| Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
| blastp_kegg | bfu:BC1G_15838 | 1 | 1056 | 1056 | n/a | 100.00 | 1056 | 98.77 | 0.00 | 0.0 | similar to polyketide synthase |
| ssl:SS1G_09240 | 10 | 1055 | 1046 | Gaps:99 | 49.73 | 2258 | 68.30 | 10.33 | 0.0 | hypothetical protein |
| pno:SNOG_11272 | 10 | 1056 | 1047 | Gaps:70 | 48.98 | 2250 | 46.10 | 17.97 | 0.0 | hypothetical protein |
| pno:SNOG_09491 | 98 | 1018 | 921 | Gaps:31 | 49.88 | 1602 | 43.55 | 18.77 | 1e-133 | hypothetical protein |
| ure:UREG_01366 | 10 | 774 | 765 | Gaps:45 | 44.96 | 1708 | 32.55 | 18.10 | 1e-100 | similar to polyketide synthase |
| cim:CIMG_02398 | 10 | 1053 | 1044 | Gaps:53 | 41.12 | 2330 | 30.69 | 18.58 | 2e-89 | hypothetical protein |
| ncr:NCU09638 | 10 | 1055 | 1046 | Gaps:52 | 33.64 | 2628 | 34.73 | 19.80 | 3e-89 | hypothetical protein |
| pan:PODANSg2799 | 16 | 1055 | 1040 | Gaps:42 | 33.44 | 2620 | 35.27 | 18.49 | 2e-88 | hypothetical protein |
| pcs:Pc21g03990 | 10 | 1049 | 1040 | Gaps:38 | 38.05 | 2365 | 30.89 | 18.89 | 8e-87 | Pc21g03990 |
| ncr:NCU02918 | 8 | 1048 | 1041 | Gaps:92 | 38.12 | 2382 | 34.80 | 16.74 | 1e-84 | hypothetical protein |
| blastp_uniprot_sprot | sp|Q02251|MCAS_MYCBO | 150 | 1050 | 901 | Gaps:72 | 28.14 | 2111 | 30.30 | 17.00 | 1e-28 | Mycocerosic acid synthase OS Mycobacterium bovis GN mas PE 1 SV 2 |
| sp|Q0C8M3|LNKS_ASPTN | 11 | 631 | 621 | Gaps:100 | 20.24 | 3038 | 28.13 | 14.31 | 4e-27 | Lovastatin nonaketide synthase OS Aspergillus terreus (strain NIH 2624 / FGSC A1156) GN lovB PE 3 SV 2 |
| sp|Q9Y8A5|LNKS_ASPTE | 11 | 631 | 621 | Gaps:100 | 20.24 | 3038 | 28.29 | 13.82 | 3e-26 | Lovastatin nonaketide synthase OS Aspergillus terreus GN lovB PE 1 SV 1 |
| sp|Q03132|ERYA2_SACER | 827 | 1053 | 227 | Gaps:9 | 6.50 | 3567 | 37.93 | 18.97 | 3e-26 | Erythronolide synthase modules 3 and 4 OS Saccharopolyspora erythraea GN eryA PE 1 SV 3 |
| sp|Q54FI3|PKS37_DICDI | 865 | 1053 | 189 | Gaps:38 | 7.18 | 2968 | 36.62 | 16.90 | 5e-24 | Probable polyketide synthase 37 OS Dictyostelium discoideum GN stlB PE 2 SV 1 |
| sp|O07798|PHAS_MYCTU | 151 | 1050 | 900 | Gaps:98 | 32.22 | 2126 | 30.95 | 16.35 | 6e-22 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis GN pks2 PE 1 SV 1 |
| sp|A5U9F4|PHAS_MYCTA | 151 | 1050 | 900 | Gaps:98 | 32.22 | 2126 | 30.95 | 16.35 | 6e-22 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) GN pks2 PE 3 SV 1 |
| sp|Q7TVK8|PHAS_MYCBO | 151 | 1050 | 900 | Gaps:98 | 32.22 | 2126 | 30.95 | 16.35 | 6e-22 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis GN pks2 PE 3 SV 1 |
| sp|A1KQG0|PHAS_MYCBP | 151 | 1050 | 900 | Gaps:98 | 32.22 | 2126 | 30.95 | 16.20 | 7e-22 | Phthioceranic/hydroxyphthioceranic acid synthase OS Mycobacterium bovis (strain BCG / Pasteur 1173P2) GN pks2 PE 3 SV 1 |
| sp|Q55E72|PKS1_DICDI | 727 | 1053 | 327 | Gaps:60 | 10.77 | 3147 | 29.20 | 22.42 | 2e-21 | Probable polyketide synthase 1 OS Dictyostelium discoideum GN stlA PE 1 SV 1 |
| blastp_pdb | 2vz9_B | 10 | 1055 | 1046 | Gaps:41 | 13.02 | 2512 | 36.39 | 20.80 | 2e-19 | mol:protein length:2512 FATTY ACID SYNTHASE |
| 2vz9_A | 10 | 1055 | 1046 | Gaps:41 | 13.02 | 2512 | 36.39 | 20.80 | 2e-19 | mol:protein length:2512 FATTY ACID SYNTHASE |
| 2vz8_B | 10 | 1055 | 1046 | Gaps:41 | 13.02 | 2512 | 36.39 | 20.80 | 2e-19 | mol:protein length:2512 FATTY ACID SYNTHASE |
| 2vz8_A | 10 | 1055 | 1046 | Gaps:41 | 13.02 | 2512 | 36.39 | 20.80 | 2e-19 | mol:protein length:2512 FATTY ACID SYNTHASE |
| 1pqw_B | 946 | 1053 | 108 | Gaps:3 | 53.03 | 198 | 47.62 | 20.95 | 5e-18 | mol:protein length:198 polyketide synthase |
| 1pqw_A | 946 | 1053 | 108 | Gaps:3 | 53.03 | 198 | 47.62 | 20.95 | 5e-18 | mol:protein length:198 polyketide synthase |
| 3jyn_A | 839 | 1007 | 169 | Gaps:7 | 53.54 | 325 | 35.63 | 17.24 | 1e-17 | mol:protein length:325 Quinone oxidoreductase |
| 3jyl_A | 839 | 1007 | 169 | Gaps:7 | 53.54 | 325 | 35.63 | 17.24 | 1e-17 | mol:protein length:325 Quinone oxidoreductase |
| 1qor_B | 866 | 1055 | 190 | Gaps:9 | 59.02 | 327 | 31.09 | 21.76 | 2e-17 | mol:protein length:327 QUINONE OXIDOREDUCTASE |
| 1qor_A | 866 | 1055 | 190 | Gaps:9 | 59.02 | 327 | 31.09 | 21.76 | 2e-17 | mol:protein length:327 QUINONE OXIDOREDUCTASE |
| rpsblast_cdd | gnl|CDD|176179 | 865 | 1053 | 189 | Gaps:3 | 64.85 | 293 | 48.95 | 18.42 | 1e-68 | 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 | 868 | 1053 | 186 | Gaps:2 | 64.58 | 288 | 50.54 | 19.35 | 2e-68 | smart00829 PKS_ER Enoylreductase. Enoylreductase in Polyketide synthases. |
| gnl|CDD|129060 | 11 | 215 | 205 | Gaps:20 | 64.09 | 298 | 34.55 | 15.71 | 2e-44 | smart00827 PKS_AT Acyl transferase domain in polyketide synthase (PKS) enzymes. |
| gnl|CDD|176189 | 836 | 1052 | 217 | Gaps:28 | 70.94 | 320 | 35.24 | 20.26 | 3e-37 | cd05286 QOR2 Quinone oxidoreductase (QOR). Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. 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 actin 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. 2-haloacrylate reductase a member of this subgroup catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR Burkholderia 2-haloacrylate reductase does not act on the quinones 1 4-benzoquinone and 1 4-naphthoquinone. 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. 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|30949 | 859 | 1056 | 198 | Gaps:12 | 62.58 | 326 | 36.76 | 19.12 | 4e-37 | COG0604 Qor NADPH:quinone reductase and related Zn-dependent oxidoreductases [Energy production and conversion / General function prediction only]. |
| gnl|CDD|176203 | 863 | 1045 | 183 | Gaps:13 | 57.59 | 323 | 37.63 | 18.82 | 5e-37 | 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|176229 | 863 | 1045 | 183 | Gaps:20 | 58.23 | 328 | 38.74 | 16.75 | 5e-35 | cd08268 MDR2 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|176180 | 862 | 1045 | 184 | Gaps:23 | 57.89 | 323 | 40.11 | 14.97 | 2e-32 | cd05276 p53_inducible_oxidoreductase PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase a medium chain dehydrogenase/reductase family member acts in the apoptotic pathway. PIG3 reduces ortho-quinones but its apoptotic activity has been attributed to oxidative stress generation since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases which catalyze the reduction of quinone to hydroxyquinone. 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|176215 | 864 | 1045 | 182 | Gaps:16 | 58.46 | 325 | 32.63 | 17.89 | 7e-32 | cd08253 zeta_crystallin Zeta-crystallin with NADP-dependent quinone reductase activity (QOR). Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and 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. 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. 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 | 860 | 1050 | 191 | Gaps:20 | 64.36 | 303 | 37.95 | 18.46 | 9e-32 | 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. |
| rpsblast_kog | gnl|CDD|36411 | 834 | 1055 | 222 | Gaps:9 | 66.37 | 336 | 30.04 | 21.52 | 3e-28 | KOG1197 KOG1197 KOG1197 Predicted quinone oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|36416 | 8 | 1055 | 1048 | Gaps:57 | 17.68 | 2376 | 29.29 | 22.14 | 5e-23 | KOG1202 KOG1202 KOG1202 Animal-type fatty acid synthase and related proteins [Lipid transport and metabolism]. |
| gnl|CDD|36412 | 849 | 1056 | 208 | Gaps:23 | 64.27 | 347 | 29.60 | 14.80 | 3e-17 | KOG1198 KOG1198 KOG1198 Zinc-binding oxidoreductase [Energy production and conversion General function prediction only]. |
| gnl|CDD|36410 | 853 | 1045 | 193 | Gaps:22 | 59.18 | 343 | 23.15 | 17.73 | 3e-13 | KOG1196 KOG1196 KOG1196 Predicted NAD-dependent oxidoreductase [General function prediction only]. |
| gnl|CDD|35248 | 866 | 995 | 130 | Gaps:7 | 38.70 | 354 | 30.66 | 15.33 | 3e-11 | KOG0025 KOG0025 KOG0025 Zn2+-binding dehydrogenase (nuclear receptor binding factor-1) [Transcription Energy production and conversion]. |
Gene Identifier
Genome Report System - copyright INRA 2011