| Acyl-coenzyme a dehydrogenase, putative [Q4QIY9] | |
|---|---|
| Systematic Name | LmjF.06.0880 [Leishmania major] |
| Gene Name | LMJF_06_0880 |
| Molecular Weight | 45296 Da |
| Protein Sequence Size | 416 |
| Function | |
| Charge | 4 |
| Isoelectric Point | 7.9105 pH |
| Description | Acyl-coenzyme a dehydrogenase, putative (EC 1.3.99.3). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 1.3.99.3 |
| Sequence | >tr|Q4QIY9|Q4QIY9_LEIMA Acyl-coenzyme a dehydrogenase, putative (EC 1.3.99.3) - Leishmania major. RTTLKGMMTRCTAPLRNAKSADLGTFFGASMPAAQSAAGFSFGLTEQQLQYQETARNFAK EKMIPVAAEYDRSMKYPHDVYKQAWELGLTNMHIPTKYGGLGASVMDGLVVQEELAYACS GMATAFEGNSLAEAPLLIAGTDVQNAKYLSRMVEEPLLAAYCVTEPTGGSDVAGMKTVAK KEGDKWVINGSKMWITNGGVANWYFVLARSEGGFTGFIVDADTPGVSLGQKEVMLGQRCS DTRSIMFENVVVPEENVVGEVGKGFQVAMRVFDFTRSAVAISAVGLARRATDEATKYARE RVTMGKPIAQHQAVAFMLAEMAAGVEACRLMTYRAGWETDQGRRNTYYASCAKMMASNLA EKCSTNAVQIFGGNGYNTGYPVEKLYRDCKIFSIYEGTTQIQHAIIGRYVTGMRC |
| DNA Sequence | >LmjF06.0880 |||acyl-coenzyme a dehydrogenase, putative|Leishmania major|chr 6|||Manual ATGCGCACCA CTTTGAAAGG GATGATGACG CGGTGCACGG CGCCGCTGCG CAATGCCAAGTCGGCGGACT TGGGCACGTT CTTCGGCGCC TCGATGCCCG CAGCCCAGTC CGCGGCCGGGTTTTCGTTCG GTCTCACGGA ACAGCAGCTG CAGTACCAGG AGACGGCGCG CAACTTCGCCAAGGAGAAGA TGATCCCTGT CGCGGCGGAG TACGACAGGT CGATGAAATA CCCCCACGATGTGTACAAGC AGGCGTGGGA GCTTGGCTTG ACTAACATGC ACATCCCTAC AAAGTACGGCGGCCTCGGTG CGAGTGTCAT GGACGGCTTG GTGGTGCAGG AGGAGCTCGC CTACGCGTGCTCGGGCATGG CGACTGCGTT CGAGGGCAAC AGCCTCGCCG AAGCGCCGCT CCTCATCGCCGGCACGGACG TGCAGAACGC TAAGTACCTC AGCCGCATGG TCGAAGAGCC GCTGCTGGCTGCGTACTGCG TGACGGAGCC GACGGGTGGG TCGGACGTGG CTGGCATGAA GACGGTTGCGAAGAAGGAGG GCGACAAGTG GGTCATCAAC GGCTCCAAGA TGTGGATCAC GAACGGCGGCGTGGCGAACT GGTACTTCGT GTTGGCGCGC AGCGAGGGTG GTTTCACTGG CTTCATCGTGGACGCCGACA CGCCTGGCGT GTCGCTCGGG CAGAAAGAAG TGATGCTTGG CCAGCGGTGCAGCGACACGC GCAGCATTAT GTTCGAGAAC GTGGTGGTGC CGGAGGAGAA CGTCGTGGGCGAGGTAGGCA AGGGCTTCCA GGTGGCCATG AGGGTGTTTG ACTTTACTCG TTCTGCGGTCGCCATCAGCG CTGTCGGGCT GGCCCGCCGC GCCACGGACG AGGCGACGAA GTACGCCCGCGAGCGCGTGA CAATGGGCAA GCCGATCGCG CAGCATCAGG CCGTCGCGTT CATGTTGGCAGAGATGGCGG CTGGCGTAGA GGCGTGCCGG CTCATGACGT ACCGCGCTGG CTGGGAAACGGATCAAGGAC GCCGCAATAC GTACTACGCT TCATGCGCCA AGATGATGGC GTCCAACCTTGCCGAGAAGT GCTCGACGAA CGCGGTGCAG ATCTTCGGGG GCAACGGCTA CAACACAGGCTACCCGGTGG AGAAGCTCTA CCGTGACTGC AAGATCTTCT CGATCTACGA GGGCACGACGCAGATCCAGC ACGCAATCAT CGGTCGTTAC GTGACGGGCA TGCGCTGCTG A |
| Acyl-coenzyme a dehydrogenase, putative Q4QIY9] | |
|---|---|
| Metabolite Information | |
| Molecular Function | acyl-CoA dehydrogenase activity; oxidoreductase activity |
| Biochemical Pathway | electron transport |
| Regulatory Pathway | |
| KEGG Pathways | K00249 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain [Homo sapiens] | 59 | 1e-128 | 454 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| fadE19 POSSIBLE ACYL-CoA DEHYDROGENASE FADE19 (MMGC) | Mycobacterium tuberculosis H37Rv | 32% | 1e-52 | 201 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00070 | Acyl-CoA dehydrogenases signatures | 163-175; | PS00072 | |
| Acylation | N-myristoylation site | 25-30; 100-105; 101-106; 122-127; 129-134; 170-175; 199-204; 213-218; 226-231; 237-242; 325-330; 374-379; | PS00008 | |
| Amidation | Amidation site | 342-345; | PS00009 | |
| Glycosylation | N-glycosylation site | 190-193; | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 289-292; 344-347; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 105-108; 125-128; 131-134; 394-397; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 4-6; 55-57; 74-76; 333-335; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 290-298; | PS00007 | |
| Acyl-coenzyme a dehydrogenase, putative [Q4QIY9] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1udyD | |
| Percent Identity | 58% | |
| Target Region | 40-425 | |
| Template Region | 11-385 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| THR | 237 | Sidechain |
| GLU | 358 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 3-THIAOCTANOYL-COENZYME A | 911.769 | C28 H48 N7 O17 P3 S2 | O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)CSCCCCC | 1udy | |
| 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 | 1udy |
| 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/4775512/Q4QIY9.pdb 2.0 377 = residues | | = | *| Ramachandran plot: 94.5% core 4.9% allow 0.3% gener 0.3% = disall | | = | +| All Ramachandrans: 5 labelled residues (out of 375) = | +| Chi1-chi2 plots: 4 labelled residues (out of 203) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.7 Bad contacts: = 1 | *| Bond len/angle: 9.8 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.12 Covalent: -0.13 Overall: = 0.03 | | = | | M/c bond lengths: 99.6% within limits 0.4% 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. |