| Citrate synthase, putative [Q4QDX2] | |
|---|---|
| Systematic Name | LmjF.18.0670 [Leishmania major] |
| Gene Name | LMJF_18_0670 |
| Molecular Weight | 50477 Da |
| Protein Sequence Size | 454 |
| Function | |
| Charge | 2 |
| Isoelectric Point | 6.7471 pH |
| Description | Citrate synthase, putative (EC 2.3.3.1). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 2.3.3.1 |
| Sequence | >tr|Q4QDX2|Q4QDX2_LEIMA Citrate synthase, putative (EC 2.3.3.1) - Leishmania major. ASSALDEMKEQMLRRWKEDQKKIDDLRKKHGHEKLCDATIDAVYGGMRGITGLVYEPSLL DPAEGIRFRGLTILECQEMLPKAPGGKEPLPEAMFWLLMTGEVPTEEQVRGLNAELHRRA DPEAIAAAQKAIAALPRNAHPMTAFSVGVLALQSYSKFAAAYAAGKSNKKTYWEYALEDS LDMLARTPAVVAMICNRETKGQVELAAPSNSDLDWAANFAKMMGYQDEEFWECMRLYLSV HADHEGGNVSAHTTTLVASALSDPYLAFSAGLNGLAGPLHGLANQEVLNYLLSMQERVKA DGVNMHDEAALEKALSNYTWELLNSGQVVPGYGHAVLRKVDPRYTCLRNFCLRHKFDDDL FKLVNTIYLIMPGILKEHGKTKNPYPNVDAHSGVLLQHYGMTNQNCYPVLFGLSRQMGVL AGVVWDRLQGRPLERPKSITTEMLAKKYLCNSL |
| DNA Sequence | >LmjF18.0670 |||citrate synthase, putative|Leishmania major|chr 18|||Manual ATGGCGTCAT CGGCATTGGA TGAGATGAAG GAGCAGATGC TGAGGCGCTG GAAAGAGGACCAGAAGAAGA TCGACGACCT CAGGAAGAAG CACGGCCATG AGAAGCTGTG CGACGCGACCATCGATGCGG TGTACGGCGG CATGCGCGGC ATCACCGGCC TCGTGTACGA GCCATCACTGCTGGACCCCG CAGAGGGCAT CCGCTTCCGC GGCCTCACGA TCCTGGAGTG CCAGGAGATGCTGCCCAAAG CGCCGGGCGG CAAGGAGCCG CTGCCGGAGG CGATGTTCTG GCTACTGATGACCGGCGAGG TGCCGACGGA GGAGCAGGTA AGGGGCCTGA ACGCGGAGCT GCACCGTCGCGCCGACCCCG AGGCGATTGC CGCGGCGCAG AAGGCGATCG CGGCGCTGCC GAGGAACGCGCACCCGATGA CGGCATTCAG TGTGGGCGTG CTTGCGCTGC AGAGCTACTC GAAGTTTGCTGCGGCTTACG CGGCGGGCAA GTCGAACAAG AAGACGTACT GGGAGTACGC GCTGGAGGACTCGCTGGACA TGCTGGCGCG CACGCCGGCG GTGGTGGCGA TGATCTGCAA CCGCGAGACCAAGGGCCAGG TGGAGTTGGC GGCACCGAGC AACAGCGACC TGGACTGGGC GGCGAACTTTGCGAAAATGA TGGGCTACCA GGACGAGGAG TTCTGGGAGT GCATGCGTCT GTACCTGTCTGTCCACGCCG ACCACGAGGG TGGAAACGTG TCGGCACACA CAACGACACT GGTTGCGTCAGCACTGAGCG ACCCCTACCT CGCCTTCAGC GCTGGCCTGA ACGGTCTTGC TGGCCCGCTGCATGGGCTGG CGAACCAGGA GGTGCTGAAT TACTTGCTCA GCATGCAGGA GCGTGTGAAGGCGGATGGCG TGAACATGCA TGATGAGGCA GCGCTCGAGA AGGCGCTGAG CAACTACACGTGGGAGTTGC TCAACTCCGG CCAGGTGGTG CCCGGCTACG GCCACGCGGT GCTGCGCAAGGTGGACCCGC GCTACACCTG TCTGCGCAAC TTCTGCCTGC GCCACAAATT TGATGACGACCTGTTCAAGC TGGTCAACAC CATCTACTTG ATCATGCCCG GCATCCTGAA GGAGCACGGTAAGACCAAGA ACCCCTACCC CAACGTCGAC GCGCACTCCG GCGTGCTACT GCAGCACTACGGGATGACAA ATCAGAACTG CTACCCGGTG CTGTTCGGCC TGTCGCGCCA GATGGGCGTCTTGGCCGGCG TCGTCTGGGA CCGCCTGCAG GGCCGCCCGC TCGAGCGCCC GAAGTCGATCACGACGGAGA TGCTCGCAAA GAAATACCTG TGCAACTCCT TGTGA |
| Citrate synthase, putative Q4QDX2] | |
|---|---|
| Metabolite Information | |
| Molecular Function | transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer |
| Biochemical Pathway | main pathways of carbohydrate metabolism |
| Regulatory Pathway | |
| KEGG Pathways | K01647 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | citrate synthase precursor, isoform a [Homo sapiens] | 54 | 1e-132 | 468 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| HP0775 penta-phosphate guanosine-3'-pyrophosphohydrolase (spoT) | Helicobacter pylori | 25% | 0.49 | 30 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00017 | ATP/GTP-binding site motif A (P-loop) | 161-168; | PS00017 | |
| PDOC00422 | Citrate synthase signature | 332-344; | PS00480 | |
| PDOC00015 | The rule PS00015 has been deleted from the PROSITE database and replaced by the following motif: PS50079 (Bipartite nuclear localization signal profile | 15-31; | PS00015 | |
| Acylation | N-myristoylation site | 46-51; 247-252; 248-253; 419-424; | PS00008 | |
| Glycosylation | N-glycosylation site | 249-252; 318-321; | PS00001 | |
| Phosphorylation | Casein kinase II phosphorylation site | 4-7; 59-62; 73-76; 172-175; 210-213; 212-215; 294-297; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 168-170; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 339-345; | PS00007 | |
| Sulfation | Tyrosine sulfation site | 169-183; 219-233; | PS00003 | |
| Citrate synthase, putative [Q4QDX2] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 2ctsA | |
| Percent Identity | 55% | |
| Target Region | 1-454 | |
| Template Region | 1-437 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| SER | 251 | Sidechain |
| HIS | 281 | Sidechain |
| HIS | 335 | Sidechain |
| ASP | 390 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 5949-29-1 | CITRIC ACID | 192.124 | C6 H8 O7 | O=C(O)CC(O)(C(=O)O)CC(=O)O | 2cts |
| 31416-98-5 | COENZYME A | 767.534 | C21 H36 N7 O16 P3 S | O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O | 2cts |
| 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/357357/Q4QDX2.pdb 2.0 455 = residues | | = | *| Ramachandran plot: 94.1% core 4.6% allow 1.0% gener 0.3% = disall | | = | +| All Ramachandrans: 9 labelled residues (out of 444) = | +| Chi1-chi2 plots: 1 labelled residues (out of 260) = | | = | | 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: = 7 | *| Bond len/angle: 7.3 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.11 Covalent: -0.15 Overall: = 0.01 | | = | | M/c bond lengths: 99.1% within limits 0.9% highlighted = | | M/c bond angles: 93.6% within limits 6.4% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |