| Aspartate carbamoyltransferase, putative [Q4QEW6] | |
|---|---|
| Systematic Name | LmjF.16.0540 [Leishmania major] |
| Gene Name | LMJF_16_0540 |
| Molecular Weight | 35340 Da |
| Protein Sequence Size | 327 |
| Function | |
| Charge | 1 |
| Isoelectric Point | 6.6 pH |
| Description | Aspartate carbamoyltransferase, putative (EC 2.1.3.2). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 2.1.3.2 |
| Sequence | >tr|Q4QEW6|Q4QEW6_LEIMA Aspartate carbamoyltransferase, putative (EC 2.1.3.2) - Leishmania major. PTFNPVASLKGQSVASAAQFSRADIDALIQLALDMKTHIEAGKTIDTLRGRVMTPLFFED SSRTLSSFCAAMMRLGGSVVNFKVETSSVNKGETLQDTIRTLDSYSDVLVLRHAKEEALE QAMSVATHPIMNAGNGAGEHPTQALLDILTIHAELGAVDGIAIALIGDLKKGRTVHSLLK LLAHNFALRKVYLIAPAGLEMPAEVLEHVATDVVKRGIAIQQASGLTPEIVADCDVLYAT RLQKERFVASAAGDADALTAFEASKASLLIDKARLAHAKAKMVVMHPLPRVDELSTDIDD DPRAAYFRQMRYGLFMRMAILFSVLS |
| DNA Sequence | >LmjF16.0540 |||aspartate carbamoyltransferase, putative|Leishmania major|chr 16|||Manual ATGCCCACCT TCAACCCGGT CGCCTCCCTC AAGGGCCAGA GTGTGGCCTC CGCTGCGCAGTTCTCGCGCG CTGACATCGA CGCCCTCATC CAGCTCGCAC TCGATATGAA GACACACATCGAGGCAGGGA AAACGATCGA CACCCTGCGC GGCCGCGTCA TGACGCCGCT GTTCTTCGAGGACAGCTCTC GCACGCTGTC GAGTTTTTGC GCGGCCATGA TGCGGCTGGG CGGCAGCGTCGTGAACTTCA AGGTGGAGAC GTCGTCTGTG AACAAGGGTG AAACGCTGCA GGACACCATTCGCACGCTGG ACTCGTACAG TGACGTGCTC GTGCTCCGCC ACGCTAAGGA GGAAGCGCTGGAGCAGGCGA TGAGTGTGGC AACGCACCCG ATCATGAACG CCGGCAACGG CGCTGGTGAGCACCCGACTC AGGCGTTGCT CGACATCCTC ACGATTCACG CCGAGCTCGG CGCCGTGGACGGCATTGCGA TCGCGTTGAT CGGGGACCTC AAGAAGGGCC GCACGGTGCA TTCGCTGCTGAAGCTGCTGG CGCACAACTT CGCGCTGAGG AAGGTGTACC TCATCGCCCC CGCGGGGCTGGAGATGCCGG CGGAGGTGCT GGAGCATGTC GCGACGGACG TGGTGAAGCG CGGGATCGCGATTCAGCAGG CGTCCGGCCT CACTCCTGAG ATTGTGGCCG ACTGCGACGT GCTCTACGCGACGCGCCTGC AGAAGGAGCG CTTTGTTGCC TCCGCTGCCG GTGACGCCGA CGCCCTGACCGCCTTTGAGG CTTCTAAAGC GAGCCTGCTG ATCGACAAGG CTCGCCTGGC ACACGCGAAGGCGAAGATGG TTGTCATGCA CCCGCTGCCT CGCGTGGATG AGCTCAGCAC CGACATTGACGACGACCCGC GTGCGGCGTA TTTCCGACAG ATGCGCTACG GCCTCTTCAT GCGCATGGCTATCCTCTTCA GCGTGCTTTC TTGA |
| Aspartate carbamoyltransferase, putative Q4QEW6] | |
|---|---|
| Metabolite Information | |
| Molecular Function | amino acid binding; aspartate carbamoyltransferase activity; carboxyl- and carbamoyltransferase activity |
| Biochemical Pathway | de novo' pyrimidine base biosynthesis; amino acid metabolism |
| Regulatory Pathway | |
| KEGG Pathways | K00609 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | carbamoylphosphate synthetase 2/aspartate transcarbamylase/dihydroorotase [Homo sapiens] | 45 | 3e-69 | 259 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| pyrB aspartate carbamoyltransferase catalytic subunit | Mycobacterium tuberculosis H37Rv | 33% | 1e-28 | 121 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| Acylation | N-myristoylation site | 12-17; 78-83; 135-140; 157-162; 161-166; | PS00008 | |
| Phosphorylation | Casein kinase II phosphorylation site | 22-25; 38-41; 95-98; 105-108; 260-263; 297-300; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 9-11; 48-50; 62-64; 99-101; | PS00005 | |
| Aspartate carbamoyltransferase, putative [Q4QEW6] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1ml4A | |
| Percent Identity | 41% | |
| Target Region | 9-328 | |
| Template Region | 2-307 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| ARG | 56 | Sidechain |
| THR | 57 | Sidechain |
| ARG | 105 | Sidechain |
| HIS | 133 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 60342-56-5 | N-(PHOSPHONACETYL)-L-ASPARTIC ACID | 255.119 | C6 H10 N O8 P | O=C(NC(C(=O)O)CC(=O)O)CP(=O)(O)O | 1ml4 |
| 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/507909/Q4QEW6.pdb 2.0 319 = residues | | = | *| Ramachandran plot: 90.0% core 9.3% allow 0.0% gener 0.7% = disall | | = | *| All Ramachandrans: 11 labelled residues (out of 317) = | +| Chi1-chi2 plots: 3 labelled residues (out of 179) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.0 Bad contacts: = 3 | *| Bond len/angle: 6.8 Morris et al class: 1 = 1 2 | +| 1 cis-peptides = | | G-factors Dihedrals: 0.02 Covalent: -0.12 Overall: = -0.03 | | = | | M/c bond lengths: 99.6% within limits 0.4% highlighted = | | M/c bond angles: 93.9% within limits 6.1% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |