|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
23-498 |
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: 816.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 23 EQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELES 102
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 103 QIDLVSSIEALDNGKTL-ALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAW 181
Cdd:cd07091 81 DRDELAALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 182 KIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDS 261
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 262 SESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFD 341
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAE-KRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 342 KANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEG 421
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 422 VEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
39-496 |
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: 644.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 39 DGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKT 118
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 119 LALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPA 198
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 199 AVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSA 278
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 279 HLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTI 358
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 359 MNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIET 438
Cdd:pfam00171 321 LKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 439 ESLSTGLKVAKMLKAGTVWINTYNDFDSR-VPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
23-500 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 627.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 23 EQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELES 102
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 103 QIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTG-DGYMNFTTLEPIGVCGQIIPWNFPIMMLAW 181
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 182 KIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDS 261
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 262 SEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFD 341
Cdd:COG1012 241 AE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA-LKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 342 KANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV-GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDF-DSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIK 499
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 20981689 500 L 500
Cdd:COG1012 479 L 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-500 |
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: 605.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 21 TYEQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhDTEWATQ-DPRERGRLLSKLADE 99
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGLKvSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 100 LESQIDLVSSIEALDNGKT-LALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMM 178
Cdd:cd07143 81 MERNLDYLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 179 LAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVA 258
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 259 VDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGN 338
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK-KLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 339 PFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTL 418
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 419 EEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
..
gi 20981689 499 KL 500
Cdd:cd07143 480 NL 481
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
26-499 |
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: 602.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 26 TGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFH-DTEWATQDPRERGRLLSKLADELESQI 104
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 105 DLVSSIEALDNGKTLALAR-GDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKI 183
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 184 APALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSE 263
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 264 SNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETEiKVGNPFDKA 343
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR-VVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 344 NFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVE 423
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20981689 424 MANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIK 499
Cdd:cd07141 406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-500 |
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: 590.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 19 GLTYEQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhDTEWATQDPRERGRLLSKLAD 98
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF-ESWWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 99 ELESQIDLVSSIEALDNGKTLAL-ARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIM 177
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 178 MLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSV 257
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 258 AVDSSeSNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETEIKVG 337
Cdd:cd07144 240 MKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 338 NPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGD---KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAK 414
Cdd:cd07144 319 SPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 415 FKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVK 494
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
....*.
gi 20981689 495 AVRIKL 500
Cdd:cd07144 479 AVHINL 484
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
45-498 |
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: 553.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVNGRTINTGDG-YMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPL 203
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGdYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 204 NALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFD 283
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 284 DANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYID 363
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARA-IRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 364 IGKKEGAKILTGGEKVG----DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETE 439
Cdd:cd07114 319 RAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 440 SLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
66-498 |
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: 550.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 66 EYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNG 145
Cdd:cd07078 1 DAAVAAARAAFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 146 RTINTGD-GYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNI 224
Cdd:cd07078 79 EVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 225 VPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQ 304
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 305 ICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV-GDKG 383
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVK-ALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 384 YFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYND 463
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 20981689 464 F-DSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07078 397 GaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
45-500 |
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: 543.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 -DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPL 203
Cdd:cd07115 79 lDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 204 NALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVaVDSSESNLKKITLELGGKSAHLVFD 283
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKI-MQGAAGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 284 DANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAyLETEIKVGNPFDKANFQGAITNRQQFDTIMNYID 363
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTS-LARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 364 IGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLST 443
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 444 GLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
24-496 |
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: 528.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 24 QPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQ 103
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 104 IDLVSSIEALDNGKTLALAR-GDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWK 182
Cdd:cd07142 82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 183 IAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSS 262
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 263 ESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETEIkVGNPFDK 342
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRV-VGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 343 ANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGV 422
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20981689 423 EMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
40-498 |
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: 517.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 40 GKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTL 119
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 120 ALAR-GDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPA 198
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 199 AVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKITLELGGKSA 278
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 279 HLVFDDA-NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAR-EWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKV--GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSG 435
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20981689 436 IETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
29-500 |
1.86e-180 |
|
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: 514.94 E-value: 1.86e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALA 188
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 189 MGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKK 268
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 269 ITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGA 348
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAK-KIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 349 ITNRQQFDTIMNYIDIGKKEGAKILTGG----EKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEM 424
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20981689 425 ANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
47-498 |
1.36e-179 |
|
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: 511.34 E-value: 1.36e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALAR-GD 125
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAF--PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 126 VTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNA 205
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 206 LYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDA 285
Cdd:cd07093 161 WLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 286 NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIG 365
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAK-ALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 366 KKEGAKILTGGEKVG----DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESL 441
Cdd:cd07093 319 RAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 442 STGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
26-496 |
2.02e-176 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 505.13 E-value: 2.02e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 26 TGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQID 105
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 106 LVSSIEALDNGKTLALARG-DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIA 184
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 185 PALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSES 264
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 265 NLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELL--AAFKAyleTEIKVGNPFDK 342
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVkkLVEKA---KDWVVGDPFDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 343 ANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGV 422
Cdd:PLN02766 338 RARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20981689 423 EMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
45-496 |
3.54e-172 |
|
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: 492.33 E-value: 3.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAF--KTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTL-EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPL 203
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIkQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 204 NALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFD 283
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 284 DANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYID 363
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVK-KLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 364 IGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLST 443
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 20981689 444 GLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
27-494 |
1.20e-169 |
|
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: 487.24 E-value: 1.20e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAF--KTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGK----TLALargDVTIAINCLRDAAAYADKVNGrTINTGDG-YMNFTTLEPIGVCGQIIPWNFPIMMLAW 181
Cdd:cd07559 80 LAVAETLDNGKpireTLAA---DIPLAIDHFRYFAGVIRAQEG-SLSEIDEdTLSYHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 182 KIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDS 261
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 262 SEsNLKKITLELGGKSAHLVFDDA-----NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKV 336
Cdd:cd07559 235 AE-NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEA-IKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 337 GNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV----GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTV 412
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 413 AKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTE 492
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
..
gi 20981689 493 VK 494
Cdd:cd07559 473 TK 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
45-498 |
1.32e-166 |
|
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: 478.65 E-value: 1.32e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQdPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLS-PAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLN 204
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 205 ALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDD 284
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 285 ANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFqGAITNRQQFDTIMNYIDI 364
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFR-ALRVGPGLEDPDL-GPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 365 GKKEGAKILTGGEKVGD---KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESL 441
Cdd:cd07109 317 ARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 442 STGLKVAKMLKAGTVWINTYndFDS---RVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNY--GAGggiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
14-496 |
7.49e-166 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 479.69 E-value: 7.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 14 ITLPNGLTYEQptgLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLL 93
Cdd:PLN02466 49 ITPPVQVSYTQ---LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 94 SKLADELESQIDLVSSIEALDNGKTLALARG-DVTIAINCLRDAAAYADKVNGRTInTGDGYMNFTTL-EPIGVCGQIIP 171
Cdd:PLN02466 126 LRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTV-PADGPHHVQTLhEPIGVAGQIIP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 172 WNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGST 251
Cdd:PLN02466 205 WNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGST 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 252 EVGKSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLE 331
Cdd:PLN02466 285 DTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARAL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 332 TEIkVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVT 411
Cdd:PLN02466 365 KRV-VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQS 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 412 VAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYT 491
Cdd:PLN02466 444 ILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYL 523
|
....*
gi 20981689 492 EVKAV 496
Cdd:PLN02466 524 QVKAV 528
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
27-500 |
9.10e-165 |
|
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: 474.64 E-value: 9.10e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK--TWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARG-DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAP 185
Cdd:cd07117 80 LAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 186 ALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsN 265
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 266 LKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANF 345
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFE-NVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 QGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVG----DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEG 421
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 422 VEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
21-499 |
2.31e-164 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 473.91 E-value: 2.31e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 21 TYEQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADEL 100
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 101 ESQIDLVSSIEALDNGK--TLALaRGDVTIAINCLRDAAAYADKVNGRTINTGDGYMN----FTTLEPIGVCGQIIPWNF 174
Cdd:cd07140 81 EEHQEELATIESLDSGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNrnltLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 175 PIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVG 254
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 255 KSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeI 334
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK-M 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 335 KVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAK 414
Cdd:cd07140 319 KIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 415 FKTLE-EGV-EMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTE 492
Cdd:cd07140 399 FDDGDvDGVlQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
....*..
gi 20981689 493 VKAVRIK 499
Cdd:cd07140 479 TKTVTIE 485
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
45-498 |
1.40e-161 |
|
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: 465.46 E-value: 1.40e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDteWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVngRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLN 204
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 205 ALYFASLCKKVgIPAGVVNIVPGPGRtVGAALTNDPRIRKLAFTGSTEVGKSVAvDSSESNLKKITLELGGKSAHLVFDD 284
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVM-ASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 285 ANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDI 364
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKA-AVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 365 GKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTG 444
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20981689 445 LKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
45-496 |
3.30e-161 |
|
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: 464.79 E-value: 3.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATqDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 -DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTL-----EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPA 198
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 199 AVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSA 278
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 279 HLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTI 358
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFE-ALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 359 MNYIDIGKKEGAKILTGGEKV--GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGI 436
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 437 ETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
27-490 |
4.12e-159 |
|
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: 460.32 E-value: 4.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE--SWSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALAR-GDVTIAINCLRDAAAYADKVNgrtiNTGDGYmnfttlEPIGVCGQIIPWNFPIMMLAWKIAP 185
Cdd:cd07111 101 FAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLD----TELAGW------KPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 186 ALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGrTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESN 265
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 266 lKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANF 345
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSH-LRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 QGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMA 425
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20981689 426 NSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAY 490
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
28-496 |
4.84e-158 |
|
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: 456.96 E-value: 4.84e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLV 107
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF--PAWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALARGD-VTIAINCLRDAA------AYADKVNGRTIntgdgymnftTLEPIGVCGQIIPWNFPIMMLA 180
Cdd:cd07138 79 AQAITLEMGAPITLARAAqVGLGIGHLRAAAdalkdfEFEERRGNSLV----------VREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 181 WKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVD 260
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 261 SSESnLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPF 340
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAE-AYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 341 DKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVG---DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKT 417
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 418 LEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
28-496 |
5.88e-158 |
|
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: 457.04 E-value: 5.88e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLV 107
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALAR-GDVTIAINCLRDAAAYADKVN----GRTINTGDGYMnftTLEPIGVCGQIIPWNFPIMMLAWK 182
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPfeerRPGSGGGHVLV---RREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 183 IAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSS 262
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 263 EsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDK 342
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVA-ALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 343 ANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVG--DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTY-NDFDSrvPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFrLDFGA--PFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
48-498 |
3.12e-156 |
|
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: 452.18 E-value: 3.12e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 48 PSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVT 127
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 128 IAINCLRDAAAYADKVNGRTINT-GDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNAL 206
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 207 YFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVaVDSSESNLKKITLELGGKSAHLVFDDAN 286
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI-AAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 287 IKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGK 366
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSR-KVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 367 KEGAKILTGGEKVGD-KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGL 445
Cdd:cd07118 322 AEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 20981689 446 KVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
45-496 |
3.50e-153 |
|
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: 444.08 E-value: 3.50e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDteWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 D-VTIAINCLRDAAAYADKVNGRTinTGD---GYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAV 200
Cdd:cd07092 79 DeLPGAVDNFRFFAGAARTLEGPA--AGEylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 201 TPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAvDSSESNLKKITLELGGKSAHL 280
Cdd:cd07092 157 TPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVA-RAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 281 VFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMN 360
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA-IRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 361 YIDiGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETES 440
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 20981689 441 LSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
27-499 |
4.18e-152 |
|
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: 442.65 E-value: 4.18e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdTEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARG-DVTIAINCLRDAAAYADKVNGRTIN------TGDGYMNFTTLEPIGVCGQIIPWNFPIMML 179
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsipsmQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 180 AWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRtVGAALTNDPRIRKLAFTGSTEVGKSVAv 259
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 260 DSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNP 339
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALS-SFQVGSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 340 FDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLE 419
Cdd:cd07113 317 MDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 420 EGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIK 499
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
28-500 |
5.60e-152 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 442.40 E-value: 5.60e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLV 107
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALAR-GDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:PRK13252 87 AALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRtVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESnL 266
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS-L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 267 KKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKA-NF 345
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVER-IRIGDPMDPAtNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 qGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV----GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEG 421
Cdd:PRK13252 324 -GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 422 VEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEM 481
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
25-500 |
8.77e-152 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 441.66 E-value: 8.77e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 25 PTGLFINNKFMkAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQI 104
Cdd:PRK13473 2 QTKLLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF--PEWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 105 DLVSSIEALDNGKTLALARGD-VTIAINCLRDAAAYADKVNGRTinTGDgYM-NFTTL---EPIGVCGQIIPWNFPIMML 179
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKA--AGE-YLeGHTSMirrDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 180 AWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAV 259
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 260 dSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNP 339
Cdd:PRK13473 235 -AAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT-LKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 340 FDKANFQGAITNRQQFDTIMNYIDIGKKEG-AKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTL 418
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 419 EEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
..
gi 20981689 499 KL 500
Cdd:PRK13473 473 KH 474
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
47-496 |
1.06e-151 |
|
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: 440.59 E-value: 1.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQ--KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNAL 206
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 207 YFASLCKKVGIPAGVVNIVPGPGRTvGAALTNDPRIRKLAFTGSTEVGKSVAvDSSESNLKKITLELGGKSAHLVFDDAN 286
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVM-SAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 287 IKktlpNLVNGI----FKNAGQICSSGSRIYVQEGIYDELLaafKAYLE--TEIKVGNPFDKANFQGAITNRQQFDTIMN 360
Cdd:cd07090 239 LE----NAVNGAmmanFLSQGQVCSNGTRVFVQRSIKDEFT---ERLVErtKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 361 YIDIGKKEGAKILTGGEKVG-----DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSG 435
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 436 IETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07090 392 VFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
45-496 |
1.30e-151 |
|
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: 440.25 E-value: 1.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHDteWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVN---GRTINTGD-GYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAV 200
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLDakaERAVPLPSeDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 201 TPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHL 280
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 281 VFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMN 360
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAE-AIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 361 YIDIGKKEGAKILTGGEK--VGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIET 438
Cdd:cd07110 317 FIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 20981689 439 ESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
29-494 |
9.62e-151 |
|
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: 438.47 E-value: 9.62e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLA-LARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPAL 187
Cdd:TIGR01804 79 KLETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 188 AMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLK 267
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 268 KITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQG 347
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTE-RIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 348 AITNRQQFDTIMNYIDIGKKEGAKILTGG---EKVG-DKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVE 423
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGgrpENVGlQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 424 MANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVK 494
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
72-496 |
3.45e-147 |
|
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: 425.88 E-value: 3.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 72 ADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNG-RTINT 150
Cdd:cd06534 3 ARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGpELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 151 GDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGR 230
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 231 TVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGS 310
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 311 RIYVQEGIYDELLAAFKayleteikvgnpfdkanfqgaitnrqqfdtimnyidigkkegakiltggekvgdkgyfirpTV 390
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 391 FYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDS-RVP 469
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpEAP 338
|
410 420
....*....|....*....|....*..
gi 20981689 470 FGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
29-496 |
4.61e-147 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 429.36 E-value: 4.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKtyPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLV 107
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFP--AWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLpSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVdSSESNL 266
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAA-AAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 267 KKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQ 346
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA-LKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 347 GAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV--GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEM 424
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20981689 425 ANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN-TYNDFDSRVPFGGVKQSGYG-REMGEEVYHAYTEVKAV 496
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
45-500 |
4.16e-144 |
|
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: 421.40 E-value: 4.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLN 204
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 205 ALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESnLKKITLELGGKSAHLVFDD 284
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 285 ANIKKTLPNLVNGI-FKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYID 363
Cdd:cd07107 237 ADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVA-AIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 364 IGKKEGAKILTGG----EKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETE 439
Cdd:cd07107 316 SAKREGARLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 440 SLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
27-500 |
3.17e-141 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 414.97 E-value: 3.17e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAF--KRWAELKAAERKRYLHKIADLIEQHADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARGDVTIAINCLRDAAAYA-DKVNGRTINTgDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAP 185
Cdd:TIGR02299 80 IAVLECLDCGQPLRQTRQQVIRAAENFRFFADKCeEAMDGRTYPV-DTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 186 ALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESn 265
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADT- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 266 LKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANF 345
Cdd:TIGR02299 238 LKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRA-IRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 QGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGD-------KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTL 418
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTfrgedlgRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 419 EEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
..
gi 20981689 499 KL 500
Cdd:TIGR02299 477 AL 478
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
45-498 |
1.41e-140 |
|
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: 412.14 E-value: 1.41e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTL-ALAR 123
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP--EWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 124 GDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPL 203
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 204 NALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFD 283
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 284 DANIKKTLPNLVNGI-FKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYI 362
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLS-KLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 363 DIGKKE-GAKILTGG----EKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:cd07108 316 DLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 438 TESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMG-EEVYHAYTEVKAVRI 498
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
47-496 |
2.17e-139 |
|
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: 409.04 E-value: 2.17e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWAtQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPL-NA 205
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQiNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 206 LYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSeSNLKKITLELGGKSAHLVFDDA 285
Cdd:cd07120 162 AIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 286 NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDIG 365
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAA-VKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 366 KKEGAKILTGGEKVGD---KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLS 442
Cdd:cd07120 320 IAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20981689 443 TGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
29-496 |
3.36e-138 |
|
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: 406.65 E-value: 3.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPAL 187
Cdd:cd07088 79 KLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIpSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 188 AMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLK 267
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 268 KITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQG 347
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMK-AVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 348 AITNRQQFDTIMNYIDIGKKEGAKILTGGEKV-GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMAN 426
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 427 SSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNdFDSRVPF-GGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINREN-FEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
43-496 |
5.49e-138 |
|
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: 405.44 E-value: 5.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 43 YPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALA 122
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK--EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 123 RGDVTIAINCLRDAAAYADKVNGRTINT-----GDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:cd07149 79 RKEVDRAIETLRLSAEEAKRLAGETIPFdaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAvdsSESNLKKITLELGGKS 277
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIA---RKAGLKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK-LVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKVGDkgyFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 438 TESLSTGLKVAKMLKAGTVWINTYNDFdsRV---PFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDSSTF--RVdhmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
64-498 |
4.10e-137 |
|
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: 402.29 E-value: 4.10e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 64 DVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKV 143
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 144 NGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPiMMLAWK-IAPALAMGNVCILKPAAVTPLN-ALYFASLCKKVGIPAG 220
Cdd:cd07104 79 EGEILpSDVPGKESMVRRVPLGVVGVISPFNFP-LILAMRsVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 221 VVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFK 300
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 301 NAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKvg 380
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKA-LPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 381 dKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN- 459
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 20981689 460 -TYNDfDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07104 393 qTVND-EPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
27-496 |
4.39e-136 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 402.57 E-value: 4.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 27 GLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDT---EWATQDPRERGRLLSKLADELESQ 103
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNkgkDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 104 IDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRT-------INTGDGYMnftTLEPIGVCGQIIPWNFPI 176
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapvslpMETFKGYV---LKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 177 MMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKS 256
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 257 VAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKV 336
Cdd:PLN02467 246 IMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN-IKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 337 GNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGD--KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAK 414
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 415 FKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVK 494
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
..
gi 20981689 495 AV 496
Cdd:PLN02467 484 QV 485
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
26-500 |
3.83e-134 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 397.34 E-value: 3.83e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 26 TGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQID 105
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 106 LVSSIEALDNGKTLALA-RGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIA 184
Cdd:PRK09847 100 ELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 185 PALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSES 264
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 265 NLKKITLELGGKSAHLVFDDA-NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKA 343
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ-NWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 344 NFQGAITNRQQFDTIMNYIDIGKKEGaKILTGGEKVGDKGYfIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVE 423
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 424 MANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL 500
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
47-498 |
2.30e-133 |
|
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: 393.62 E-value: 2.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TIAINCLRDAAAYADKVNGRTINT-GDGYMNFTTLEPIGVCGQIIPWNFPiMMLAWK-IAPALAMGNVCILKPAAVTPLN 204
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYP-LILATKkVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 205 ALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSeSNLKKITLELGGKSAHLVFDD 284
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 285 ANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDI 364
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK-LKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 365 GKKEGAKILTGGEKVGDkgyFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTG 444
Cdd:cd07150 320 AVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 20981689 445 LKVAKMLKAGTVWIN--TYNDfDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07150 397 FKLAERLESGMVHINdpTILD-EAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
29-496 |
2.63e-129 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 384.81 E-value: 2.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF--PSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINT--GDGYMnFTTLEPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSpfPDRRL-LVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESnL 266
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 267 KKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLeTEIKVGNPFDKANFQ 346
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAV-QKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 347 GAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMAN 426
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 427 SSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
29-498 |
4.22e-129 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 383.62 E-value: 4.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFhdTEW-ATQDPReRGRLLSKLADELESQIDL 106
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF--PEWrKVPAPR-RAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTG-DGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAP 185
Cdd:cd07131 79 LARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 186 ALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESN 265
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 266 lKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANF 345
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAK-RLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 QGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV----GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEG 421
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 422 VEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYN-DFDSRVPFGGVKQSGYG-REMGEEVYHAYTEVKAVRI 498
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTiGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
29-498 |
1.08e-125 |
|
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: 374.98 E-value: 1.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMkAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK--EWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTG-DGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPAL 187
Cdd:cd07086 79 RLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 188 AMGNVCILKPAAVTPLNAL----YFASLCKKVGIPAGVVNIVPGPGrTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSE 263
Cdd:cd07086 159 VCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 264 SNlKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAF-KAYleTEIKVGNPFDK 342
Cdd:cd07086 238 RF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLvKAY--KQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 343 ANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV--GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKV--AKMLKAGTVWINT-YNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVR 497
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 20981689 498 I 498
Cdd:cd07086 475 I 475
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
29-494 |
1.81e-125 |
|
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: 374.48 E-value: 1.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAK--EAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGK----TLAlarGDVTIAIN-------CLRDAAAYADKVNGRTINtgdgymnFTTLEPIGVCGQIIPWNFPIM 177
Cdd:cd07116 82 VAETWDNGKpvreTLA---ADIPLAIDhfryfagCIRAQEGSISEIDENTVA-------YHFHEPLGVVGQIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 178 MLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSV 257
Cdd:cd07116 152 MATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 258 AVDSSEsNLKKITLELGGKSAHLVF------DDANIKKTLPNLVNGIFkNAGQICSSGSRIYVQEGIYDELLAafKAYLE 331
Cdd:cd07116 231 MQYASE-NIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFME--RALER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 332 TE-IKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEK----VGDKGYFIRPTVFYDVNeDMRIVKEEIF 406
Cdd:cd07116 307 VKaIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 407 GPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEV 486
Cdd:cd07116 386 GPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMM 465
|
....*...
gi 20981689 487 YHAYTEVK 494
Cdd:cd07116 466 LDHYQQTK 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
44-498 |
1.15e-124 |
|
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: 371.68 E-value: 1.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 44 PVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALAR 123
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 124 GDVTIAINCLRDAAAYADKVNGRTINTgDGY------MNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPV-DAYeynerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSeSNLKKITLELGGKS 277
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVK-KLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEkvGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20981689 438 TESLSTGLKVAKMLKAGTVWIN--TYNDFDSrVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINdsTRFRWDN-LPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
32-499 |
6.56e-119 |
|
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: 357.00 E-value: 6.56e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 32 NKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVSSIE 111
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 112 ALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMG 190
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILpSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 191 NVCILKPAAVTPLNA-LYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKI 269
Cdd:cd07151 159 NAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 270 TLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAI 349
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVK-ALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 350 TNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDkgyFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSE 429
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 430 FGLGSGIETESLSTGLKVAKMLKAGTVWIN--TYNDfDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIK 499
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
65-498 |
2.83e-118 |
|
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: 354.07 E-value: 2.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 65 VEYAIECADRAFHDteWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRdaaAYADkvN 144
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICR---YYAE--N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 145 G------RTINTGDGYmNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIP 218
Cdd:cd07100 74 AeafladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 219 AGVVNIVPGPGRTVgAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGI 298
Cdd:cd07100 153 EGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 299 FKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEK 378
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMA-ALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 379 VGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWI 458
Cdd:cd07100 310 PDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 20981689 459 NTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07100 390 NGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
28-479 |
2.33e-117 |
|
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: 354.99 E-value: 2.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKfmKAQDGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVG-----KSVAVDS 261
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriyeRAAKVQP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 262 SESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFD 341
Cdd:cd07124 271 GQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKA-LKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 342 KANFQGAITNRQQFDTIMNYIDIGKKEGaKILTGGE--KVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLE 419
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 420 EGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN--TYNDFDSRVPFGGVKQSGYG 479
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
45-498 |
2.00e-116 |
|
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: 350.58 E-value: 2.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARG 124
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGA--ENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 125 DVTIAINCLRDAAAYADKVNGRTINTGDGYMN-----FTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAA 199
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 200 VTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVavdSSESNLKKITLELGGKSAH 279
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL---RANAGGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 280 LVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIM 359
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVK-KLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 360 NYIDIGKKEGAKILTGGEKvgdKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETE 439
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 440 SLSTGLKVAKMLKAGTVWINTYNDFDS-RVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
47-496 |
6.12e-114 |
|
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: 343.82 E-value: 6.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQ--RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TIAINCLRDAAAYADKVNG-RTINTGDGYMNFT---TLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTP 202
Cdd:cd07099 80 LLALEAIDWAARNAPRVLApRKVPTGLLMPNKKatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 203 LNALYFASLCKKVGIPAGVVNIVPGPGRTvGAALTnDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVF 282
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 283 DDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPF-DKANFqGAITNRQQFDTIMNY 361
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKAR-ALRPGADDiGDADI-GPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 362 IDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESL 441
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 442 STGLKVAKMLKAGTVWIN--TYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
43-494 |
6.64e-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: 343.84 E-value: 6.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 43 YPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTewATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALA 122
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPM--RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 123 RGDVTIAINCLRDAAAYADKVNGRTIN-----TGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPldisaRGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPgRTVGAALTNDPRIRKLAFTGSTEVGKSVavdSSESNLKKITLELGGKS 277
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDL---KARAGKKKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKA-LKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKvgdKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20981689 438 TESLSTGLKVAKMLKAGTVWINTYNDFdsRV---PFGGVKQSGYGREmGeeVYHA---YTEVK 494
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINDVPTF--RVdhmPYGGVKDSGIGRE-G--VRYAieeMTEPR 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
26-496 |
3.48e-106 |
|
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: 324.86 E-value: 3.48e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 26 TGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQID 105
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAF--PAWSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 106 LVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIA 184
Cdd:cd07085 79 ELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLeNVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 185 PALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVaVDSSES 264
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYI-YERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 265 NLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKAN 344
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAK-KLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 345 FQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV----GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtyndfdsrVP---------FGGVKQS--GYGREMGEEVYHA 489
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSffGDLHFYGKDGVRF 467
|
....*..
gi 20981689 490 YTEVKAV 496
Cdd:cd07085 468 YTQTKTV 474
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-483 |
2.34e-105 |
|
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: 321.55 E-value: 2.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 56 EVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRD 135
Cdd:cd07152 6 EVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 136 AAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNA-LYFASLCKK 214
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 215 VGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNL 294
Cdd:cd07152 164 AGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 295 VNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILT 374
Cdd:cd07152 242 AWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAK-HLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 375 GGEKvgdKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAG 454
Cdd:cd07152 321 GGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTG 397
|
410 420 430
....*....|....*....|....*....|.
gi 20981689 455 TVWIN--TYNDfDSRVPFGGVKQSGYGREMG 483
Cdd:cd07152 398 MLHINdqTVND-EPHNPFGGMGASGNGSRFG 427
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
37-496 |
1.80e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 319.52 E-value: 1.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 37 AQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNG 116
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 117 KTLALARGDVT-IAINCL---RDAAAY--ADKVNG------RTINTGDgymnfttlePIGVCGQIIPWNFPIMMLAWKIA 184
Cdd:PRK09407 106 KARRHAFEEVLdVALTARyyaRRAPKLlaPRRRAGalpvltKTTELRQ---------PKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 185 PALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNdpRIRKLAFTGSTEVGKSVAVDSSEs 264
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGR- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 265 NLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKAN 344
Cdd:PRK09407 254 RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVR-AMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 345 FQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKG-YFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVE 423
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20981689 424 MANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN-----TYNDFDSrvPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
46-496 |
4.23e-103 |
|
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: 316.17 E-value: 4.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 46 EDPSTENTVCEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGD 125
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 126 VTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLE---PIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTP 202
Cdd:cd07101 79 VLDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVnrrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 203 LNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNdpRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVF 282
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 283 DDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYI 362
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTR-ALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 363 DIGKKEGAKILTGGEKVGDKG-YFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESL 441
Cdd:cd07101 315 DDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 442 STGLKVAKMLKAGTVWIN-----TYNDFDSrvPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
64-498 |
5.62e-103 |
|
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: 315.29 E-value: 5.62e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 64 DVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKV 143
Cdd:cd07105 1 DADQAVEAAAAAFP--AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 144 NGRTIN-TGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVV 222
Cdd:cd07105 79 IGGSIPsDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 223 NIV---PGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIF 299
Cdd:cd07105 159 NVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 300 KNAGQICSSGSRIYVQEGIYDELLAAFKAyleteiKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGG-EK 378
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKA------AAEKLFAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 379 VGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWI 458
Cdd:cd07105 312 ESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 20981689 459 N--TYNDfDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:cd07105 392 NgmTVHD-EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
29-481 |
5.19e-102 |
|
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: 314.12 E-value: 5.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAqDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTeWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGW-WPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTInTGDGymNFTTL--------EPIGVCGQIIPWNFPIMMLA 180
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSL-PGDW--FPGTKgkiaqvrrEPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 181 WKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAvd 260
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 261 sSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLeTEIKVGNPF 340
Cdd:cd07082 238 -KQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV-AKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 341 DKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEkvGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNdfdSR----VPFGGVKQSGYGRE 481
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC---QRgpdhFPFLGRKDSGIGTQ 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
28-477 |
1.50e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 309.17 E-value: 1.50e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKFMKAQDgkTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDL 106
Cdd:PRK03137 39 LIIGGERITTED--KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 107 VSSIEALDNGKTLALARGDVTIAINCL----RDAAAYADkvnGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWK 182
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLeyyaRQMLKLAD---GKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 183 IAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVG-----KSV 257
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlriyeRAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 258 AVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAyLETEIKVG 337
Cdd:PRK03137 272 KVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVE-LTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 338 NPFDKAnFQGAITNRQQFDTIMNYIDIGKKEGaKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKT 417
Cdd:PRK03137 351 NPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20981689 418 LEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINT--------YNdfdsrvPFGGVKQSG 477
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctgaivgYH------PFGGFNMSG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
29-494 |
1.92e-99 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 307.60 E-value: 1.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLAD-ELESQIDLv 107
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL--PAWRALTAKERANILRRWFNlMMEHQDDL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTL-EPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:PRK11241 91 ARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIkQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNL 266
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 267 KKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQ 346
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVS-KLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 347 GAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMAN 426
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20981689 427 SSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVK 494
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
93-496 |
3.46e-97 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 299.34 E-value: 3.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 93 LSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINT---GDGYMNFTtlEPIGVCGQI 169
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSdrpGENILLFK--RALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 170 IPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTG 249
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 250 STEVGKSVaVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAY 329
Cdd:PRK10090 159 SVSAGEKI-MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 330 LEtEIKVGNPFDKANFQ-GAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGP 408
Cdd:PRK10090 238 MQ-AVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 409 VVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNdFDSRVPF-GGVKQSGYGREMGEEVY 487
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREN-FEAMQGFhAGWRKSGIGGADGKHGL 395
|
....*....
gi 20981689 488 HAYTEVKAV 496
Cdd:PRK10090 396 HEYLQTQVV 404
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
43-498 |
1.04e-96 |
|
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: 299.66 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 43 YPVEDPSTENTVCEVSSATTEDVEYAIECAdRAFHdtewATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALA 122
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA-ASYR----STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 123 RGDVTIAINCLRDAAAYADKVNGRTIN-----TGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFScdltaNGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAvdsSESNLKKITLELGGKS 277
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA---ATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFkAYLETEIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLL-VEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKVgdkGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20981689 438 TESLSTGLKVAKMLKAGTVWINTYNDFDSR-VPFGGVKQSGYG-REMGEEVYHAYTEVKAVRI 498
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
35-483 |
1.48e-93 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 293.31 E-value: 1.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 35 MKAQDGKTYPV----EDPSTEN------------TVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLAD 98
Cdd:TIGR01237 25 VKEQLGKTYPLvingERVETENkivsinpcdkseVVGTVSKASQEHAEHALQAAAKAFE--AWKKTDPEERAAILFKAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 99 ELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTG-DGYMNFTTLEPIGVCGQIIPWNFPIM 177
Cdd:TIGR01237 103 IVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSrEGETNQYVYTPTGVTVVISPWNFPFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 178 MLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVG--- 254
Cdd:TIGR01237 183 IMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGtri 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 255 --KSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLET 332
Cdd:TIGR01237 263 feRAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 333 eIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGaKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTV 412
Cdd:TIGR01237 343 -LKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAF 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20981689 413 AKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN--TYNDFDSRVPFGGVKQSGYGREMG 483
Cdd:TIGR01237 421 IRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
48-496 |
3.46e-93 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 290.69 E-value: 3.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 48 PSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVT 127
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 128 IAINCLRDAAAYADKV--NGRTINTgDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNA 205
Cdd:cd07102 81 GMLERARYMISIAEEAlaDIRVPEK-DGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 206 LYFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDA 285
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 286 NIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDIG 365
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKG-YKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 366 KKEGAKILTGGEK---VGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLS 442
Cdd:cd07102 317 IAKGARALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 20981689 443 TGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
47-496 |
1.15e-90 |
|
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: 284.58 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALAR-GD 125
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQ--REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 126 VTIAINCLRDAAAYADKV---NGRTINTGDGY-MNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVT 201
Cdd:cd07098 80 ILVTCEKIRWTLKHGEKAlrpESRPGGLLMFYkRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 202 PLNALYFASLCKKV----GIPAGVVNIVPGPGRTvGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESnLKKITLELGGKS 277
Cdd:cd07098 160 AWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQA-LRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKVGD----KGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLG 433
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20981689 434 SGIETESLSTGLKVAKMLKAGTVWIntyNDFDS-----RVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAI---NDFGVnyyvqQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
40-490 |
3.22e-85 |
|
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: 270.62 E-value: 3.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 40 GKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTL 119
Cdd:cd07130 11 GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 120 ALARGDVTIAInclrDAAAYA----DKVNGRTINTG-DGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCI 194
Cdd:cd07130 89 PEGLGEVQEMI----DICDFAvglsRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 195 LKPAAVTPLNAL----YFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKIT 270
Cdd:cd07130 165 WKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA-RFGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 271 LELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAF-KAYleTEIKVGNPFDKANFQGAI 349
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLkKAY--KQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 350 TNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFyDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSE 429
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20981689 430 FGLGSGIETESLStglKVAKMLKA-----GTVWINtyndfdsrVP---------FGGVKQSGYGREMGEEVYHAY 490
Cdd:cd07130 400 QGLSSSIFTTDLR---NAFRWLGPkgsdcGIVNVN--------IGtsgaeiggaFGGEKETGGGRESGSDAWKQY 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
47-498 |
3.23e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 262.37 E-value: 3.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFHDteWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TiaiNCLRDAAAYADK---------VNGRTINTGDGYMNFttlEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:PRK09406 85 L---KCAKGFRYYAEHaealladepADAAAVGASRAYVRY---QPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALtNDPRIRKLAFTGSTEVGKSVAVDSSESnLKKITLELGGKS 277
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 278 AHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDT 357
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA-LRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 358 IMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIE 437
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 438 TESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRI 498
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
9-483 |
3.61e-82 |
|
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: 264.06 E-value: 3.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 9 AEPVKITLPNGLTYEQPTGLFINNKFmkAQDGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPR 87
Cdd:cd07125 16 LEALADALKAFDEKEWEAIPIINGEE--TETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFA--GWSATPVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 88 ERGRLLSKLADELESQ-IDLVS--SIEAldnGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTG-DGYMNFTTLEPI 163
Cdd:cd07125 92 ERAEILEKAADLLEANrGELIAlaAAEA---GKTLADADAEVREAIDFCRYYAAQARELFSDPELPGpTGELNGLELHGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 164 GVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIR 243
Cdd:cd07125 169 GVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 244 KLAFTGSTEVGKSVAvdSSESNLKKITL----ELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIY 319
Cdd:cd07125 249 GVIFTGSTETAKLIN--RALAERDGPILpliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 320 DELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEgAKILTGGEKVGDKGYFIRPTVFYDVNEDmr 399
Cdd:cd07125 327 ERFIEMLKGAMA-SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 400 IVKEEIFGPVVTVAKFK--TLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtyndfdsRV--------- 468
Cdd:cd07125 403 DLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-------RNitgaivgrq 475
|
490
....*....|....*
gi 20981689 469 PFGGVKQSGYGREMG 483
Cdd:cd07125 476 PFGGWGLSGTGPKAG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
45-485 |
6.89e-76 |
|
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: 245.79 E-value: 6.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 45 VEDPSTENTVCEVSSATTEDVEYAIECADRAFHD-TEWATqdPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALAR 123
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 124 GDVTIAINCLRDAAAYADKVNGRTI-----NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPA 198
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIpmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 199 AVTPLNALYFASLCKKVGIPAGVVNIVPgPGRTVGAALTNDPRIRKLAFTGSTEVGKSVavdssESNLK---KITLELGG 275
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 276 KSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQF 355
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAE-KLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 356 DTIMNYIDIGKKEGAKILTGGEKVGDKGYfiRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSG 435
Cdd:cd07148 314 DRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 436 IETESLSTGLKVAKMLKAGTVWINTYNDFdsRV---PFGGVKQSGYG--------REMGEE 485
Cdd:cd07148 392 VFTKDLDVALKAVRRLDATAVMVNDHTAF--RVdwmPFAGRRQSGYGtggipytmHDMTQE 450
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-496 |
8.92e-75 |
|
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: 244.41 E-value: 8.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 43 YPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALA 122
Cdd:cd07083 35 VSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 123 RGDVTIAINCLRDAAAYADKVNGRT--INTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAV 200
Cdd:cd07083 113 IDDVAEAIDFIRYYARAALRLRYPAveVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAED 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 201 TPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSV--AVDSSESN---LKKITLELGG 275
Cdd:cd07083 193 AVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeAAARLAPGqtwFKRLYVETGG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 276 KSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQF 355
Cdd:cd07083 273 KNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAE-RLSVGPPEENGTDLGPVIDAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 356 DTIMNYIDIGKKEGaKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKT--LEEGVEMANSSEFGLG 433
Cdd:cd07083 352 AKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20981689 434 SGIETESLSTGLKVAKMLKAGTVWINTyNDFDSRV---PFGGVKQSGYGREMGEEVY-HAYTEVKAV 496
Cdd:cd07083 431 GGVYSRKREHLEEARREFHVGNLYINR-KITGALVgvqPFGGFKLSGTNAKTGGPHYlRRFLEMKAV 496
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
47-496 |
2.01e-74 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 242.07 E-value: 2.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 47 DPSTENTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDV 126
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 127 TIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNAL 206
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 207 YFASLCKKVGIPAGVVNIVPGPGRTVGAALtNDPRIRKLAFTGSTEVGKSVAVDSSESnLKKITLELGGKSAHLVFDDAN 286
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 287 IKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLeTEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGK 366
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAA-AALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 367 KEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLK 446
Cdd:PRK13968 328 AEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 20981689 447 VAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:PRK13968 408 MAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
28-496 |
2.00e-68 |
|
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: 227.07 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 28 LFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLV 107
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 108 SSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTL-EPIGVCGQIIPWNFPIMMLAWKIAPA 186
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIrQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 187 LAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGaALTNDPRIRKLAFTGSTEVGKSVAVDSSESNl 266
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 267 KKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSrIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQ 346
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAE-KIRIGPGDDPGAEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 347 GAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGY----FIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGV 422
Cdd:TIGR01722 317 GPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 423 EMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTyndfDSRVP-----FGGVKQSGYG--REMGEEVYHAYTEVKA 495
Cdd:TIGR01722 397 ALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPlpyfsFTGWKDSFFGdhHIYGKQGTHFYTRGKT 472
|
.
gi 20981689 496 V 496
Cdd:TIGR01722 473 V 473
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
39-487 |
2.31e-67 |
|
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: 224.79 E-value: 2.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 39 DGKTYPVEDPST-ENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGK 117
Cdd:TIGR01238 49 DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 118 TLALARGDVTIAINCLRdaaAYADKVNgrtintgDGYMNFTTlEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP 197
Cdd:TIGR01238 127 TIHNAIAEVREAVDFCR---YYAKQVR-------DVLGEFSV-ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 198 AAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSV--AVDSSESNLKKITLELGG 275
Cdd:TIGR01238 196 AEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqTLAQREDAPVPLIAETGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 276 KSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQF 355
Cdd:TIGR01238 276 QNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQ-ELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 356 DTIMNYIDIGKKEGAKI---LTGGEKVGDKGYFIRPTVFY--DVNEdmriVKEEIFGPVVTVAKFKT--LEEGVEMANSS 428
Cdd:TIGR01238 355 QNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFEldDIAE----LSEEVFGPVLHVVRYKAreLDQIVDQINQT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 429 EFGLGSGIETESLSTGLKVAKMLKAGTVWINTyNDFDSRV---PFGGVKQSGYGREMGEEVY 487
Cdd:TIGR01238 431 GYGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQVGAVVgvqPFGGQGLSGTGPKAGGPHY 491
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
37-479 |
4.96e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 225.51 E-value: 4.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 37 AQDGKTYPVEDPSTEN-TVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDL---VSSIEA 112
Cdd:PRK11905 563 DVDGGTRPVLNPADHDdVVGTVTEASAEDVERALAAAQAAF--PEWSATPAAERAAILERAADLMEAHMPElfaLAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 113 ldnGKTLALARGDVTIAINCLRdaaAYADkvngRTINTGDGymnfTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNV 192
Cdd:PRK11905 641 ---GKTLANAIAEVREAVDFLR---YYAA----QARRLLNG----PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 193 CILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKITL- 271
Cdd:PRK11905 707 VLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLi 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 272 -ELGGKSAHLVFDDAnikktLP-----NLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANF 345
Cdd:PRK11905 787 aETGGQNAMIVDSSA-----LPeqvvaDVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMD-ELRIGDPWRLSTD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 346 QG-AITNRQQfDTIMNYIDIGKKEGAKI--LTGGEKVgDKGYFIRPTVFyDVnEDMRIVKEEIFGPVVTVAKFKT--LEE 420
Cdd:PRK11905 861 VGpVIDAEAQ-ANIEAHIEAMRAAGRLVhqLPLPAET-EKGTFVAPTLI-EI-DSISDLEREVFGPVLHVVRFKAdeLDR 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTyNDFDSRV---PFGGVKQSGYG 479
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NIIGAVVgvqPFGGEGLSGTG 997
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
64-480 |
3.66e-62 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 209.05 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 64 DVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVT-------IAINclrda 136
Cdd:cd07095 1 QVDAAVAAARAAF--PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAamagkidISIK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 137 aAYADKVNGRTINTGDGyMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVG 216
Cdd:cd07095 74 -AYHERTGERATPMAQG-RAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 217 IPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVN 296
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 297 GIFKNAGQICSSGSRIYVQEGIY-DELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTG 375
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAK-RLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 376 GEKVGDKGYFIRPTVFyDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGT 455
Cdd:cd07095 310 MERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420
....*....|....*....|....*.
gi 20981689 456 V-WINTYNDFDSRVPFGGVKQSGYGR 480
Cdd:cd07095 389 VnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
52-477 |
1.09e-59 |
|
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: 205.13 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 52 NTVCEVSSATTEDVEYAIECADRAFHdtEWATQDPRERGRLLSKLADELESQI--DLVSSIeALDNGKTLALARGDVTI- 128
Cdd:cd07123 58 HVLATYHYADAALVEKAIEAALEARK--EWARMPFEDRAAIFLKAADLLSGKYryELNAAT-MLGQGKNVWQAEIDAACe 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 129 AINCLRDAAAYADKV-NGRTINTGDGYMNFTTLEPI-GVCGQIIPWNFPIMMLAWKIAPALaMGNVCILKPAAVTPLNAL 206
Cdd:cd07123 135 LIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 207 YFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKS----VAVDSSE-SNLKKITLELGGKSAHLV 281
Cdd:cd07123 214 LVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSlwkqIGENLDRyRTYPRIVGETGGKNFHLV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 282 FDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAITNRQQFDTIMNY 361
Cdd:cd07123 294 HPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK-EIKMGDPDDFSNFMGAVIDEKAFDRIKGY 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 362 IDIGKKE-GAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTV-----AKF-KTLEegvEMANSSEFGLGS 434
Cdd:cd07123 373 IDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVyvypdSDFeETLE---LVDTTSPYALTG 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 20981689 435 GI---ETESLSTGLKVAKMlKAGTVWINtyndfD-------SRVPFGGVKQSG 477
Cdd:cd07123 450 AIfaqDRKAIREATDALRN-AAGNFYIN-----DkptgavvGQQPFGGARASG 496
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
39-477 |
7.94e-59 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 203.09 E-value: 7.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 39 DGKTYPVEDPSTENTV-CEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDL-VSSIEALDNG 116
Cdd:TIGR01236 44 SNERIPQVNPHNHQAVlAKATNATEEDAMKAVEAALDA--KKDWSNLPFYDRAAIFLKAADLLSGPYRYeILAATMLGQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 117 KTLALARGD-VTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPI-GVCGQIIPWNFPIMMLAWKIAPALaMGNVCI 194
Cdd:TIGR01236 122 KTVYQAEIDaVAELIDFFRFNVKYARELYAQQPISAPGEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPAL-MGNTVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 195 LKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKS----VAVDSSE-SNLKKI 269
Cdd:TIGR01236 201 WKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHlwkkVAQNLDRyHNFPRI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 270 TLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAI 349
Cdd:TIGR01236 281 VGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQ-SVKVGDPDDFRGFMGAV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 350 TNRQQFDTIMNYIDIGKK--EGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTV-----AKFKTLEEGV 422
Cdd:TIGR01236 360 IDEQSFDKIVKYIEDAKKdpEALTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVyvypdDKYKEILDLV 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 423 EmaNSSEFGLGSGIETESLSTGLKVAKMLK--AGTVWIN--TYNDFDSRVPFGGVKQSG 477
Cdd:TIGR01236 440 D--STSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
35-479 |
1.33e-58 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 209.41 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 35 MKAQDGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQID-LVSSI-- 110
Cdd:COG4230 564 GEAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAF--PAWSATPVEERAAILERAADLLEAHRAeLMALLvr 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 111 EAldnGKTLALARGDVTIAINCLRDAAAYADKVNGrtintgdgymNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMG 190
Cdd:COG4230 642 EA---GKTLPDAIAEVREAVDFCRYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 191 NVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKIT 270
Cdd:COG4230 709 NTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVP 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 271 L--ELGGK-------SAHL--VFDDAnikktlpnlVNGIFKNAGQICSSgSRI-YVQEGIYDELLAAFKAYLEtEIKVGN 338
Cdd:COG4230 789 LiaETGGQnamivdsSALPeqVVDDV---------LASAFDSAGQRCSA-LRVlCVQEDIADRVLEMLKGAMA-ELRVGD 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 339 PFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGG-EKVGDKGYFIRPTVFydvnE--DMRIVKEEIFGPVVTVAKF 415
Cdd:COG4230 858 PADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPlPEECANGTFVAPTLI----EidSISDLEREVFGPVLHVVRY 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20981689 416 K--TLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtyndfdsR------V---PFGGVKQSGYG 479
Cdd:COG4230 934 KadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-------RniigavVgvqPFGGEGLSGTG 1001
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
19-490 |
1.98e-58 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 201.22 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 19 GLTYEQPtGLFINNKFmkAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIE-CADRAfhdTEWATQDPRERGRLLSKLA 97
Cdd:PLN02315 15 GLSSRNL-GCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRaCEEAA---KIWMQVPAPKRGEIVRQIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 98 DELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPI 176
Cdd:PLN02315 89 DALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIpSERPNHMMMEVWNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 177 MMLAWKIAPALAMGNVCILKPAAVTPLNAL----YFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTE 252
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 253 VGKSVAvDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAF-KAYle 331
Cdd:PLN02315 248 VGLMVQ-QTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLlTVY-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 332 TEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFyDVNEDMRIVKEEIFGPVVT 411
Cdd:PLN02315 325 KQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 412 VAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKA--GTVWINT-YNDFDSRVPFGGVKQSGYGREMGEEVYH 488
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWK 483
|
..
gi 20981689 489 AY 490
Cdd:PLN02315 484 QY 485
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
161-488 |
3.00e-58 |
|
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: 198.52 E-value: 3.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLawkIAP---ALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALT 237
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 238 nDPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEG 317
Cdd:cd07087 174 -AEPFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 318 IYDELLAAFKAYLETEIkvG-NPFDKANFqGAITNRQQFDTIMNYIDigkkeGAKILTGGEkVGDKGYFIRPTVFYDVNE 396
Cdd:cd07087 252 IKDELIEELKKAIKEFY--GeDPKESPDY-GRIINERHFDRLASLLD-----DGKVVIGGQ-VDKEERYIAPTILDDVSP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 397 DMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVwinTYND-----FDSRVPFG 471
Cdd:cd07087 323 DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV---CVNDvllhaAIPNLPFG 399
|
330
....*....|....*..
gi 20981689 472 GVKQSGYGRemgeevYH 488
Cdd:cd07087 400 GVGNSGMGA------YH 410
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
39-479 |
1.36e-57 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 206.20 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 39 DGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQID-LVS--SIEAld 114
Cdd:PRK11904 560 EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAeLIAlcVREA-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 115 nGKTLALARGDVTIAINCLRDAAAYADKVNGRTIN-TG-DGYMNFTTLEPIGV--CgqIIPWNFPIMMLAWKIAPALAMG 190
Cdd:PRK11904 636 -GKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKlPGpTGESNELRLHGRGVfvC--ISPWNFPLAIFLGQVAAALAAG 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 191 NVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKIT 270
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVP 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 271 L--ELGGKSAHLVfdDANikkTLP-----NLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKA 343
Cdd:PRK11904 793 LiaETGGQNAMIV--DST---ALPeqvvdDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA-ELKVGDPRLLS 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 344 NFQGAITNRQQFDTIMNYIDIGKKEgAKILTGGE--KVGDKGYFIRPTVFydvnE--DMRIVKEEIFGPVVTVAKFKT-- 417
Cdd:PRK11904 867 TDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPlpAGTENGHFVAPTAF----EidSISQLEREVFGPILHVIRYKAsd 941
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20981689 418 LEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtyndfdsR------V---PFGGVKQSGYG 479
Cdd:PRK11904 942 LDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-------RnqigavVgvqPFGGQGLSGTG 1005
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
29-459 |
1.90e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 198.05 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF--PLWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 SIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTI-NTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPAL 187
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLpNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 188 AMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGaALTNDPRIRKLAFTGSTEVGKSVAVDSSESNlK 267
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKG-K 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 268 KITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYV---QEGIYDELLAAFKAYletEIKVGNPFDkAN 344
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAKAL---KVTCGSEPD-AD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 345 FqGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKV----GDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEE 420
Cdd:PLN02419 429 L-GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDE 507
|
410 420 430
....*....|....*....|....*....|....*....
gi 20981689 421 GVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN 459
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
161-496 |
1.86e-54 |
|
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: 188.59 E-value: 1.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALTNDP 240
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 rIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYD 320
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 321 ELLAAFKAYLE-----TEIKVGNPfDKANfqgaITNRQQFDTIMNYIDIGKKEGAKILTGGEkVGDKGYFIRPTVFYDVN 395
Cdd:cd07134 255 AFVEHLKAEIEkfygkDAARKASP-DLAR----IVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 396 EDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINT--YNDFDSRVPFGGV 473
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvLHFLNPNLPFGGV 408
|
330 340
....*....|....*....|...
gi 20981689 474 KQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07134 409 NNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
161-491 |
3.19e-53 |
|
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: 185.79 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLawkIAP---ALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALT 237
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 238 NDPrIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEG 317
Cdd:cd07136 174 DQK-FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 318 IYDELLAAFKAYLeTEIKVGNPFDKANFqGAITNRQQFDTIMNYIDIGKkegakILTGGeKVGDKGYFIRPTVFYDVNED 397
Cdd:cd07136 252 VKEKFIKELKEEI-KKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGK-----IVFGG-NTDRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 398 MRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINtyndfD-------SRVPF 470
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----DtimhlanPYLPF 398
|
330 340
....*....|....*....|.
gi 20981689 471 GGVKQSGYGRemgeevYHAYT 491
Cdd:cd07136 399 GGVGNSGMGS------YHGKY 413
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
29-500 |
1.92e-52 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 184.96 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 29 FINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVS 108
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 109 siEALDngKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMN------------FTTLEPIGVCGQIIPWNFPI 176
Cdd:PLN00412 97 --ECLV--KEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVSdsfpgnernkycLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 177 MMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGStEVGKS 256
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 257 VavdSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKV 336
Cdd:PLN00412 252 I---SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA-KLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 337 GNPFDKANFQGAITNRQQfDTIMNYIDIGKKEGAKILTGGEKVGDkgyFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFK 416
Cdd:PLN00412 328 GPPEDDCDITPVVSESSA-NFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 417 TLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTY-----NDFdsrvPFGGVKQSGYGREMGEEVYHAYT 491
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApargpDHF----PFQGLKDSGIGSQGITNSINMMT 479
|
....*....
gi 20981689 492 EVKAVRIKL 500
Cdd:PLN00412 480 KVKSTVINL 488
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
161-496 |
3.05e-51 |
|
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: 179.99 E-value: 3.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMmLAwkIAP---ALAMGNVCILKPAAVTP-LNALyFASLCKKVgIPAGVVNIVPGpGRTVGAAL 236
Cdd:cd07133 100 QPLGVVGIIVPWNYPLY-LA--LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-GADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 237 TNDPrIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQE 316
Cdd:cd07133 174 SSLP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 317 GIYDELLAAFKAYLETEIK--VGNPfDKAnfqgAITNRQQFDTIMNYIDIGKKEGAKILTGGEK--VGDKGYFIRPTVFY 392
Cdd:cd07133 252 DKLEEFVAAAKAAVAKMYPtlADNP-DYT----SIINERHYARLQGLLEDARAKGARVIELNPAgeDFAATRKLPPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 393 DVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVwinTYNDFDSRV---- 468
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV---TINDTLLHVaqdd 403
|
330 340
....*....|....*....|....*....
gi 20981689 469 -PFGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07133 404 lPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-487 |
4.67e-51 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 187.49 E-value: 4.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 39 DGKTYPVEDPS-TENTVCEVSSATTEDVEYAIECADRAfhDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGK 117
Cdd:PRK11809 657 AGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 118 TLALARGDVTIAINCLRdaaAYADKVNgrtintgDGYMNfTTLEPIG--VCgqIIPWNFPIMMLAWKIAPALAMGNVCIL 195
Cdd:PRK11809 735 TFSNAIAEVREAVDFLR---YYAGQVR-------DDFDN-DTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 196 KPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVG----KSVAvDSSESNLKKITL 271
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVArllqRNLA-GRLDPQGRPIPL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 272 --ELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLEtEIKVGNPFDKANFQGAI 349
Cdd:PRK11809 881 iaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMA-ECRMGNPDRLSTDIGPV 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 350 TNRQQFDTIMNYIDIGKKEGAKI----LTGGEKVgDKGYFIRPTVFY--DVNEdmriVKEEIFGPVVTVAKFK--TLEEG 421
Cdd:PRK11809 960 IDAEAKANIERHIQAMRAKGRPVfqaaRENSEDW-QSGTFVPPTLIEldSFDE----LKREVFGPVLHVVRYNrnQLDEL 1034
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20981689 422 VEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTyNDFDSRV---PFGGVKQSGYGREMGEEVY 487
Cdd:PRK11809 1035 IEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAGGPLY 1102
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
26-477 |
1.75e-50 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 179.38 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 26 TGLFINNKFMKAQdGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQID 105
Cdd:PRK09457 1 MTLWINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF--PAWARLSFEERQAIVERFAALLEENKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 106 LVSSIEALDNGKTLALARGDVT-----IAINclrdAAAYADKVNGRTINTGDGyMNFTTLEPIGVCGQIIPWNFPIMMLA 180
Cdd:PRK09457 78 ELAEVIARETGKPLWEAATEVTaminkIAIS----IQAYHERTGEKRSEMADG-AAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 181 WKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGpGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVD 260
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 261 SSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIY-DELLAAFKAyLETEIKVGNP 339
Cdd:PRK09457 232 FAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVA-VAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 340 F-DKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFyDVNEDMRIVKEEIFGPVVTVAKFKTL 418
Cdd:PRK09457 311 DaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 419 EEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTV-WINTYNDFDSRVPFGGVKQSG 477
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
161-499 |
1.78e-49 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 176.76 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALTNDP 240
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 rIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYD 320
Cdd:PTZ00381 186 -FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 321 ELLAAFKayleTEIK--VGNPFDKANFQGAITNRQQFDTIMNYIdigKKEGAKILTGGEkVGDKGYFIRPTVFYDVNEDM 398
Cdd:PTZ00381 264 KFIEALK----EAIKefFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGE-VDIENKYVAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 399 RIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWIN--TYNDFDSRVPFGGVKQS 476
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVGNS 415
|
330 340
....*....|....*....|...
gi 20981689 477 GYGREMGEEVYHAYTEVKAVRIK 499
Cdd:PTZ00381 416 GMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
161-496 |
9.02e-48 |
|
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: 170.86 E-value: 9.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKvGIPAGVVNIVPGPGRTVGAALtnDP 240
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQGGVPETTALL--EQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 RIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYD 320
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 321 ELLAAFKAYLEtEIKVGNPFDKANFqGAITNRQQFDTIMNYIDigkKEGAKILTGGEKvGDKGYFIRPTVFYDVNEDMRI 400
Cdd:cd07135 263 EFVEELKKVLD-EFYPGGANASPDY-TRIVNPRHFNRLKSLLD---TTKGKVVIGGEM-DEATRFIPPTIVSDVSWDDSL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 401 VKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKV-AKMLKAGTVWINTYNDFDSR-VPFGGVKQSGY 478
Cdd:cd07135 337 MSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHIlTRTRSGGVVINDTLIHVGVDnAPFGGVGDSGY 416
|
330
....*....|....*...
gi 20981689 479 GREMGEEVYHAYTEVKAV 496
Cdd:cd07135 417 GAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
93-499 |
4.00e-38 |
|
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: 144.67 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 93 LSKLADELESQIdlvssIEAL--DNGKT--------LALARGDVTIAINCLRDAAAyADKVNGRTINTGDGYmnFTTLEP 162
Cdd:cd07132 29 LLRMLEENEDEI-----VEALakDLRKPkfeavlseILLVKNEIKYAISNLPEWMK-PEPVKKNLATLLDDV--YIYKEP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 163 IGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLckkvgIPAGVVN----IVPGpgrtvGAALTN 238
Cdd:cd07132 101 LGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLG-----GVEETT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 239 ---DPRIRKLAFTGSTEVGKSVAVDSSEsNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQ 315
Cdd:cd07132 171 ellKQRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 316 EGIYDELLAAFKAYLEtEIKVGNPFDKANFqGAITNRQQFDTIMNYIdigkkEGAKILTGGEkVGDKGYFIRPTVFYDVN 395
Cdd:cd07132 250 PEVQEKFVEALKKTLK-EFYGEDPKESPDY-GRIINDRHFQRLKKLL-----SGGKVAIGGQ-TDEKERYIAPTVLTDVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 396 EDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTglkVAKML---KAGTVwinTYND------FDS 466
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKV---INKILsntSSGGV---CVNDtimhytLDS 395
|
410 420 430
....*....|....*....|....*....|...
gi 20981689 467 rVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIK 499
Cdd:cd07132 396 -LPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
91-496 |
1.63e-37 |
|
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: 142.94 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 91 RLLSKLADELESQIdlvssIEAL--DNGKT--------LALARGDVTIAINCLRDAAAyADKVNGrTINTGDGYMNFTTl 160
Cdd:cd07137 28 KGLLRLVDENEDDI-----FAALrqDLGKPsaesfrdeVSVLVSSCKLAIKELKKWMA-PEKVKT-PLTTFPAKAEIVS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALTnDP 240
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALL-EQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 RIRKLAFTGSTEVGKsVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFK-NAGQICSSGSRIYVQEGIY 319
Cdd:cd07137 177 KWDKIFFTGSPRVGR-IIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLVEESFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 320 DELLAAFKAYLETeIKVGNPFDKANFQgAITNRQQFDTIMNYIDiGKKEGAKILTGGEKVGDKGYfIRPTVFYDVNEDMR 399
Cdd:cd07137 256 PTLIDALKNTLEK-FFGENPKESKDLS-RIVNSHHFQRLSRLLD-DPSVADKIVHGGERDEKNLY-IEPTILLDPPLDSS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 400 IVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVwinTYND-----FDSRVPFGGVK 474
Cdd:cd07137 332 IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDtvvqyAIDTLPFGGVG 408
|
410 420
....*....|....*....|..
gi 20981689 475 QSGYGREMGEEVYHAYTEVKAV 496
Cdd:cd07137 409 ESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
161-496 |
4.15e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 125.54 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGPGRTVGAALtnDP 240
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL--EQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 RIRKLAFTGSTEVGKsVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFK-NAGQICSSGSRIYVQEGIY 319
Cdd:PLN02174 188 KWDKIFYTGSSKIGR-VIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 320 DELLAAFKAYLETeIKVGNPFDKANFQgAITNRQQFDTIMNYIDiGKKEGAKILTGGEKvGDKGYFIRPTVFYDVNEDMR 399
Cdd:PLN02174 267 PKVIDAMKKELET-FYGKNPMESKDMS-RIVNSTHFDRLSKLLD-EKEVSDKIVYGGEK-DRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 400 IVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDS--RVPFGGVKQSG 477
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESG 422
|
330
....*....|....*....
gi 20981689 478 YGREMGEEVYHAYTEVKAV 496
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
161-496 |
1.51e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 115.21 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNIVPGpGRTVGAALTnDP 240
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLL-QH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 241 RIRKLAFTGSTEVGKsVAVDSSESNLKKITLELGGKSAhLVFDDANIKKTLPNLVNGIFKN-----AGQICSSGSRIYVQ 315
Cdd:PLN02203 184 KWDKIFFTGSPRVGR-IIMTAAAKHLTPVALELGGKCP-CIVDSLSSSRDTKVAVNRIVGGkwgscAGQACIAIDYVLVE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 316 EGIYDELLAAFKAYLETEIkvGNPFDKANFQGAITNRQQFDTIMNYIDiGKKEGAKILTGGeKVGDKGYFIRPTVFYDVN 395
Cdd:PLN02203 262 ERFAPILIELLKSTIKKFF--GENPRESKSMARILNKKHFQRLSNLLK-DPRVAASIVHGG-SIDEKKLFIEPTILLNPP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 396 EDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVwinTYND------FDSrVP 469
Cdd:PLN02203 338 LDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDaiiqyaCDS-LP 413
|
330 340
....*....|....*....|....*..
gi 20981689 470 FGGVKQSGYGREMGEEVYHAYTEVKAV 496
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
89-434 |
1.14e-25 |
|
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: 109.25 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 89 RGRLLSKLADELESQIDLVSSIEALDNGKTLALA-RGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTT---LEPIG 164
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAeNICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQShgyRWPYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 165 VCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGI-PAGVVNIVPGPGRTvGAALTNDPRIR 243
Cdd:cd07084 103 PVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT-MQALLLHPNPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 244 KLAFTGSTEVGKSVAVDSSESnlkKITLELGGKSAHLVFDDANIKKTLP-NLVNGIFKNAGQICSSGSRIYVQEGIYDE- 321
Cdd:cd07084 182 MVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQSMLFVPENWSKTp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 322 LLAAFKAYLETEIkvgnpfDKANFQGAItnrQQFDTIMNYIDIGKKEGAKILTGG--EKVGDKGYFI----RPTVFYDVN 395
Cdd:cd07084 259 LVEKLKALLARRK------LEDLLLGPV---QTFTTLAMIAHMENLLGSVLLFSGkeLKNHSIPSIYgacvASALFVPID 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 20981689 396 EDMR---IVKEEIFGPVVTVAKFKTLEEgVEMANSSEFGLGS 434
Cdd:cd07084 330 EILKtyeLVTEEIFGPFAIVVEYKKDQL-ALVLELLERMHGS 370
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
36-434 |
3.83e-24 |
|
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: 105.43 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 36 KAQDGKTYPVEDPSTENTVCEVSSAT---TEDVEYAIECADRA-----FHdtewatqdprERGRLLSKLADEL----ESQ 103
Cdd:cd07128 10 HAGTGDGRTLHDAVTGEVVARVSSEGldfAAAVAYAREKGGPAlraltFH----------ERAAMLKALAKYLmerkEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 104 IDLvssieALDNGKTLALARGDVTIAINCLrdaAAYADKV-----NGRTINTGD--------GYMNFTTLEPI-GVCGQI 169
Cdd:cd07128 80 YAL-----SAATGATRRDSWIDIDGGIGTL---FAYASLGrrelpNAHFLVEGDveplskdgTFVGQHILTPRrGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 170 IPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPlnalYFASLCKKV----GI-PAGVVNIVPGPGRTVGAALTNDPRIrk 244
Cdd:cd07128 152 NAFNFPVWGMLEKFAPALLAGVPVIVKPATATA----YLTEAVVKDivesGLlPEGALQLICGSVGDLLDHLGEQDVV-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 245 lAFTGSTEVGK------SVAVDSSESNLKKITLelggKSAHLVFD--------DANIKKtlpnLVNGIFKNAGQICSSGS 310
Cdd:cd07128 226 -AFTGSAATAAklrahpNIVARSIRFNAEADSL----NAAILGPDatpgtpefDLFVKE----VAREMTVKAGQKCTAIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 311 RIYVQEGIYDELLAAFKAYLETeIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEgAKILTGG----EKVG---DKG 383
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAK-VVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfEVVGadaEKG 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 20981689 384 YFIRPTVFYDVNED-MRIVKE-EIFGPVVTVAKFKTLEEGVEMANSsefGLGS 434
Cdd:cd07128 375 AFFPPTLLLCDDPDaATAVHDvEAFGPVATLMPYDSLAEAIELAAR---GRGS 424
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
40-425 |
4.76e-22 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 99.01 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 40 GKTYPVEDPSTENTVCEVSSattEDVEYAiecadRAFhdtEWATQDP---------RERGRLLSKLADELESQIDLVSSI 110
Cdd:PRK11903 18 GAGTPLFDPVTGEELVRVSA---TGLDLA-----AAF---AFAREQGgaalraltyAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 111 EALDNGKTLALARGDVTIAINCLRDAAAYADKVNG-RTINTGDG--------YMNFTTLEPI-GVCGQIIPWNFPIMMLA 180
Cdd:PRK11903 87 ATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDaRLLRDGEAvqlgkdpaFQGQHVLVPTrGVALFINAFNFPAWGLW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 181 WKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGI-PAGVVNIVPGPGRTVGAALTNdprIRKLAFTGSTEVGK---- 255
Cdd:PRK11903 167 EKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQP---FDVVSFTGSAETAAvlrs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 256 --SVAVDSSESNLKKITLelggKSAHLVFDDANIKKTLPNLVNGIFKN----AGQICSSGSRIYVQEGIYDELLAAFKAY 329
Cdd:PRK11903 244 hpAVVQRSVRVNVEADSL----NSALLGPDAAPGSEAFDLFVKEVVREmtvkSGQKCTAIRRIFVPEALYDAVAEALAAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 330 LeTEIKVGNPFDKANFQGAITNRQQFDTIMNYIDiGKKEGAKILTGGEKVG------DKGYFIRPTVFY--DVNEDMRIV 401
Cdd:PRK11903 320 L-AKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLGasDPDAATAVH 397
|
410 420
....*....|....*....|....
gi 20981689 402 KEEIFGPVVTVAKFKTLEEGVEMA 425
Cdd:PRK11903 398 DVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
65-429 |
7.80e-16 |
|
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: 79.51 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 65 VEYAIECADRAFhdTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRdaaAYADKVN 144
Cdd:cd07129 1 VDAAAAAAAAAF--ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLR---LFADLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 145 -----GRTINTGDG----------YMNFTTLEPIGVCGqiiPWNFPimmLAWKI-----APALAMGNVCILKPAAVTPLN 204
Cdd:cd07129 76 egswlDARIDPADPdrqplprpdlRRMLVPLGPVAVFG---ASNFP---LAFSVaggdtASALAAGCPVVVKAHPAHPGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 205 ALYFASLCKKV----GIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKS-VAVDSSESNLKKITLELGgkSAH 279
Cdd:cd07129 150 SELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRAlFDAAAARPEPIPFYAELG--SVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 280 LVFddanikkTLPN------------LVNGIFKNAGQICSSGSRIYVQEGI-YDELLAAFKAYLEtEIKVG---NPFDKA 343
Cdd:cd07129 228 PVF-------ILPGalaergeaiaqgFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALA-AAPAQtmlTPGIAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 344 NFQGAITNRQQFDtimnyidigkkeGAKILTGGEkVGDKGYFIRPTVFY-DV-----NEDMRivkEEIFGPVVTVAKFKT 417
Cdd:cd07129 300 AYRQGVEALAAAP------------GVRVLAGGA-AAEGGNQAAPTLFKvDAaaflaDPALQ---EEVFGPASLVVRYDD 363
|
410
....*....|..
gi 20981689 418 LEEGVEMANSSE 429
Cdd:cd07129 364 AAELLAVAEALE 375
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
162-416 |
4.92e-10 |
|
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: 61.74 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 162 PIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTnDPR 241
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL-EAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 242 IRKLAFTGSTEVGKSVAVDSSesnlKKITLELGGksahlvFDdaniKKTL-PNLVN----------GIFKNAGQICSSGS 310
Cdd:cd07126 221 PRMTLFTGSSKVAERLALELH----GKVKLEDAG------FD----WKILgPDVSDvdyvawqcdqDAYACSGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 311 RIY-----VQEGIYDEL-LAAFKAYLEtEIKVGNPFdkanfqgAITNRQQFDTIMNYIDIgkkEGAKILTGGEKVGDKGY 384
Cdd:cd07126 287 ILFahenwVQAGILDKLkALAEQRKLE-DLTIGPVL-------TWTTERILDHVDKLLAI---PGAKVLFGGKPLTNHSI 355
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 20981689 385 -----FIRPTVFY------DVNEDMRIVKEEIFGPVVTVAKFK 416
Cdd:cd07126 356 psiygAYEPTAVFvpleeiAIEENFELVTTEVFGPFQVVTEYK 398
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
159-428 |
4.30e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 55.56 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 159 TLEPIGV-----CGQIIPWN-FPIMMlawkiaPALAMGNVCILKP--AAVTPLnALYfASLCKKVGIPAG-----VVNIV 225
Cdd:cd07127 190 TVVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAAILPL-AIT-VQVAREVLAEAGfdpnlVTLAA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 226 PGPGRTVGAALTNDPRIRKLAFTGSTEVGksvavDSSESNLKKITL--ELGGKSAHLVFDDANIKKTLPNLVNGIFKNAG 303
Cdd:cd07127 262 DTPEEPIAQTLATRPEVRIIDFTGSNAFG-----DWLEANARQAQVytEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 304 QICSSGSRIYV-QEGI--------YDELLAAfkayLETEIK--VGNPFDKANFQGAITNRQQFDTIMNyidigKKEGAKI 372
Cdd:cd07127 337 QMCTTPQNIYVpRDGIqtddgrksFDEVAAD----LAAAIDglLADPARAAALLGAIQSPDTLARIAE-----ARQLGEV 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 373 LTGGEKVGDKGY---FIR-PTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSS 428
Cdd:cd07127 408 LLASEAVAHPEFpdaRVRtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
80-345 |
8.80e-08 |
|
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: 54.15 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 80 EWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLA------LAR-GDVTIAINCLRDAAAYADKVNGRTIN--T 150
Cdd:cd07077 9 TLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRslianwIAMmGCSESKLYKNIDTERGITASVGHIQDvlL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 151 GDGYMNFTTLEPIGVCGQIIPWNFPIMMLAwKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVgIPAGVVNI----VP 226
Cdd:cd07077 89 PDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-DAAHGPKIlvlyVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 227 GPGRTVGAALTNDPRIRKLAFTGStevgkSVAVDSSESNLKKI-TLELGGKSAHLVFDD-ANIKKTLPNLVNGIFKNaGQ 304
Cdd:cd07077 167 HPSDELAEELLSHPKIDLIVATGG-----RDAVDAAVKHSPHIpVIGFGAGNSPVVVDEtADEERASGSVHDSKFFD-QN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 20981689 305 ICSSGSRIYVQEGIYDELL---------AAFKAYLETEIKVGNPFDKANF 345
Cdd:cd07077 241 ACASEQNLYVVDDVLDPLYeefklklvvEGLKVPQETKPLSKETTPSFDD 290
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
161-427 |
8.51e-06 |
|
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: 48.26 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 161 EPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP---AAVTPLNAL-YFASLCKKVGIPAGVVNIVPGPGRTVGAAL 236
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 237 TNDPRIRKLAFTGSTEVGKsvAVDSSesnlKKITLELG-GKSAHLVFDDANIKKTLPNLVNG-IFKNaGQICSSGSRIYV 314
Cdd:cd07122 174 MKHPDVDLILATGGPGMVK--AAYSS----GKPAIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 315 QEGIYDELLAAFK---AYL----ETEiKVGNPF--DKANFQGAITNrQQFDTIMNYIDIGKKEGAKILTGGEK-VGDKGY 384
Cdd:cd07122 247 DDEIYDEVRAELKrrgAYFlneeEKE-KLEKALfdDGGTLNPDIVG-KSAQKIAELAGIEVPEDTKVLVAEETgVGPEEP 324
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 20981689 385 FIRptvfydvnedmrivkeEIFGPVVTVAKFKTLEEGVEMANS 427
Cdd:cd07122 325 LSR----------------EKLSPVLAFYRAEDFEEALEKARE 351
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
138-327 |
3.36e-05 |
|
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: 46.10 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 138 AYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKP----AAVTPLNALYFASLCK 213
Cdd:cd07081 71 VYKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20981689 214 KVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGstevGKSVaVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPN 293
Cdd:cd07081 151 AAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAV-VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQS 225
|
170 180 190
....*....|....*....|....*....|....
gi 20981689 294 LVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFK 327
Cdd:cd07081 226 IVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFE 259
|
|
| |
