| Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
| blastp_kegg | bfu:BC1G_04310 | 1 | 2417 | 2417 | n/a | 100.00 | 2417 | 98.80 | 0.00 | 0.0 | similar to polyketide synthase |
| ssl:SS1G_02211 | 1 | 2226 | 2226 | Gaps:12 | 100.00 | 2148 | 77.28 | 8.33 | 0.0 | hypothetical protein |
| pno:SNOG_15965 | 137 | 2416 | 2280 | Gaps:110 | 99.83 | 2298 | 58.81 | 15.13 | 0.0 | hypothetical protein |
| aor:AO090011000015 | 6 | 2415 | 2410 | Gaps:159 | 97.92 | 2407 | 45.91 | 18.80 | 0.0 | polyketide synthase modules and related proteins |
| nfi:NFIA_023490 | 6 | 2417 | 2412 | Gaps:100 | 95.88 | 2405 | 45.92 | 17.56 | 0.0 | polyketide synthase putative |
| afm:AFUA_8G00370 | 7 | 2416 | 2410 | Gaps:167 | 96.95 | 2462 | 43.19 | 17.34 | 0.0 | polyketide synthase |
| ncr:NCU02918 | 6 | 2415 | 2410 | Gaps:190 | 91.06 | 2382 | 34.53 | 18.03 | 0.0 | hypothetical protein |
| ani:AN7084.2 | 7 | 2417 | 2411 | Gaps:83 | 94.56 | 2388 | 47.03 | 17.67 | 0.0 | hypothetical protein |
| afv:AFLA_038310 | 886 | 2416 | 1531 | Gaps:57 | 94.73 | 1481 | 44.40 | 20.81 | 0.0 | PKS-like enzyme putative |
| ang:An01g01130 | 2 | 2416 | 2415 | Gaps:139 | 92.53 | 2396 | 35.05 | 18.18 | 0.0 | hypothetical protein |
| blastp_uniprot_sprot | sp|Q0C8M3|LNKS_ASPTN | 2 | 2416 | 2415 | Gaps:176 | 54.67 | 3038 | 31.97 | 17.64 | 1e-158 | Lovastatin nonaketide synthase OS Aspergillus terreus (strain NIH 2624 / FGSC A1156) GN lovB PE 3 SV 2 |
| sp|Q9Y8A5|LNKS_ASPTE | 2 | 2416 | 2415 | Gaps:174 | 54.67 | 3038 | 32.15 | 17.16 | 1e-158 | Lovastatin nonaketide synthase OS Aspergillus terreus GN lovB PE 1 SV 1 |
| sp|Q03133|ERYA3_SACER | 1 | 2227 | 2227 | Gaps:174 | 69.23 | 3172 | 31.97 | 17.21 | 1e-113 | Erythronolide synthase modules 5 and 6 OS Saccharopolyspora erythraea GN eryA PE 1 SV 4 |
| sp|O07798|PHAS_MYCTU | 8 | 2415 | 2408 | Gaps:163 | 88.33 | 2126 | 30.40 | 18.58 | 1e-111 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis GN pks2 PE 1 SV 1 |
| sp|A5U9F4|PHAS_MYCTA | 8 | 2415 | 2408 | Gaps:163 | 88.33 | 2126 | 30.40 | 18.58 | 1e-111 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) GN pks2 PE 3 SV 1 |
| sp|Q7TVK8|PHAS_MYCBO | 8 | 2415 | 2408 | Gaps:163 | 88.33 | 2126 | 30.40 | 18.58 | 1e-111 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis GN pks2 PE 3 SV 1 |
| sp|A1KQG0|PHAS_MYCBP | 8 | 2415 | 2408 | Gaps:163 | 88.33 | 2126 | 30.40 | 18.53 | 1e-110 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis (strain BCG / Pasteur 1173P2) GN pks2 PE 3 SV 1 |
| sp|Q10977|PPSA_MYCTU | 7 | 2417 | 2411 | Gaps:134 | 60.98 | 1876 | 33.39 | 17.13 | 1e-109 | Phenolpthiocerol synthesis polyketide synthase ppsA OS Mycobacterium tuberculosis GN ppsA PE 3 SV 2 |
| sp|Q03132|ERYA2_SACER | 7 | 2416 | 2410 | Gaps:235 | 71.04 | 3567 | 31.22 | 17.76 | 1e-103 | Erythronolide synthase modules 3 and 4 OS Saccharopolyspora erythraea GN eryA PE 1 SV 3 |
| sp|Q869W9|PKS16_DICDI | 5 | 2396 | 2392 | Gaps:221 | 67.69 | 2603 | 29.06 | 19.30 | 1e-102 | Probable polyketide synthase 16 OS Dictyostelium discoideum GN pks16 PE 2 SV 1 |
| blastp_pdb | 2hg4_F | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_E | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_D | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_C | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_B | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_A | 1 | 914 | 914 | Gaps:83 | 96.51 | 917 | 34.12 | 16.61 | 1e-115 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2qo3_B | 7 | 822 | 816 | Gaps:60 | 87.43 | 915 | 33.25 | 17.12 | 1e-104 | mol:protein length:915 EryAII Erythromycin polyketide synthase modul |
| 2qo3_A | 7 | 822 | 816 | Gaps:60 | 87.43 | 915 | 33.25 | 17.12 | 1e-104 | mol:protein length:915 EryAII Erythromycin polyketide synthase modul |
| 3hhd_D | 74 | 972 | 899 | Gaps:85 | 87.46 | 965 | 31.75 | 17.89 | 5e-76 | mol:protein length:965 Fatty acid synthase |
| 3hhd_C | 74 | 972 | 899 | Gaps:85 | 87.46 | 965 | 31.75 | 17.89 | 5e-76 | mol:protein length:965 Fatty acid synthase |
| rpsblast_cdd | gnl|CDD|129058 | 9 | 434 | 426 | Gaps:8 | 100.00 | 424 | 46.70 | 18.16 | 1e-171 | smart00825 PKS_KS Beta-ketoacyl synthase. The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. |
| gnl|CDD|33130 | 4 | 993 | 990 | Gaps:72 | 90.10 | 1061 | 36.51 | 15.79 | 1e-171 | COG3321 COG3321 Polyketide synthase modules and related proteins [Secondary metabolites biosynthesis transport and catabolism]. |
| gnl|CDD|29420 | 7 | 431 | 425 | Gaps:6 | 100.00 | 421 | 50.83 | 17.81 | 1e-149 | cd00833 PKS polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products called polyketides by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs complexes of several monofunctional subunits.. |
| gnl|CDD|129062 | 1737 | 2028 | 292 | Gaps:6 | 100.00 | 288 | 51.39 | 16.32 | 1e-118 | smart00829 PKS_ER Enoylreductase. Enoylreductase in Polyketide synthases. |
| gnl|CDD|176179 | 1734 | 2028 | 295 | Gaps:2 | 100.00 | 293 | 48.12 | 19.45 | 1e-114 | cd05195 enoyl_red enoyl reductase of polyketide synthase. Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. |
| gnl|CDD|129060 | 544 | 852 | 309 | Gaps:15 | 100.00 | 298 | 39.60 | 15.77 | 2e-85 | smart00827 PKS_AT Acyl transferase domain in polyketide synthase (PKS) enzymes. |
| gnl|CDD|149646 | 2052 | 2231 | 180 | Gaps:5 | 100.00 | 181 | 40.88 | 15.47 | 2e-60 | pfam08659 KR KR domain. This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group. |
| gnl|CDD|163029 | 8 | 881 | 874 | Gaps:139 | 35.52 | 2582 | 25.19 | 17.12 | 7e-58 | TIGR02813 omega_3_PfaA polyketide-type polyunsaturated fatty acid synthase PfaA. Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB PfaC and PfaD and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA also included with the reach of this model appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis an alternative to the more familiar iterated mechanism of chain extension and desaturation and in most cases are encoded near genes for homologs of PfaB PfaC and/or PfaD. |
| gnl|CDD|129055 | 2052 | 2230 | 179 | Gaps:5 | 100.00 | 180 | 38.33 | 16.11 | 8e-56 | smart00822 PKS_KR This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group. |
| gnl|CDD|143886 | 7 | 258 | 252 | Gaps:20 | 99.59 | 243 | 40.91 | 13.22 | 2e-54 | pfam00109 ketoacyl-synt Beta-ketoacyl synthase N-terminal domain. The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine. |
| rpsblast_kog | gnl|CDD|36416 | 6 | 2239 | 2234 | Gaps:198 | 67.30 | 2376 | 30.27 | 18.20 | 1e-114 | KOG1202 KOG1202 KOG1202 Animal-type fatty acid synthase and related proteins [Lipid transport and metabolism]. |
| gnl|CDD|36411 | 1708 | 2028 | 321 | Gaps:24 | 94.35 | 336 | 26.18 | 21.14 | 9e-30 | KOG1197 KOG1197 KOG1197 Predicted quinone oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|36608 | 85 | 433 | 349 | Gaps:37 | 80.91 | 440 | 24.16 | 17.42 | 3e-24 | KOG1394 KOG1394 KOG1394 3-oxoacyl-(acyl-carrier-protein) synthase (I and II) [Lipid transport and metabolism Secondary metabolites biosynthesis transport and catabolism]. |
| gnl|CDD|36412 | 1738 | 2028 | 291 | Gaps:32 | 88.47 | 347 | 24.76 | 17.92 | 2e-22 | KOG1198 KOG1198 KOG1198 Zinc-binding oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|38137 | 542 | 836 | 295 | Gaps:38 | 76.94 | 386 | 25.93 | 14.48 | 6e-13 | KOG2926 KOG2926 KOG2926 Malonyl-CoA:ACP transacylase [Lipid transport and metabolism]. |
| gnl|CDD|36414 | 2042 | 2228 | 187 | Gaps:22 | 75.39 | 256 | 22.80 | 18.13 | 6e-10 | KOG1200 KOG1200 KOG1200 Mitochondrial/plastidial beta-ketoacyl-ACP reductase [Lipid transport and metabolism]. |
| gnl|CDD|35248 | 1728 | 1997 | 270 | Gaps:31 | 78.81 | 354 | 25.09 | 16.85 | 1e-09 | KOG0025 KOG0025 KOG0025 Zn2+-binding dehydrogenase (nuclear receptor binding factor-1) [Transcription Energy production and conversion]. |
Gene Identifier
Genome Report System - copyright INRA 2011