|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-534 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 1126.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 1 MASRRVSSLLSRSFMSSSRSIFSLRGMN----RGAQRYSNLAAAVENTITPPVKVEHTQLLIGGRFVDAVSGKTFPTLDP 76
Cdd:PLN02466 1 MAARRISSLLSRSLSASSSALLRSRGRNggrgRGIRRFSTAAAAVEEPITPPVQVSYTQLLINGQFVDAASGKTFPTLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 77 RNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEVP 156
Cdd:PLN02466 81 RTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 157 MLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALL 236
Cdd:PLN02466 161 MFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 237 VGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNLKAVTLELGGKSPFIVCEDADV 316
Cdd:PLN02466 241 AAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 317 DQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEA 396
Cdd:PLN02466 321 DKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVES 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 397 GATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLM 476
Cdd:PLN02466 401 GATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLS 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18395300 477 RALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSLKNPAWL 534
Cdd:PLN02466 481 RALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKNPAWL 538
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
51-526 |
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: 998.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 51 VEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEK 130
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 131 HNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSW 210
Cdd:cd07142 81 HADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 211 KLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELA 290
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 291 SKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKS 370
Cdd:cd07142 241 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 371 GIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
51-525 |
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: 882.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 51 VEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEK 130
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 131 HNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSW 210
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 211 KLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELA 290
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 291 SKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKS 370
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 371 GIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
49-525 |
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: 810.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 49 VKVEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSKILFRFADL 127
Cdd:cd07141 2 PEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 128 IEKHNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLM 207
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 208 LSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIIL 287
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 288 ELASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDP 367
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 368 FKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLD 447
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395300 448 EVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
50-534 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 708.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 50 KVEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIE 129
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 130 KHNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLS 209
Cdd:PLN02766 97 EHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 210 WKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILEL 289
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 290 ASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFK 369
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 370 SGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEV 449
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 450 IARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSLK 529
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLY 496
|
....*
gi 18395300 530 NPAWL 534
Cdd:PLN02766 497 NSPWL 501
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
62-524 |
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: 666.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 62 FVDAvSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETW 141
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 142 DNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNT 221
Cdd:pfam00171 78 ENGKPLAE-ARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 222 VVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLE 301
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 302 LGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSE 381
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 382 QFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLA 461
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 462 AGVFTQNLDTAHRLMRALRVGTVWINCFDVLDA-SIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
54-524 |
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: 664.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdEGPWP-KMTAYERSKILFRFADLIEKHN 132
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGlKVSGSKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 133 DEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKL 212
Cdd:cd07143 86 DYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 213 GPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASK 292
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 293 SNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGI 372
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIAR 452
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395300 453 ANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
54-524 |
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: 654.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSKILFRFADLIEKHND 133
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF-ESWWSKVTGEERGELLDKLADLVEKNRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 134 EIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:cd07144 87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkS 293
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-Q 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 294 NLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKR-NVGDPFKSGI 372
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLG---SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEV 449
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 450 IARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
68-524 |
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: 626.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 68 GKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPY 147
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 148 EQSAQIEVPMLARVFRYYAGWADKIHGMTMPGdgPHHVQTL--HEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPT--GPDALALitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNLKAVTLELGGK 305
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 306 SPFIVCEDA-DVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFN 384
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 385 KILKYIKHGVEAGATLQAGGDRL--GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAA 462
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395300 463 GVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
94-526 |
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: 618.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 94 NRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIH 173
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE-ALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 174 GMTMP-GDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVN 252
Cdd:cd07078 78 GEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 253 IVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQG 332
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 333 QCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL-GSKG 411
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 412 YYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDV 491
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 18395300 492 -LDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07078 397 gAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
73-525 |
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: 604.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPY-EQSA 151
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIrETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 152 QieVPMLARVFRYYAGWADKIHGMTMPGD-GPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQT 230
Cdd:cd07114 81 Q--VRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 231 PLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIV 310
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 311 CEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQFNKILK 388
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERlvARARAIR--VGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 389 YIKHGVEAGATLQAGGDRLG----SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGV 464
Cdd:cd07114 316 YVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 465 FTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07114 396 WTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
58-529 |
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: 603.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQSaQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALA 217
Cdd:cd07119 82 LETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 218 CGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKA 297
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 298 VTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQ 377
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 378 VDSEQFNKILKYIKHGVEAGATLQAGGDRLG----SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARA 453
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395300 454 NNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSLK 529
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ... |
54-528 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];
Pssm-ID: 223944 [Multi-domain] Cd Length: 472 Bit Score: 596.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSgkTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHND 133
Cdd:COG1012 1 YKLLIDGEWVDGAS--TIEVINPATGEVIATVPAATAEDVDAAVAAARAAFE--AWSRLSAEERAAILRRIADLLEARAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 134 EIAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:COG1012 77 ELAALITLETGKPISE-ARGEIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKs 293
Cdd:COG1012 156 PALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 294 NLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIE 373
Cdd:COG1012 235 NLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 374 QGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGskGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARA 453
Cdd:COG1012 315 LGPLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 454 NNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWIN--CFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSL 528
Cdd:COG1012 393 NDTEYGLAAAIFTRDLARAFRVARRLEAGMVGINdyTGGADIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIKL 469
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
73-524 |
0e+00 |
|
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: 589.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQ 152
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPL 232
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 233 SALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCE 312
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 313 DADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKH 392
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGS----KGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQN 468
Cdd:cd07093 318 ARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395300 469 LDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
73-528 |
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: 575.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQ 152
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPL 232
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 233 SALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILElASKSNLKAVTLELGGKSPFIVCE 312
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQ-GAAGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 313 DADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKH 392
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTA 472
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395300 473 HRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSL 528
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
55-528 |
0e+00 |
|
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: 552.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 55 QLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQSAQIEVPMLARVFRYYA-------GWADKIHGMTMPgdgphhvQTLHEPIGVAGQIIPWNFPLLM 207
Cdd:cd07559 80 LAVAETLDNGKPIRETLAADIPLAIDHFRYFAgviraqeGSLSEIDEDTLS-------YHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 208 LSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIIL 287
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 288 ELASKsNLKAVTLELGGKSPFIVCEDA-----DVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKR 362
Cdd:cd07559 232 QYAAE-NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 363 NVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGS----KGYYIQPTVFSDVKDDMLIATDEIFGPVQ 438
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 439 TILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNY 518
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
490
....*....|
gi 18395300 519 LQVKAVVTSL 528
Cdd:cd07559 471 QQTKNILVSY 480
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
74-524 |
0e+00 |
|
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: 549.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQI 153
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAE-ARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKIHGMTMPGDGPHH-VQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPL 232
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPAPGKrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 233 SALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkSNLKAVTLELGGKSPFIVCE 312
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 313 DADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQFNKILKYI 390
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKlvERVKKLK--VGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 391 KHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLD 470
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 18395300 471 TAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
55-524 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 543.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 55 QLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKIILELASKSn 294
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 295 LKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQ 374
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL----GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
73-524 |
0e+00 |
|
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: 534.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEqSAQ 152
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIE-EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPL 232
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 233 SALLVGKLLHEAGLPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCE 312
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 313 DADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKH 392
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGSK-----GYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQ 467
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 468 NLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
49-524 |
0e+00 |
|
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 Cd Length: 486 Bit Score: 528.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 49 VKVEHtQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLI 128
Cdd:cd07140 2 LKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 129 EKHNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDG--PHHVQTL--HEPIGVAGQIIPWNFP 204
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarPNRNLTLtkREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 205 LLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGK 284
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 285 IILELASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNV 364
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 365 GDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFK 444
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 445 --DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVK 522
Cdd:cd07140 401 dgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
..
gi 18395300 523 AV 524
Cdd:cd07140 481 TV 482
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
74-525 |
0e+00 |
|
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: 523.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQI 153
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAF-ESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQ-ARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLS 233
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 234 ALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCED 313
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 314 ADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGdpfkSGIEQ---GPQVDSEQFNKILKYI 390
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG----PGLEDpdlGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 391 KHGVEAGATLQAGGDRL---GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQ 467
Cdd:cd07109 315 ARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 18395300 468 NLDTAHRLMRALRVGTVWINC-FDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
76-524 |
0e+00 |
|
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: 518.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 76 PRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQIEV 155
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQ-ARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 156 PMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSA 234
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGlVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 235 LLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDA 314
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 315 DVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGV 394
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 395 EAGATLQAGGDRLGS-KGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAH 473
Cdd:cd07118 322 AEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 18395300 474 RLMRALRVGTVWINCFdvLDAS--IPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07118 402 TVARRIRAGTVWVNTF--LDGSpeLPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-525 |
0e+00 |
|
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: 518.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGphhvQTLHEPIGVAGQIIPWNFPLLMLSWKLGPA 215
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNS----LVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 216 LACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSnL 295
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-V 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 296 KAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQG 375
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 376 PQVDSEQFNKILKYIKHGVEAGATLQAGG----DRLgSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIA 451
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 452 RANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
58-522 |
0e+00 |
|
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: 516.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE--WAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALA 217
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 218 CGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkSNLKA 297
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 298 VTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQ 377
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 378 VDSEQFNKILKYIKHGVEAGATLQAGGDRLG----SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARA 453
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395300 454 NNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVK 522
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
55-528 |
3.15e-176 |
|
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: 505.07 E-value: 3.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 55 QLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsN 294
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 295 LKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQ 374
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGS----KGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSL 528
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
56-519 |
3.69e-176 |
|
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: 505.01 E-value: 3.69e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHgMTMPGdgphhvqtlHEPIGVAGQIIPWNFPLLMLSWKLGPA 215
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-TELAG---------WKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 216 LACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKIILELASKSNl 295
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 296 KAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQG 375
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 376 PQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANN 455
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 456 SRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYL 519
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
73-526 |
7.12e-175 |
|
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: 500.73 E-value: 7.12e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQ 152
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDE-AA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIH-----GMTMPGDGpHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTA 227
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLDakaerAVPLPSED-FKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 228 EQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSP 307
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 308 FIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKIL 387
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 388 KYIKHGVEAGATLQAGGDR--LGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVF 465
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 466 TQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-525 |
1.23e-172 |
|
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: 495.56 E-value: 1.23e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKI-HGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkSN 294
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-ER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 295 LKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQ 374
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLG--SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIAR 452
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395300 453 ANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDvLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
74-525 |
4.83e-172 |
|
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: 493.68 E-value: 4.83e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWpKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKP--YEQSA 151
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 152 QIEVPMLArvFRYYAGWADK-----IHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKT 226
Cdd:cd07089 81 QVDGPIGH--LRYFADLADSfpwefDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 227 AEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkSNLKAVTLELGGKS 306
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 307 PFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKI 386
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 387 LKYIKHGVEAGATLQAGGDRL--GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGV 464
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 465 FTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
98-525 |
5.11e-172 |
|
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: 490.20 E-value: 5.11e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 98 AAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAqIEVPMLARVFRYYAGWADKIHGMTM 177
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 178 PGDGPHHV-QTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSG 256
Cdd:cd06534 78 PSPDPGGEaYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 257 FGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCC 336
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 337 AGSRTFVHERVYDEFVEKAKaralkrnvgdpfksgieqgpqvdseqfnkilkyikhgveagatlqaggdrlgskgyyiqp 416
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 417 TVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVL-DAS 495
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGPE 336
|
410 420 430
....*....|....*....|....*....|
gi 18395300 496 IPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
53-524 |
2.71e-171 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 492.50 E-value: 2.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 53 HTQLLIGGRFVDAvSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHN 132
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 133 DEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMT----MPGdgpHHVQTLHEPIGVAGQIIPWNFPLLML 208
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAageyLEG---HTSMIRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 209 SWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILE 288
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 289 LASKSnLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPF 368
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 369 KSGIEQGPQVDSEQFNKILKYIKHGVEAG-ATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLD 447
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 448 EVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
58-525 |
3.29e-171 |
|
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: 492.17 E-value: 3.29e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPH-HVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPAL 216
Cdd:cd07088 80 LIVEEQGKTLSL-ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNeNIFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 217 ACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLK 296
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 297 AVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGP 376
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 377 QVDSEQFNKILKYIKHGVEAGATLQAGGDRL-GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANN 455
Cdd:cd07088 318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 456 SRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDvLDASIPF-GGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINREN-FEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
74-526 |
2.01e-168 |
|
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: 484.14 E-value: 2.01e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQI 153
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTL-HEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPL 232
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIrREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 233 SALLVGKLLHEaGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCE 312
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 313 DADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKh 392
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTA 472
Cdd:cd07092 317 RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 18395300 473 HRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
48-533 |
1.20e-164 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 476.53 E-value: 1.20e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 48 PVKVEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDE---GPWPKMTAYERSKILFRF 124
Cdd:PLN02467 2 AIPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 125 ADLIEKHNDEIAALETWDNGKPYEQSAQiEVPMLARVFRYYAGWADKIHG-----MTMPGDgPHHVQTLHEPIGVAGQII 199
Cdd:PLN02467 82 AAKITERKSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLKEPLGVVGLIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 200 PWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGS 279
Cdd:PLN02467 160 PWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 280 TDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARA 359
Cdd:PLN02467 240 TATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 360 LKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLG--SKGYYIQPTVFSDVKDDMLIATDEIFGPV 437
Cdd:PLN02467 319 KNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 438 QTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNN 517
Cdd:PLN02467 399 LCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLEN 478
|
490
....*....|....*.
gi 18395300 518 YLQVKAVVTSLKNPAW 533
Cdd:PLN02467 479 YLSVKQVTKYISDEPW 494
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
57-524 |
1.68e-161 |
|
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 Cd Length: 473 Bit Score: 467.50 E-value: 1.68e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAVSGKtfPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYEQSAQiEVPMLARVFRYYAGWADKIHGMTMPGDGPH-HVQTLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:cd07097 80 ARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGvEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASkSN 294
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 295 LKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQ 374
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL--GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIAR 452
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 453 ANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDV-LDASIPFGGYKMSGIG-REKGIYSLNNYLQVKAV 524
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
73-525 |
2.08e-160 |
|
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: 464.14 E-value: 2.08e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQ 152
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIHGMTMPGdGPHHVQ-TLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTP 231
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPF-GPDVLTyTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 232 LSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVC 311
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 312 EDADVDQAVELAHFAL-FFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYI 390
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 391 KHGVEA-GATLQAGG----DRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVF 465
Cdd:cd07108 316 DLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 466 TQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYS-LNNYLQVKAVV 525
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
74-524 |
7.39e-159 |
|
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: 459.69 E-value: 7.39e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQI 153
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAE-AQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKIHgmTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLS 233
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 234 ALLVGKLLHEAgLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCED 313
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 314 ADVDQAVE-LAHFAlFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKH 392
Cdd:cd07106 234 VDIDAVAPkLFWGA-FINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTA 472
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 18395300 473 HRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
58-527 |
7.50e-154 |
|
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: 448.44 E-value: 7.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALA 217
Cdd:cd07116 83 AETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 218 CGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKA 297
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 298 VTLELGGKSPFIVCE------DADVDQAVElaHFALF-FNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKS 370
Cdd:cd07116 241 VTLELGGKSPNIFFAdvmdadDAFFDKALE--GFVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 371 GIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDR----LGSKGYYIQPTVFSDvKDDMLIATDEIFGPVQTILKFKDL 446
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 447 DEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
.
gi 18395300 527 S 527
Cdd:cd07116 478 S 478
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
58-524 |
6.55e-153 |
|
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: 445.73 E-value: 6.55e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDeGPWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTM----PGDGPHHVQ--TLHEPIGVAGQIIPWNFPLLMLSWK 211
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsiPSMQGERYTafTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 212 LGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKIILELAS 291
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 292 kSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSG 371
Cdd:cd07113 242 -SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 372 IEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPT--VFSDVKDDMLiaTDEIFGPVQTILKFKDLDEV 449
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 450 IARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
54-529 |
7.05e-153 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 446.26 E-value: 7.05e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHND 133
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 134 EIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:PRK09847 100 ELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKS 293
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 294 NLKAVTLELGGKSPFIVCEDA-DVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGI 372
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGgdRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIAR 452
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 453 ANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSLK 529
Cdd:PRK09847 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
58-524 |
9.38e-153 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 445.71 E-value: 9.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDavSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSKILFRFADLIEKHNDEIAA 137
Cdd:TIGR03216 5 INGAFVE--SGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAAL-KGPWGKMTVAERADLLYAVADEIERRFDDFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 138 LETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHG----MTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:TIGR03216 82 AEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTecfeMATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWKVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFG-ATAGAAIASHMDVDKVAFTGSTDVGKIILELASK 292
Cdd:TIGR03216 162 PALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGpDSAGEFLTRHPGVDAITFTGETRTGSAIMKAAAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 293 SnLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGI 372
Cdd:TIGR03216 242 G-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGG------DRLGSkGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDL 446
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfgDALAG-GAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDSE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395300 447 DEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:TIGR03216 400 EEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNV 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
54-524 |
7.38e-150 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 438.74 E-value: 7.38e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHND 133
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 134 EIAALETWDNGKPYeQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPH-HVQTLHEPIGVAGQIIPWNFPLLMLSWKL 212
Cdd:PLN02278 103 DLAQLMTLEQGKPL-KEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDrRLLVLKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 213 GPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASK 292
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 293 SnLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGI 372
Cdd:PLN02278 262 T-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIAR 452
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395300 453 ANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
57-524 |
2.53e-149 |
|
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 Cd Length: 478 Bit Score: 436.78 E-value: 2.53e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAVSGKTFPTLDPRNG-EVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPE--WRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:cd07131 80 ARLVTREMGKPLAE-GRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAmTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSN 294
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 295 lKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQ 374
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL----GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDV-LDASIPFGGYKMSGIG-REKGIYSLNNYLQVKAV 524
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
92-524 |
3.10e-149 |
|
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: 434.65 E-value: 3.10e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 92 DVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAAL---ETwdnGKPYeQSAQIEVPMLARVFRYYAGW 168
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADWlirES---GSTR-PKAAFEVGAAIAILREAAGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 169 ADKIHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLmLSWK-LGPALACGNTVVLKTAEQTPLS-ALLVGKLLHEAG 245
Cdd:cd07104 75 PRRPEGEILPSDVPGKESmVRRVPLGVVGVISPFNFPLI-LAMRsVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 246 LPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHF 325
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 326 ALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAG 403
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKlvAKAKALP--VGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 404 GDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGT 483
Cdd:cd07104 311 GTY---EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 18395300 484 VWINCFDVLD-ASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07104 388 VHINDQTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
71-525 |
9.61e-149 |
|
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: 434.33 E-value: 9.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 71 FPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPwpKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQs 150
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 151 AQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-----TLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07149 78 ARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEgrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIIlelASKSNLKAVTLELGGK 305
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI---ARKAGLKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 306 SPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNK 385
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 386 ILKYIKHGVEAGATLQAGGDRLGSkgyYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVF 465
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 466 TQNLDTAHRLMRALRVGTVWINcfDVLDASI---PFGGYKMSGIGREkGI-YSLNNYLQVKAVV 525
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIN--DSSTFRVdhmPYGGVKESGTGRE-GPrYAIEEMTEIKLVC 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-524 |
1.21e-146 |
|
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: 428.67 E-value: 1.21e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 71 FPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYeQS 150
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTY-GK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 151 AQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLmLSWK-LGPALACGNTVVLKTAE 228
Cdd:cd07150 78 AWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSmSVRRPLGVVAGITPFNYPLI-LATKkVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 229 QTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPF 308
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 309 IVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILK 388
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 389 YIKHGVEAGATLQAGGdrlGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQN 468
Cdd:cd07150 316 QVEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 469 LDTAHRLMRALRVGTVWINCFDVLD-ASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
73-524 |
2.75e-146 |
|
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: 427.95 E-value: 2.75e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYeqSAQ 152
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPV--SAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 I-EVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTP 231
Cdd:cd07107 77 LgDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 232 LSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSnLKAVTLELGGKSPFIVC 311
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 312 EDADVDQAVELAHFALFFN-QGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYI 390
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 391 KHGVEAGATLQAGGDR----LGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFT 466
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 18395300 467 QNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
56-524 |
1.72e-140 |
|
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: 415.47 E-value: 1.72e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVDavSGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGP 214
Cdd:cd07124 111 LAAWMVLEVGKNWAE-ADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 215 ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASK-- 292
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 293 ---SNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFK 369
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 370 SGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAG-GDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDE 448
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGeVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395300 449 VIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWIN--CFDVLDASIPFGGYKMSGIG-REKGIYSLNNYLQVKAV 524
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
73-525 |
1.72e-133 |
|
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: 395.17 E-value: 1.72e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWpKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQ 152
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGE-AR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGWADKIHGMTM---PGDgphhVQTLH-EPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAE 228
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIepePGS----FSLVLrEPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 229 QTPLSALLVGKLLHEA-GLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSP 307
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 308 FIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKIL 387
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 388 KYIKHGVEAGATLQAGGDRLG---SKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGV 464
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 465 FTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
60-524 |
1.78e-133 |
|
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: 395.52 E-value: 1.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 60 GRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALE 139
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 140 TWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGP---HHVqtLHEPIGVAGQIIPWNFPLLMLSWKLGPAL 216
Cdd:cd07151 79 IRESGSTRIK-ANIEWGAAMAITREAATFPLRMEGRILPSDVPgkeNRV--YREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 217 ACGNTVVLKTAEQTPLSA-LLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNL 295
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 296 KAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQG 375
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 376 PQVDSEQFNKILKYIKHGVEAGATLQAGGDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANN 455
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 456 SRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLD-ASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
71-509 |
2.85e-133 |
|
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: 394.79 E-value: 2.85e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 71 FPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQS 150
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 151 aQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHH-----VQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07145 79 -RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYnerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIIlelASK--SNLKAVTLELG 303
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI---ASKagGTGKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 304 GKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQF 383
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 384 NKILKYIKHGVEAGATLQAGGDRLGskGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAG 463
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 18395300 464 VFTQNLDTAHRLMRALRVGTVWINC-----FDvldaSIPFGGYKMSGIGRE 509
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDstrfrWD----NLPFGGFKKSGIGRE 439
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
57-524 |
1.67e-131 |
|
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: 391.16 E-value: 1.67e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAvSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIA 136
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 137 ALETWDNGKPYeQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLMLSWKLGPA 215
Cdd:cd07086 79 RLVSLEMGKIL-PEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLmEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 216 LACGNTVVLKTAEQTPLSALLVGKLLHEA----GLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELAS 291
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 292 KSNlKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSG 371
Cdd:cd07086 237 RRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 372 IEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL--GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEV 449
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395300 450 IARANNSRYGLAAGVFTQNLDTAHRLMRALRV--GTVWINcFDVLDASI--PFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVN-IPTSGAEIggAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
56-524 |
1.98e-125 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 376.97 E-value: 1.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVDavSGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQsAQIEVPMLARVFRYYA----GWADKIHGMTMPGDgphHVQTLHEPIGVAGQIIPWNFPLLMLSW 210
Cdd:PRK03137 115 FSAWLVKEAGKPWAE-ADADTAEAIDFLEYYArqmlKLADGKPVESRPGE---HNRYFYIPLGVGVVISPWNFPFAIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 211 KLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELA 290
Cdd:PRK03137 191 MTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 291 SKSN-----LKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVG 365
Cdd:PRK03137 271 AKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 366 DPfKSGIEQGPQVDSEQFNKILKYIKHGVEAGaTLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKD 445
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 446 LDEVIARANNSRYGLAAGVFTQNldtAHRLMRALR---VGTVWIN--CFDVLDASIPFGGYKMSGIGREKG--IYsLNNY 518
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNN---REHLEKARRefhVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLF 504
|
....*.
gi 18395300 519 LQVKAV 524
Cdd:PRK03137 505 LQAKTV 510
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
74-526 |
3.22e-125 |
|
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: 374.25 E-value: 3.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEqSAQI 153
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRA-DAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKI-------HGMTMPgdgpHHVQTL-HEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVlaprkvpTGLLMP----NKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIAShmDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGK 305
Cdd:cd07099 154 PSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 306 SPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQF 383
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARlvAKARALR--PGADDIGDADIGPMTTARQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 384 NKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAG 463
Cdd:cd07099 309 DIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 464 VFTQNLDTAHRLMRALRVGTVWINcfDVL-DASI---PFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSIN--DVLlTAGIpalPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
93-526 |
2.98e-124 |
|
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: 370.64 E-value: 2.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 93 VNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQIEVPMLARVFRYYAgwaDKI 172
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAE-ARAEVEKCAWICRYYA---ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 173 HGM----TMPGDGPH-HVQtlHEPIGVAGQIIPWNFPLlmlsWK----LGPALACGNTVVLKTAEQTPLSALLVGKLLHE 243
Cdd:cd07100 75 EAFladePIETDAGKaYVR--YEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 244 AGLPDGV-VNIVSGFGATAgaAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVEL 322
Cdd:cd07100 149 AGFPEGVfQNLLIDSDQVE--AIIADPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 323 AHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQA 402
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 403 GGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVG 482
Cdd:cd07100 306 GGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 18395300 483 TVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07100 386 MVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
75-525 |
3.54e-124 |
|
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: 371.38 E-value: 3.54e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 75 DPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQIE 154
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKD-ARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 155 VPMLARVFRYYAGWADKIHGMTMPGD-----GPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQ 229
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 230 TPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKiilELASKSNLKAVTLELGGKSPFI 309
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE---ALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 310 VCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKY 389
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 390 IKHGVEAGATLQAGGDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNL 469
Cdd:cd07094 319 VEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 470 DTAHRLMRALRVGTVWINCFDVLDA-SIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
55-528 |
5.49e-124 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 371.93 E-value: 5.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 55 QLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGP-HHVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:PRK11241 90 LARLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKs 293
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 294 NLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIE 373
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 374 QGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARA 453
Cdd:PRK11241 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 454 NNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSL 528
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
74-525 |
6.21e-123 |
|
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: 368.22 E-value: 6.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARkafdeGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYeQSAQI 153
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCL-KDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 154 EVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQ-----TLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAE 228
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTANGKarkifTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 229 QTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIIlelASKSNLKAVTLELGGKSPF 308
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 309 IVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQFNKI 386
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLlvEKSAALV--VGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 387 LKYIKHGVEAGATLQAGGDRLGSkgyYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFT 466
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQGA---LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395300 467 QNLDTAHRLMRALRVGTVWIN---CFDVldASIPFGGYKMSGIG-REKGIYSLNNYLQVKAVV 525
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNevpGFRS--ELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
92-524 |
3.13e-121 |
|
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: 363.05 E-value: 3.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 92 DVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPyEQSAQIEVPMLARVFRYYAGWADK 171
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 172 IHGMTMPGDGPHHVQ-TLHEPIGVAGQIIPWNFPLLmlswkLG-----PALACGNTVVLKTAEQTPLSALLVGKLLHEAG 245
Cdd:cd07105 78 IIGGSIPSDKPGTLAmVVKEPVGVVLGIAPWNAPVI-----LGtraiaYPLAAGNTVVLKASELSPRTHWLIGRVFHEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 246 LPDGVVNIVSGFGATAGA---AIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVEL 322
Cdd:cd07105 153 LPKGVLNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 323 AHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRnvgdpFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQA 402
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 403 GG-DRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRV 481
Cdd:cd07105 307 GGlADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIES 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 18395300 482 GTVWINCFDVLD-ASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:cd07105 387 GAVHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
63-527 |
1.06e-119 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 362.27 E-value: 1.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 63 VDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWD 142
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 143 NGKPyEQSAQIEVPMLARVFRYYAGWADKI-----HGMTMPGDGphHVQTLHEPIGVAGQIIPWNFPL-LMLSWKLgPAL 216
Cdd:PRK09407 104 TGKA-RRHAFEEVLDVALTARYYARRAPKLlaprrRAGALPVLT--KTTELRQPKGVVGVISPWNYPLtLAVSDAI-PAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 217 ACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHmdVDKVAFTGSTDVGKIILELASkSNLK 296
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 297 AVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQ 374
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAfvAAVRAMR--LGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 375 GPQVDSEQFNKILKYIKHGVEAGATLQAGGDR---LGSkgYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIA 451
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKArpdLGP--LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 452 RANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWIN-----CFDVLDAsiPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
.
gi 18395300 527 S 527
Cdd:PRK09407 491 Q 491
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
57-526 |
2.44e-119 |
|
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: 359.58 E-value: 2.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAvSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSKILFRFADLIEKHNDEIA 136
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 137 ALETWDNGKPYeQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTL-----HEPIGVAGQIIPWNFPLLMLSWK 211
Cdd:cd07082 83 NLLMWEIGKTL-KDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKiaqvrREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 212 LGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELAS 291
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 292 KsnlKAVTLELGGKSPFIVCEDADVDQAV-ELAHFALFFNqGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKS 370
Cdd:cd07082 242 M---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 371 GIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGskGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVI 450
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCF-----DVLdasiPFGGYKMSGIGREkGI-YSLNNYLQVKAV 524
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQ-GIgDALRSMTRRKGI 470
|
..
gi 18395300 525 VT 526
Cdd:cd07082 471 VI 472
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
79-507 |
1.67e-116 |
|
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: 351.60 E-value: 1.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 79 GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKpYEQSAQIEVPML 158
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 159 ARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSA-LLV 237
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 238 GKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVD 317
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 318 QAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAG 397
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 398 ATLQAGGDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMR 477
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|.
gi 18395300 478 ALRVGTVWINCFDVLDASI-PFGGYKMSGIG 507
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHnPFGGMGASGNG 423
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
75-526 |
1.73e-116 |
|
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: 351.61 E-value: 1.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 75 DPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPyEQSAQIE 154
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKA-RRHAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 155 VPMLARVFRYYAGWADKI-----HGMTMPGDGphHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQ 229
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPVLT--RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 230 TPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHmdVDKVAFTGSTDVGKIILELASkSNLKAVTLELGGKSPFI 309
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 310 VCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKY 389
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 390 IKHGVEAGATLQAGGDR---LGSkgYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFT 466
Cdd:cd07101 314 VDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 467 QNLDTAHRLMRALRVGTVWIN-----CFDVLDAsiPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
121-524 |
2.14e-114 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 344.80 E-value: 2.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 121 LFRFADLIEKHNDEIAALETWDNGKPyEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGP-HHVQTLHEPIGVAGQII 199
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKI-QQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPgENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 200 PWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGS 279
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 280 TDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARA 359
Cdd:PRK10090 160 VSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 360 LKRNVGDPFK-SGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQ 438
Cdd:PRK10090 239 QAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 439 TILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDASIPF-GGYKMSGIGREKGIYSLNN 517
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-RENFEAMQGFhAGWRKSGIGGADGKHGLHE 397
|
....*..
gi 18395300 518 YLQVKAV 524
Cdd:PRK10090 398 YLQTQVV 404
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
71-525 |
3.96e-114 |
|
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: 345.77 E-value: 3.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 71 FPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDegPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQs 150
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 151 AQIEVPMLARVFRYYAGWADKIHGMTMPGDGP-----HHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07147 78 ARGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVsgfgaTAGAAIASHMDVDK----VAFTGSTDVGKIILELASKsnlKAVTLE 301
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVL-----PCSRDDADLLVTDEriklLSFTGSPAVGWDLKARAGK---KKVVLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 302 LGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVD 379
Cdd:cd07147 230 LGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRlvARVKALK--TGDPKDDATDVGPMIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 380 SEQFNKILKYIKHGVEAGATLQAGGDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYG 459
Cdd:cd07147 308 ESEAERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 460 LAAGVFTQNLDTAHRLMRALRVGTVWINcfDV----LDaSIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:cd07147 385 LQAGVFTRDLEKALRAWDELEVGGVVIN--DVptfrVD-HMPYGGVKDSGIGREGVRYAIEEMTEPRLLV 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
54-528 |
8.62e-114 |
|
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: 345.66 E-value: 8.62e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 54 TQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHND 133
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 134 EIAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHH-VQTLHEPIGVAGQIIPWNFPLLMLSWKL 212
Cdd:cd07085 79 ELARLITLEHGKTLAD-ARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIdTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 213 GPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASK 292
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 293 SNlKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGI 372
Cdd:cd07085 237 NG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 373 EQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRL----GSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDE 448
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 449 VIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINC-FDVLDASIPFGGYKMSGIGrEKGIY---SLNNYLQVKaV 524
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpIPVPLAFFSFGGWKGSFFG-DLHFYgkdGVRFYTQTK-T 473
|
....
gi 18395300 525 VTSL 528
Cdd:cd07085 474 VTSR 477
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
76-507 |
4.01e-107 |
|
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: 327.67 E-value: 4.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 76 PRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQiEV 155
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 156 P-MLARVfRYYAGWADK-IHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLS 233
Cdd:cd07102 80 RgMLERA-RYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 234 ALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHmDVDKVAFTGSTDVGKIIlELASKSNLKAVTLELGGKSPFIVCED 313
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAI-QRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 314 ADVDQAVE-LAHFAlFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKH 392
Cdd:cd07102 237 ADLDAAAEsLVDGA-FFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 393 GVEAGATLQAGGDRLGS---KGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNL 469
Cdd:cd07102 316 AIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 18395300 470 DTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIG 507
Cdd:cd07102 396 ARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
75-526 |
2.85e-95 |
|
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: 297.67 E-value: 2.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 75 DPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIE 154
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 155 VPMLARVFRYYAGWADK-------IHGMTMPgdgpHHVQTLH-EPIGVAGQIIPWNFPLLMLswkLGPALAC---GNTVV 223
Cdd:cd07098 80 ILVTCEKIRWTLKHGEKalrpesrPGGLLMF----YKRARVEyEPLGVVGAIVSWNYPFHNL---LGPIIAAlfaGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 224 LKTAEQTPLSALLVGKLLHEA----GLPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKIILELASKSnLKAVT 299
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 300 LELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVD 379
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 380 SEQFNKILKYIKHGVEAGATLQAGGDRLGS----KGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANN 455
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395300 456 SRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDV--LDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnyYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
73-509 |
3.04e-93 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 292.03 E-value: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYeQSAQ 152
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTL-ASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGwadkiHGMTMPGDGPHHVQTL--------HEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVL 224
Cdd:PRK09406 82 AEALKCAKGFRYYAE-----HAEALLADEPADAAAVgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 225 KTAEQTPLSALLVGKLLHEAGLPDGVVNIVSgFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSnLKAVTLELGG 304
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 305 KSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQ 382
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKfvARMAALR--VGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 383 FNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAA 462
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18395300 463 GVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGRE 509
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
67-511 |
8.47e-89 |
|
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: 281.02 E-value: 8.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 67 SGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKP 146
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 147 YeQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVqtLHE---PIGVAGQIIPWNFPLLMLSWKLGPALACGNTVV 223
Cdd:cd07130 88 L-PEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHR--MMEqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 224 LKTAEQTPLSAL----LVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKsNLKAVT 299
Cdd:cd07130 165 WKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA-RFGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 300 LELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKR-NVGDPFKSGIEQGPQV 378
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLK-KAYKQvRIGDPLDDGTLVGPLH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 379 DSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSdVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRY 458
Cdd:cd07130 322 TKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQ 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 459 GLAAGVFTQNLDTAHRLMRAL--RVGTVWINcfdvldasIP---------FGGYKMSGIGREKG 511
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN--------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
52-511 |
4.34e-84 |
|
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: 269.45 E-value: 4.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 52 EHTQLLIGGRFVDAVSGKTfpTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEK 130
Cdd:cd07083 17 RAYPLVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKT--WKDWPQEDRARLLLKAADLLRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 131 HNDEIAALETWDNGKPYEQSAQiEVPMLARVFRYYAGWADKIHGMT--MPGDGPHHVQTLHEPIGVAGQIIPWNFPLLML 208
Cdd:cd07083 93 RRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAveVVPYPGEDNESFYVGLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 209 SWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILE 288
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 289 LASK-----SNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRN 363
Cdd:cd07083 252 AAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 364 VGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGaTLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKF 443
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395300 444 KDLD--EVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcfDVLDASI----PFGGYKMSGIGREKG 511
Cdd:cd07083 411 KDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN--RKITGALvgvqPFGGFKLSGTNAKTG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
36-520 |
5.99e-80 |
|
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: 259.44 E-value: 5.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 36 NLAAAVENTITPpvKVEHTQLLIGGRFVDavsGKTFPTLDP-RNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTA 114
Cdd:cd07125 18 ALADALKAFDEK--EWEAIPIINGEETET---GEGAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAG--WSATPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 115 YERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQIEVPMLARVFRYYAGWADKIhgMTMPG-DGPH-HVQTLH-EP 191
Cdd:cd07125 91 EERAEILEKAADLLEANRGELIALAAAEAGKTLAD-ADAEVREAIDFCRYYAAQAREL--FSDPElPGPTgELNGLElHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 192 IGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDV 271
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 272 DKVAFTGSTDVGKIILELASKSNLKAVTL--ELGGKSPFIVCEDADVDQAV-ELAHFAlFFNQGQCCCAGSRTFVHERVY 348
Cdd:cd07125 248 DGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVkDVVQSA-FGSAGQRCSALRLLYLQEEIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 349 DEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGvEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLi 428
Cdd:cd07125 327 ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELM-RGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDL- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 429 aTDEIFGPVQTILKFK--DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcfdvldASI--------PF 498
Cdd:cd07125 405 -TTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN------RNItgaivgrqPF 477
|
490 500
....*....|....*....|..
gi 18395300 499 GGYKMSGIGREKGIYslnNYLQ 520
Cdd:cd07125 478 GGWGLSGTGPKAGGP---NYLL 496
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
96-526 |
1.96e-79 |
|
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: 255.14 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 96 AVAAARKAFDEG-----PWpkmtayeRSKILFRFADLIEKHNDEI-AALETwDNGKPYEQSAQIEVPMLARVFRYY---- 165
Cdd:cd07087 3 LVARLRETFLTGktrslEW-------RKAQLKALKRMLTENEEEIaAALYA-DLGKPPAEAYLTEIAVVLGEIDHAlkhl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 166 AGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLswkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLH 242
Cdd:cd07087 75 KKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 243 EAgLPDGVVNIVSGFGATAGAAIASHMDvdKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVEL 322
Cdd:cd07087 152 KY-FDPEAVAVVEGGVEVATALLAEPFD--HIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 323 AHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRNVG-DPFKSGiEQGPQVDSEQFNKILKYIKHGveagaTLQ 401
Cdd:cd07087 228 IAWGKFLNAGQTCIAPDYVLVHESIKDELIEELK-KAIKEFYGeDPKESP-DYGRIINERHFDRLASLLDDG-----KVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 402 AGGDRLGSKgYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRV 481
Cdd:cd07087 301 IGGQVDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18395300 482 GTVWIN--CFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07087 380 GGVCVNdvLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
55-507 |
3.11e-78 |
|
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: 253.65 E-value: 3.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 55 QLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSKILFRFADLIEKHNDE 134
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 135 IAALETWDNGKPYEqSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPH-HVQTLHEPIGVAGQIIPWNFPLLMLSWKLG 213
Cdd:TIGR01722 80 IAELITAEHGKTHS-DALGDVARGLEVVEHACGVNSLLKGETSTQVATRvDVYSIRQPLGVCAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 214 PALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKS 293
Cdd:TIGR01722 159 IAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 294 NlKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSrTFVHERVYDEFVEKAKARALKRNVGDPFKSGIE 373
Cdd:TIGR01722 238 G-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 374 QGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGY----YIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEV 449
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395300 450 IARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcfdvldASIP-------FGGYKMSGIG 507
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN------VPIPvplpyfsFTGWKDSFFG 454
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
95-513 |
4.47e-78 |
|
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: 251.76 E-value: 4.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 95 RAVAAARKAFdegpwpkmTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEV-PMLA---RVFRYYAGWA- 169
Cdd:cd07134 8 QAHALALRAS--------TAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlPVLSeinHAIKHLKKWMk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 170 -DKI-HGMTMPGDgphHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLP 247
Cdd:cd07134 80 pKRVrTPLLLFGT---KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 248 DGVVnIVSGFGATAGAAIAshMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFAL 327
Cdd:cd07134 157 DEVA-VFEGDAEVAQALLE--LPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 328 FFNQGQCCCAGSRTFVHERVYDEFVEKAKArALKRNVGDpfKSGIEQGPQ----VDSEQFNKILKYIKHGVEAGATLQAG 403
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLKA-EIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 404 GDrLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGT 483
Cdd:cd07134 310 GQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGG 388
|
410 420 430
....*....|....*....|....*....|..
gi 18395300 484 VWIN--CFDVLDASIPFGGYKMSGIGREKGIY 513
Cdd:cd07134 389 VVVNdvVLHFLNPNLPFGGVNNSGIGSYHGVY 420
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
92-513 |
2.25e-76 |
|
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: 247.18 E-value: 2.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 92 DVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKP-YEqsAQIEV-PMLARV------FR 163
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWE--AQTEVaAMAGKIdisikaYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 164 YYAGwaDKIHGMtmpGDGPHHVQtlHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHE 243
Cdd:cd07095 77 ERTG--ERATPM---AQGRAVLR--HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 244 AGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNLKAVTLELGGKSPFIVCEDADVDQAVELA 323
Cdd:cd07095 150 AGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 324 HFALFFNQGQCCCAGSRTFVHE-RVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQA 402
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 403 GGDRLGSKGYYIQP-----TVFSDVKDdmliatDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMR 477
Cdd:cd07095 309 AMERLVAGTAFLSPgiidvTDAADVPD------EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 18395300 478 ALRVGTVWINCFDVLDAS-IPFGGYKMSGIGREKGIY 513
Cdd:cd07095 383 RIRAGIVNWNRPTTGASStAPFGGVGLSGNHRPSAYY 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
74-507 |
1.09e-75 |
|
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: 246.18 E-value: 1.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 74 LDPRNGEVIAQVSEGDAEDVNRAVAAARKAF-DEGPWpkMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPY----- 147
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLvdakv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 148 EQSAQIE-VPMLARVFRYYAGwaDKI-HGMTMPGDGpHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLK 225
Cdd:cd07148 82 EVTRAIDgVELAADELGQLGG--REIpMGLTPASAG-RIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 226 TAEQTPLSALLVGKLLHEAGLPDGVVNIVsgfgaTAGAAIASHMDVD-KVA---FTGSTDVGKIIlelasKSNLKAVT-- 299
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAV-----PCENAVAEKLVTDpRVAffsFIGSARVGWML-----RSKLAPGTrc 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 300 -LELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQV 378
Cdd:cd07148 229 aLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 379 DSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYyiQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRY 458
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 18395300 459 GLAAGVFTQNLDTAHRLMRALRVGTVWIN---CFDVldASIPFGGYKMSGIG 507
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNdhtAFRV--DWMPFAGRRQSGYG 436
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
73-524 |
1.84e-74 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 243.23 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 73 TLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQsAQ 152
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQ-AR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 153 IEVPMLARVFRYYAGwadkiHGMTMPGDGPHHVQT-----LHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTA 227
Cdd:PRK13968 88 AEVAKSANLCDWYAE-----HGPAMLKAEPTLVENqqaviEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 228 EQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIaSHMDVDKVAFTGSTDVGKIILELASKSnLKAVTLELGGKSP 307
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 308 FIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrnVGDPFKSGIEQGPQVDSEQFNK 385
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERfvAAAAALK--MGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 386 ILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVF 465
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 18395300 466 TQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAV 524
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
35-507 |
2.96e-72 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 248.57 E-value: 2.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 35 SNLAAAVENTITPPvkvEHTQLLIGGrfvdavSGKTFPTLDPRNGE-VIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMT 113
Cdd:PRK11904 537 EPLAAAIAAFLEKQ---WQAGPIING------EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTP 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 114 AYERSKILFRFADLIEKHNDEIAAL------ETWDNGkpyeqsaqievpmLARV-----F-RYYAGWADKIHGM--TMPG 179
Cdd:PRK11904 606 VEERAAILERAADLLEANRAELIALcvreagKTLQDA-------------IAEVreavdFcRYYAAQARRLFGApeKLPG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 180 -DGPHHVQTLHePIGVAGQIIPWNFPLLMLswkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVS 255
Cdd:PRK11904 673 pTGESNELRLH-GRGVFVCISPWNFPLAIF---LGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLP 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 256 GFGATAGAAIASHMDVDKVAFTGSTDVGKII-LELASKSNlKAVTL--ELGGKSPFIVceDAD------VDQAVELAhfa 326
Cdd:PRK11904 749 GDGATVGAALTADPRIAGVAFTGSTETARIInRTLAARDG-PIVPLiaETGGQNAMIV--DSTalpeqvVDDVVTSA--- 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 327 lFFNQGQCCCAGSRTFVHERVYDEFVE--KAKARALKrnVGDPFKSGIEQGPQVDSEQFNKILKYIKHgVEAGATL--QA 402
Cdd:PRK11904 823 -FRSAGQRCSALRVLFVQEDIADRVIEmlKGAMAELK--VGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLlaQL 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 403 GGDRLGSKGYYIQPTVF--SDVKDdmliATDEIFGPVQTILKFK--DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRA 478
Cdd:PRK11904 899 PLPAGTENGHFVAPTAFeiDSISQ----LEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADR 974
|
490 500 510
....*....|....*....|....*....|..
gi 18395300 479 LRVGTVWINcFDVLDASI---PFGGYKMSGIG 507
Cdd:PRK11904 975 VRVGNVYVN-RNQIGAVVgvqPFGGQGLSGTG 1005
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
101-513 |
7.87e-69 |
|
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: 227.75 E-value: 7.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 101 RKAFDEGPWPkmTAYERSKILFRFADLIEKHNDEIA-ALETWDNGKPYEQSAQIEV-PMLARVfRYY----AGW--ADKI 172
Cdd:cd07133 8 KAAFLANPPP--SLEERRDRLDRLKALLLDNQDALAeAISADFGHRSRHETLLAEIlPSIAGI-KHArkhlKKWmkPSRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 173 HgmTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLlMLSwkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDg 249
Cdd:cd07133 85 H--VGLLFLPAKAEVEYQPLGVVGIIVPWNYPL-YLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 250 VVNIVSGfGATAGAAIaSHMDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFF 329
Cdd:cd07133 159 EVAVVTG-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 330 NQGQCCCAGSRTFVHERVYDEFVEKAKARALKRnvgdpFKSGIEqGPQ----VDSEQFNKILKYIKHGVEAGATL----Q 401
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-----YPTLAD-NPDytsiINERHYARLQGLLEDARAKGARVielnP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 402 AGGDRLGSKgyYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRV 481
Cdd:cd07133 310 AGEDFAATR--KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHS 387
|
410 420 430
....*....|....*....|....*....|....
gi 18395300 482 GTVWIN--CFDVLDASIPFGGYKMSGIGREKGIY 513
Cdd:cd07133 388 GGVTINdtLLHVAQDDLPFGGVGASGMGAYHGKE 421
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
57-511 |
1.98e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 226683 [Multi-domain] Cd Length: 769 Bit Score: 231.90 E-value: 1.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAvsGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:COG4230 117 IVNGAPVAG--GEPRPVINPADpDDIVGTVTEATEADVEQALEAAVAAAPI--WSATPPAERAAILERAADLMEAQMPQL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 AALETWDNGKPYeQSAQIEVPMLARVFRYYAGWADKihgmTMPGDGphhvqtlHEPIGVAGQIIPWNFPLLMLSWKLGPA 215
Cdd:COG4230 193 MGLLVREAGKTL-SNAIAEVREAVDFLRYYAGQARD----TFGNLT-------HRPLGPVVCISPWNFPLAIFTGQIAAA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 216 LACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNL 295
Cdd:COG4230 261 LAAGNSVLAKPAEQTPLIAAQAVRLLHEAGVPPGVLQLLPGRGETVGAALTADARVAGVMFTGSTEVARLIQRQLAKRQG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 296 KAVTL--ELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIE 373
Cdd:COG4230 341 RPIPLiaETGGQNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCLQEDVADRILTMLKGAMAELRVGNPDRLTTD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 374 QGPQVDSEQFNKILKYIK---------HGVEAGATLQaggdrlgsKGYYIQPTVFS-DVKDDMliaTDEIFGPVQTILKF 443
Cdd:COG4230 421 VGPVIDAEAKANIEKHIQtmrskgrlvHQAAAPNSLQ--------KGTFVAPTLIElENLDEL---QREVFGPVLHVVRY 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395300 444 K--DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDASI---PFGGYKMSGIGREKG 511
Cdd:COG4230 490 KrdELDEVIDQINATGYGLTLGVHTRIDETIAHVTERAHAGNLYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 561
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
189-526 |
2.66e-67 |
|
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: 223.64 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 189 HEPIGVAGQIIPWNFPLLMLswkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAI 265
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 266 ASHMDvdKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHE 345
Cdd:cd07135 182 EQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 346 RVYDEFVEKAKaRALKRNvgdpFKSGIEQGPQ----VDSEQFNKILKYIKhgvEAGATLQAGGDRLGSKgYYIQPTVFSD 421
Cdd:cd07135 259 SVYDEFVEELK-KVLDEF----YPGGANASPDytriVNPRHFNRLKSLLD---TTKGKVVIGGEMDEAT-RFIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 422 VKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWIN--CFDVLDASIPFG 499
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtLIHVGVDNAPFG 409
|
330 340
....*....|....*....|....*..
gi 18395300 500 GYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07135 410 GVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-505 |
2.21e-66 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 222.53 E-value: 2.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 56 LLIGGRFVdAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI 135
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 136 A---ALETwdnGKPYEQSAQiEV-PMLARV---FRYYagwadkiHGMTMP--GDGPHHVQTL-HEPIGVAGQIIPWNFPL 205
Cdd:PRK09457 80 AeviARET---GKPLWEAAT-EVtAMINKIaisIQAY-------HERTGEkrSEMADGAAVLrHRPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 206 LMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKI 285
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 286 ILELASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVY-DEFVEKAKARALKRNV 364
Cdd:PRK09457 228 LHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 365 GDPFKSgiEQ---GPQVDSEQFNKILKYIKHGVEAGA------TLQAGGDRLGSKGyYIQPTVFSDVKDdmliatDEIFG 435
Cdd:PRK09457 308 GRWDAE--PQpfmGAVISEQAAQGLVAAQAQLLALGGksllemTQLQAGTGLLTPG-IIDVTGVAELPD------EEYFG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 436 PVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTV-WINCFDVLDASIPFGGYKMSG 505
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
190-534 |
4.56e-66 |
|
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: 220.84 E-value: 4.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 190 EPIGVAGQIIPWNFPLLMLswkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAGAAIA 266
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 267 SHMDvdKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHER 346
Cdd:cd07136 175 QKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 347 VYDEFVEKAKARALKRNVGDPFKSgiEQGPQVDSEQ-FNKILKYIKHGveagaTLQAGG--DRlgsKGYYIQPTVFSDVK 423
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLES--PDYGRIINEKhFDRLAGLLDNG-----KIVFGGntDR---ETLYIEPTILDNVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 424 DDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcfdvlDASI------- 496
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----DTIMhlanpyl 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 18395300 497 PFGGYKMSGIGREKGIYSLNNYLQVKAVVtslKNPAWL 534
Cdd:cd07136 397 PFGGVGNSGMGSYHGKYSFDTFSHKKSIL---KKSTWF 431
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
53-511 |
6.03e-65 |
|
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: 219.40 E-value: 6.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 53 HTQLLIGGRFVDavSGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKH 131
Cdd:TIGR01238 37 QAAPIIGHSYKA--DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT--WNATPAKERAAKLDRLADLLELH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 132 NDEIAALETWDNGKPYEQSAQiEVPMLARVFRYYAGWADKIHGmtmpgdgphhvQTLHEPIGVAGQIIPWNFPLLMLSWK 211
Cdd:TIGR01238 113 MPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVRDVLG-----------EFSVESRGVFVCISPWNFPLAIFTGQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 212 LGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELAS 291
Cdd:TIGR01238 181 ISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 292 KSNLKAVTL--ELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFK 369
Cdd:TIGR01238 261 QREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 370 SGIEQGPQVDSEQFNKILKYIKHGVEAGAT---LQAGGDRLGSKGYYIQPTVFSdvKDDMLIATDEIFGPVQTILKFK-- 444
Cdd:TIGR01238 341 LTTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaqLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKar 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 445 DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDASI---PFGGYKMSGIGREKG 511
Cdd:TIGR01238 419 ELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN-RNQVGAVVgvqPFGGQGLSGTGPKAG 487
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
57-533 |
3.78e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 214.23 E-value: 3.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSKILFRFADLIEKHNDEIA 136
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 137 ALETWDNGKPyEQSAQIEVPMLARVFRYYA-------GWADKIHGMTMPGDGPHHVQTLHE-PIGVAGQIIPWNFPLLML 208
Cdd:PLN00412 97 ECLVKEIAKP-AKDAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKiPLGVVLAIPPFNYPVNLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 209 SWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGStDVGkiiLE 288
Cdd:PLN00412 176 VSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG---IA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 289 LASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPf 368
Cdd:PLN00412 252 ISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 369 KSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRlgsKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDE 448
Cdd:PLN00412 331 EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 449 VIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDAS-IPFGGYKMSGIGREKGIYSLNNYLQVKAVVTS 527
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKSTVIN 487
|
....*.
gi 18395300 528 LKNPAW 533
Cdd:PLN00412 488 LPKPSY 493
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
64-507 |
3.83e-62 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 220.89 E-value: 3.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 64 DAVSGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWD 142
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 143 NGKPYeQSAQIEVPMLARVFRYYAGWADKihgmtMPGDGPHhvqtlhEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTV 222
Cdd:PRK11905 640 AGKTL-ANAIAEVREAVDFLRYYAAQARR-----LLNGPGH------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTV 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 223 VLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKII-LELASKSNlKAVTL- 300
Cdd:PRK11905 708 LAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqRTLAKRSG-PPVPLi 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 301 -ELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKArALK-RNVGDPFKSGIEQGPQV 378
Cdd:PRK11905 787 aETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKG-AMDeLRIGDPWRLSTDVGPVI 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 379 DSEQFNKILKYIKHGVEAGATL-QAGGDRLGSKGYYIQPTVF-----SDVKddmliatDEIFGPVQTILKFK--DLDEVI 450
Cdd:PRK11905 866 DAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIeidsiSDLE-------REVFGPVLHVVRFKadELDRVI 938
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 451 ARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDA---SIPFGGYKMSGIG 507
Cdd:PRK11905 939 DDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgVQPFGGEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
117-525 |
5.11e-62 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 211.43 E-value: 5.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 117 RSKILFRFADLIEKHNDEI-AALETwDNGKPYEQSAQIEVP--------MLARVFRYYAGWADKIHGMTMPGDGphhvQT 187
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFsEAVHK-DLGRHPFETKMTEVLltvaeiehLLKHLDEYLKPEKVDTVGVFGPGKS----YI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 188 LHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGfGATAGAAIAS 267
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 268 HmDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERV 347
Cdd:PTZ00381 184 E-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 348 YDEFVEKAKaRALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKhgvEAGATLQAGGDrLGSKGYYIQPTVFSDVKDDML 427
Cdd:PTZ00381 262 KDKFIEALK-EAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGE-VDIENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 428 IATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWIN--CFDVLDASIPFGGYKMSG 505
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVGNSG 416
|
410 420
....*....|....*....|
gi 18395300 506 IGREKGIYSLNNYLQVKAVV 525
Cdd:PTZ00381 417 MGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
35-505 |
5.38e-61 |
|
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: 209.37 E-value: 5.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 35 SNLAAAVENTITPPVKVehtQLLIGGRFVDavSGKTFPTLDPRN-GEVIAQVSEGDAEDVNRAVAAARKAFDEgpWPKMT 113
Cdd:cd07123 17 AKLQEALAELKSLTVEI---PLVIGGKEVR--TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKE--WARMP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 114 AYERSKILFRFADLIE-KHNDEIAALETWDNGKPYEQsAQIEVPM-LARVFRYYAGWADKIHGMtmpgdgphhvQTLHEP 191
Cdd:cd07123 90 FEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQ-AEIDAACeLIDFLRFNVKYAEELYAQ----------QPLSSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 192 IGVAGQ------------IIPWNFPLLMLSWKLGPALAcGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGA 259
Cdd:cd07123 159 AGVWNRleyrplegfvyaVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 260 TAGAAIASHMDVDKVAFTGSTDVGKIILELASkSNLKA------VTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQ 333
Cdd:cd07123 238 VVGDTVLASPHLAGLHFTGSTPTFKSLWKQIG-ENLDRyrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 334 CCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEA-GATLQAGGDRLGSKGY 412
Cdd:cd07123 317 KCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 413 YIQPTVF--SDVKDDMLiaTDEIFGPVQTILKFKD--LDEVIARANN-SRYGLAAGVFTQNLDTAHRLMRALR--VGTVW 485
Cdd:cd07123 397 FVEPTVIetTDPKHKLM--TEEIFGPVLTVYVYPDsdFEETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFY 474
|
490 500
....*....|....*....|....
gi 18395300 486 INcfDVLDASI----PFGGYKMSG 505
Cdd:cd07123 475 IN--DKPTGAVvgqqPFGGARASG 496
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
31-530 |
7.67e-60 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 208.06 E-value: 7.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 31 AQRYSNLAAAVENTITP--PVKVEHtqlLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFdegP 108
Cdd:PLN02419 92 ALRSSWLSTSPEQSTQPqmPPRVPN---LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF---P 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 109 -WPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSaQIEVPMLARVFRYYAGWADKIHGMTMPG-DGPHHVQ 186
Cdd:PLN02419 166 lWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEYLPNvSNGVDTY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 187 TLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGaAIA 266
Cdd:PLN02419 245 SIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AIC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 267 SHMDVDKVAFTGSTDVGKIILELASKSNlKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSR-TFVHE 345
Cdd:PLN02419 324 DDEDIRAVSFVGSNTAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 346 RVY--DEFVEKAKarALKRNVGDpfKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGY----YIQPTVF 419
Cdd:PLN02419 403 AKSweDKLVERAK--ALKVTCGS--EPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTIL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 420 SDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCfdVLDASIP-- 497
Cdd:PLN02419 479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPff 556
|
490 500 510
....*....|....*....|....*....|....*.
gi 18395300 498 -FGGYKMSGIGREK--GIYSLNNYLQVKAVVTSLKN 530
Cdd:PLN02419 557 sFTGNKASFAGDLNfyGKAGVDFFTQIKLVTQKQKD 592
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
67-520 |
2.24e-58 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 201.99 E-value: 2.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 67 SGKTFPTLDPRNGEVIAQVSEGDAEDVN---RAVAAARKAfdegpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDN 143
Cdd:PLN02315 32 NGPLVSSVNPANNQPIAEVVEASLEDYEeglRACEEAAKI-----WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 144 GKPYEQSAQiEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQT-LHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTV 222
Cdd:PLN02315 107 GKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMeVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 223 VLKTAEQTPLSAL----LVGKLLHEAGLPDGVVNIVSGfGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNLKAV 298
Cdd:PLN02315 186 VWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 299 tLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQV 378
Cdd:PLN02315 265 -LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 379 DSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFsDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRY 458
Cdd:PLN02315 344 TPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395300 459 GLAAGVFTQNLDTAHRLmralrVGTVWINCfDVLDASIP---------FGGYKMSGIGREKGIYSLNNYLQ 520
Cdd:PLN02315 423 GLSSSIFTRNPETIFKW-----IGPLGSDC-GIVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMR 487
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
96-514 |
1.10e-50 |
|
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: 179.72 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 96 AVAAARKAFDEGpwpKMTAYE-RSKILFRFADLIEKHNDEI-AALETwDNGKPYEQSAQIEVPMLARVFRYYAgwaDKIH 173
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEfRIQQLEALLRMLEENEDEIvEALAK-DLRKPKFEAVLSEILLVKNEIKYAI---SNLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 174 GMTMPGDGPHHVQTL-------HEPIGVAGQIIPWNFPLLMLswkLGP---ALACGNTVVLKTAEQTPLSALLVGKLLHE 243
Cdd:cd07132 76 EWMKPEPVKKNLATLlddvyiyKEPLGVVLIIGAWNYPLQLT---LVPlvgAIAAGNCVVIKPSEVSPATAKLLAELIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 244 AGLPD--GVVnivsgfgaTAGAAIASHM---DVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQ 318
Cdd:cd07132 153 YLDKEcyPVV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 319 AVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKhgveaGA 398
Cdd:cd07132 224 AARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALK-KTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS-----GG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 399 TLQAGGDrLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRA 478
Cdd:cd07132 298 KVAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSN 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18395300 479 LRVGTVWINcfDVL----DASIPFGGYKMSGIGREKGIYS 514
Cdd:cd07132 377 TSSGGVCVN--DTImhytLDSLPFGGVGNSGMGAYHGKYS 414
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
93-526 |
9.75e-49 |
|
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: 174.14 E-value: 9.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 93 VNRAVAAARKAFDEGpwpKMTAYE-RSKILFRFADLIEKHNDEI-AALETwDNGKPYEQSAQIEVPMLAR----VFRYYA 166
Cdd:cd07137 1 APRLVRELRETFRSG---RTRSAEwRKSQLKGLLRLVDENEDDIfAALRQ-DLGKPSAESFRDEVSVLVSscklAIKELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 167 GWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLhEAGL 246
Cdd:cd07137 77 KWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 247 PDGVVNIVSGfGATAGAAIASHmDVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVceDADVDQAVELAHFA 326
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIV--DSTVDLKVAVRRIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 327 L---FFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAG 403
Cdd:cd07137 231 GgkwGCNNGQACIAPDYVLVEESFAPTLIDALK-NTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 404 gdRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGT 483
Cdd:cd07137 310 --ERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 18395300 484 VWIN--CFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:cd07137 388 VTFNdtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
32-511 |
2.87e-47 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 177.09 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 32 QRYSNLAAAVENTITPPVKVEHtqlLIGGRFVDAVSGKTFPTLDPRngEVIAQVSEGDAEDVNRAVAAARKAfdeGP-WP 110
Cdd:PRK11809 628 HRLASLSSALLASAHQKWQAAP---MLEDPVAAGEMSPVINPADPR--DIVGYVREATPAEVEQALESAVNA---APiWF 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 111 KMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYeQSAQIEVPMLARVFRYYAGWADkihgmtmpgdgPHHVQTLHE 190
Cdd:PRK11809 700 ATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTF-SNAIAEVREAVDFLRYYAGQVR-----------DDFDNDTHR 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 191 PIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMD 270
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADAR 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 271 VDKVAFTGSTDVGKII-LELASK--SNLKAVTL--ELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHE 345
Cdd:PRK11809 848 VRGVMFTGSTEVARLLqRNLAGRldPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQD 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 346 RVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIK------HGVEAGATLQAGGDRLGSkgyYIQPTVF 419
Cdd:PRK11809 928 DVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQamrakgRPVFQAARENSEDWQSGT---FVPPTLI 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 420 S-DVKDDMliaTDEIFGPVQTILKFK--DLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINcFDVLDASI 496
Cdd:PRK11809 1005 ElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVV 1080
|
490
....*....|....*...
gi 18395300 497 ---PFGGYKMSGIGREKG 511
Cdd:PRK11809 1081 gvqPFGGEGLSGTGPKAG 1098
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
87-526 |
1.07e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 142.17 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 87 EGDAEDVNRAVAAARKAFDEGPwPKMTAYERSKI--LFRFadLIEKHNDEIAALETwDNGKPYEQSAQIEVPMLARVFRY 164
Cdd:PLN02203 2 EAPGETLEGSVAELRETYESGR-TRSLEWRKSQLkgLLRL--LKDNEEAIFKALHQ-DLGKHRVEAYRDEVGVLTKSANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 165 ----YAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKL 240
Cdd:PLN02203 78 alsnLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 241 LhEAGLPDGVVNIVSGfgataGAAIASHM---DVDKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIV-CEDA-- 314
Cdd:PLN02203 158 I-PKYLDSKAVKVIEG-----GPAVGEQLlqhKWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSsr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 315 DVDQAVELAHFALFFN-QGQCCCAGSRTFVHERVYDEFVEKAKArALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHG 393
Cdd:PLN02203 231 DTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKS-TIKKFFGENPRESKSMARILNKKHFQRLSNLLKDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 394 VEAGATLQAGGdrLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAH 473
Cdd:PLN02203 310 RVAASIVHGGS--IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKR 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 474 RLMRALRVGTVWINcfdvlDA-------SIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 526
Cdd:PLN02203 388 RILSETSSGSVTFN-----DAiiqyacdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLR 442
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
90-525 |
1.76e-36 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 141.34 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 90 AEDVNRAVAAARKAFDEGpwpKMTAYE-RSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEVPMLAR----VFRY 164
Cdd:PLN02174 9 AADASILVTELRRSFDDG---VTRGYEwRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNsiklALKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 165 YAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLhEA 244
Cdd:PLN02174 86 LKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 245 GLPDGVVNIVSGFGATAGAAIASHMDvdKVAFTGSTDVGKIILELASKsNLKAVTLELGGKSPFIVCEDADVDQAVELAH 324
Cdd:PLN02174 165 YLDSSAVRVVEGAVTETTALLEQKWD--KIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 325 FALF-FNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGiEQGPQVDSEQFNKILKYIKHGvEAGATLQAG 403
Cdd:PLN02174 242 AGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEK-EVSDKIVYG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 404 GDRlGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGT 483
Cdd:PLN02174 320 GEK-DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 18395300 484 VWINCFDVLDA--SIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 525
Cdd:PLN02174 399 IVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
93-466 |
1.27e-34 |
|
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: 135.44 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 93 VNRAVAAARKafDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEVPmlARVFRYYA--GWAD 170
Cdd:cd07084 1 PERALLAADI--STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGD--QVQLRARAfvIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 171 KIHGMTM--PGDGP----HHVQTlhePIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEA 244
Cdd:cd07084 77 RIPHEPGnhLGQGLkqqsHGYRW---PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 245 G-LPDGVVNIVSGFGATaGAAIASHMDVDKVAFTGSTDVGKiilELASKSNLKAVTLELGGKSPFIVCEDAD-VDQAVEL 322
Cdd:cd07084 154 GlLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAE---KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 323 AHFALFFNQGQCCCAGSRTFVHERVYDE-FVEKAKARALKRNVGDPFksgieqgpqVDSEQFNKILKYIKH-GVEAGATL 400
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLL---------LGPVQTFTTLAMIAHmENLLGSVL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395300 401 QAGG------DRLGSKGYYIQPTVFSDVKDDM---LIATDEIFGPVQTILKFKDLDE--VIARANNSRYGLAAGVFT 466
Cdd:cd07084 301 LFSGkelknhSIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYS 377
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
58-473 |
1.82e-32 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 130.59 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVDAvSGKTFPTLDPRNGEVIAQVSeGDAEDVNRAVAAARKafDEGPWPKMTAY-ERSKILFRFADLIEKHNDEIA 136
Cdd:PRK11903 9 VAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYaQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 137 ALETwDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGP------------HHVQTlhePI-GVAGQIIPWNF 203
Cdd:PRK11903 85 DIAT-ANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgQHVLV---PTrGVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 204 PLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAG-LPDGVVNIVSGFGATAGAAIAShMDVdkVAFTGSTDV 282
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQP-FDV--VSFTGSAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 283 GKIILELAS------KSNLKAVTLELGgkspfIVCEDADVDQAVelahFALFFNQ---------GQCCCAGSRTFVHERV 347
Cdd:PRK11903 238 AAVLRSHPAvvqrsvRVNVEADSLNSA-----LLGPDAAPGSEA----FDLFVKEvvremtvksGQKCTAIRRIFVPEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 348 YDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHgVEAGATLQAGGDRLG------SKGYYIQPTVF-- 419
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFAlvdadpAVAACVGPTLLga 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 18395300 420 SDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQnlDTAH 473
Cdd:PRK11903 388 SDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSD--DAAF 439
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
58-524 |
1.60e-30 |
|
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: 124.69 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 58 IGGRFVdAVSGKTFPTLDPRNGEVIAQVSeGDAEDVNRAVAAARKafDEGP-WPKMTAYERSKILFRFADLIEKHNDEIA 136
Cdd:cd07128 5 VAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE--KGGPaLRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 137 ALETWDNGKpyEQSAQIEVPMLARVFRYYAGWADKIhgmtMPG-----DGP------------HHVQTlhePI-GVAGQI 198
Cdd:cd07128 81 ALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRE----LPNahflvEGDveplskdgtfvgQHILT---PRrGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 199 IPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAG-LPDGVVNIVSGfgatAGAAIASHMDV-DKVAF 276
Cdd:cd07128 152 NAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 277 TGSTDVGKIileLASKSNLKA----VTLELGGKSPFIVCEDADVDQAvelaHFALFFNQ---------GQCCCAGSRTFV 343
Cdd:cd07128 228 TGSAATAAK---LRAHPNIVArsirFNAEADSLNAAILGPDATPGTP----EFDLFVKEvaremtvkaGQKCTAIRRAFV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 344 HERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQfnkilkyiKHGVEAG-ATLQAGGDRLGS------------- 409
Cdd:cd07128 301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQ--------REDVRAAvATLLAEAEVVFGgpdrfevvgadae 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 410 KGYYIQPTVFsdVKDDMLIATD----EIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRAL--RVGT 483
Cdd:cd07128 373 KGAFFPPTLL--LCDDPDAATAvhdvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAapYHGR 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18395300 484 VWINCFDVLDASI----PF-----GGYKMSGIGRE-KGIYSLNNYLQVKAV 524
Cdd:cd07128 451 LLVLNRDSAKESTghgsPLpqlvhGGPGRAGGGEElGGLRGVKHYMQRTAV 501
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
93-487 |
2.53e-20 |
|
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: 93.76 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 93 VNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEI---AALETwdnGKPyEQSAQIEVP-------MLARVF 162
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLP-EARLQGELGrttgqlrLFADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 163 RyyAG-WADKIHGMTMPGDGPH---HVQTLHEPIGVAGQIIPWNFPLlMLSWKLG---PALACGNTVVLKTAEQTPLSAL 235
Cdd:cd07129 75 R--EGsWLDARIDPADPDRQPLprpDLRRMLVPLGPVAVFGASNFPL-AFSVAGGdtaSALAAGCPVVVKAHPAHPGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 236 LVGKLLHEA----GLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNL-KAVTLELGGKSPFIV 310
Cdd:cd07129 152 LVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 311 CEDADVDQAVELAH-FA--LFFNQGQCC----------CAGSRTFVhERVYDEFVEKAKARALKRNVGDPFKSGIEQgpq 377
Cdd:cd07129 232 LPGALAERGEAIAQgFVgsLTLGAGQFCtnpglvlvpaGPAGDAFI-AALAEALAAAPAQTMLTPGIAEAYRQGVEA--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 378 vdseqfnkiLKyikhgvEAGATLQAGGDRLGSKGYYIQPTVFSdVKDDMLIATD----EIFGPVQTILKFKDLDEVIARA 453
Cdd:cd07129 308 ---------LA------AAPGVRVLAGGAAAEGGNQAAPTLFK-VDAAAFLADPalqeEVFGPASLVVRYDDAAELLAVA 371
|
410 420 430
....*....|....*....|....*....|....*...
gi 18395300 454 NNSRYGLAAGVF--TQNLDTAHRLMRAL--RVGTVWIN 487
Cdd:cd07129 372 EALEGQLTATIHgeEDDLALARELLPVLerKAGRLLFN 409
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
57-464 |
2.26e-17 |
|
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: 84.85 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 57 LIGGRFVDAVSGKTFptLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYER----SKILFRFADLIEKHN 132
Cdd:cd07126 2 LVAGKWKGASNYTTL--LDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERyllyGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 133 DE--IAALETWDNGKPYEQsAQIEVPMLARVFRYYAGwaDKIH----GMTMPGDgpHHVQTLHE---PIGVAGQIIPWNF 203
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQ-ALGEVVVTRKFLENFAG--DQVRflarSFNVPGD--HQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 204 PLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGaAIASHMDVDKVAFTGSTDVG 283
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 284 -KIILELASKsnlkaVTLELGGKSPFIVCED-ADVDQAVELAHFALFFNQGQCCCAGSRTFVHER-VYDEFVEKAKARAL 360
Cdd:cd07126 234 eRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 361 KRNVGDpfksgIEQGPqVDSEQFNKILKYIKHGVE-AGATLQAGGDRLgsKGYYI-------QPT-VF-----SDVKDDM 426
Cdd:cd07126 309 QRKLED-----LTIGP-VLTWTTERILDHVDKLLAiPGAKVLFGGKPL--TNHSIpsiygayEPTaVFvpleeIAIEENF 380
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18395300 427 LIATDEIFGPVQTILKFKD--LDEVIARANNSRYGLAAGV 464
Cdd:cd07126 381 ELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAV 420
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
113-356 |
8.78e-13 |
|
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: 69.94 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 113 TAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEVPMLARV----------FRYYAGWADKIHGMTMPGDGP 182
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSesklyknidtERGITASVGHIQDVLLPDNGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 183 HHVQTlhEPIGVAGQIIPWNFPLLMLSwKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAgLPDGVVNIVSGFGATAG 262
Cdd:cd07077 94 TYVRA--FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-DAAHGPKILVLYVPHPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 263 AAIA----SHMDVDKVAFTGSTDVGKIILelaSKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQgQCCCAG 338
Cdd:cd07077 170 DELAeellSHPKIDLIVATGGRDAVDAAV---KHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NACASE 245
|
250
....*....|....*...
gi 18395300 339 SRTFVHERVYDEFVEKAK 356
Cdd:cd07077 246 QNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
93-358 |
1.45e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 50.73 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 93 VNRAVAAARKAFDEgpWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKpyeqsAQIEVPMLARVF--RY-YAGWA 169
Cdd:cd07081 1 LDDAVAAAKVAQQG--LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGM-----GRVEDKVIKNHFaaEYiYNVYK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 170 DKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVL----KTAEQTPLSALLVGKLLHEAG 245
Cdd:cd07081 74 DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 246 LPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGstdvGKIILELASKSNLKAVTLElGGKSPFIVCEDADVDQAVELAHF 325
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVG-AGNTPVVIDETADIKRAVQSIVK 228
|
250 260 270
....*....|....*....|....*....|...
gi 18395300 326 ALFFNQGQCCCAGSRTFVHERVYDEFVEKAKAR 358
Cdd:cd07081 229 SKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQ 261
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
190-488 |
2.39e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 40.55 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 190 EPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVL----KTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAI 265
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFsphpRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 266 ASHMDVDKVAFTGstdvGKIILELASKSNLKAvtleLG---GKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTF 342
Cdd:cd07122 174 MKHPDVDLILATG----GPGMVKAAYSSGKPA----IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 343 VHERVYDEFVEkakarALKRNvGDPFksgieqgpqVDSEQFNKILKYIkhgVEAGATLQAggDRLGSKGYYIQPTVFSDV 422
Cdd:cd07122 246 VDDEIYDEVRA-----ELKRR-GAYF---------LNEEEKEKLEKAL---FDDGGTLNP--DIVGKSAQKIAELAGIEV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395300 423 KDD--MLIATDEIFG-----------PVQTILKFKDLDEVIARA----NNSRYGLAAGVFTQNLDTAHRLMRALRVGTVW 485
Cdd:cd07122 306 PEDtkVLVAEETGVGpeeplsreklsPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSRIL 385
|
...
gi 18395300 486 INC 488
Cdd:cd07122 386 VNT 388
|
|
|