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Trypanothione reductase [Q4QJG7]
Systematic NameLmjF.05.0350 [Leishmania major]
Gene NameTRYR
Molecular Weight53144 Da
Protein Sequence Size491
Function
Charge-3
Isoelectric Point6.1 pH
DescriptionTrypanothione reductase (EC 1.8.1.12).
Subcellular Locationcytoplasm[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]
Metabolite Information
Molecular Functiondisulfide oxidoreductase activity; oxidoreductase activity; trypanothione-disulfide reductase activity
Biochemical Pathwayelectron transport; regulation of cell redox homeostasis
Regulatory Pathway
KEGG PathwaysK00383
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensglutathione reductase [Homo sapiens]332e-64243
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
gor Glutathione reductase (EC 1.6.4.2)Escherichia coli MG165535%1e-76281
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00016Cell attachment sequence222-224; PS00016
PDOC00073Pyridine nucleotide-disulphide oxidoreductases class-I active site49-59; PS00076
AcylationN-myristoylation site11-16; 15-20; 16-21; 50-55; 105-110; 161-166; 196-201; 205-210; 300-305; 342-347; 448-453; 459-464; PS00008
AmidationAmidation site480-483; PS00009
GlycosylationN-glycosylation site107-110; 402-405; PS00001
PhosphorylationCasein kinase II phosphorylation site177-180; 259-262; 274-277; 317-320; 378-381; 433-436; 463-466; 464-467; PS00006
PhosphorylationProtein kinase C phosphorylation site26-28; 109-111; 303-305; 329-331; 470-472; PS00005
PhosphorylationTyrosine kinase phosphorylation site316-323; PS00007
SulfationTyrosine sulfation site176-190; 271-285; PS00003
Trypanothione reductase [Q4QJG7]
Model Information
Template PDB ID1fecB
Percent Identity77%
Target Region1-491
Template Region2-485
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
CYS52Unknown
CYS57Unknown
LYS60Unknown
TYR198Unknown
GLU202Unknown
Co-Factor
Metal Description
FADBinds 1 FAD per subunit
Ligands
CAS number Name Mol. Weight Mol. Formula Smile Notation PDB Reference
16426-55-4FLAVIN-ADENINE DINUCLEOTIDE785.55C27 H33 N9 O15 P2O=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)C1fec
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/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.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database