| Enolase [Q4QFL8] | |
|---|---|
| Systematic Name | LmjF.14.1160 [Leishmania major] |
| Gene Name | ENOL |
| Molecular Weight | 46092 Da |
| Protein Sequence Size | 429 |
| Function | |
| Charge | -4 |
| Isoelectric Point | 5.5515 pH |
| Description | Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase). |
| Subcellular Location | N.A.[Predict] |
| E. C. Number | 4.2.1.11 |
| Sequence | >tr|Q4QFL8|Q4QFL8_LEIMA Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) - Leishmania major. PIRKVYAREVLDSRGNPTVEVELMTEAGVFRSAVPSGASTGVHEACELRDGDKARYCGAG CTQAVKNVNEILAPALVGKEESDQAGLDKMMCELDGTKNKSKLGANAILGCSMAISKAAA AKAGVPLYRYIASLAGTKDIRLPVPCFNVINGGKHAGNILPFQEFMIAPTKATSFREALR MGSEVYHALKVIIKSKYGQDAVNVGDEGGFAPPIKHIDEPLPILMEAIEKAGHKGKFAIC MDCAASEAYDAERKMYNLTFKNPEPTYVSAAELQATYERWVAEYPLVSIEDPFAEDNFDE FSAITKALAGKAQIVGDDLTVTNVKRVTMAIEKSACNSLLLKINQIGTISESIAAAKLCM ENGWSVMVSHRSGETEDTYIADLSVGLGTGQIKTGAPCRGERTAKLNQLLRIEEEIGSTA TYGYPGWA |
| DNA Sequence | >LmjF14.1160 |ENOL||enolase|Leishmania major|chr 14|||Manual ATGCCGATCC GAAAGGTTTA CGCCCGCGAG GTGCTCGACT CCCGCGGCAA CCCGACCGTTGAGGTCGAGT TGATGACGGA GGCCGGCGTT TTCCGCTCCG CTGTGCCTTC CGGCGCGTCGACTGGCGTGC ATGAGGCGTG CGAGCTGCGC GACGGCGACA AGGCGCGCTA CTGTGGCGCCGGCTGCACGC AGGCGGTGAA GAACGTGAAC GAGATCCTTG CGCCGGCGCT TGTGGGCAAGGAAGAGTCGG ACCAGGCCGG CCTCGACAAG ATGATGTGTG AGCTGGACGG GACAAAGAACAAGAGCAAGC TCGGCGCAAA CGCGATCCTG GGCTGCTCGA TGGCGATCAG CAAGGCCGCCGCGGCGAAGG CTGGCGTGCC GCTGTACAGG TACATCGCGA GTCTCGCCGG GACGAAGGATATCCGCCTGC CTGTGCCGTG CTTCAACGTG ATCAACGGTG GCAAGCACGC CGGCAACATCCTGCCGTTCC AGGAGTTCAT GATTGCGCCG ACGAAGGCGA CGTCGTTCCG CGAGGCGCTGCGCATGGGCT CGGAGGTATA CCACGCGCTC AAGGTGATCA TCAAGAGCAA GTACGGCCAGGACGCCGTGA ACGTCGGCGA CGAGGGCGGC TTCGCGCCGC CGATCAAGCA TATCGACGAGCCGCTGCCGA TCCTGATGGA GGCGATTGAG AAGGCTGGGC ACAAGGGCAA GTTCGCGATCTGCATGGACT GCGCGGCAAG CGAAGCGTAT GACGCGGAGA GGAAGATGTA CAACCTGACATTCAAGAACC CCGAGCCGAC GTACGTGTCC GCGGCGGAGT TGCAGGCGAC CTATGAGCGCTGGGTCGCGG AGTACCCGCT GGTGTCCATC GAGGACCCGT TCGCGGAAGA CAACTTTGACGAGTTCTCGG CGATCACGAA GGCACTTGCC GGGAAGGCTC AGATCGTCGG TGATGACCTGACGGTGACAA ACGTGAAGCG TGTGACGATG GCGATCGAGA AGTCTGCGTG CAACTCGCTGCTACTAAAAA TCAACCAGAT CGGCACGATC AGCGAGTCGA TCGCAGCGGC GAAGCTGTGCATGGAGAACG GGTGGTCTGT GATGGTGTCG CACCGTAGCG GCGAGACGGA GGACACGTACATTGCTGACC TGTCCGTGGG CCTGGGAACC GGCCAGATCA AGACCGGCGC GCCGTGCCGTGGCGAGCGCA CTGCGAAGCT GAACCAGCTG CTGCGCATCG AGGAGGAGAT CGGGTCCACTGCTACGTACG GCTACCCCGG CTGGGCGTAA |
| Enolase Q4QFL8] | |
|---|---|
| Metabolite Information | |
| Molecular Function | phosphopyruvate hydratase activity |
| Biochemical Pathway | glycolysis; cellular component unknown; phosphopyruvate hydratase complex |
| Regulatory Pathway | |
| KEGG Pathways | K01689 |
| Orthologs | ||||
| Homologs | GI | Percent Identity | Evalue | Score |
| Homo sapiens | enolase 2 [Homo sapiens] | 60 | 1e-139 | 492 |
| DEG Information | ||||
| DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
| eno enolase | Bacillus subtilis | 51% | 1e-113 | 402 |
| Post Translational Modification | ||||
| PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
| PDOC00148 | Enolase signature | 340-353; | PS00164 | |
| PDOC00595 | Formate--tetrahydrofolate ligase signatures | 100-103; 258-261; | PS00722 | |
| Acylation | N-myristoylation site | 29-34; 38-43; 42-47; 59-64; 61-66; 111-116; 153-158; 387-392; 391-396; 418-423; | PS00008 | |
| Glycosylation | N-glycosylation site | 100-103; 258-261; | PS00001 | |
| Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 326-329; | PS00004 | |
| Phosphorylation | Casein kinase II phosphorylation site | 175-178; 270-273; 289-292; 349-352; | PS00006 | |
| Phosphorylation | Protein kinase C phosphorylation site | 175-177; 260-262; 370-372; 404-406; | PS00005 | |
| Phosphorylation | Tyrosine kinase phosphorylation site | 50-57; 262-268; | PS00007 | |
| Sulfation | Tyrosine sulfation site | 373-387; | PS00003 | |
| Enolase [Q4QFL8] | ||
|---|---|---|
| Model Information | ||
| Template PDB ID | 1oepA | |
| Percent Identity | 77% | |
| Target Region | 1-429 | |
| Template Region | 1-422 | |
| Domain Information | ||
|---|---|---|
| Domains | Start | End |
| Active Site Information | ||
|---|---|---|
| Residue | Active Site Number | Functional Part |
| GLU | 165 | Sidechain |
| GLU | 208 | Sidechain |
| HIS | 371 | Sidechain |
| LYS | 394 | Sidechain |
| Co-Factor | |
|---|---|
| Metal | Description |
| Mg | Required for catalysis and for stabilizing the dimer |
| Ligands | |||||
|---|---|---|---|---|---|
| CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
| 25322-68-3 | 1,2-ETHANEDIOL | 62.068 | C2 H6 O2 | OCCO | 1oep |
| 14808-79-8 | SULFATE ION | 96.063 | O4 S   | [O-]S([O-])(=O)=O | 1oep |
| 23713-49-7 | ZINC ION | 65.409 | Zn | [Zn+2] | 1oep |
| 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/273217/Q4QFL8.pdb 2.0 429 = residues | | = | *| Ramachandran plot: 91.9% core 7.8% allow 0.0% gener 0.3% = disall | | = | *| All Ramachandrans: 13 labelled residues (out of 427) = | +| Chi1-chi2 plots: 1 labelled residues (out of 233) = | | = | | 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: 7.4 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.08 Covalent: -0.14 Overall: = 0.00 | | = | | M/c bond lengths: 99.3% within limits 0.7% highlighted = | | M/c bond angles: 94.1% within limits 5.9% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |