C-1-tetrahydrofolate synthase, cytoplasmic, putative [Q4Q735] | |
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Systematic Name | LmjF.30.2600 [Leishmania major] |
Gene Name | FTHS |
Molecular Weight | 66569 Da |
Protein Sequence Size | 622 |
Function | |
Charge | 2 |
Isoelectric Point | 6.7 pH |
Description | C-1-tetrahydrofolate synthase, cytoplasmic, putative (EC 6.3.4.3) (EC 1.5.1.5) (EC 3.5.4.9). |
Subcellular Location | N.A.[Predict] |
E. C. Number | 1.5.1.5; 3.5.4.9; 6.3.4.3 |
Sequence | >tr|Q4Q735|Q4Q735_LEIMA C-1-tetrahydrofolate synthase, cytoplasmic, putative (EC 6.3.4.3) (EC 1.5.1.5) (EC 3.5.4.9) - Leishmania ATRKLHCVWPVPADIDIAQSVDAQPITSIAEAAGILLSELSPYGSTRAKVKLSVLKRLEG CPNGKYVVVAGMNPTPLGEGKSTTTIGLAQALGAHLHRRCFACIRQPSQGPTFGIKGGAA GGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQDDAALYRRLTDELKT FTPIMQKRLDKLGIRKTDPKSLTEEERVCFARLDVDPGTISWRRVTDVNDRFLRDIEIGM GKAEKGISRRTGFDISVASEVMAILALVDDLADMRQRLGAIQVAKSKTGASVTAEDVGCA GAMAVLMKDAVEPTLMQTLEGTPVLVHAGPFGNIAHGNSSVVADRIALKLAGADGFVLTE AGFGADMGCEKFFNIKCRTSGLKPDAAVLVATVRALKYHGGVEPKDAAKENADALRAGLS NLVRHIQNIRKFGVPVVVALNRFSTDTEAELALVKELATQEGDAADVVVTDHWSKGGAGA VGLAQALIRVTETAPSNFQLLYPSNASLKEKIETVCREIYGAAGVEYLNDTEEKLADFEK MGYGDFPVCMAKTQYSFSHNPELRGAPTGFTVPIRDVRVNCGAKFVFPLLGDISTMPGLP TRPAYYNIDIDCETGRIVGLS |
DNA Sequence | >LmjF30.2600 |||c-1-tetrahydrofolate synthase, cytoplasmic, putative|Leishmania major|chr 30|||Manual ATGGCCACCC GGAAGCTGCA CTGCGTGTGG CCGGTGCCGG CTGACATCGA CATTGCCCAAAGTGTCGATG CCCAGCCGAT CACGAGTATC GCCGAGGCCG CGGGTATACT TCTTTCGGAGCTGAGCCCGT ATGGCAGCAC CCGCGCCAAG GTGAAGCTGA GCGTTCTGAA GCGTTTGGAGGGCTGTCCAA ACGGCAAGTA CGTCGTGGTG GCGGGCATGA ACCCCACCCC GTTGGGGGAAGGGAAGAGCA CCACGACGAT CGGCCTCGCC CAGGCTCTCG GTGCTCATCT ACACCGACGCTGCTTTGCGT GCATTCGCCA ACCGTCTCAA GGACCGACCT TCGGTATCAA GGGTGGTGCCGCGGGAGGCG GCTACAGCCA GGTGATTCCA ATGGAAGATT TTAACCTCCA CGGCACCGGCGACATACATG CCATCACCGC AGCGAACAAC CTCCTTGCCG CGGCGCTTGA CACCCGCATCTTCCACGAGC GGACGCAGGA CGACGCCGCG CTTTACCGCC GTCTCACCGA CGAGCTGAAAACGTTCACAC CGATTATGCA GAAGCGGCTC GATAAGCTCG GCATCCGCAA AACAGACCCCAAGTCGCTGA CGGAGGAGGA GCGCGTCTGC TTTGCGCGGC TGGACGTCGA CCCTGGCACCATTTCCTGGC GCCGCGTCAC CGATGTCAAC GACCGTTTCC TGCGCGACAT CGAGATCGGGATGGGCAAGG CGGAGAAGGG CATCAGCCGG CGCACCGGCT TCGACATTTC GGTCGCGTCCGAGGTGATGG CCATTCTGGC GCTCGTGGAC GATTTGGCCG ACATGCGCCA GCGCCTGGGAGCGATCCAGG TGGCCAAAAG CAAGACGGGC GCATCGGTGA CGGCTGAGGA TGTGGGCTGTGCCGGGGCCA TGGCGGTGCT GATGAAGGAT GCGGTCGAGC CGACGCTGAT GCAGACGCTGGAGGGCACCC CCGTGCTGGT GCATGCCGGC CCCTTCGGCA ATATTGCGCA CGGGAACAGCAGCGTCGTCG CCGACCGCAT CGCCCTCAAG CTGGCCGGTG CGGACGGCTT TGTGCTGACGGAGGCCGGCT TCGGTGCAGA TATGGGCTGC GAGAAGTTCT TCAACATCAA GTGCCGCACGAGCGGGCTGA AGCCGGATGC GGCGGTGCTC GTGGCGACGG TGCGCGCACT GAAGTACCACGGCGGTGTGG AGCCAAAGGA TGCTGCCAAG GAGAACGCGG ATGCCTTGCG TGCCGGCCTGAGCAACCTTG TTCGGCATAT TCAGAACATT CGCAAGTTTG GGGTGCCAGT GGTGGTGGCGCTGAACCGGT TCAGCACCGA CACGGAGGCG GAGCTGGCGC TGGTGAAGGA GCTGGCGACGCAGGAGGGTG ACGCGGCGGA TGTTGTGGTC ACAGATCACT GGTCCAAGGG CGGTGCTGGGGCCGTCGGTC TTGCCCAGGC GCTCATCCGC GTCACGGAGA CGGCGCCATC GAACTTCCAGCTGCTTTACC CAAGCAACGC GTCGCTCAAG GAGAAGATCG AGACGGTGTG CCGCGAGATTTACGGTGCCG CTGGCGTGGA GTATCTCAAC GACACAGAGG AGAAGCTGGC GGACTTCGAGAAGATGGGCT ACGGCGACTT TCCTGTATGC ATGGCAAAGA CACAGTACAG CTTCTCGCACAACCCCGAGC TGCGTGGGGC GCCGACCGGC TTCACTGTCC CCATCCGCGA CGTCCGCGTCAACTGCGGCG CAAAGTTCGT GTTTCCTCTG CTGGGCGACA TCTCCACGAT GCCTGGTCTGCCGACTCGAC CGGCGTACTA CAATATCGAC ATCGACTGCG AGACGGGAAG GATTGTGGGTCTTTCGTAA |
C-1-tetrahydrofolate synthase, cytoplasmic, putative Q4Q735] | |
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Metabolite Information | |
Molecular Function | ATP binding; formate-tetrahydrofolate ligase activity |
Biochemical Pathway | folic acid and derivative biosynthesis |
Regulatory Pathway | |
KEGG Pathways | K01938 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | methylenetetrahydrofolate dehydrogenase 1 [Homo sapiens] | 56 | 0 | 690 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
Rv3422c hypothetical protein | Mycobacterium tuberculosis H37Rv | 25% | 1.2 | 29.3 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00595 | Formate--tetrahydrofolate ligase signatures | 115-125; | PS00721 | |
PDOC00595 | Formate--tetrahydrofolate ligase signatures | 391-402; | PS00722 | |
Acylation | N-myristoylation site | 35-40; 45-50; 61-66; 88-93; 115-120; 118-123; 119-124; 122-127; 194-199; 240-245; 290-295; 299-304; 365-370; 477-482; 483-488; 566-571; | PS00008 | |
Glycosylation | N-glycosylation site | 339-342; 506-509; 530-533; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 173-176; 224-227; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 29-32; 165-168; 202-205; 204-207; 252-255; 294-297; 446-449; 448-451; 508-511; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 3-5; 46-48; 222-224; 249-251; 393-395; 508-510; 615-617; | PS00005 | |
Phosphorylation | Tyrosine kinase phosphorylation site | 164-172; | PS00007 | |
Sulfation | Tyrosine sulfation site | 521-535; | PS00003 |
C-1-tetrahydrofolate synthase, cytoplasmic, putative [Q4Q735] | ||
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Model Information | ||
Template PDB ID | 1fpmB | |
Percent Identity | 46% | |
Target Region | 16-622 | |
Template Region | 8-548 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
LYS | 67 | 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 |
18459-37-5 | CESIUM ION | 132.905 | Cs | [Cs+] | 1fpm |
14808-79-8 | SULFATE ION | 96.063 | O4 S | [O-]S([O-])(=O)=O | 1fpm |
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/849526/Q4Q735.pdb 2.0 607 = residues | | = | *| Ramachandran plot: 88.8% core 9.8% allow 0.6% gener 0.8% = disall | | = | *| All Ramachandrans: 30 labelled residues (out of 605) = | +| Chi1-chi2 plots: 6 labelled residues (out of 323) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 7.1 Bad contacts: = 11 | *| Bond len/angle: 8.1 Morris et al class: 1 = 1 3 | +| 1 cis-peptides = | | G-factors Dihedrals: -0.05 Covalent: -0.17 Overall: = -0.09 | | = | | M/c bond lengths: 99.4% within limits 0.6% highlighted = | | M/c bond angles: 94.2% within limits 5.8% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |