Glutamate dehydrogenase, putative [Q4Q7X1] | |
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Systematic Name | LmjF.28.2910 [Leishmania major] |
Gene Name | LMJF_28_2910 |
Molecular Weight | 49130 Da |
Protein Sequence Size | 452 |
Function | |
Charge | 0.5 |
Isoelectric Point | 6.6607 pH |
Description | Glutamate dehydrogenase, putative (EC 1.4.1.4). |
Subcellular Location | N.A.[Predict] |
E. C. Number | 1.4.1.4 |
Sequence | >tr|Q4Q7X1|Q4Q7X1_LEIMA Glutamate dehydrogenase, putative (EC 1.4.1.4) - Leishmania major ASGCLKYASVDDFIAKCILSRDPYQPEFTQAVREVMTSLWPFLQKNPKYTQDGLLERIVE PERVIQFRVPWVDDKGVTHVNRAFRVQFNSAIGPYKGGMRFHPSVNLSILKFLGFEQTFK NSLTTLPMGGGKGGADFDPKGKSDCEVMRFCQSLVAELYRHIGADTDVPAGDIGVGSREV GYMNGMYWKLRNTNECTFTGKGLAFQGSAIRPEATGYGLVYFVQSMLTHVNDSLEGKTVL VSGSGNVAQYAIEKCMELGAKVITASDSKGYIQDPSGFDKVKLAKLMKLKNECRGTLEEY ARETGVTYVPGKRPWCVKADIALPCATQNEIEGADAKTMLTNGVKLVAEGANMPTTEEAT EIFQKAGVLFAPGKASNAGGVAISGLEMSQNAARLVWDAEEVDSRLRSIMSSIHDSCVQY GEKDGKVSYVDGANIAGFVKVADAMLALGIV |
DNA Sequence | >LmjF28.2910 |||glutamate dehydrogenase, putative|Leishmania major|chr 28|||Manual ATGGCCTCGG GTTGTCTCAA GTATGCGTCT GTGGACGACT TCATCGCGAA GTGCATCTTGTCTCGCGACC CGTATCAGCC TGAATTCACG CAGGCTGTCC GCGAGGTGAT GACGTCGCTGTGGCCGTTCC TGCAGAAGAA CCCCAAGTAC ACTCAGGATG GCCTGCTGGA GCGCATTGTGGAGCCGGAGC GCGTGATTCA GTTCCGTGTC CCTTGGGTGG ATGACAAGGG CGTCACCCACGTCAACCGCG CCTTCCGCGT CCAGTTCAAC TCTGCCATCG GCCCCTACAA GGGAGGCATGCGTTTTCACC CCTCCGTCAA CCTCTCTATC CTCAAGTTCC TTGGCTTCGA GCAGACCTTCAAGAACTCAC TCACGACGCT GCCCATGGGT GGTGGCAAGG GCGGTGCCGA CTTCGACCCGAAGGGCAAGA GCGACTGCGA GGTGATGCGC TTCTGCCAGT CACTCGTGGC GGAGCTCTATCGGCACATCG GCGCCGACAC GGACGTGCCG GCGGGCGACA TCGGCGTCGG TAGTCGCGAGGTGGGCTACA TGAACGGCAT GTACTGGAAG CTGCGGAACA CGAACGAGTG CACCTTTACCGGTAAGGGCC TCGCCTTCCA GGGCAGTGCA ATCCGCCCTG AGGCTACGGG GTACGGCCTCGTGTACTTCG TGCAGTCGAT GCTGACGCAC GTCAACGACT CGCTCGAGGG AAAGACTGTCCTCGTGTCGG GCTCCGGCAA CGTTGCGCAG TACGCGATCG AGAAGTGCAT GGAGCTCGGAGCGAAGGTCA TTACAGCTTC CGACTCAAAG GGCTACATAC AAGACCCGAG CGGCTTCGACAAGGTGAAGT TGGCGAAGCT GATGAAGCTG AAGAACGAGT GCCGTGGGAC GCTGGAGGAATACGCGAGGG AGACGGGCGT CACGTACGTG CCGGGCAAGC GCCCGTGGTG TGTGAAAGCCGATATCGCCC TCCCGTGCGC CACACAGAAC GAGATCGAGG GGGCCGACGC CAAGACGATGTTGACGAACG GCGTGAAGCT GGTCGCCGAG GGTGCCAACA TGCCGACGAC GGAGGAAGCTACGGAGATCT TCCAGAAAGC GGGTGTACTG TTCGCCCCTG GCAAGGCCTC CAACGCCGGTGGCGTGGCCA TCTCCGGGCT TGAGATGTCG CAGAACGCGG CGCGCCTGGT GTGGGACGCCGAGGAGGTCG ACAGCCGCCT GCGCAGCATC ATGTCCAGCA TCCACGACTC GTGCGTGCAGTACGGCGAAA AGGATGGCAA GGTCAGCTAT GTGGACGGCG CAAACATTGC TGGCTTTGTGAAGGTGGCGG ATGCCATGCT GGCTCTCGGC ATCGTCTAG |
Glutamate dehydrogenase, putative Q4Q7X1] | |
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Metabolite Information | |
Molecular Function | oxidoreductase activity |
Biochemical Pathway | amino acid metabolism |
Regulatory Pathway | |
KEGG Pathways | K00262 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | glutamate dehydrogenase 2 [Homo sapiens] | 28 | 3e-33 | 140 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
gatD Galactitol-1-phosphate 5-dehydrogenase (EC 1.1.1.251) | Escherichia coli MG1655 | 38% | 0.034 | 33.9 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00071 | Glu / Leu / Phe / Val dehydrogenases active site | 127-140; | PS00074 | |
Acylation | N-myristoylation site | 130-135; 131-136; 381-386; 386-391; 433-438; | PS00008 | |
Amidation | Amidation site | 311-314; | PS00009 | |
Glycosylation | N-glycosylation site | 107-110; 232-235; | PS00001 | |
Phosphorylation | Casein kinase II phosphorylation site | 10-13; 144-147; 265-268; 277-280; 297-300; 328-331; 356-359; 385-388; 413-416; 429-432; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 119-121; 200-202; | PS00005 | |
Sulfation | Tyrosine sulfation site | 294-308; 414-428; | PS00003 |
Glutamate dehydrogenase, putative [Q4Q7X1] | ||
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Model Information | ||
Template PDB ID | 1hrdC | |
Percent Identity | 56% | |
Target Region | 1-452 | |
Template Region | 1-449 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
LYS | 133 | Sidechain |
ASP | 173 | Sidechain |
Co-Factor | |
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Metal | Description |
Ligands | |||||
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CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
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/77996/Q4Q7X1.pdb 2.0 452 = residues | | = | +| Ramachandran plot: 91.5% core 8.3% allow 0.3% gener 0.0% = disall | | = | +| All Ramachandrans: 12 labelled residues (out of 450) = | +| Chi1-chi2 plots: 1 labelled residues (out of 247) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 3.2 Bad contacts: = 3 | *| Bond len/angle: 8.1 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.15 Covalent: -0.10 Overall: = 0.06 | | = | | M/c bond lengths: 99.3% within limits 0.7% highlighted = | *| M/c bond angles: 95.0% within limits 5.0% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |