|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1-374 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 810.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07141 66 MDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07141 146 VGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07141 226 DKVAFTGSTEVGKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07141 306 VKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKE 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07141 386 EIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVW 439
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-374 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 757.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07091 62 MDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07091 142 IGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07091 222 DKIAFTGSTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07091 302 VEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKE 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07091 382 EIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVW 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
1-374 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 628.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07142 62 MTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07142 142 IGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07142 222 DKVAFTGSTEVGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07142 302 VEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARD 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07142 382 EIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVW 435
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-374 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 606.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:PLN02466 196 IGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:PLN02466 276 DKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEF 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:PLN02466 356 VEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQD 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVW 489
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-374 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 575.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVGV 83
Cdd:cd07143 68 SKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 84 CGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKV 163
Cdd:cd07143 148 CGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 164 AFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVER 243
Cdd:cd07143 228 AFTGSTLVGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 244 SVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREEIF 323
Cdd:cd07143 308 FKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIF 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 704546197 324 GPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07143 388 GPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVW 438
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
3-374 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 571.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVG 82
Cdd:cd07144 67 GEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDK 162
Cdd:cd07144 147 VCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVE 242
Cdd:cd07144 227 IAFTGSTATGRLVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 243 RSVEKAKSR-VVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD---RGYFVQPTIFGDVQDNMTIA 318
Cdd:cd07144 306 KFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIV 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07144 386 KEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVW 441
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-374 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 557.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:pfam00171 48 TPAAERAAILRKAADLLEERKDELAELETLENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:pfam00171 127 LGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:pfam00171 207 RKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:pfam00171 286 VEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:pfam00171 366 EIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVW 419
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-374 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 556.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:PLN02766 79 MSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:PLN02766 159 IGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:PLN02766 239 DKVSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:PLN02766 319 VKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQD 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PLN02766 399 EIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIW 452
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-374 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 552.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSiSYLVDLDMVVKCLRYYAGWSDKFHGKTIPI-DGDFFCYTRHE 79
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSpDPGELAIVRRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:cd07078 96 PLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07078 176 VDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNA-AADRGYFVQPTIFGDVQDNMTIA 318
Cdd:cd07078 255 FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGKGYFVPPTVLTDVDPDMPIA 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07078 335 QEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVW 390
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-374 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 551.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHE 79
Cdd:COG1012 62 TPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRRE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:COG1012 141 PLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:COG1012 221 VDKISFTGSTAVGRRIAAAAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD-RGYFVQPTIFGDVQDNMTIA 318
Cdd:COG1012 300 FVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIA 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:COG1012 380 REEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVW 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1-374 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 528.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07119 56 LPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07119 135 VGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07119 215 DLVSFTGGTATGRSIMRAAAG-NVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD----RGYFVQPTIFGDVQDNMT 316
Cdd:cd07119 294 VAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMR 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07119 374 IVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVW 431
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-374 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 520.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07112 45 LSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07112 125 LGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDA-DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07112 205 DALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNA--AADRGYFVQPTIFGDVQDNMTI 317
Cdd:cd07112 285 FLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRI 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07112 365 AREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVW 421
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
1-374 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 518.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDldmvvkCLRYYAGWSDKFHGKTIPID-GDFFC 74
Cdd:cd07114 40 LTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetraqVRYLAE------WYRYYAGLADKIEGAVIPVDkGDYLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:cd07114 114 FTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA----DRGYFVQPTIFGD 310
Cdd:cd07114 273 SIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSgadlGAGYFFEPTILAD 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704546197 311 VQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07114 353 VTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVW 416
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-374 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 513.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07115 38 MDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07115 118 VGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07115 198 DKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07115 277 LERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07115 357 EIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVW 410
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1-374 |
6.48e-170 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 481.68 E-value: 6.48e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07093 38 MSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07093 118 VGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07093 198 DLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGN----AAADRGYFVQPTIFGDVQDNMT 316
Cdd:cd07093 277 LERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGrpelPDLEGGYFVEPTVITGLDNDSR 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07093 357 VAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVW 414
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
2-374 |
1.07e-162 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 464.51 E-value: 1.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPV 81
Cdd:cd07559 58 SVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07559 138 GVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDA-----DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 236
Cdd:cd07559 217 KLAFTGSTTVGRLIMQYAAE-NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 237 YHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA----DRGYFVQPTIFGDVQ 312
Cdd:cd07559 296 YDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlgglDKGYFYEPTLIKGGN 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704546197 313 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07559 376 NDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVW 437
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-374 |
4.20e-162 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 462.16 E-value: 4.20e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07090 38 TSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDV 160
Cdd:cd07090 117 LGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07090 196 AKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA-----DRGYFVQPTIFGDVQDNM 315
Cdd:cd07090 275 TERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDM 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07090 355 TIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCW 413
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-374 |
2.69e-156 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 448.48 E-value: 2.69e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPID----GDFFCYT 76
Cdd:cd07140 64 MNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISS 156
Cdd:cd07140 144 KREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 157 HMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 236
Cdd:cd07140 224 HPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 237 YHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMT 316
Cdd:cd07140 304 HDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMF 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 317 IAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07140 384 IAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVF 443
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
1-374 |
7.60e-156 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 446.56 E-value: 7.60e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:TIGR01804 54 MSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:TIGR01804 134 LGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:TIGR01804 214 AKVSFTGGVPTGKKIMAAAAG-HLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERF 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGG----NAAADRGYFVQPTIFGDVQDNMT 316
Cdd:TIGR01804 293 LARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGgrpeNVGLQNGFFVEPTVFADCTDDMT 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:TIGR01804 373 IVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVW 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-373 |
6.58e-155 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 443.60 E-value: 6.58e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEP 80
Cdd:cd07109 39 LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07109 118 HGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07109 198 DHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSkTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADR---GYFVQPTIFGDVQDNMTI 317
Cdd:cd07109 277 LERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRL 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07109 356 AQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQV 411
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-374 |
1.88e-154 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 443.55 E-value: 1.88e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLI-ERDRAyLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHE 79
Cdd:PRK13252 63 MTAMERSRILRRAVDILrERNDE-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTaGAAISSHMD 159
Cdd:PRK13252 142 PLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:PRK13252 221 IAKVSFTGGVPTGKKVMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNA----AADRGYFVQPTIFGDVQDNM 315
Cdd:PRK13252 300 FEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDM 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PRK13252 380 TIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICW 438
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
3-374 |
5.75e-153 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 438.71 E-value: 5.75e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWS---DKFHGKTIPI-DGDFFCYTRH 78
Cdd:cd07110 40 GAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHM 158
Cdd:cd07110 119 EPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 DVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH 238
Cdd:cd07110 199 GIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIAD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA--DRGYFVQPTIFGDVQDNMT 316
Cdd:cd07110 278 AFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSR 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07110 358 IWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVW 415
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-374 |
6.43e-153 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 435.12 E-value: 6.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIP-IDGDFFCYTRHE 79
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPsPDPGGEAYVRRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:cd06534 92 PLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd06534 172 VDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVekaksrvvgnpfdskteqgpqvdeeqfkkilgyissgkregakllcggnaaadrgyfvqpTIFGDVQDNMTIAR 319
Cdd:cd06534 251 FVEKLV------------------------------------------------------------TVLVDVDPDMPIAQ 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 320 EEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd06534 271 EEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVY 325
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-374 |
2.07e-150 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 432.15 E-value: 2.07e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPIDG-DFFCYTRHE 79
Cdd:cd07118 40 MSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:cd07118 119 PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07118 199 VDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADR-GYFVQPTIFGDVQDNMTIA 318
Cdd:cd07118 278 FVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIA 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVW 413
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-374 |
2.59e-149 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 430.34 E-value: 2.59e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPV 81
Cdd:cd07117 58 TVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07117 138 GVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07117 217 KLAFTGSTEVGRDVAIAAAK-KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGG----NAAADRGYFVQPTIFGDVQDNMTI 317
Cdd:cd07117 296 AKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRV 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07117 376 AQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-374 |
4.69e-147 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 424.22 E-value: 4.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 5 HRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAG------WSDKFHGKTIpidgdffcytRH 78
Cdd:cd07138 59 ERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHM 158
Cdd:cd07138 129 EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 DVDKVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH 238
Cdd:cd07138 209 DVDMVSFTGSTRAGKRVAEAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAA---ADRGYFVQPTIFGDVQDNM 315
Cdd:cd07138 288 EAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRpegLERGYFVKPTVFADVTPDM 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07138 368 TIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVH 426
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
3-373 |
1.52e-146 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 422.23 E-value: 1.52e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPI-DGDFFCYTRHEPV 81
Cdd:cd07103 40 ARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07103 119 GVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVG-HLIQKAAaeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07103 199 KISFTGSTAVGkLLMAQAA--DTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07103 277 VEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07103 357 ETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMV 409
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-373 |
4.09e-139 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 403.66 E-value: 4.09e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVG 82
Cdd:cd07108 40 ARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDK 162
Cdd:cd07108 120 VVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFAL-FFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07108 199 VTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKRE-GAKLLCGGNAAAD----RGYFVQPTIFGDVQDNMT 316
Cdd:cd07108 278 EKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWR 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07108 358 LAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWV 414
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
4-374 |
1.14e-138 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 404.11 E-value: 1.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGK-----TIPIDgDFFCYTRH 78
Cdd:PLN02467 72 AVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHM 158
Cdd:PLN02467 150 EPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 DVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH 238
Cdd:PLN02467 230 GVDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIAS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD--RGYFVQPTIFGDVQDNMT 316
Cdd:PLN02467 309 EFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQ 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PLN02467 389 IWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVW 446
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-374 |
1.30e-137 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 399.70 E-value: 1.30e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGK-TIPIDGDFFCYT--- 76
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 -RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAIS 155
Cdd:cd07089 119 vRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 156 SHMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 235
Cdd:cd07089 199 TDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 236 IYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA--DRGYFVQPTIFGDVQD 313
Cdd:cd07089 278 RYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDN 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 314 NMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07089 358 DMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVG 418
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
6-374 |
4.67e-137 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 398.24 E-value: 4.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGktiPIDGDFF----CYTRHEPV 81
Cdd:cd07092 43 RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEaGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07092 120 GVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07092 199 MVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISsGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREE 321
Cdd:cd07092 278 AALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 322 IFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07092 357 IFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVW 409
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-374 |
8.87e-136 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 395.95 E-value: 8.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHE 79
Cdd:cd07131 56 VPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07131 215 VDVVSFTGSTEVGERIGETCARPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAA----ADRGYFVQPTIFGDVQDNM 315
Cdd:cd07131 294 FLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDM 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07131 374 RIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITY 432
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-373 |
1.69e-135 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 395.08 E-value: 1.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIP-IDGDFFCYTRHEPVGVC 84
Cdd:cd07097 61 RADILDKAGDELEARKEELARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 85 GQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVA 164
Cdd:cd07097 140 GLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 165 FTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVERS 244
Cdd:cd07097 220 FTGSTAVGRRIAAAAA-ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEAL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 245 VEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNA--AADRGYFVQPTIFGDVQDNMTIAREEI 322
Cdd:cd07097 299 VERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEI 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 704546197 323 FGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07097 379 FGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVV 429
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-374 |
3.63e-135 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 393.05 E-value: 3.63e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLvDLDMVVKCLRYYAGWSDKfhGKTIPIDGDFFCYTRHEPVGVCG 85
Cdd:cd07106 43 RRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 86 QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGyGPTAGAAISSHMDVDKVAF 165
Cdd:cd07106 120 AIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 166 TGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVERSV 245
Cdd:cd07106 198 TGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 246 EKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREEIFGP 325
Cdd:cd07106 277 ALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGP 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 704546197 326 VMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07106 357 VLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVW 405
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
4-374 |
3.96e-135 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 394.28 E-value: 3.96e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGK-TIPIDGDFFCYTRHEPVG 82
Cdd:PRK13473 61 KERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDK 162
Cdd:PRK13473 141 VVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVE 242
Cdd:PRK13473 220 VSLTGSIATGKHVLSAAA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 243 RSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREG-AKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREE 321
Cdd:PRK13473 299 KLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQRE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 322 IFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PRK13473 379 VFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTW 431
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
6-374 |
8.92e-134 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 390.99 E-value: 8.92e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDK----FHGktipidgdffcytrHEPV 81
Cdd:cd07111 83 RARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLldteLAG--------------WKPV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVD 161
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07111 228 KVAFTGSTEVGRALRRATAGTG-KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREE 321
Cdd:cd07111 307 RKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEE 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 322 IFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07111 387 IFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVW 439
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
6-374 |
1.77e-133 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 389.43 E-value: 1.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSiSYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVGVCG 85
Cdd:cd07107 43 RARMLRELATRLREHAEELALIDALDCGNPVS-AMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 86 QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAF 165
Cdd:cd07107 122 RIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 166 TGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFN-QGQCCCAGSRTYVQEDIYHEFVERS 244
Cdd:cd07107 201 IGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 245 VEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD----RGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07107 280 VERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIARE 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07107 360 EIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-373 |
1.88e-133 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 389.63 E-value: 1.88e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTI---PIDGDffCYTR 77
Cdd:cd07139 57 LSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGyGPTAGAAISSH 157
Cdd:cd07139 135 REPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07139 214 PGVDKVSFTGSTAAGRRIAAVCGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGN--AAADRGYFVQPTIFGDVQDNM 315
Cdd:cd07139 293 DEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDM 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07139 373 RIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTV 430
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
3-374 |
1.40e-132 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 387.39 E-value: 1.40e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHEPV 81
Cdd:cd07088 56 AIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07088 135 GVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07088 215 MISLTGSTEAGQKIMEAAAE-NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFM 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA-DRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07088 294 EKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQE 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07088 374 EIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETY 427
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
3-374 |
7.69e-131 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 383.34 E-value: 7.69e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVG 82
Cdd:cd07116 59 VAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDK 162
Cdd:cd07116 139 VVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSD--ADMDWAVDQA--HFALF-FNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07116 218 VAFTGETTTGRLIMQYASE-NIIPVTLELGGKSPNIFFADvmDADDAFFDKAleGFVMFaLNQGEVCTCPSRALIQESIY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAA-----ADRGYFVQPTIFGdvQ 312
Cdd:cd07116 297 DRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelgglLGGGYYVPTTFKG--G 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704546197 313 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07116 375 NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVW 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
6-374 |
1.31e-124 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 368.07 E-value: 1.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPVGVCG 85
Cdd:PRK09847 83 RKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 86 QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAF 165
Cdd:PRK09847 163 AIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 166 TGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDA-DMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVERS 244
Cdd:PRK09847 243 TGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 245 VEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGaKLLCGGNAAADRGYfVQPTIFGDVQDNMTIAREEIFG 324
Cdd:PRK09847 323 KQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFG 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 704546197 325 PVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PRK09847 401 PVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVF 450
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
1-374 |
2.91e-124 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 366.38 E-value: 2.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTI------PIDGDFFC 74
Cdd:cd07113 57 TTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTaGAAI 154
Cdd:cd07113 137 FTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07113 216 ISHPDVAKVSFTGSVATGKKIGRQAA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDN 314
Cdd:cd07113 295 SKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSAD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVW 434
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-374 |
6.81e-124 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 366.55 E-value: 6.81e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPV 81
Cdd:cd07124 89 PPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07124 168 GVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAA-----ESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 236
Cdd:cd07124 248 FIAFTGSREVGLRIYERAAkvqpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 237 YHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGaKLLCGGNAAAD--RGYFVQPTIFGDVQDN 314
Cdd:cd07124 328 YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPD 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07124 407 HRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLY 466
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
6-373 |
1.55e-123 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 363.00 E-value: 1.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPIDGD-FFCYTRHEPVGVC 84
Cdd:cd07104 24 RAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIAILREAAGLPRRPEGEILPSDVPgKESMVRRVPLGVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 85 GQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLS-ALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKV 163
Cdd:cd07104 103 GVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 164 AFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVER 243
Cdd:cd07104 183 SFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 244 SVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAadrGYFVQPTIFGDVQDNMTIAREEIF 323
Cdd:cd07104 262 LVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIF 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 704546197 324 GPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07104 339 GPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-373 |
4.95e-121 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 357.41 E-value: 4.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLvDLDMVVKCLRYYAGWSDKFHGKTIPIDG-DFFCYTRHEPV 81
Cdd:cd07150 42 PSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:cd07150 121 GVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVG-HLIQKAAAesNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07150 201 MVTFTGSTAVGrEIAEKAGR--HLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAadrGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07150 279 VKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFRE 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07150 356 ETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMV 408
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1-373 |
1.22e-120 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 356.66 E-value: 1.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPIDG-----DFFCY 75
Cdd:cd07145 40 LPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 76 TRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAIS 155
Cdd:cd07145 119 TVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 156 SHMDVDKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 235
Cdd:cd07145 199 TNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 236 IYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNaaADRGYFVQPTIFGDVQDNM 315
Cdd:cd07145 278 VYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDM 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGV 413
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1-373 |
4.71e-120 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 354.98 E-value: 4.71e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPysISY-LVDLDMVVKCLRYYAGWSDKFHGKTIPIDG-----DFFC 74
Cdd:cd07149 40 LPAYERAEILERAAQLLEERREEFARTIALEAGKP--IKDaRKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAesnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07149 198 VTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAaadRGYFVQPTIFGDVQDN 314
Cdd:cd07149 275 DIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPD 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07149 352 MKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGV 410
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-363 |
1.21e-115 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 344.55 E-value: 1.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHEPV 81
Cdd:cd07086 56 APRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEA----GFPPGVVNIVPGYGPtAGAAISSH 157
Cdd:cd07086 135 GVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIQKAAAESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07086 214 PRVPLVSFTGSTEVGRRVGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAA--ADRGYFVQPTIFGDVQDNM 315
Cdd:cd07086 293 DEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDA 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANY 363
Cdd:cd07086 373 RIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFR 420
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-373 |
2.26e-115 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 344.37 E-value: 2.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPI-DGDFFCYTRHEPV 81
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 161
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 162 KVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREE 321
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREE 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 704546197 322 IFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PLN02278 401 VFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIV 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
2-374 |
1.43e-107 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 323.14 E-value: 1.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRHEPV 81
Cdd:cd07120 40 DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 82 GVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEA-GFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07120 119 GVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07120 199 DVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD---RGYFVQPTIFGDVQDNMTI 317
Cdd:cd07120 278 RDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADI 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07120 358 VQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVW 414
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
6-373 |
6.63e-105 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 316.30 E-value: 6.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID-----GDFFCYTRHEP 80
Cdd:cd07094 45 RMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:cd07094 124 VGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAesnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEF 240
Cdd:cd07094 204 AMLSFTGSAAVGEALRANAG---GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 241 VERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAaadRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07094 281 IEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTE 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07094 358 ETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGV 410
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-374 |
6.80e-105 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 315.17 E-value: 6.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKF-HGKTIPIDGDFfCYTRHEPVG 82
Cdd:cd07100 21 AERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAFlADEPIETDAGK-AYVRYEPLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLlmqaWK----LGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHM 158
Cdd:cd07100 99 VVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAIIADPR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 dVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH 238
Cdd:cd07100 175 -VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIA 318
Cdd:cd07100 253 EFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAY 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07100 333 DEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-373 |
7.44e-105 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 316.09 E-value: 7.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLvDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFF----CYTRHE 79
Cdd:cd07099 40 EGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EVLLALEAIDWAARNAPRVLAPRKVPTGLLMpnkkATVEYR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISShmD 159
Cdd:cd07099 119 PYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--G 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07099 197 VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAR 319
Cdd:cd07099 276 FVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMR 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 320 EEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07099 356 EETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAV 409
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
10-371 |
8.08e-104 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 312.06 E-value: 8.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 10 LNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID---GDFFCYTRhePVGVCGQ 86
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 87 IIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFT 166
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 167 GSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVERSVE 246
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 247 KAKSRVVGNPFD-SKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIAREEIFGP 325
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 704546197 326 VMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAG 371
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
79-373 |
3.02e-101 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 307.31 E-value: 3.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSA-LYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSH 157
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEH 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07151 209 PVPRLISFTGSTPVGRHIGELAGR-HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAadrGYFVQPTIFGDVQDNMTI 317
Cdd:cd07151 288 DEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEI 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07151 365 AREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMT 420
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
4-373 |
6.62e-100 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 303.46 E-value: 6.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKClRYYAGWSDKF-----HGKTIPIdgdffcYTR- 77
Cdd:cd07101 40 AERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA-RYYARRAERLlkprrRRGAIPV------LTRt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 ---HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:cd07101 113 tvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHmdVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07101 193 VDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRG-YFVQPTIFGDVQD 313
Cdd:cd07101 270 SVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTE 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 314 NMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07101 350 DMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTV 409
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-371 |
1.31e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 304.55 E-value: 1.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDLdmvvkcLRYYA----GWSDkfhGKTI-PIDGD 71
Cdd:PRK03137 93 SPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAeadadTAEAIDF------LEYYArqmlKLAD---GKPVeSRPGE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 72 FFCYtRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAG 151
Cdd:PRK03137 164 HNRY-FYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 152 AAISSHMDVDKVAFTGSTEVGHLIQKAAAESN-----LKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCA 226
Cdd:PRK03137 243 DYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 227 GSRTYVQEDIYHEFVERSVEKAKSRVVGNPfDSKTEQGPQVDEEQFKKILGYISSGKREGaKLLCGGNAAADRGYFVQPT 306
Cdd:PRK03137 323 CSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPT 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 307 IFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAG 371
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG 465
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-373 |
6.17e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 303.34 E-value: 6.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDmVVKCLRYYAGWSDKF-----HGKTIPIdgdffcYTR 77
Cdd:PRK09407 75 VRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLD-VALTARYYARRAPKLlaprrRAGALPV------LTK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 ----HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAA 153
Cdd:PRK09407 148 ttelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 154 ISSHmdVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 233
Cdd:PRK09407 228 LVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVH 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 234 EDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRG-YFVQPTIFGDVQ 312
Cdd:PRK09407 305 ESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVT 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 313 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PRK09407 385 PDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTV 445
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
1-373 |
3.46e-98 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 298.82 E-value: 3.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGkpySISY--LVDLDMVVKCLRYYAGWSDKFHGKTIPIDGDFFCYTRH 78
Cdd:cd07152 32 TPPRERAAVLRRAADLLEEHADEIADWIVRESG---SIRPkaGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYV-ANLIKEAGFPPGVVNIVPGyGPTAGAAISSH 157
Cdd:cd07152 109 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViARLFEEAGLPAGVLHVLPG-GADAGEALVED 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07152 188 PNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAaadRGYFVQPTIFGDVQDNMTI 317
Cdd:cd07152 267 DAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DGLFYRPTVLSGVKPGMPA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGML 399
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-373 |
5.43e-98 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 298.50 E-value: 5.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIPID-----GDFFCYTR 77
Cdd:cd07146 39 RYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-RYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSH 157
Cdd:cd07146 118 REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIqkaAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:cd07146 198 PDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAaadRGYFVQPTIFGDVQDNMTI 317
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAEL 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07146 352 VTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTV 407
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-373 |
5.85e-96 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 294.04 E-value: 5.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIP-IDGDFFCYTRHEPVG 82
Cdd:cd07085 60 LKRQQVMFKFRQLLEENLDELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDK 162
Cdd:cd07085 139 VVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVE 242
Cdd:cd07085 218 VSFVGSTPVGEYIYERAA-ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 243 RSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA----DRGYFVQPTIFGDVQDNMTIA 318
Cdd:cd07085 297 KLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIY 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07085 377 KEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV 431
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
6-373 |
7.72e-95 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 290.30 E-value: 7.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPysISYLV-DLDMVVKCLRYYAGWSDK-FHGKTIPIDGDFFCYTRHEPVGV 83
Cdd:cd07102 42 RKAIVTRAVELLAANTDEIAEELTWQMGRP--IAQAGgEIRGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 84 CGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHmDVDKV 163
Cdd:cd07102 120 VLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 164 AFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFVER 243
Cdd:cd07102 199 SFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 244 SVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGN---AAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07102 278 FVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMRE 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704546197 321 EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07102 358 ETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTV 410
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
1-373 |
2.24e-93 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 286.45 E-value: 2.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIPIDGD-----FFCY 75
Cdd:cd07147 40 LPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 76 TRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGygPTAGAAI- 154
Cdd:cd07147 119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAEsnlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07147 197 VTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAaadRGYFVQPTIFGDVQDN 314
Cdd:cd07147 274 SVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPD 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGV 409
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1-373 |
1.26e-91 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 281.39 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPySISYLVDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHE 79
Cdd:cd07105 19 TPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQIIGGSIPSDkPGTLAMVVKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIV---PGYGPTAGAAISS 156
Cdd:cd07105 98 PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEALIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 157 HMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 236
Cdd:cd07105 178 HPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 237 YHEFVERSVEKAKSRvvgnpFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAA-DRGYFVQPTIFGDVQDNM 315
Cdd:cd07105 257 ADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADEsPSGTSMPPTILDNVTPDM 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07105 332 DIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
6-373 |
1.86e-90 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 279.84 E-value: 1.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPY---------SISYLVDLDMVVKclryyagwsdKFHGKTIPIDGDFF--- 73
Cdd:cd07082 63 RIDCLHKFADLLKENKEEVANLLMWEIGKTLkdalkevdrTIDYIRDTIEELK----------RLDGDSLPGDWFPGtkg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 74 --CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAG 151
Cdd:cd07082 133 kiAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 152 AAISSHMDVDKVAFTGSTEVGHLIQKAAAesnLKRVTLELGGKSPNIIMSDADMDWAVDQ-AHFALFFNqGQCCCAGSRT 230
Cdd:cd07082 213 DPLVTHGRIDVISFTGSTEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEiVKGALSYS-GQRCTAIKRV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 231 YVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNaaADRGYFVQPTIFGD 310
Cdd:cd07082 289 LVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDP 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704546197 311 VQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07082 367 VTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTV 429
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
2-374 |
1.68e-89 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 278.67 E-value: 1.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKF--HGKTIPIDGDFFCYTrHE 79
Cdd:TIGR01237 89 DPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELakGKPVNSREGETNQYV-YT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAA-----ESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAkvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGaKLLCGGNAAADRGYFVQPTIFGDVQDN 314
Cdd:TIGR01237 327 KVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRK 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:TIGR01237 406 ARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLY 465
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-373 |
2.59e-86 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 269.47 E-value: 2.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDLdmvvkcLRYYAGWSDKFHGKTIP-IDGDFFC 74
Cdd:PRK11241 67 LTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAeakgeISYAASF------IEWFAEEGKRIYGDTIPgHQADKRL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:PRK11241 141 IVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGEL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:PRK11241 221 TSNPLVRKLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDN 314
Cdd:PRK11241 300 GVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPAN 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PRK11241 380 AKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIV 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
77-373 |
1.30e-80 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 254.15 E-value: 1.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 RHEPVGVCGQIIPWNFPL--LmqawkLGPALA---TGNVVVMKVAEQTPLSALYVANLIKEA----GFPPGVVNIVPGYG 147
Cdd:cd07098 117 EYEPLGVVGAIVSWNYPFhnL-----LGPIIAalfAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 148 PTaGAAISSHMDVDKVAFTGSTEVGHLIQKAAAESnLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAG 227
Cdd:cd07098 192 ET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 228 SRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAAD----RGYFV 303
Cdd:cd07098 270 ERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYF 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 304 QPTIFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07098 350 PPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
6-374 |
6.31e-74 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 237.86 E-value: 6.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYsISYLVDLDMVVKCLRYYAGWSDKFHGKTI------PIDGDFFcytrHE 79
Cdd:cd07083 79 RARLLLKAADLLRRRRRELIATLTYEVGKNW-VEAIDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESF----YV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 159
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAE-----SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:cd07083 234 IRGINFTGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGaKLLCGGNAAADRGYFVQPTIFGDVQDN 314
Cdd:cd07083 314 GAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPK 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704546197 315 MTIAREEIFGPVMQILKFKTIE--EVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:cd07083 393 ARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLY 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-361 |
6.46e-74 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 237.10 E-value: 6.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDL-DMVVkclryyaGWSDKFHGKTIPID-GDFFCY 75
Cdd:cd07130 55 APKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPeglgeVQEMIDIcDFAV-------GLSRQLYGLTIPSErPGHRMM 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 76 TRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEA----GFPPGVVNIVPGyGPTAG 151
Cdd:cd07130 128 EQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 152 AAISSHMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTY 231
Cdd:cd07130 207 EALVKDPRVPLVSFTGSTAVGRQVGQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 232 VQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFgDV 311
Cdd:cd07130 286 VHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EG 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 704546197 312 QDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKA 361
Cdd:cd07130 365 LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-373 |
1.33e-73 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 237.48 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 5 HRGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDLdmvvkcLRYYAGWSDK-FHGKTIPidgdffCYTRH 78
Cdd:cd07125 92 ERAEILEKAADLLEANRGELIALAAAEAGKTLAdadaeVREAIDF------CRYYAAQARElFSDPELP------GPTGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EP--------VGVCgqIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTA 150
Cdd:cd07125 160 LNglelhgrgVFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 151 GAAISSHMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGS 228
Cdd:cd07125 238 GEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 229 RTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREgAKLLCGGNAAADRGYFVQPTIF 308
Cdd:cd07125 318 LLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGII 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 309 GDVqdNMTIAREEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07125 397 EIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNL 461
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
6-374 |
3.88e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 234.63 E-value: 3.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlvdlDMVVKC---LRYYAGWSDKFHGKTiPID----GDFFCYTRH 78
Cdd:PRK09406 47 RARWANAAADLLEAEADQVAALMTLEMGKTLASAK----AEALKCakgFRYYAEHAEALLADE-PADaaavGASRAYVRY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLlmqaWKL----GPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPgYGPTAGAAI 154
Cdd:PRK09406 122 QPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIqKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQE 234
Cdd:PRK09406 197 LRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDN 314
Cdd:PRK09406 276 DVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPD 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PRK09406 356 MRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVF 415
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
74-373 |
4.39e-68 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 220.56 E-value: 4.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 74 CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGygptaGAA 153
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 154 ISSH---MDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRT 230
Cdd:cd07134 168 VAQAlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 231 YVQEDIYHEFVERsVEKAKSRVVGNpfDSKTEQGPQ----VDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVqPT 306
Cdd:cd07134 247 FVHESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PT 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 307 IFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGV 389
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
2-373 |
2.99e-64 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 210.46 E-value: 2.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLI-ERDRAYLAALETlDNGKPYSISYLVDLDMVVKCLRYY----AGWSDKFHGKTIPIDGDFFCYT 76
Cdd:cd07087 18 SLEWRKAQLKALKRMLtENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHAlkhlKKWMKPRRVSVPLLLQPAKAYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 RHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGyGPTAGAA 153
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 154 ISSHmDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 233
Cdd:cd07087 172 LLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 234 EDIYHEFVERSVEKAKSRVVGNPFDSKtEQGPQVDEEQFKKILGYIssgkrEGAKLLCGGNA-AADRgyFVQPTIFGDVQ 312
Cdd:cd07087 250 ESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLL-----DDGKVVIGGQVdKEER--YIAPTILDDVS 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 313 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
3-373 |
5.25e-64 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 210.74 E-value: 5.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYsISYLVDLDMVVKCLRYYAGWSDKFHGKTIPID-----GDFFCYTR 77
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPL-VDAKVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSH 157
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 mdvdKVA---FTGSTEVG-HLIQKAAAESnlkRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 233
Cdd:cd07148 202 ----RVAffsFIGSARVGwMLRSKLAPGT---RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 234 EDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYfvQPTIFGDVQD 313
Cdd:cd07148 275 AEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPR 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 314 NMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAV 412
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
6-373 |
2.30e-62 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 205.97 E-value: 2.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPY------SISYLVDLDMVVKCLRYYAGwsdkfhGKTIPIdGDFFCYTRHE 79
Cdd:cd07095 24 RAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHERTG------ERATPM-AQGRAVLRHR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGyGPTAGAAISSHMD 159
Cdd:cd07095 97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEALAAHEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 160 VDKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH- 238
Cdd:cd07095 176 IDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFgDVQDNMTIA 318
Cdd:cd07095 256 AFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGII-DVTDAADVP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07095 335 DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
2-373 |
3.56e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 205.41 E-value: 3.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLIERDRAYLA-ALETLDNGKPYSISYLVDLDMVVKCLRYY----AGWSdkfhgKTIPIDGDFF--- 73
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAeAISADFGHRSRHETLLAEILPSIAGIKHArkhlKKWM-----KPSRRHVGLLflp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 74 --CYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTP-LSALyVANLIKEAgFPPGVVNIVPGyG 147
Cdd:cd07133 93 akAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 148 PTAGAAISShMDVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAG 227
Cdd:cd07133 167 ADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 228 SRTYVQEDIYHEFVERSVEKAKSR---VVGNPfdsktEQGPQVDEEQFKKILGYISSGKREGAKLL-CGGNA-AADRGYF 302
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLNPAGeDFAATRK 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 303 VQPTIFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV 390
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-373 |
2.43e-61 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 212.75 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGK--PYSISYL---VDLdmvvkcLRYYAGWSDKFHGKTIPIDGdffcytr 77
Cdd:PRK11904 606 VEERAAILERAADLLEANRAELIALCVREAGKtlQDAIAEVreaVDF------CRYYAAQARRLFGAPEKLPG------- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 hePVG-------------VCgqIIPWNFPLlmqAWKLGP---ALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVN 141
Cdd:PRK11904 673 --PTGesnelrlhgrgvfVC--ISPWNFPL---AIFLGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 142 IVPGYGPTAGAAISSHMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFN 219
Cdd:PRK11904 746 LLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRS 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 220 QGQCCCAGSRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREgAKLLCGGNAAAD- 298
Cdd:PRK11904 826 AGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGt 904
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 299 -RGYFVQPTIFGdvQDNMTIAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PRK11904 905 eNGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNV 980
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
2-364 |
1.91e-60 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 201.19 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 2 DASHRGKLLNRLADLI-ERDRAYLAALEtLDNGKPYSISYLVDLDMVVKCLRYY----AGWSDK---------FHGKtip 67
Cdd:cd07136 18 DVEFRIEQLKKLKQAIkKYENEILEALK-KDLGKSEFEAYMTEIGFVLSEINYAikhlKKWMKPkrvktpllnFPSK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 68 idgdffCYTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVP 144
Cdd:cd07136 94 ------SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 145 GYGPTAGAAISSHMDvdKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCC 224
Cdd:cd07136 164 GGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 225 CAGSRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKtEQGPQVDEEQFKKILGYISSGkregaKLLCGGNAAADRGYfVQ 304
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGNTDRETLY-IE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 305 PTIFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYV 364
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKV 373
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
1-374 |
1.11e-58 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 197.83 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 1 MDASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDkfhgktipidgDFFCYTRHEP 80
Cdd:TIGR01238 93 TPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVR-----------DVLGEFSVES 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 160
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYH 238
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 239 EFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREG---AKLLCGGNAAADRGYFVQPTIFGdvQDNM 315
Cdd:TIGR01238 321 RVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDI 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 316 TIAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:TIGR01238 399 AELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCY 459
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-373 |
1.23e-58 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 197.41 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 4 SHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISyLVDLDMVVKCLRYYAGWSDKFHGKTIP-IDGDFFCYTRHEPVG 82
Cdd:TIGR01722 60 AQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 83 VCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDK 162
Cdd:TIGR01722 139 VCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 163 VAFTGSTEVGHLIQKAAAESNlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSrTYVQEDIYHEFVE 242
Cdd:TIGR01722 218 VSFVGSTPIGRYIHTTGSAHG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 243 RSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGY----FVQPTIFGDVQDNMTIA 318
Cdd:TIGR01722 296 EIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAY 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 319 REEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:TIGR01722 376 QEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQV 430
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-373 |
1.45e-57 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 202.09 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAAL---E---TLDNGkpysISYL---VDLdmvvkcLRYYAGWSDKfhgktipidgDFF 73
Cdd:COG4230 614 VEERAAILERAADLLEAHRAELMALlvrEagkTLPDA----IAEVreaVDF------CRYYAAQARR----------LFA 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 74 CYTRHEPVGVCGQIIPWNFPLlmqAWKLGP---ALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTA 150
Cdd:COG4230 674 APTVLRGRGVFVCISPWNFPL---AIFTGQvaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETV 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 151 GAAISSHMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGS 228
Cdd:COG4230 751 GAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALR 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 229 RTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGaKLL--CGGNAAADRGYFVQPT 306
Cdd:COG4230 831 VLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVhqLPLPEECANGTFVAPT 909
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704546197 307 IF--GDVQDnmtiAREEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:COG4230 910 LIeiDSISD----LEREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNV 976
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-373 |
1.98e-57 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 193.21 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMQawkLGP---ALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAG 151
Cdd:cd07135 103 RIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 152 AAISSHMDvdKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTY 231
Cdd:cd07135 179 ALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 232 VQEDIYHEFVERSvEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKRegaKLLCGGNA-AADRgyFVQPTIFGD 310
Cdd:cd07135 256 VDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKG---KVVIGGEMdEATR--FIPPTIVSD 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704546197 311 VQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
3-373 |
2.60e-56 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.55 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGK--PYSISYL---VDLdmvvkcLRYYAGwsdkfHGKTIPIDgdffcyTR 77
Cdd:PRK11905 611 AAERAAILERAADLMEAHMPELFALAVREAGKtlANAIAEVreaVDF------LRYYAA-----QARRLLNG------PG 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLlmqAWKLG---PALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:PRK11905 674 HKPLGPVVCISPWNFPL---AIFTGqiaAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 SSHMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYV 232
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 233 QEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLL-CGGNAAADRGYFVQPTIFgDV 311
Cdd:PRK11905 831 QEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI-EI 909
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704546197 312 qDNMTIAREEIFGPVMQILKFKT--IEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PRK11905 910 -DSISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNI 972
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
78-374 |
3.15e-52 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 180.06 E-value: 3.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSH 157
Cdd:PRK13968 124 YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MdVDKVAFTGSTEVGHLIqKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIY 237
Cdd:PRK13968 204 R-IAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFGDVQDNMTI 317
Cdd:PRK13968 282 SAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTA 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 704546197 318 AREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTVW 374
Cdd:PRK13968 362 FREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVF 418
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
87-357 |
9.45e-52 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 180.09 E-value: 9.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 87 IIPWNFPLLMQAWKLGPALaTGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFT 166
Cdd:cd07123 177 VSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 167 GSTEVGHLIQKAAAES-----NLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIYHEFV 241
Cdd:cd07123 256 GSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 242 ERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKRE-GAKLLCGGNAAADRGYFVQPTIFGDVQDNMTIARE 320
Cdd:cd07123 336 ERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTE 415
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 704546197 321 EIFGPVMQILKF--KTIEEVIERAND-SKYGLAAAVFTKD 357
Cdd:cd07123 416 EIFGPVLTVYVYpdSDFEETLELVDTtSPYALTGAIFAQD 455
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
3-356 |
8.20e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 174.64 E-value: 8.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGK--PYSISylvDLDMVVKCLRYYAGWSDKFHGKTIPID-GDFFCYTRHE 79
Cdd:PLN02315 77 APKRGEIVRQIGDALRAKLDYLGRLVSLEMGKilAEGIG---EVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSAL----YVANLIKEAGFPPGVVNIVPGyGPTAGAAIS 155
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 156 SHMDVDKVAFTGSTEVGHLIQKAAaESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 235
Cdd:PLN02315 233 KDTRIPLVSFTGSSKVGLMVQQTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 236 IYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGNAAADRGYFVQPTIFgDVQDNM 315
Cdd:PLN02315 312 IYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDA 390
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 704546197 316 TIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTK 356
Cdd:PLN02315 391 DVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTR 431
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-373 |
6.79e-49 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 174.16 E-value: 6.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYSISYlVDLDMVVKCLRYYAGWSDKFHGKTIP-IDGDFFCYTRHEPVGVC 84
Cdd:PLN02419 175 RQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVC 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 85 GQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGaAISSHMDVDKVA 164
Cdd:PLN02419 254 AGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 165 FTGSTEVG-HLIQKAAAESnlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDIyHEFVER 243
Cdd:PLN02419 333 FVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 244 SVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKLLCGGN----AAADRGYFVQPTIFGDVQDNMTIAR 319
Cdd:PLN02419 410 LVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGNFIGPTILSGVTPDMECYK 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 320 EEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PLN02419 490 EEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI 543
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
58-373 |
9.22e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 171.48 E-value: 9.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 58 SDKFHGKtipiDGDFFCYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPP 137
Cdd:PLN00412 140 SDSFPGN----ERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 138 GVVNIVPGYGPTAGAAISSHMDVDKVAFTGStEVGHLIQKAAAESNLKrvtLELGGKSPNIIMSDADMDWAVDQAHFALF 217
Cdd:PLN00412 216 GLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 218 FNQGQCCCAGSRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSkTEQGPQVDEEQFKKILGYISSGKREGAKLLcggNAAA 297
Cdd:PLN00412 292 SYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVVSESSANFIEGLVMDAKEKGATFC---QEWK 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 298 DRGYFVQPTIFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:PLN00412 368 REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTV 443
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
77-374 |
1.01e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 171.29 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 RHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGyGPTAGAAISS 156
Cdd:PRK09457 131 RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 157 HMDVDKVAFTGSTEVGHLIQKAAAESNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQEDI 236
Cdd:PRK09457 210 HPDIDGLLFTGSANTGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 237 Y-HEFVERSVEKAKSRVVGNPFDSKTE-QGPQVDEEQFKKILG----YISSGkreGAKLLCGGNAAADRGyFVQPTIFgD 310
Cdd:PRK09457 290 QgDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAaqaqLLALG---GKSLLEMTQLQAGTG-LLTPGII-D 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 311 VQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV-W 374
Cdd:PRK09457 365 VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnW 429
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
74-357 |
1.64e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 170.98 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 74 CYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGYGPTAGAA 153
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 154 ISSHMDVdkVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQ 233
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 234 EDIYHEFVErSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYIssgKREGAKLLCGGNA-AADRgyFVQPTIFGDVQ 312
Cdd:PTZ00381 259 RSIKDKFIE-ALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGEVdIENK--YVAPTIIVNPD 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 704546197 313 DNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 357
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED 377
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
5-369 |
6.08e-48 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 169.97 E-value: 6.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 5 HRGKLLNRLADLIE-RDRAYLAALETLDNGK-PY-----SISYLVDLdmvvkcLRYYAGWSDKFHGKTiPIDGD-FFCYT 76
Cdd:TIGR01236 92 DRAAIFLKAADLLSgPYRYEILAATMLGQSKtVYqaeidAVAELIDF------FRFNVKYARELYAQQ-PISAPgEWNRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 77 RHEPV-GVCGQIIPWNFPLLMQAWKLGPALaTGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAIS 155
Cdd:TIGR01236 165 EYRPLeGFVYAISPFNFTAIAGNLAGAPAL-MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 156 SHMDVDKVAFTGSTEV-GHLIQKAAAE----SNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRT 230
Cdd:TIGR01236 244 ADPDLAGIHFTGSTNTfKHLWKKVAQNldryHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 231 YVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKL--LCGGNAAADRGYFVQPTIF 308
Cdd:TIGR01236 324 YVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEALtiLYGGKYDDSQGYFVEPTVV 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704546197 309 GDVQDNMTIAREEIFGPVMQIL-----KFKTIEEVIERAndSKYGLAAAVFTKDLDKANYVSQGLR 369
Cdd:TIGR01236 404 ESKDPDHPLMSEEIFGPVLTVYvypddKYKEILDLVDST--SQYGLTGAVFAKDRKAILEADKKLR 467
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
6-356 |
3.05e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 166.69 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKPYS-----ISYLVDLdmvvkcLRYYAGW-SDKFHGKTipidgdffcytrHE 79
Cdd:PRK11809 706 RAAILERAADLMEAQMQTLMGLLVREAGKTFSnaiaeVREAVDF------LRYYAGQvRDDFDNDT------------HR 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVG--VCgqIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAGFPPGVVNIVPGYGPTAGAAISSH 157
Cdd:PRK11809 768 PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVAD 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 158 MDVDKVAFTGSTEVGHLIQKAAA---ESNLKRVTL--ELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYV 232
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 233 QEDIyhefVERSVEKAK----SRVVGNPFDSKTEQGPQVDEEQFKKILGYISSGKREGAKL--LCGGNAAA-DRGYFVQP 305
Cdd:PRK11809 926 QDDV----ADRTLKMLRgamaECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqAARENSEDwQSGTFVPP 1001
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704546197 306 TI-----FGDVQdnmtiarEEIFGPVMQILKFK--TIEEVIERANDSKYGLAAAVFTK 356
Cdd:PRK11809 1002 TLieldsFDELK-------REVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTR 1052
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
6-357 |
2.89e-43 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 155.84 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLI-ERDRAYLAALEtLDNGKPYSISYLVDLDMVVKCLRY----YAGWS-DKFHGKTIP--IDGdffCYTR 77
Cdd:cd07132 22 RIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEWMkPEPVKKNLAtlLDD---VYIY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 78 HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLI-----KEAgFPpgVVnivpgygpTAGA 152
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC-YP--VV--------LGGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 153 AISSHM---DVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSr 229
Cdd:cd07132 167 EETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 230 tYV--QEDIYHEFVERSVEKAKSRVVGNPFDSKtEQGPQVDEEQFKKILGYISSGkregaKLLCGGN-AAADRgyFVQPT 306
Cdd:cd07132 245 -YVlcTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLLSGG-----KVAIGGQtDEKER--YIAPT 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 704546197 307 IFGDVQDNMTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 357
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
10-373 |
9.26e-40 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 146.02 E-value: 9.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 10 LNRLADLI-ERDRAYLAALETlDNGKPYSISYLVDLDMVVK----CLRYYAGWSDKFHGK----TIPIDGDFFCytrhEP 80
Cdd:cd07137 27 LKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSscklAIKELKKWMAPEKVKtpltTFPAKAEIVS----EP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 81 VGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAgFPPGVVNIVPGyGPTAGAAISSHmDV 160
Cdd:cd07137 102 LGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-KW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 161 DKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALF-FNQGQCCCAGSRTYVQEDIYHE 239
Cdd:cd07137 179 DKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 240 FVERSVEKAKSRVVGNPFDSKtEQGPQVDEEQFKKiLGYISSGKREGAKLLCGGNAAADRGYfVQPTIFGDVQDNMTIAR 319
Cdd:cd07137 258 LIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQR-LSRLLDDPSVADKIVHGGERDEKNLY-IEPTILLDPPLDSSIMT 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 320 EEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKDLDKANYVSQGLRAGTV 373
Cdd:cd07137 335 EEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV 388
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
79-357 |
9.23e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 122.14 E-value: 9.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKeAGFPPGVVNIVPGyGPTAGAAISSHm 158
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 DVDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNI---IMSDADMDWAVDQAHFALFFN-QGQCCCAGSRTYVQE 234
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 235 DIYHEFVERSVEKAKSRVVGNPFDSKTeQGPQVDEEQFKKILGYISSgKREGAKLLCGGNAAADRgYFVQPTIFGDVQDN 314
Cdd:PLN02203 263 RFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPTILLNPPLD 339
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 704546197 315 MTIAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 357
Cdd:PLN02203 340 SDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN 382
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
3-357 |
9.50e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 116.18 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 3 ASHRGKLLNRLADLIERDRAYLAALETLDNGKPYSISYLVDLDMVVKCLRYYAGWSDKFH---GKTIPIDGDFFCYTRHE 79
Cdd:cd07084 20 LPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPhepGNHLGQGLKQQSHGYRW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIKEAG-FPPGVVNIVPGYGPTaGAAISSHM 158
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-MQALLLHP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 DVDKVAFTGSTEVGhliQKAAAESNLKRVTLELGGKSPNIIMSDAD-MDWAVDQAHFALFFNQGQCCCAGSRTYVQEDiy 237
Cdd:cd07084 179 NPKMVLFTGSSRVA---EKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPEN-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 hEFVERSVEKAKSRVvgnpfDSKTEQGPQVDEEQFKKILGYISS-GKREGAKLLCGG------NAAADRGYFVQPTIF-- 308
Cdd:cd07084 254 -WSKTPLVEKLKALL-----ARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVLLFSGkelknhSIPSIYGACVASALFvp 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 704546197 309 GDVQDNMTIA-REEIFGPVMQILKFK-----TIEEVIERANDSkygLAAAVFTKD 357
Cdd:cd07084 328 IDEILKTYELvTEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSND 379
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
6-357 |
8.09e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 111.33 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLI--ERDRAYLAALEtldNGKPYSISYLVDLDMVVKCLRYYAGWSDKFHGKTIPIDGD---------FFc 74
Cdd:PRK11903 65 RAALLAAIVKVLqaNRDAYYDIATA---NSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpaFQ- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 yTRHEPV---GVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLSALYVANLIKEAG-FPPGVVNIVPGy 146
Cdd:PRK11903 141 -GQHVLVptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 147 gptAGAAISSHMD-VDKVAFTGSTEVGHLIQK-AAAESNLKRVTLELGGKSPNIIMSDAdmdwAVDQAHFALFFNQ---- 220
Cdd:PRK11903 215 ---SSAGLLDHLQpFDVVSFTGSAETAAVLRShPAVVQRSVRVNVEADSLNSALLGPDA----APGSEAFDLFVKEvvre 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 221 -----GQCCCAGSRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYISsGKREGAKLLCGG-- 293
Cdd:PRK11903 288 mtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGgg 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 294 ----NAAADRGYFVQPTIFG-DVQDNMTIARE-EIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 357
Cdd:PRK11903 367 falvDADPAVAACVGPTLLGaSDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
79-357 |
8.63e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 105.13 E-value: 8.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 79 EPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALYVANLIkEAGFPPGVVNIVPGYGPTAGAAISSHM 158
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 159 dvDKVAFTGSTEVGHLIQKAAAEsNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALF-FNQGQCCCAGSRTYVQEDIY 237
Cdd:PLN02174 190 --DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 238 HEFVERSVEKAKSRVVGNPFDSKtEQGPQVDEEQFKKiLGYISSGKREGAKLLCGGNaaADRGYF-VQPTIFGDVQDNMT 316
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGE--KDRENLkIAPTILLDVPLDSL 342
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 704546197 317 IAREEIFGPVMQILKFKTIEEVIERANDSKYGLAAAVFTKD 357
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN 383
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-368 |
1.97e-23 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 101.58 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLAD-LIERDRAYlaaletldngkpYSISYL---------VDLDMVVKCLRYYAGW------SDKFH--GKTIP 67
Cdd:cd07128 61 RAAMLKALAKyLMERKEDL------------YALSAAtgatrrdswIDIDGGIGTLFAYASLgrrelpNAHFLveGDVEP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 68 I--DGDFF----CYTRHepvGVCGQIIPWNFPllmqAW----KLGPALATGNVVVMKVAEQTPLSALYVANLIKEAG-FP 136
Cdd:cd07128 129 LskDGTFVgqhiLTPRR---GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 137 PGVVNIVPGygptAGAAISSHMDV-DKVAFTGSTEVG-------HLIQKAAaesnlkRVTLELGGKSPNIIMSDAdmdwA 208
Cdd:cd07128 202 EGALQLICG----SVGDLLDHLGEqDVVAFTGSAATAaklrahpNIVARSI------RFNAEADSLNAAILGPDA----T 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 209 VDQAHFALFFNQ---------GQCCCAGSRTYVQEDIYHEFVERSVEKAKSRVVGNPFDSKTEQGPQVDEEQFKKILGYI 279
Cdd:cd07128 268 PGTPEFDLFVKEvaremtvkaGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 280 SSgKREGAKLLCGGN-------AAADRGYFVQPTIF-GDVQDNMTIARE-EIFGPVMQILKFKTIEEVIERANDSKYGLA 350
Cdd:cd07128 348 AT-LLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLV 426
|
410
....*....|....*...
gi 704546197 351 AAVFTKDLDKANYVSQGL 368
Cdd:cd07128 427 ASVVTNDPAFARELVLGA 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
49-364 |
7.57e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 66.37 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 49 KCLRYYAGWSDKFHGKTIPIDGDFFCYTRHE---PVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLSALY 125
Cdd:cd07126 108 KFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 126 VANLIKEAGFPPGVVNIVPGYGPTAGAAISShMDVDKVAFTGSTEVGHliqkaaaesnlkRVTLELGGKspnIIMSDADM 205
Cdd:cd07126 188 FLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSKVAE------------RLALELHGK---VKLEDAGF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 206 DWAV---------------DQAHFALffnQGQCCCAGSRTYVQED-IYHEFVERSVEKAKSRVVGN----PFDSKTEQGP 265
Cdd:cd07126 252 DWKIlgpdvsdvdyvawqcDQDAYAC---SGQKCSAQSILFAHENwVQAGILDKLKALAEQRKLEDltigPVLTWTTERI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 266 QvdeEQFKKILGYissgkrEGAKLLCGGNAAADRGYfvqPTIFGDVQ--------------DNMTIAREEIFGPvMQIL- 330
Cdd:cd07126 329 L---DHVDKLLAI------PGAKVLFGGKPLTNHSI---PSIYGAYEptavfvpleeiaieENFELVTTEVFGP-FQVVt 395
|
330 340 350
....*....|....*....|....*....|....*.
gi 704546197 331 --KFKTIEEVIERANDSKYGLAAAVFTKDLDKANYV 364
Cdd:cd07126 396 eyKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
6-366 |
3.20e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 61.08 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 6 RGKLLNRLADLIERDRAYLAALETLDNGKpYSISYLVDLDMVVKC-----------LRYYAGWSDKFHGKTIPIDGDffC 74
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGA-YIRSLIANWIAMMGCsesklyknidtERGITASVGHIQDVLLPDNGE--T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 75 YTRHEPVGVCGQIIPWNFPLLMqAWKLGPALATGNVVVMKVAEQTPLSAlYVANLIKEAGFPPGVVNIVPGYGPTAGAAI 154
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHGPKILVLYVPHPSDEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 155 S----SHMDVDKVAFTGSTEVGHLIQKAaaeSNLKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCccagsrt 230
Cdd:cd07077 173 AeellSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 231 yvqediyheFVERSVekaksRVVGNPFDSKTeqgpqvdeEQFKKILGYISSGKREGAKLLcggnaaadrgyfvqptiFGD 310
Cdd:cd07077 243 ---------ASEQNL-----YVVDDVLDPLY--------EEFKLKLVVEGLKVPQETKPL-----------------SKE 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 311 VQDNMTIAREEIFGPVMQILKFKTIEEVIERAND--SKYG--LAAAVFTKDLDKANYVSQ 366
Cdd:cd07077 284 TTPSFDDEALESMTPLECQFRVLDVISAVENAWMiiESGGgpHTRCVYTHKINKVDDFVQ 343
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
80-343 |
4.08e-10 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 61.02 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 80 PVGVCGqiiPWNFPLlmqAWK-LG----PALATGNVVVMKVAEQTP-LSALyVANLI----KEAGFPPGVVNIVPGYGPT 149
Cdd:cd07129 108 PVAVFG---ASNFPL---AFSvAGgdtaSALAAGCPVVVKAHPAHPgTSEL-VARAIraalRATGLPAGVFSLLQGGGRE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 150 AGAAISSHMDVDKVAFTGSTEVGHLIQKAAAesnlKR-----VTLELGGKSPNIIMSDADMDWAVDQAH-FA--LFFNQG 221
Cdd:cd07129 181 VGVALVKHPAIKAVGFTGSRRGGRALFDAAA----ARpepipFYAELGSVNPVFILPGALAERGEAIAQgFVgsLTLGAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 222 Q-CCCAGSRTYVQEDIYHEFVE---RSVEKAKSRVVGNPfdskteqgpqvdeeqfkKILGYISSGKRE-----GAKLLCG 292
Cdd:cd07129 257 QfCTNPGLVLVPAGPAGDAFIAalaEALAAAPAQTMLTP-----------------GIAEAYRQGVEAlaaapGVRVLAG 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 704546197 293 GnAAADRGYFVQPTIFG-DVQDNMT--IAREEIFGPVMQILKFKTIEEVIERAN 343
Cdd:cd07129 320 G-AAAEGGNQAAPTLFKvDAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
84-235 |
6.87e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 47.86 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 84 CGQIIPWN-FPLLMQAwklgpaLATGNVVVMKVAEQTPLS-ALYVA---NLIKEAGFPPGVVNIV--PGYGPTAGaAISS 156
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVKPHPAAILPlAITVQvarEVLAEAGFDPNLVTLAadTPEEPIAQ-TLAT 274
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704546197 157 HMDVDKVAFTGSTEVG-HLIQKAAAesnlKRVTLELGGKSPNIIMSDADMDWAVDQAHFALFFNQGQCCCAGSRTYVQED 235
Cdd:cd07127 275 RPEVRIIDFTGSNAFGdWLEANARQ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD 350
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