| Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
| blastp_kegg | ssl:SS1G_03591 | 1 | 2215 | 2215 | n/a | 100.00 | 2215 | 97.70 | 0.00 | 0.0 | hypothetical protein |
| bfu:BC1G_13114 | 259 | 2210 | 1952 | Gaps:79 | 89.89 | 2176 | 71.27 | 11.09 | 0.0 | hypothetical protein |
| act:ACLA_087700 | 7 | 2208 | 2202 | Gaps:186 | 90.14 | 2444 | 39.63 | 17.88 | 0.0 | polyketide synthase putative |
| ang:An11g05570 | 3 | 1979 | 1977 | Gaps:354 | 82.93 | 2502 | 30.31 | 16.00 | 0.0 | hypothetical protein |
| afv:AFLA_128060 | 4 | 2205 | 2202 | Gaps:183 | 90.39 | 2591 | 37.53 | 17.72 | 0.0 | polyketide synthase putative |
| afm:AFUA_2G01290 | 4 | 2188 | 2185 | Gaps:250 | 91.18 | 2609 | 37.83 | 17.65 | 0.0 | polyketide synthase |
| ssl:SS1G_11404 | 7 | 2205 | 2199 | Gaps:144 | 82.05 | 2524 | 39.16 | 18.40 | 0.0 | hypothetical protein |
| nfi:NFIA_033590 | 4 | 2188 | 2185 | Gaps:239 | 91.25 | 2606 | 37.72 | 17.66 | 0.0 | polyketide synthase putative |
| act:ACLA_098370 | 10 | 2212 | 2203 | Gaps:254 | 92.68 | 2582 | 36.48 | 16.01 | 0.0 | polyketide synthase putative |
| act:ACLA_094600 | 1 | 2188 | 2188 | Gaps:162 | 89.30 | 2599 | 38.17 | 17.75 | 0.0 | polyketide synthase putative |
| blastp_uniprot_sprot | sp|Q0C8M3|LNKS_ASPTN | 1 | 1750 | 1750 | Gaps:181 | 48.72 | 3038 | 33.31 | 16.15 | 1e-123 | Lovastatin nonaketide synthase OS Aspergillus terreus (strain NIH 2624 / FGSC A1156) GN lovB PE 3 SV 2 |
| sp|Q9Y8A5|LNKS_ASPTE | 1 | 1750 | 1750 | Gaps:187 | 48.72 | 3038 | 33.51 | 15.95 | 1e-123 | Lovastatin nonaketide synthase OS Aspergillus terreus GN lovB PE 1 SV 1 |
| sp|Q10977|PPSA_MYCTU | 9 | 817 | 809 | Gaps:121 | 43.28 | 1876 | 33.25 | 17.12 | 1e-101 | Phenolpthiocerol synthesis polyketide synthase ppsA OS Mycobacterium tuberculosis GN ppsA PE 3 SV 2 |
| sp|Q03131|ERYA1_SACER | 9 | 817 | 809 | Gaps:252 | 53.02 | 3491 | 30.58 | 18.15 | 5e-97 | Erythronolide synthase modules 1 and 2 OS Saccharopolyspora erythraea GN eryA PE 1 SV 1 |
| sp|Q869W9|PKS16_DICDI | 11 | 2001 | 1991 | Gaps:249 | 58.51 | 2603 | 30.01 | 18.06 | 6e-93 | Probable polyketide synthase 16 OS Dictyostelium discoideum GN pks16 PE 2 SV 1 |
| sp|Q869X2|PKS17_DICDI | 11 | 2001 | 1991 | Gaps:234 | 58.53 | 2604 | 29.53 | 18.24 | 3e-92 | Probable polyketide synthase 17 OS Dictyostelium discoideum GN pks17 PE 3 SV 1 |
| sp|O07798|PHAS_MYCTU | 7 | 1985 | 1979 | Gaps:147 | 53.95 | 2126 | 32.35 | 17.00 | 2e-90 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis GN pks2 PE 1 SV 1 |
| sp|A5U9F4|PHAS_MYCTA | 7 | 1985 | 1979 | Gaps:147 | 53.95 | 2126 | 32.35 | 17.00 | 2e-90 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) GN pks2 PE 3 SV 1 |
| sp|Q7TVK8|PHAS_MYCBO | 7 | 1985 | 1979 | Gaps:147 | 53.95 | 2126 | 32.35 | 17.00 | 2e-90 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis GN pks2 PE 3 SV 1 |
| sp|A1KQG0|PHAS_MYCBP | 7 | 1985 | 1979 | Gaps:132 | 52.45 | 2126 | 32.47 | 17.22 | 6e-90 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis (strain BCG / Pasteur 1173P2) GN pks2 PE 3 SV 1 |
| blastp_pdb | 2hg4_F | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_E | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_D | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_C | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_B | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2hg4_A | 9 | 809 | 801 | Gaps:136 | 85.82 | 917 | 31.64 | 17.41 | 7e-92 | mol:protein length:917 6-Deoxyerythronolide B Synthase |
| 2qo3_B | 9 | 806 | 798 | Gaps:151 | 87.54 | 915 | 30.71 | 17.98 | 3e-90 | mol:protein length:915 EryAII Erythromycin polyketide synthase modul |
| 2qo3_A | 9 | 806 | 798 | Gaps:151 | 87.54 | 915 | 30.71 | 17.98 | 3e-90 | mol:protein length:915 EryAII Erythromycin polyketide synthase modul |
| 3hhd_D | 9 | 825 | 817 | Gaps:167 | 81.04 | 965 | 33.25 | 13.81 | 5e-76 | mol:protein length:965 Fatty acid synthase |
| 3hhd_C | 9 | 825 | 817 | Gaps:167 | 81.04 | 965 | 33.25 | 13.81 | 5e-76 | mol:protein length:965 Fatty acid synthase |
| rpsblast_cdd | gnl|CDD|129058 | 12 | 386 | 375 | Gaps:52 | 99.76 | 424 | 44.92 | 12.29 | 1e-147 | 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 | 8 | 817 | 810 | Gaps:122 | 76.15 | 1061 | 35.40 | 14.73 | 1e-134 | COG3321 COG3321 Polyketide synthase modules and related proteins [Secondary metabolites biosynthesis transport and catabolism]. |
| gnl|CDD|29420 | 9 | 383 | 375 | Gaps:52 | 100.00 | 421 | 46.79 | 11.88 | 1e-127 | 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|176179 | 1680 | 1973 | 294 | Gaps:5 | 100.00 | 293 | 53.24 | 17.06 | 1e-116 | 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|129062 | 1683 | 1973 | 291 | Gaps:9 | 100.00 | 288 | 53.12 | 15.28 | 1e-115 | smart00829 PKS_ER Enoylreductase. Enoylreductase in Polyketide synthases. |
| gnl|CDD|129060 | 512 | 824 | 313 | Gaps:27 | 97.32 | 298 | 38.28 | 14.48 | 6e-88 | smart00827 PKS_AT Acyl transferase domain in polyketide synthase (PKS) enzymes. |
| gnl|CDD|176203 | 1653 | 1974 | 322 | Gaps:29 | 99.38 | 323 | 34.89 | 17.13 | 1e-58 | cd08241 QOR1 Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 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. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. 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. In human ADH catalysis the zinc ion helps coordinate the alcohol followed by deprotonation of a histidine the ribose of NAD a serine then the alcohol which allows the transfer of a hydride to NAD+ creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria the active site zinc binds an aldehyde polarizing it and leading to the reverse reaction. |
| gnl|CDD|176213 | 1676 | 1973 | 298 | Gaps:16 | 99.01 | 303 | 37.00 | 18.33 | 5e-55 | cd08251 polyketide_synthase 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 have 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|176236 | 1653 | 1973 | 321 | Gaps:41 | 99.11 | 337 | 34.43 | 16.77 | 1e-52 | cd08275 MDR3 Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins is a diverse group of proteins related to the first identified member class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities including the founding alcohol dehydrogenase (ADH) quinone reductase sorbitol dehydrogenase formaldehyde dehydrogenase butanediol DH ketose reductase cinnamyl reductase and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine two cysteines and a water molecule. The second zinc seems to play a structural role affects subunit interactions and is typically coordinated by 4 cysteines. |
| gnl|CDD|30949 | 1653 | 1975 | 323 | Gaps:19 | 99.39 | 326 | 33.02 | 16.05 | 5e-51 | COG0604 Qor NADPH:quinone reductase and related Zn-dependent oxidoreductases [Energy production and conversion / General function prediction only]. |
| rpsblast_kog | gnl|CDD|36416 | 76 | 1976 | 1901 | Gaps:177 | 44.82 | 2376 | 34.27 | 15.87 | 2e-97 | KOG1202 KOG1202 KOG1202 Animal-type fatty acid synthase and related proteins [Lipid transport and metabolism]. |
| gnl|CDD|36412 | 1653 | 1976 | 324 | Gaps:30 | 97.98 | 347 | 30.00 | 13.82 | 4e-34 | KOG1198 KOG1198 KOG1198 Zinc-binding oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|36411 | 1647 | 1974 | 328 | Gaps:35 | 97.32 | 336 | 24.46 | 17.74 | 7e-28 | KOG1197 KOG1197 KOG1197 Predicted quinone oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|36608 | 108 | 382 | 275 | Gaps:21 | 62.73 | 440 | 30.43 | 17.75 | 3e-26 | KOG1394 KOG1394 KOG1394 3-oxoacyl-(acyl-carrier-protein) synthase (I and II) [Lipid transport and metabolism Secondary metabolites biosynthesis transport and catabolism]. |
| gnl|CDD|38137 | 498 | 770 | 273 | Gaps:23 | 70.47 | 386 | 22.79 | 18.01 | 2e-15 | KOG2926 KOG2926 KOG2926 Malonyl-CoA:ACP transacylase [Lipid transport and metabolism]. |
| gnl|CDD|35248 | 1709 | 1868 | 160 | Gaps:4 | 45.76 | 354 | 29.01 | 19.14 | 3e-14 | KOG0025 KOG0025 KOG0025 Zn2+-binding dehydrogenase (nuclear receptor binding factor-1) [Transcription Energy production and conversion]. |
| gnl|CDD|35246 | 1653 | 1975 | 323 | Gaps:62 | 95.28 | 360 | 22.45 | 15.45 | 3e-13 | KOG0023 KOG0023 KOG0023 Alcohol dehydrogenase class V [Secondary metabolites biosynthesis transport and catabolism]. |
| gnl|CDD|36410 | 1719 | 1975 | 257 | Gaps:38 | 74.93 | 343 | 23.35 | 16.34 | 4e-11 | KOG1196 KOG1196 KOG1196 Predicted NAD-dependent oxidoreductase [General function prediction only]. |
Gene Identifier
Genome Report System - copyright INRA 2011