGGCAGCAA GCACAAGGAA TTTATGATCC GCATCATCAC GGACCAACCCAGCGGCGAGG TGCTGGGCGT TCACATGCTC GGCGACAGTG CGCCTGAGAT CATCCAGAGCGTCGGCATTT GCATGAAGAT GGGCGCCAAG ATCAGTGACT TCCACAACAC CATCGGAGTCCACCCGACAA GCGCCGAGGA GCTCTGCTCC ATGCGCACTC CGGCGTACTT CTACGAAAATGGCAAGCGCG TCGAAAAGCT GAGCAGCAAC CTCTGA |
Trypanothione reductase Q4QJG7] | |
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Metabolite Information | |
Molecular Function | disulfide oxidoreductase activity; oxidoreductase activity; trypanothione-disulfide reductase activity |
Biochemical Pathway | electron transport; regulation of cell redox homeostasis |
Regulatory Pathway | |
KEGG Pathways | K00383 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | glutathione reductase [Homo sapiens] | 33 | 2e-64 | 243 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
gor Glutathione reductase (EC 1.6.4.2) | Escherichia coli MG1655 | 35% | 1e-76 | 281 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00016 | Cell attachment sequence | 222-224; | PS00016 | |
PDOC00073 | Pyridine nucleotide-disulphide oxidoreductases class-I active site | 49-59; | PS00076 | |
Acylation | N-myristoylation site | 11-16; 15-20; 16-21; 50-55; 105-110; 161-166; 196-201; 205-210; 300-305; 342-347; 448-453; 459-464; | PS00008 | |
Amidation | Amidation site | 480-483; | PS00009 | |
Glycosylation | N-glycosylation site | 107-110; 402-405; | PS00001 | |
Phosphorylation | Casein kinase II phosphorylation site | 177-180; 259-262; 274-277; 317-320; 378-381; 433-436; 463-466; 464-467; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 26-28; 109-111; 303-305; 329-331; 470-472; | PS00005 | |
Phosphorylation | Tyrosine kinase phosphorylation site | 316-323; | PS00007 | |
Sulfation | Tyrosine sulfation site | 176-190; 271-285; | PS00003 |
Trypanothione reductase [Q4QJG7] | ||
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Model Information | ||
Template PDB ID | 1fecB | |
Percent Identity | 77% | |
Target Region | 1-491 | |
Template Region | 2-485 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
CYS | 52 | Unknown |
CYS | 57 | Unknown |
LYS | 60 | Unknown |
TYR | 198 | Unknown |
GLU | 202 | Unknown |
Co-Factor | |
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Metal | Description |
FAD | Binds 1 FAD per subunit |
Ligands | |||||
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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 | 1fec |
Mutational Information | ||
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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/1010958/Q4QJG7.pdb 2.0 491 = residues | | = | *| Ramachandran plot: 92.8% core 6.9% allow 0.0% gener 0.2% = disall | | = | +| All Ramachandrans: 8 labelled residues (out of 489) = | +| Chi1-chi2 plots: 2 labelled residues (out of 267) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 5.1 Bad contacts: = 2 | *| Bond len/angle: 10.0 Morris et al class: 1 = 1 2 | +| 3 cis-peptides = | | G-factors Dihedrals: 0.10 Covalent: -0.13 Overall: = 0.02 | | = | | M/c bond lengths: 99.5% within limits 0.5% highlighted = | *| M/c bond angles: 94.5% within limits 5.5% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |