|
Name |
Accession |
Description |
Interval |
E-value |
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
16-485 |
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: 645.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 16 MKRDHYRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIM 93
Cdd:COG1012 1 MTTPEYPLFIGGEWVAaaSGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 94 RERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG-TVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMA 172
Cdd:COG1012 79 EERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 173 AWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIME 252
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 253 KASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFD 332
Cdd:COG1012 239 AAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 333 KGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGkeRRVEGfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQD 412
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGG--RRPDG-EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDD 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4512364 413 EREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPF-SAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEY 469
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
31-485 |
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: 604.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 31 DSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGK 110
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 111 AISAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP 190
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 191 ASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSP 270
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 271 NLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIID 350
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGATIALGGKerrvEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSA 430
Cdd:pfam00171 322 KYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 431 IWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGT-PFGGYKESGFGRELCVETLDLY 485
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEY 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
25-485 |
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: 587.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDS--DETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07091 8 INNEFVDSvsGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:cd07091 88 LESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT-LKR 260
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLKK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 VTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSI 340
Cdd:cd07091 248 VTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 ISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:cd07091 328 VSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAF-PGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFdAAVPFGGFKQSGFGRELGEEGLEEY 468
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-485 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 584.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 -QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPI 196
Cdd:cd07093 79 rDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 197 TAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFAD 276
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 277 ADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSA 356
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 357 EEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4512364 437 GRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFY 447
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
25-485 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 576.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSDE--TFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07119 2 IDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAA 182
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 183 GCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVT 262
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 263 LELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIIS 342
Cdd:cd07119 242 LELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 343 RDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRAND 422
Cdd:cd07119 322 AEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4512364 423 TKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07119 402 TPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEY 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
38-485 |
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: 562.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVNNVPNG-FLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPI 196
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGdYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 197 TAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFAD 276
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 277 ADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSA 356
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 357 EEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07114 321 REEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4512364 437 GRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREY 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
59-485 |
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: 540.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 59 EKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG 138
Cdd:cd07078 1 DAAVAAARAAFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 139 TV-NNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNT 217
Cdd:cd07078 79 EViPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 218 VAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQS 297
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 298 CEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKErrvEGFEN 377
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKR---LEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 378 GHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNC-P 456
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDyS 395
|
410 420
....*....|....*....|....*....
gi 4512364 457 FSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07078 396 VGAEPSAPFGGVKQSGIGREGGPYGLEEY 424
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-485 |
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: 524.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 34 ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAIS 113
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 114 AAQP-QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPAS 192
Cdd:cd07112 82 DALAvDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 193 LTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT-LKRVTLELGGKSPN 271
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 272 LVFADA-DMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIID 350
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGATIALGGKERRVEGfenGHWY-EPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGS 429
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTET---GGFFvEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 430 AIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKY 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-485 |
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: 522.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 Q-INQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPI 196
Cdd:cd07115 79 LdVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 197 TAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFAD 276
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 277 ADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSA 356
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 357 EEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07115 319 REEGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4512364 437 GRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-485 |
1.74e-180 |
|
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: 513.39 E-value: 1.74e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPIT 197
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 198 AILLNEICHEAGVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADA 277
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 278 DMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAE 357
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 358 EEGATIALGGKERRVE-GFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07090 318 QEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4512364 437 GRATRVAHQLEAGIVMVNcPFSAFP-GTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07090 398 QRAHRVIAQLQAGTCWIN-TYNISPvEVPFGGYKQSGFGRENGTAALEHY 446
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-476 |
4.63e-180 |
|
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: 513.04 E-value: 4.63e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07559 1 YDNFINGEWVApsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQP-QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVA 177
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 178 PALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADA-----DMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFD 332
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 333 KGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQD 412
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4512364 413 EREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAFP-GTPFGGYKESGFGRE 476
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNC-YHQYPaHAPFGGYKKSGIGRE 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-476 |
2.47e-179 |
|
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: 510.05 E-value: 2.47e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQ 118
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 119 INQAIEDFEFYAGAIVGHRGTVnnVP---NGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTP 195
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRT--IPspaPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 196 ITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFA 275
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 276 DADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRS 355
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 356 AEEEGATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKD 435
Cdd:cd07103 318 AVAKGAKVLTGGK--RLGL--GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4512364 436 QGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRE 476
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGRE 434
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
38-485 |
2.64e-174 |
|
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: 497.64 E-value: 2.64e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVN-NVP---NGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASL 193
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLDAKAErAVPlpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 194 TPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLV 273
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 274 FADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYV 353
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 354 RSAEEEGATIALGGkeRRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWT 433
Cdd:cd07110 319 ARGKEEGARLLCGG--RRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 4512364 434 KDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNY 448
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
25-485 |
5.88e-174 |
|
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: 497.41 E-value: 5.88e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:TIGR01804 2 IDGEYVEDSagTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:TIGR01804 80 LETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRV 261
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 262 TLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSII 341
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 342 SRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRAN 421
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4512364 422 DTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHY 463
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
41-477 |
8.27e-174 |
|
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: 496.47 E-value: 8.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 41 PAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQIN 120
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 121 QAIEDFEFYAG-AIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAI 199
Cdd:cd07118 84 GAADLWRYAASlARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 200 LLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADM 279
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 280 EAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEE 359
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 360 GATIALGGKerrVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRA 439
Cdd:cd07118 324 GATLLLGGE---RLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 4512364 440 TRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGREL 477
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGREL 438
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
20-485 |
1.88e-172 |
|
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: 493.79 E-value: 1.88e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGK-WRKYPVGKRARVLNQIAAIMRER 96
Cdd:cd07141 6 YTKIFINNEWHDsvSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 97 FQELVEIEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:cd07141 86 RAYLASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAS 255
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 256 HT-LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKG 334
Cdd:cd07141 246 KSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 335 THVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDER 414
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4512364 415 EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEY 472
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
25-476 |
2.51e-172 |
|
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: 492.79 E-value: 2.51e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07138 3 IDGAWVAPAgtETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQP-QINQAIEDFEFYAGAI-----VGHRGtvnnvpNGFLnytQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAAADALkdfefEERRG------NSLV---VREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASH 256
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 TLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTH 336
Cdd:cd07138 232 TVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 337 VGSIISRDQLEIIDSYVRSAEEEGATIALGGKErRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREV 416
Cdd:cd07138 312 LGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 417 IKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAfPGTPFGGYKESGFGRE 476
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN-PGAPFGGYKQSGNGRE 449
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
25-477 |
2.01e-170 |
|
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: 488.96 E-value: 2.01e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSDE--TFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07143 11 INGEFVDSVHggTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAI-SAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:cd07143 91 IEALDNGKTFgTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT-LKR 260
Cdd:cd07143 171 AGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnLKK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 VTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSI 340
Cdd:cd07143 251 VTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 ISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:cd07143 331 VSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGREL 477
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGREL 463
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-485 |
1.74e-168 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 484.00 E-value: 1.74e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:PRK13252 7 QSLYIDGAYVEatSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQP-QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVA 177
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVvDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 178 PALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHV 337
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 338 GSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVI 417
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN----CPfsafPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgeSP----AEMPVGGYKQSGIGRENGIATLEHY 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
25-485 |
2.35e-168 |
|
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: 483.45 E-value: 2.35e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDS--DETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07144 12 INNEFVKSsdGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE-SWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAI-SAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:cd07144 91 IEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRV 261
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 262 TLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKK-LQLGDPFDKGTHVGSI 340
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 ISRDQLEIIDSYVRSAEEEGATIALGGkERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGG-EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKA 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07144 410 NDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-485 |
5.48e-167 |
|
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: 479.64 E-value: 5.48e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07117 1 YGLFINGEWVKgsSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK--TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQP-QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVA 177
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 178 PALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHV 337
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 338 GSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVI 417
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAFP-GTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT-YNQIPaGAPFGGYKKSGIGRETHKSMLDAY 465
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-485 |
6.61e-167 |
|
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: 479.05 E-value: 6.61e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKyPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP-Q 118
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 119 INQAIEDFEFYAGAIVGHRGTVNN-VPNGFLNYTQ----KEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASL 193
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLpVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 194 TPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLV 273
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 274 FADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYV 353
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 354 RSAEEEGATIALGGKerRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWT 433
Cdd:cd07089 322 ARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 4512364 434 KDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEF 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-485 |
5.34e-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: 476.34 E-value: 5.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVgKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQ 118
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPA-ERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 119 INQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITA 198
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 199 ILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADAD 278
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 279 MEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDkGTHVGSIISRDQLEIIDSYVRSAEE 358
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 359 EGATIALGGkeRRVEG-FENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQG 437
Cdd:cd07109 320 RGARIVAGG--RIAEGaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4512364 438 RATRVAHQLEAGIVMVNCPFSAfpG---TPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAG--GgieLPFGGVKKSGHGREKGLEALYNY 446
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
20-485 |
4.96e-165 |
|
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: 475.06 E-value: 4.96e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERF 97
Cdd:cd07142 3 HTKLFINGQFVDaaSGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 98 QELVEIEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:cd07142 83 DELAALETWDNGKPYEqARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASH 256
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 T-LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGT 335
Cdd:cd07142 243 SnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 336 HVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEgfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDERE 415
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGD--RIG--SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 416 VIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNY 468
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-485 |
5.62e-165 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 474.78 E-value: 5.62e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVDSD-ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:PRK13473 2 QTKLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAA-QPQINQAIEDFEFYAGAIVGHRGTVNN--VPnGFLNYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:PRK13473 80 EFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGeyLE-GHTSMIRRDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAS 255
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 256 HTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGT 335
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 336 HVGSIISRDQLEIIDSYVRSAEEEG-ATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDER 414
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGE--APDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4512364 415 EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDY 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
25-486 |
1.81e-162 |
|
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: 468.21 E-value: 1.81e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERV--DSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07139 3 IGGRWVapSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQP-QINQAIEDFEFYAGAIVG-----HRGTVNnvpnGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:cd07139 83 LWTAENGMPISWSRRaQGPGPAALLRYYAALARDfpfeeRRPGSG----GGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAgAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASH 256
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVP-ADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 TLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTH 336
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 337 VGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREV 416
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGG--RPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 417 IKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNcPFSAFPGTPFGGYKESGFGRELCVETLDLYI 486
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYL 464
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-486 |
9.11e-162 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 467.38 E-value: 9.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 22 RMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQE 99
Cdd:PLN02766 22 KLFINGEFVDaaSGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 100 LVEIEVLNSGKAISAAQP-QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT- 257
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHV 337
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 338 GSIISRDQLEIIDSYVRSAEEEGATIALGGKerrvEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVI 417
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLYI 486
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYL 486
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-485 |
3.81e-161 |
|
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: 464.11 E-value: 3.81e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAI-SAAQP 117
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLhLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVNN--VPnGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTP 195
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGeyLP-GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 196 ITAILLNEICHEaGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFA 275
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 276 DADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRS 355
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 356 AeEEGATIALGGkeRRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKD 435
Cdd:cd07092 318 A-PAHARVLTGG--RRAEG--PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4512364 436 QGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDY 442
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-480 |
1.28e-159 |
|
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: 460.29 E-value: 1.28e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAI-SAAQPQ 118
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 119 INQAIEDFEFYAGAIVGHRGtvNNVP--NGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPI 196
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKG--ETLPfgPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 197 TAILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFAD 276
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 277 ADMEAAVAGSLFGIYFN-TGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRS 355
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 356 A-EEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTK 434
Cdd:cd07108 318 GlSTSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4512364 435 DQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVE 480
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLE 443
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
25-486 |
7.68e-158 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 457.66 E-value: 7.68e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAF--DHGK-WRKYPVGKRARVLNQIAAIMRERFQE 99
Cdd:PLN02467 12 IGGEWREPVlgKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKdWARTTGAVRAKYLRAIAAKITERKSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 100 LVEIEVLNSGKAISAAQPQINQAIEDFEFYAG---AIVGHRGTVNNVP-NGFLNYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:PLN02467 92 LAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaeALDAKQKAPVSLPmETFKGYVLKEPLGVVGLITPWNYPLLMATWK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAS 255
Cdd:PLN02467 172 VAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 256 HTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGT 335
Cdd:PLN02467 252 QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGC 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 336 HVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDERE 415
Cdd:PLN02467 332 RLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4512364 416 VIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLYI 486
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
21-486 |
2.12e-157 |
|
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: 455.80 E-value: 2.12e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07140 6 HQLFINGEFVDAEggKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAA-QPQINQAIEDFEFYAG---AIVGHRGTVNNV-PNGFLNYTQKEPVGVCAQIIPWNYPLMMAA 173
Cdd:cd07140 86 ELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGwcdKIQGKTIPINQArPNRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 174 WKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEK 253
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 254 -ASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFD 332
Cdd:cd07140 246 cAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 333 KGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQD 412
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 413 E--REVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLYI 486
Cdd:cd07140 402 GdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
21-485 |
1.87e-155 |
|
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: 450.16 E-value: 1.87e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVDSDETFETFNPA-KGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQE 99
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFP--AWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 100 LVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG-TVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGeTLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTL 258
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 259 KRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVG 338
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 339 SIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIK 418
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 419 RANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAF-PGTPFGGYKESGFG-RELCVETLDLY 485
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVdYHVPFGGRKGSSYGpREQGEAALEFY 465
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-476 |
2.62e-153 |
|
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: 445.30 E-value: 2.62e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 19 DHYRMVINGE--RVDSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRER 96
Cdd:cd07111 20 RSFGHFINGKwvKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE--SWSALPGHVRARHLYRIARHIQKH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 97 FQELVEIEVLNSGKAISAAQP-QINQAIEDFEFYAG-------AIVGHrgtvnnvpngflnytqkEPVGVCAQIIPWNYP 168
Cdd:cd07111 98 QRLFAVLESLDNGKPIRESRDcDIPLVARHFYHHAGwaqlldtELAGW-----------------KPVGVVGQIVPWNFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 169 LMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGK 248
Cdd:cd07111 161 LLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 249 DIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLG 328
Cdd:cd07111 240 ALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 329 DPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVE 408
Cdd:cd07111 320 DPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 409 TFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAF-PGTPFGGYKESGFGRE 476
Cdd:cd07111 396 TFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING-HNLFdAAAGFGGYRESGFGRE 463
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-485 |
5.33e-150 |
|
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: 435.42 E-value: 5.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFYAGaIVGHRGTVNNVPNGFLnYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAI 199
Cdd:cd07106 81 GGAVAWLRYTAS-LDLPDEVIEDDDTRRV-ELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 200 LLNEICHEAgVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADM 279
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 280 EAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEE 359
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 360 GATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRA 439
Cdd:cd07106 317 GAKVLAGGE--PLDG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4512364 440 TRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEY 438
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
25-476 |
8.24e-150 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 436.81 E-value: 8.24e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:PLN02278 29 IGGKWTDAYdgKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTVnnVPNGFLN---YTQKEPVGVCAQIIPWNYPLMMAAWKVAPA 179
Cdd:PLN02278 107 LMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDI--IPSPFPDrrlLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 180 LAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLK 259
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 260 RVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGS 339
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 340 IISRDQLEIIDSYVRSAEEEGATIALGGKeRRVEGfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKR 419
Cdd:PLN02278 345 LINEAAVQKVESHVQDAVSKGAKVLLGGK-RHSLG---GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 420 ANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRE 476
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGRE 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
38-482 |
8.91e-150 |
|
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: 435.27 E-value: 8.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPIT 197
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 198 AILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADA 277
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 278 DMEAAVAGSLFGIYFN-TGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSA 356
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 357 EEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4512364 437 GRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETL 482
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEEL 443
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
25-474 |
1.16e-149 |
|
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: 435.54 E-value: 1.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07088 2 INGEFVPssSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTV--NNVPNGFLnYTQKEPVGVCAQIIPWNYPLMMAAWKVAPAL 180
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIipSDRPNENI-FIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 181 AAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKR 260
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 VTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSI 340
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 ISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGK--RPEG-EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNC-PFSAFPGtpF-GGYKESGFG 474
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINReNFEAMQG--FhAGWKKSGLG 449
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
36-483 |
7.82e-149 |
|
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: 432.93 E-value: 7.82e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 36 FETFNPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAA 115
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 116 QPQINQAIEDFE---FYAGAIVGHRGTVNNVPNG--FLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP 190
Cdd:cd07145 79 RVEVERTIRLFKlaaEEAKVLRGETIPVDAYEYNerRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 191 ASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSP 270
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 271 NLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIID 350
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGATIALGGKerRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSA 430
Cdd:cd07145 319 NLVNDAVEKGGKILYGGK--RDEGS----FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4512364 431 IWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFGRELCVETLD 483
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTML 446
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
63-485 |
9.90e-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: 423.95 E-value: 9.90e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 63 QAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG-TVN 141
Cdd:cd06534 1 AAARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGpELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 142 NVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGA 221
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 222 GSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEAR 301
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 302 SRLFVHEEIYDEFIEEFItrakklqlgdpfdkgthvgsiisrdqleiidsyvrsaeeegatialggkerrvegfenghwy 381
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 382 epTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCP-FSAF 460
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSsIGVG 334
|
410 420
....*....|....*....|....*
gi 4512364 461 PGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEY 359
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-486 |
2.81e-146 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 429.23 E-value: 2.81e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 19 DHYRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRER 96
Cdd:PLN02466 56 SYTQLLINGQFVDaaSGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 97 FQELVEIEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVnnVPNGFLNYTQ--KEPVGVCAQIIPWNYPLMMAA 173
Cdd:PLN02466 136 NDELAALETWDNGKPYEqSAKAELPMFARLFRYYAGWADKIHGLT--VPADGPHHVQtlHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 174 WKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEK 253
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 254 ASHT-LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFD 332
Cdd:PLN02466 294 AAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 333 KGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQD 412
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4512364 413 EREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAFPGT-PFGGYKESGFGRELCVETLDLYI 486
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAiPFGGYKMSGIGREKGIYSLNNYL 523
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-476 |
6.70e-146 |
|
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: 424.25 E-value: 6.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 58 AEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFeFYAGAIVGH- 136
Cdd:cd07104 2 VDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL-REAAGLPRRp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 137 RGTV--NNVPnGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPIT-AILLNEICHEAGVPEG 213
Cdd:cd07104 79 EGEIlpSDVP-GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 214 VVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFN 293
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 294 TGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerrve 373
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 374 gfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMV 453
Cdd:cd07104 313 --YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420
....*....|....*....|....
gi 4512364 454 NC-PFSAFPGTPFGGYKESGFGRE 476
Cdd:cd07104 391 NDqTVNDEPHVPFGGVKASGGGRF 414
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-476 |
9.48e-146 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 424.82 E-value: 9.48e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 36 FETFNPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAA 115
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 116 QPQINQAIEDFEFYAGAIVGHRGTVnnVP---NGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPAS 192
Cdd:cd07150 79 WFETTFTPELLRAAAGECRRVRGET--LPsdsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 193 LTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNL 272
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 273 VFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSY 352
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 353 VRSAEEEGATIALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIW 432
Cdd:cd07150 317 VEDAVAKGAKLLTGGK-------YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 4512364 433 TKDQGRATRVAHQLEAGIVMVNCP-FSAFPGTPFGGYKESGFGRE 476
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPtILDEAHVPFGGVKASGFGRE 434
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
21-485 |
5.24e-143 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 419.13 E-value: 5.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVDSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdHGKWRKYPVGKRARVLNQIAAIMRERFQEL 100
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAAL-KGPWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 101 VEIEVLNSGKAIS-AAQPQINQAIEDFEFYAGAI--VGHRGTVNNVPNG--FLNYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:TIGR03216 80 LAAEVADTGKPRSlASHLDIPRGAANFRVFADVVknAPTECFEMATPDGkgALNYAVRKPLGVVGVISPWNLPLLLMTWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAG-SVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKA 254
Cdd:TIGR03216 160 VGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGpDSAGEFLTRHPGVDAITFTGETRTGSAIMKAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 255 SHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKG 334
Cdd:TIGR03216 240 ADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 335 THVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRV-EGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDE 413
Cdd:TIGR03216 320 TNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDFgDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDSE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4512364 414 REVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:TIGR03216 400 EEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFY 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
25-485 |
1.44e-141 |
|
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: 415.21 E-value: 1.44e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKG-EILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELV 101
Cdd:cd07131 3 IGGEWVDSAsgETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFP--EWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 102 EIEVLNSGKAISAAQPQINQAIEDFEFYAGAivGHR--GTV--NNVPNGFlNYTQKEPVGVCAQIIPWNYPLMMAAWKVA 177
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGE--GRRlfGETvpSELPNKD-AMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 178 PALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHV 337
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 338 GSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVI 417
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS-AFPGTPFGGYKESGFG-RELCVETLDLY 485
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAF 467
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
36-476 |
4.33e-140 |
|
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: 410.45 E-value: 4.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 36 FETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKwrKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAA 115
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 116 QPQINQAIEDFEFYA-GAIVGHRGTVN--NVPNGF--LNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP 190
Cdd:cd07149 79 RKEVDRAIETLRLSAeEAKRLAGETIPfdASPGGEgrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 191 ASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAShtLKRVTLELGGKSP 270
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 271 NLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIID 350
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGATIALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSA 430
Cdd:cd07149 317 EWVEEAVEGGARLLTGGK-------RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4512364 431 IWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFGRE 476
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGRE 436
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
21-476 |
3.67e-137 |
|
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: 404.14 E-value: 3.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 21 YRMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07116 1 YDNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAI-SAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVA 177
Cdd:cd07116 79 MLAVAETWDNGKPVrETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 178 PALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:cd07116 159 PALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADME------AAVAG-SLFGiyFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDP 330
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADVMDAddaffdKALEGfVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 331 FDKGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNvTPDMKAVQEEIFGPVVVVETF 410
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 411 QDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCpFSAFP-GTPFGGYKESGFGRE 476
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNC-YHLYPaHAAFGGYKQSGIGRE 460
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-486 |
3.62e-135 |
|
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: 397.87 E-value: 3.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPvGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPIT 197
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 198 AILLNEICHEA-GVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFAD 276
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 277 ADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSA 356
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 357 EEEGATIALGGkERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQ 436
Cdd:cd07120 320 IAAGAEVVLRG-GPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4512364 437 GRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLYI 486
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-474 |
1.27e-134 |
|
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: 398.52 E-value: 1.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVDSDETFETFNPAK-GEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07124 32 EYPLVIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT- 257
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 -----LKRVTLELGGKSPNLVFADADMEAAVAG---SLFGiyFNtGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGD 329
Cdd:cd07124 270 pgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGivrSAFG--FQ-GQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 330 PFDKGTHVGSIISRDQLEIIDSYVRSAEEEGaTIALGGkeRRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVET 409
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGG--EVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 410 FQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS-AFPGT-PFGGYKESGFG 474
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITgALVGRqPFGGFKMSGTG 490
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-475 |
2.57e-134 |
|
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: 396.29 E-value: 2.57e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 27 GERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAfdHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIE 104
Cdd:cd07151 1 GEWRDgtSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 105 VLNSGKAISAAQPQINQAIEDFEfyAGAIVGHRGTVNNVPN---GFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITR--EAATFPLRMEGRILPSdvpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITA-ILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKR 260
Cdd:cd07151 157 LGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 VTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSI 340
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 ISRDQLEIIDSYVRSAEEEGATIALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFGR 475
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdQPVNDEPHVPFGGEKNSGLGR 445
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-488 |
2.17e-133 |
|
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: 394.24 E-value: 2.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGERVDSD-ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07086 2 VIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAG---AIVGHrgTVNN-VPNGFLnYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGlsrMLYGL--TIPSeRPGHRL-MEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEA----GVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKA 254
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 255 SHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKG 334
Cdd:cd07086 236 ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 335 THVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDER 414
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 415 EVIKRANDTKFGLGSAIWTKDQGRATRV--AHQLEAGIVMVNCPFS-AFPGTPFGGYKESGFGRELCVETLDLYIGR 488
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-475 |
7.87e-133 |
|
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: 391.97 E-value: 7.87e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQ--RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFYAGAI--VGHRGTV--NNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTP 195
Cdd:cd07099 80 LLALEAIDWAARNAprVLAPRKVptGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 196 ITAILLNEICHEAGVPEGVVNTVAGAGSVvGDYLVGHEdVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFA 275
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 276 DADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRS 355
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 356 AEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKD 435
Cdd:cd07099 318 AVAKGAKALTGGARSNGGGP----FYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 4512364 436 QGRATRVAHQLEAGIVMVNCP--FSAFPGTPFGGYKESGFGR 475
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVllTAGIPALPFGGVKDSGGGR 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
58-477 |
2.48e-131 |
|
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: 387.20 E-value: 2.48e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 58 AEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAgaivghr 137
Cdd:cd07100 1 IEAALDRAHAAFL--AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYA------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 138 gtvNNVPNgFL-----------NYTQKEPVGVCAQIIPWNYPLmmaaWKV----APALAAGCSVVVKPASLTPITAILLN 202
Cdd:cd07100 72 ---ENAEA-FLadepietdagkAYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 203 EICHEAGVPEGVVNTVAGAGSVVgDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAA 282
Cdd:cd07100 144 ELFREAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 283 VAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGAT 362
Cdd:cd07100 223 VKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 363 IALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRV 442
Cdd:cd07100 303 LLLGGK--RPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERV 378
|
410 420 430
....*....|....*....|....*....|....*
gi 4512364 443 AHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGREL 477
Cdd:cd07100 379 ARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGREL 413
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
25-485 |
4.11e-131 |
|
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: 388.34 E-value: 4.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERV--DSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdHGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07113 4 IDGRPVagQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAF-VSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQP-QINQAIEDFEFYAG---AIVGHRGTVN-NVPNG--FLNYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGwatKINGETLAPSiPSMQGerYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKAS 255
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 256 HTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGT 335
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 336 HVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDERE 415
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 416 VIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLDLY 485
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDY 467
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
40-476 |
3.83e-128 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 379.85 E-value: 3.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:TIGR01780 3 NPATGEIIGSVPDQGVDETEAAIRAAYEAFK--TWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFYAGAIVGHRGTVNNVPN-GFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITA 198
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQsDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 199 ILLNEICHEAGVPEGVVNTVAG-AGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADA 277
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 278 DMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAE 357
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 358 EEGATIALGGKeRRVEGfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQG 437
Cdd:TIGR01780 321 EKGAKVVTGGK-RHELG---GNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLS 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 4512364 438 RATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRE 476
Cdd:TIGR01780 397 RIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGRE 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
25-474 |
7.49e-128 |
|
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: 379.94 E-value: 7.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDS--DETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07085 5 INGEWVESktTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG-TVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGeYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVgDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRV 261
Cdd:cd07085 163 CGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 262 TLELGGKSPNLVFADADME---AAVAGSLFGiyfNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVG 338
Cdd:cd07085 242 QALGGAKNHAVVMPDADLEqtaNALVGAAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 339 SIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIK 418
Cdd:cd07085 319 PVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 419 RANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSA-FPGTPFGGYKESGFG 474
Cdd:cd07085 399 IINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVpLAFFSFGGWKGSFFG 455
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-483 |
4.17e-127 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 378.85 E-value: 4.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 22 RMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHGKWRKYPVGKRARVLNQIAAIMRERFQE 99
Cdd:PRK09847 21 RLFINGEYTAaaENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 100 LVEIEVLNSGKAIS-AAQPQINQAIEDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:PRK09847 101 LALLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT- 257
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADA-DMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTH 336
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 337 VGSIISRDQLEIIDSYVRSAEEEGATIalggkerrVEGFENGH--WYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDER 414
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKGQLL--------LDGRNAGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 415 EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRELCVETLD 483
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALE 481
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
36-476 |
7.03e-126 |
|
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: 374.27 E-value: 7.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 36 FETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAA 115
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 116 QPQINQAIEDFEFYAGAIVGHRGTVNN---VPN--GFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP 190
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPldiSARgeGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 191 ASLTPITAILLNEICHEAGVPEGVVNtVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHtlKRVTLELGGKSP 270
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFS-VLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 271 NLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIID 350
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGATIALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSA 430
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4512364 431 IWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFGRE 476
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGIGRE 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-476 |
7.10e-122 |
|
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: 364.06 E-value: 7.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAE--NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFYAGAIVGHRGTVnnVPNGF-------LNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPAS 192
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEE--IPLDAtqgsdnrLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 193 LTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAShtLKRVTLELGGKSPNL 272
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 273 VFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSY 352
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 353 VRSAEEEGATIALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIW 432
Cdd:cd07094 319 VEEAVEAGARLLCGGE-------RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 4512364 433 TKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFGRE 476
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
25-482 |
1.26e-121 |
|
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: 363.81 E-value: 1.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD-ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdHGKWRKYPVGKRARVLNQIAAIMRERFQELVEI 103
Cdd:cd07082 6 INGEWKESSgKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 104 EVLNSGKAISAAQPQ-------INQAIEDFEFYAGAIVghRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:cd07082 85 LMWEIGKTLKDALKEvdrtidyIRDTIEELKRLDGDSL--PGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKasH 256
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ--H 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 TLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTH 336
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 337 VGSIISRDQLEIIDSYVRSAEEEGATIALGGkerrveGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREV 416
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 417 IKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGT-PFGGYKESGFGRELCVETL 482
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDAL 461
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
20-472 |
3.85e-121 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 364.26 E-value: 3.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVDSDETFETFNPA-KGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:PRK03137 36 DYPLIIGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIV--GHRGTVNNVPnGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:PRK03137 114 EFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLklADGKPVESRP-GEHNRYFYIPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASH 256
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 T------LKRVTLELGGKSPNLVFADADMEAAVAG---SLFGiyFNtGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQL 327
Cdd:PRK03137 273 VqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESivaSAFG--FS-GQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 328 GDPFDKgTHVGSIISRDQLEIIDSYVRSAEEEGATIaLGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFGPVVVV 407
Cdd:PRK03137 350 GNPEDN-AYMGPVINQASFDKIMSYIEIGKEEGRLV-LGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4512364 408 ETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN--CPfSAFPGT-PFGGYKESG 472
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCT-GAIVGYhPFGGFNMSG 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-475 |
4.52e-120 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 361.89 E-value: 4.52e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 31 DSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAfdHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGK 110
Cdd:PRK09407 29 AAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 111 AISAAQPQINQAIEDFEFYAGAIVG------HRGTvnnVPngFLNYT--QKEPVGVCAQIIPWNYPLMMAAWKVAPALAA 182
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRAPKllaprrRAGA---LP--VLTKTteLRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 183 GCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVghEDVNKVAFTGSTPIGKDIMEKASHTLKRVT 262
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 263 LELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIIS 342
Cdd:PRK09407 260 LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLIS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 343 RDQLEIIDSYVRSAEEEGATIALGGKERRVEG--FenghwYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRA 420
Cdd:PRK09407 340 EAQLETVSAHVDDAVAKGATVLAGGKARPDLGplF-----YEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4512364 421 NDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPG---TPFGGYKESGFGR 475
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGsvdAPMGGMKDSGLGR 472
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-475 |
7.67e-118 |
|
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: 353.54 E-value: 7.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 41 PAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQIN 120
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQR--AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 121 QAIEDFEFYAGAIVG------HRGTVnnvPngFLNYT--QKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPAS 192
Cdd:cd07101 81 DVAIVARYYARRAERllkprrRRGAI---P--VLTRTtvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 193 LTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVnkVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNL 272
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 273 VFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSY 352
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 353 VRSAEEEGATIALGGKERRVEGfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIW 432
Cdd:cd07101 314 VDDAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4512364 433 TKDQGRATRVAHQLEAGIVMVNCPFSAFPG---TPFGGYKESGFGR 475
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGYAAAWAsidAPMGGMKDSGLGR 436
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-475 |
2.92e-115 |
|
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: 346.10 E-value: 2.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 57 HAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGH 136
Cdd:cd07105 1 DADQAVEAAAAAF--PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 137 R-GTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVV 215
Cdd:cd07105 79 IgGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 216 NTV----AGAGSVVgDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIY 291
Cdd:cd07105 159 NVVthspEDAPEVV-EALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 292 FNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDpfdkgTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERR 371
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 372 VEGfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIV 451
Cdd:cd07105 313 SPS---GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420
....*....|....*....|....*
gi 4512364 452 MVNCP-FSAFPGTPFGGYKESGFGR 475
Cdd:cd07105 390 HINGMtVHDEPTLPHGGVKSSGYGR 414
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
25-476 |
6.04e-114 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 344.58 E-value: 6.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSD--ETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:PRK11241 15 INGEWLDANngEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQA---IEDF-----EFYAGAIVGHRgtvnnvPNGFLnYTQKEPVGVCAQIIPWNYPLMMAAW 174
Cdd:PRK11241 93 LMTLEQGKPLAEAKGEISYAasfIEWFaeegkRIYGDTIPGHQ------ADKRL-IVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 175 KVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKA 254
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 255 SHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKG 334
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 335 THVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEgfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDER 414
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4512364 415 EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGRE 476
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGRE 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
37-474 |
1.02e-112 |
|
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: 340.49 E-value: 1.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 37 ETFNPAKGEILATVAKASREHAEKAVQAARHAfdHGKWRKYpvgKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQ 116
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAASY--RSTLTRY---QRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 117 PQINQAIEDFEFYAGAIVGHRGTV---NNVPNG--FLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPA 191
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESfscDLTANGkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 192 SLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHtlKRVTLELGGKSPN 271
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 272 LVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDS 351
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 352 YVRSAEEEGATIALGGkERRvegfenGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAI 431
Cdd:cd07146 315 RVEEAIAQGARVLLGN-QRQ------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 4512364 432 WTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFG 474
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDSGLG 431
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
44-474 |
1.06e-112 |
|
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: 340.04 E-value: 1.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 44 GEILATVAKASREHAEKAVQAARHAfdHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAI 123
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 124 EDFEFYAGAIVGHRGTVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITA-ILLN 202
Cdd:cd07152 79 GELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 203 EICHEAGVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAA 282
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 283 VAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGAT 362
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 363 IALGGKerrvegfENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRV 442
Cdd:cd07152 318 LEAGGT-------YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430
....*....|....*....|....*....|...
gi 4512364 443 AHQLEAGIVMVN-CPFSAFPGTPFGGYKESGFG 474
Cdd:cd07152 391 ADRLRTGMLHINdQTVNDEPHNPFGGMGASGNG 423
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-474 |
1.74e-110 |
|
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: 334.60 E-value: 1.74e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFY----AGAIVGHRgtvnnVPN--GFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASL 193
Cdd:cd07102 80 RGMLERARYMisiaEEALADIR-----VPEkdGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 194 TPITAILLNEICHEAGVPEGVVNTVAGaGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLV 273
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 274 FADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYV 353
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 354 RSAEEEGATIALGGKERRvEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWT 433
Cdd:cd07102 314 ADAIAKGARALIDGALFP-EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4512364 434 KDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFG 474
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-477 |
2.23e-98 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 303.58 E-value: 2.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 38 TFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQP 117
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFR--DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFYAG----------AIVGHRGTVNNvpngflnYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVV 187
Cdd:PRK09406 83 EALKCAKGFRYYAEhaealladepADAAAVGASRA-------YVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 188 VKPASLTPITAILLNEICHEAGVPEGVVNTV-AGAGSVvgDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELG 266
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCFQTLlVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 267 GKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQL 346
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 347 EIIDSYVRSAEEEGATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFG 426
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGK--RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4512364 427 LGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGREL 477
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGREL 440
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
86-474 |
2.78e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.04 E-value: 2.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 86 LNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEF-------YAGAIVGHRGTVNNVpngflnYTQKEPVGV 158
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYmaewarrYEGEIIQSDRPGENI------LLFKRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 159 CAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKV 238
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 239 AFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEF 318
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 319 ITRAKKLQLGDPFDKGT-HVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQ 397
Cdd:PRK10090 235 GEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGK--AVEG--KGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 398 EEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCP-FSAFPGtpF-GGYKESGFG 474
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREnFEAMQG--FhAGWRKSGIG 387
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
39-475 |
3.86e-96 |
|
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: 298.06 E-value: 3.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKA-ISAAQP 117
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR--EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 118 QINQAIEDFEFyagaIVGHRGTV---NNVPNGFLNYTQK-----EPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVK 189
Cdd:cd07098 79 EILVTCEKIRW----TLKHGEKAlrpESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 190 PASLTPITAILLNEICHEA----GVPEGVVNTVAGAGSVvGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLEL 265
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 266 GGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQ 345
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 346 LEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKF 425
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 4512364 426 GLGSAIWTKDQGRATRVAHQLEAGIVMVNcPFSAF---PGTPFGGYKESGFGR 475
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAIN-DFGVNyyvQQLPFGGVKGSGFGR 445
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
24-476 |
2.47e-91 |
|
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: 286.03 E-value: 2.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGERVDSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVEI 103
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 104 EVLNSGKAISAAQPQINQAIE--DF------EFYAGAIVGHRgtvnnvPNGFLnYTQKEPVGVCAQIIPWNYPLMMAAWK 175
Cdd:cd07130 80 VSLEMGKILPEGLGEVQEMIDicDFavglsrQLYGLTIPSER------PGHRM-MEQWNPLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 176 VAPALAAGCSVVVKPASLTPITAI----LLNEICHEAGVPEGVVNTVAGaGSVVGDYLVGHEDVNKVAFTGSTPIGKDIM 251
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 252 EKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPF 331
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 332 DKGTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKerRVEGfeNGHWYEPTVITnVTPDMKAVQEEIFGPVVVVETFQ 411
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGK--VIDG--PGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4512364 412 DEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQL--EAGIVMVNCPFS-AFPGTPFGGYKESGFGRE 476
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSgAEIGGAFGGEKETGGGRE 454
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-474 |
4.01e-91 |
|
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: 285.62 E-value: 4.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 22 RMVINGERVD--SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQE 99
Cdd:TIGR01722 2 NHWIGGKFAEgaSGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 100 LVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRG-TVNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAP 178
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGeTSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 179 ALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGaGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTL 258
Cdd:TIGR01722 160 AIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 259 KRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIyDEFIEEFITRAKKLQLGDPFDKGTHVG 338
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 339 SIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIK 418
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 419 RANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSA-FPGTPFGGYKESGFG 474
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVpLPYFSFTGWKDSFFG 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
20-474 |
4.70e-88 |
|
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: 278.31 E-value: 4.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 20 HYRMVINGERVDSDETFETFNP-AKGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQ 98
Cdd:cd07083 18 AYPLVIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 99 ELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTVNNVPN--GFLNYTQKEPVGVCAQIIPWNYPLMMAAWKV 176
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPypGEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 177 APALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAS- 255
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 256 -----HTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDP 330
Cdd:cd07083 256 lapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 331 FDKGTHVGSIISRDQLEIIDSYVRSAEEEGaTIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETF 410
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGK--RLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4512364 411 QDER--EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS-AFPGT-PFGGYKESGFG 474
Cdd:cd07083 411 KDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgALVGVqPFGGFKLSGTN 478
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-477 |
4.50e-87 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 274.82 E-value: 4.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 40 NPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQI 119
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 120 NQAIEDFEFYAG---AIVGHRGTVNNVPNGFLNYtqkEPVGVCAQIIPWNYPLmmaaWKV----APALAAGCSVVVKPAS 192
Cdd:PRK13968 91 AKSANLCDWYAEhgpAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 193 LTPITAILLNEICHEAGVPEGV---VN-TVAGAGSVVGDylvghEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGK 268
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVygwLNaDNDGVSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 269 SPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEI 348
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 349 IDSYVRSAEEEGATIALGGKerRVEGfeNGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLG 428
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGE--KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4512364 429 SAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGTPFGGYKESGFGREL 477
Cdd:PRK13968 395 ATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGREL 443
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
37-474 |
4.07e-84 |
|
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: 266.98 E-value: 4.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 37 ETFNPAKGEILATVAKASREHAEKAVQAARHAF-DHGKWrkYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAA 115
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 116 QPQINQAIEDFEFYAGAIVGHRGTvnNVPNGF-------LNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVV 188
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGR--EIPMGLtpasagrIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 189 KPASLTPITAILLNEICHEAGVPEGVVNTVAgAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTlKRVTLELGGK 268
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 269 SPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEI 348
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 349 IDSYVRSAEEEGATIALGGKeRRVEGFenghwYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLG 428
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGK-RLSDTT-----YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4512364 429 SAIWTKDQGRATRVAHQLEAGIVMVNCPfSAF--PGTPFGGYKESGFG 474
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDH-TAFrvDWMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
24-474 |
4.70e-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: 263.29 E-value: 4.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGERVDSDETFETFNPA-KGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:cd07125 36 IINGEETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIeDF-EFYAGAIVGHRGTVN-NVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPAL 180
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAI-DFcRYYAAQARELFSDPElPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 181 AAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEK-ASHTLK 259
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRAlAERDGP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 260 RVTL--ELGGKSPNLVFADADMEAAVA---GSLFGiyfNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKG 334
Cdd:cd07125 273 ILPLiaETGGKNAMIVDSTALPEQAVKdvvQSAFG---SAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 335 THVGSIISRDQLEIIDSYVRSAEEEGATIalggKERRVEGfENGHWYEPTVITNVTPDmkAVQEEIFGPVVVVETFQDER 414
Cdd:cd07125 350 TDVGPLIDKPAGKLLRAHTELMRGEAWLI----APAPLDD-GNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAED 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4512364 415 --EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS-AFPGT-PFGGYKESGFG 474
Cdd:cd07125 423 ldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITgAIVGRqPFGGWGLSGTG 486
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-474 |
9.51e-72 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 238.88 E-value: 9.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGERVDSDET--FETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELV 101
Cdd:PLN02419 117 LIGGSFVESQSSsfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 102 EIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGT-VNNVPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPAL 180
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 181 AAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVgDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKR 260
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 VTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRL-FVHEEiyDEFIEEFITRAKKLQLGDPFDKGTHVGS 339
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDA--KSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 340 IISRDQLEIIDSYVRSAEEEGATIALGGKERRVEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKR 419
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4512364 420 ANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSA-FPGTPFGGYKESGFG 474
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVpLPFFSFTGNKASFAG 567
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-474 |
6.12e-71 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 233.88 E-value: 6.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 19 DHYRMVINGE--RVDSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAfdHGKWRKYPVGKRARVLNQIAAIMRER 96
Cdd:PLN00412 14 DVYKYYADGEwrTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 97 FQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGA---IVGHRGTVNNVP---NGFLNY--TQKEPVGVCAQIIPWNYP 168
Cdd:PLN00412 92 KAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEgvrILGEGKFLVSDSfpgNERNKYclTSKIPLGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 169 LMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTpIGK 248
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 249 DIMEKAShtLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLG 328
Cdd:PLN00412 251 AISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 329 DPFDKGThVGSIISRDQLEIIDSYVRSAEEEGATIAlggKERRVEGfeNGHWyePTVITNVTPDMKAVQEEIFGPVVVVE 408
Cdd:PLN00412 329 PPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREG--NLIW--PLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4512364 409 TFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGT-PFGGYKESGFG 474
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
150-475 |
2.03e-70 |
|
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: 230.11 E-value: 2.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 150 YTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYL 229
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 230 VGHEDvnKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEE 309
Cdd:cd07087 174 AEPFD--HIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 310 IYDEFIEEfITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVrsaeeEGATIALGGkerrvEGFENGHWYEPTVITNV 389
Cdd:cd07087 252 IKDELIEE-LKKAIKEFYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGG-----QVDKEERYIAPTILDDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 390 TPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAF-PGTPFGG 467
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdVLLHAAiPNLPFGG 400
|
....*...
gi 4512364 468 YKESGFGR 475
Cdd:cd07087 401 VGNSGMGA 408
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
152-475 |
7.30e-69 |
|
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: 226.34 E-value: 7.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 152 QKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVvntvagaGSVVGDYLVG 231
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-------AVFEGDAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 232 HE----DVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVH 307
Cdd:cd07134 170 QAllelPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 308 EEIYDEFIEEFITRAKKLQLGDPFDKGT-HVGSIISRDQLEIIDSYVRSAEEEGATIALGGKERrvegfENGHWYEPTVI 386
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 387 TNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAF--PGTP 464
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFlnPNLP 404
|
330
....*....|.
gi 4512364 465 FGGYKESGFGR 475
Cdd:cd07134 405 FGGVNNSGIGS 415
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-475 |
1.50e-64 |
|
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: 215.21 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 57 HAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVGH 136
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 137 RGTVNNvPNGFLN-YTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVV 215
Cdd:cd07095 79 TGERAT-PMAQGRaVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 216 NTVAGAGSvVGDYLVGHEDVNKVAFTGSTPIGKDIMEK-ASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNT 294
Cdd:cd07095 158 NLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 295 GQSCEARSRLFVHE-EIYDEFIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEGATiALGGKERRVE 373
Cdd:cd07095 237 GQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGE-PLLAMERLVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 374 GfenGHWYEPTVItNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMV 453
Cdd:cd07095 316 G---TAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNW 391
|
410 420
....*....|....*....|...
gi 4512364 454 NCPFSAFPGT-PFGGYKESGFGR 475
Cdd:cd07095 392 NRPTTGASSTaPFGGVGLSGNHR 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
150-475 |
6.20e-62 |
|
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: 208.51 E-value: 6.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 150 YTQKEPVGVCAQIIPWNYPLMMAawkVAP---ALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVG 226
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 227 DYLvgHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFV 306
Cdd:cd07136 171 ELL--DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 307 HEEIYDEFIEEFITRAKKLQLGDPFDKGtHVGSIISRDQLEIIDSYVrsaeeEGATIALGGKERRvegfeNGHWYEPTVI 386
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDR-----ETLYIEPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 387 TNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS--AFPGTP 464
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLP 397
|
330
....*....|.
gi 4512364 465 FGGYKESGFGR 475
Cdd:cd07136 398 FGGVGNSGMGS 408
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
81-475 |
8.81e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 207.72 E-value: 8.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 81 KRARVLNQIAAIMRERFQELVEievlnsgkAISAaqpqinqaieDFefyagaivGHR-----------GTVNNvpngfLN 149
Cdd:cd07133 21 ERRDRLDRLKALLLDNQDALAE--------AISA----------DF--------GHRsrhetllaeilPSIAG-----IK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 150 YTQK--------------------------EPVGVCAQIIPWNYPLMMAawkVAP---ALAAGCSVVVKPASLTPITAIL 200
Cdd:cd07133 70 HARKhlkkwmkpsrrhvgllflpakaeveyQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 201 LNEICHEAGVPEGVvnTVAGAGSVVG--------DYLVghedvnkvaFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNL 272
Cdd:cd07133 147 LAELLAEYFDEDEV--AVVTGGADVAaafsslpfDHLL---------FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 273 VFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKL--QLGDPFDkgthVGSIISRDQLEIID 350
Cdd:cd07133 216 IAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPD----YTSIINERHYARLQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 351 SYVRSAEEEGAT-IALGGKErrvEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGS 429
Cdd:cd07133 292 GLLEDARAKGARvIELNPAG---EDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLAL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4512364 430 AIWTKDQGRATRVAHQLEAGIVMVNCPFS--AFPGTPFGGYKESGFGR 475
Cdd:cd07133 369 YYFGEDKAEQDRVLRRTHSGGVTINDTLLhvAQDDLPFGGVGASGMGA 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
24-454 |
1.31e-61 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 217.88 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGErVDSDETFETFNPAKG-EILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:COG4230 561 LIAGE-AASGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFP--AWSATPVEERAAILERAADLLEAHRAELMA 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIeDF-EFYAGAIVGHrgtvnnvpngFLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:COG4230 638 LLVREAGKTLPDAIAEVREAV-DFcRYYAAQARRL----------FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDImekaSHTL-KR 260
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----NRTLaAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 261 ----VTL--ELGGKspNLVFAD--ADMEAAVA---GSLFGiyfNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGD 329
Cdd:COG4230 783 dgpiVPLiaETGGQ--NAMIVDssALPEQVVDdvlASAFD---SAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGD 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 330 PFDKGTHVGSIISRDQLEIIDSYVRSAEEEGATIA---LGgkerrvEGFENGHWYEPTVITnvTPDMKAVQEEIFGPVVV 406
Cdd:COG4230 858 PADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHqlpLP------EECANGTFVAPTLIE--IDSISDLEREVFGPVLH 929
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4512364 407 VETFQDER--EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN 454
Cdd:COG4230 930 VVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
24-474 |
2.80e-59 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 210.83 E-value: 2.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGervdSDETFETFNPAKGE-ILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:PRK11904 556 IING----EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAELIA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIeDF-EFYA-------GAIVGHRGtvnnvPNGFLNYTQKEPVGVCAQIIPWNYPLMMAAW 174
Cdd:PRK11904 630 LCVREAGKTLQDAIAEVREAV-DFcRYYAaqarrlfGAPEKLPG-----PTGESNELRLHGRGVFVCISPWNFPLAIFLG 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 175 KVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDImeka 254
Cdd:PRK11904 704 QVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARII---- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 255 SHTL-KR----VTL--ELGGKspNLVFADA---------DmeaaVAGSLFGiyfNTGQSCEARSRLFVHEEIYDEFIEEF 318
Cdd:PRK11904 780 NRTLaARdgpiVPLiaETGGQ--NAMIVDStalpeqvvdD----VVTSAFR---SAGQRCSALRVLFVQEDIADRVIEML 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 319 ITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEEG---ATIALGgkerrvEGFENGHWYEPTVITnvTPDMKA 395
Cdd:PRK11904 851 KGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP------AGTENGHFVAPTAFE--IDSISQ 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 396 VQEEIFGPVVVVETFQDER--EVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGT-PFGGYKES 471
Cdd:PRK11904 923 LEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrNQIGAVVGVqPFGGQGLS 1002
|
...
gi 4512364 472 GFG 474
Cdd:PRK11904 1003 GTG 1005
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-472 |
3.89e-58 |
|
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: 200.51 E-value: 3.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 23 MVINGERVDSDETFETFNPAK-GEILATVAKASREHAEKAVQAARHAfdHGKWRKYPVGKRARVLNQIAAIMRERF-QEL 100
Cdd:cd07123 35 LVIGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLSGKYrYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 101 VEIEVLNSGKaiSAAQPQINQAIE--DF----EFYAGAIVGHRGTVNnvPNGFLNYTQKEPV-GVCAQIIPWNYPLMMAA 173
Cdd:cd07123 113 NAATMLGQGK--NVWQAEIDAACEliDFlrfnVKYAEELYAQQPLSS--PAGVWNRLEYRPLeGFVYAVSPFNFTAIGGN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 174 WKVAPALAaGCSVVVKPASltpiTAILLN----EICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKD 249
Cdd:cd07123 189 LAGAPALM-GNVVLWKPSD----TAVLSNylvyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 250 IMEKAS------HTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAK 323
Cdd:cd07123 264 LWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 324 KLQLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEEE-GATIALGGKERRVEGFenghWYEPTVITNVTPDMKAVQEEIFG 402
Cdd:cd07123 344 EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY----FVEPTVIETTDPKHKLMTEEIFG 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4512364 403 PVVVVETFQDER--EVIKRANDT-KFGLGSAIWTKDQgRATRVAHQL---EAGIVMVNC-PFSAFPGT-PFGGYKESG 472
Cdd:cd07123 420 PVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDR-KAIREATDAlrnAAGNFYINDkPTGAVVGQqPFGGARASG 496
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
59-475 |
4.99e-58 |
|
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: 197.83 E-value: 4.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 59 EKAVQAARHAFDHGK-----WRKYPvgkrarvLNQIAAIMRERFQELVEIEVLNSGKA--------ISAAQPQINQAIED 125
Cdd:cd07135 8 DSIHSRLRATFRSGKtkdleYRLWQ-------LKQLYWAVKDNEEAIVEALKKDLGRPpfetllteVSGVKNDILHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 126 FEFYAGaivGHRGTVNNVPNGFLN-YTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEI 204
Cdd:cd07135 81 LKKWAK---DEKVKDGPLAFMFGKpRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 205 CHEAgVPEGVVNTVAGAGSVVGDYLVGHEDvnKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVA 284
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 285 GSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKgTHVGSIISRDQLEIIDSYVrsaEEEGATIA 364
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLL---DTTKGKVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 365 LGGKERRVEGFenghwYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAH 444
Cdd:cd07135 311 IGGEMDEATRF-----IPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT 385
|
410 420 430
....*....|....*....|....*....|...
gi 4512364 445 QLEAGIVMVNCPF--SAFPGTPFGGYKESGFGR 475
Cdd:cd07135 386 RTRSGGVVINDTLihVGVDNAPFGGVGDSGYGA 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
150-474 |
1.02e-57 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 198.71 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 150 YTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAgVPEGVVNTVAGAGSVVGDYL 229
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 230 VGHEDVnkVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEE 309
Cdd:PTZ00381 183 KEPFDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 310 IYDEFIEEFiTRAKKLQLGDPFDKGTHVGSIISRDQLEIIDSYVrsaEEEGATIALGGkerrvEGFENGHWYEPTVITNV 389
Cdd:PTZ00381 261 IKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGG-----EVDIENKYVAPTIIVNP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 390 TPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAF-PGTPFGG 467
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLnPNLPFGG 411
|
....*..
gi 4512364 468 YKESGFG 474
Cdd:PTZ00381 412 VGNSGMG 418
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
25-472 |
1.24e-55 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 192.87 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVD-SDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDHgkWRKYPVGKRARVLNQIAAIMRERFQELVEI 103
Cdd:PRK09457 5 INGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 104 EVLNSGKaisaaqPQINQAIEdfefyAGAIVG---------HRGT---VNNVPNG--FLNYtqkEPVGVCAQIIPWNYPL 169
Cdd:PRK09457 83 IARETGK------PLWEAATE-----VTAMINkiaisiqayHERTgekRSEMADGaaVLRH---RPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 170 MMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGaGSVVGDYLVGHEDVNKVAFTGSTPIGKD 249
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 250 IMEK-ASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIY-DEFIEEFITRAKKLQL 327
Cdd:PRK09457 228 LHRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 328 GDPF-DKGTHVGSIISRDQLE-IIDSYVRsaeeegaTIALGGKE----RRVE---GFENghwyePTVI--TNVT--PDmk 394
Cdd:PRK09457 308 GRWDaEPQPFMGAVISEQAAQgLVAAQAQ-------LLALGGKSllemTQLQagtGLLT-----PGIIdvTGVAelPD-- 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 395 avqEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAFPGT-PFGGYKESG 472
Cdd:PRK09457 374 ---EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAaPFGGVGASG 449
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
27-474 |
1.00e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 197.78 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 27 GERVDSDETFETFNPAK-GEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEV 105
Cdd:PRK11905 560 AGGDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFP--EWSATPAAERAAILERAADLMEAHMPELFALAV 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 106 LNSGKAISAAQPQINQAIeDF-EFYAgaivghrgtvNNVPNGFLNyTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGC 184
Cdd:PRK11905 638 REAGKTLANAIAEVREAV-DFlRYYA----------AQARRLLNG-PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 185 SVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDI-MEKASHTLKRVTL 263
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqRTLAKRSGPPVPL 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 264 --ELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGSII 341
Cdd:PRK11905 786 iaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVI 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 342 SRDQLEIIDSYVRSAEEEGATIAlggkerRV---EGFENGHWYEPTVITnvTPDMKAVQEEIFGPVVVVETFQDER--EV 416
Cdd:PRK11905 866 DAEAQANIEAHIEAMRAAGRLVH------QLplpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADEldRV 937
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 417 IKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGT-PFGGYKESGFG 474
Cdd:PRK11905 938 IDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrNIIGAVVGVqPFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
25-488 |
1.93e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 190.43 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 25 INGERVDSDETFETFNPAKGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIE 104
Cdd:PLN02315 25 VGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAK--IWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 105 VLNSGKAISAAQPQINQAIEDFEFYAGAIVGHRGTVnnVPNGFLNYTQKE---PVGVCAQIIPWNYPLMMAAWKVAPALA 181
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSI--IPSERPNHMMMEvwnPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 182 AGCSVVVKPASLTPITAI----LLNEICHEAGVPEGVVNTVAGaGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHT 257
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 258 LKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHV 337
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 338 GSIISRDQLEIIDSYVRSAEEEGATIALGGKERRVEgfenGHWYEPTVItNVTPDMKAVQEEIFGPVVVVETFQDEREVI 417
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESE----GNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRV--AHQLEAGIVMVNCPFS-AFPGTPFGGYKESGFGRELCVETLDLYIGR 488
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNgAEIGGAFGGEKATGGGREAGSDSWKQYMRR 488
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-474 |
2.50e-52 |
|
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: 184.34 E-value: 2.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 24 VINGERVDSDETFETFNPA-KGEILATVAKASREHAEKAVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVE 102
Cdd:TIGR01238 41 IIGHSYKADGEAQPVTNPAdRRDIVGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLELHMPELMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 103 IEVLNSGKAISAAQPQINQAIEDFEFYAgaivghrgtvNNVPNGFLNYTQKePVGVCAQIIPWNYPLMMAAWKVAPALAA 182
Cdd:TIGR01238 119 LCVREAGKTIHNAIAEVREAVDFCRYYA----------KQVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 183 GCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEK-ASHTLKRV 261
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTlAQREDAPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 262 TL--ELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGS 339
Cdd:TIGR01238 268 PLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 340 IISRDQLEIIDSYVRSAEEEGATIALGGKERRVEgFENGHWYEPTVITnvTPDMKAVQEEIFGPVVVVETFQDER--EVI 417
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIV 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN-CPFSAFPGT-PFGGYKESGFG 474
Cdd:TIGR01238 425 DQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVqPFGGQGLSGTG 483
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
59-475 |
2.36e-51 |
|
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: 180.50 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 59 EKAVQAARHAFDHGKWRkyPVGKRARVLNQIAAIMRERFQELVEievlnsgkAISA--AQPQINQAIEDFEFYAGAIvgh 136
Cdd:cd07132 1 AEAVRRAREAFSSGKTR--PLEFRIQQLEALLRMLEENEDEIVE--------ALAKdlRKPKFEAVLSEILLVKNEI--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 137 RGTVNN---------VPNGFLN-----YTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLN 202
Cdd:cd07132 68 KYAISNlpewmkpepVKKNLATllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 203 EI--------CH---EAGVPEGVvntvagagsvvgdyLVGHEDVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPN 271
Cdd:cd07132 148 ELipkyldkeCYpvvLGGVEETT--------------ELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 272 LVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEfITRAKKLQLGDPFDKGTHVGSIISRDQLEIIDS 351
Cdd:cd07132 214 YVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEA-LKKTLKEFYGEDPKESPDYGRIINDRHFQRLKK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 352 YVrsaeeEGATIALGGkerrvEGFENGHWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAI 431
Cdd:cd07132 293 LL-----SGGKVAIGG-----QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYV 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4512364 432 WTKDQGRATRVAHQLEAGIVMVN--CPFSAFPGTPFGGYKESGFGR 475
Cdd:cd07132 363 FSNNKKVINKILSNTSSGGVCVNdtIMHYTLDSLPFGGVGNSGMGA 408
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
27-474 |
9.12e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 168.61 E-value: 9.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 27 GERVDSDETFETFNPA-KGEILATVAKASREHAEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEV 105
Cdd:PRK11809 652 EDPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAP--IWFATPPAERAAILERAADLMEAQMQTLMGLLV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 106 LNSGKAISAAQPQINQAIEDFEFYAGaivghrgtvnNVPNGFLNYTQKePVGVCAQIIPWNYPLMMAAWKVAPALAAGCS 185
Cdd:PRK11809 730 REAGKTFSNAIAEVREAVDFLRYYAG----------QVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 186 VVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTL----KRV 261
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPI 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 262 TL--ELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRAKKLQLGDPFDKGTHVGS 339
Cdd:PRK11809 879 PLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGP 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 340 IISRDQLEIIDSYVRSAEEEGATIALGGKErRVEGFENGHWYEPTVITnvTPDMKAVQEEIFGPVVVVETFQDER--EVI 417
Cdd:PRK11809 959 VIDAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVRYNRNQldELI 1035
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4512364 418 KRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPF-SAFPGT-PFGGYKESGFG 474
Cdd:PRK11809 1036 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMvGAVVGVqPFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
154-475 |
1.20e-38 |
|
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: 145.63 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 154 EPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEIcheagVPEGVVNT---VAGAGSVVGDYLV 230
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-----IPEYLDTKaikVIEGGVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 231 GHEdVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIY-FNTGQSCEARSRLFVHEE 309
Cdd:cd07137 175 EQK-WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 310 IYDEFIEEFITRAKKLQLGDPfdkgthvgsIISRDQLEIIDS--YVRSAE-----EEGATIALGGKERrvegfENGHWYE 382
Cdd:cd07137 254 FAPTLIDALKNTLEKFFGENP---------KESKDLSRIVNShhFQRLSRllddpSVADKIVHGGERD-----EKNLYIE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 383 PTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFSAF-- 460
Cdd:cd07137 320 PTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYai 399
|
330
....*....|....*
gi 4512364 461 PGTPFGGYKESGFGR 475
Cdd:cd07137 400 DTLPFGGVGESGFGA 414
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-477 |
7.53e-34 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 132.75 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 59 EKAVQAARHafDHGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGK----AISAAQPQINQAIEDFEFYAGAIv 134
Cdd:cd07084 2 ERALLAADI--STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmfAENICGDQVQLRARAFVIYSYRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 135 gHRGTVNNVPNG--FLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAG-VP 211
Cdd:cd07084 79 -PHEPGNHLGQGlkQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 212 EGVVNTVAGAGSvVGDYLVGHEDVNKVAFTGSTPIGKDIMEKASHTlkRVTLELGGKSPNLVFADADMEAAVAGSL-FGI 290
Cdd:cd07084 158 PEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCvQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 291 YFNTGQSCEARSRLFVHEeiyDEFIEEFITRAKKLqLGDPFDKGTHVGSIISRDQLEIIDSyvrSAEEEGATIALGGKEr 370
Cdd:cd07084 235 TACSGQKCTAQSMLFVPE---NWSKTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAH---MENLLGSVLLFSGKE- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 371 rVEGFENGHWYEPTVITNV----TPDMK---AVQEEIFGPVVVVETFQDERE--VIKRANDTKFGLGSAIWTKDQGRATR 441
Cdd:cd07084 307 -LKNHSIPSIYGACVASALfvpiDEILKtyeLVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 4512364 442 VAHQLE-AGIVMVNCPF--SAFPGTPFG-GYKESGFGREL 477
Cdd:cd07084 386 LIGNLWvAGRTYAILRGrtGVAPNQNHGgGPAADPRGAGI 425
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-474 |
1.17e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 121.31 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 154 EPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEIChEAGVPEGVVNTVAGAGSVVGDYLvgHE 233
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL--EQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 234 DVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIY-FNTGQSCEARSRLFVHEEIYD 312
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 313 EFIEefitrAKKLQLGDPFDKgthvGSIISRDQLEIID-------SYVRSAEEEGATIALGGKERRvegfENGHwYEPTV 385
Cdd:PLN02174 268 KVID-----AMKKELETFYGK----NPMESKDMSRIVNsthfdrlSKLLDEKEVSDKIVYGGEKDR----ENLK-IAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 386 ITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVN--CPFSAFPGT 463
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTL 413
|
330
....*....|.
gi 4512364 464 PFGGYKESGFG 474
Cdd:PLN02174 414 PFGGVGESGMG 424
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
154-475 |
7.94e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 118.68 E-value: 7.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 154 EPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLneichEAGVPE----GVVNTVAGaGSVVGDYL 229
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL-----AANIPKyldsKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 230 VGHEdVNKVAFTGSTPIGKDIMEKASHTLKRVTLELGGKSPNLV---FADADMEAAV---AGSLFGIYfnTGQSCEARSR 303
Cdd:PLN02203 181 LQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVnriVGGKWGSC--AGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 304 LFVHEEIYDEFIEEFITRAKKLQLGDPFDKGtHVGSIISRDQLE-----IIDSYVRSAEEEGATIAlggkerrvegfENG 378
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQrlsnlLKDPRVAASIVHGGSID-----------EKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 379 HWYEPTVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEAGIVMVNCPFS 458
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
330
....*....|....*....
gi 4512364 459 AF--PGTPFGGYKESGFGR 475
Cdd:PLN02203 406 QYacDSLPFGGVGESGFGR 424
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
39-477 |
2.91e-28 |
|
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: 117.37 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATVAKASREHAEkavqAARHAFDHG--KWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQ 116
Cdd:cd07128 20 HDAVTGEVVARVSSEGLDFAA----AVAYAREKGgpALRALTFHERAAMLKALAKYLMERKEDLYALSAATGATRRDSWI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 117 pQINQAIEDFEFYAG--------AIVGHRGTVNNVPNG--FLN---YTQKEpvGVCAQIIPWNYPlmmaAW----KVAPA 179
Cdd:cd07128 96 -DIDGGIGTLFAYASlgrrelpnAHFLVEGDVEPLSKDgtFVGqhiLTPRR--GVAVHINAFNFP----VWgmleKFAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 180 LAAGCSVVVKPASLTPITAILLNEICHEAGV-PEGVVNTVAGAgsvVGDYL--VGHEDVnkVAFTGSTPIGKdimekash 256
Cdd:cd07128 169 LLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLdhLGEQDV--VAFTGSAATAA-------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 257 TLKRvtlelggkSPNLV------FADAD-MEAAVAG-------SLFGIYFN---------TGQSCEARSRLFVHEEIYDE 313
Cdd:cd07128 236 KLRA--------HPNIVarsirfNAEADsLNAAILGpdatpgtPEFDLFVKevaremtvkAGQKCTAIRRAFVPEARVDA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 314 FIEEFITRAKKLQLGDPFDKGTHVGSIISRDQLEiidsYVRSAEE---EGATIALGGKERRVE---GFENGHWYEPTVIT 387
Cdd:cd07128 308 VIEALKARLAKVVVGDPRLEGVRMGPLVSREQRE----DVRAAVAtllAEAEVVFGGPDRFEVvgaDAEKGAFFPPTLLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 388 NVTPD-MKAVQE-EIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEA--GIVMVNCPFSAF--- 460
Cdd:cd07128 384 CDDPDaATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRDSAKest 463
|
490 500
....*....|....*....|...
gi 4512364 461 -PGTPF-----GGYKESGFGREL 477
Cdd:cd07128 464 gHGSPLpqlvhGGPGRAGGGEEL 486
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
39-477 |
7.40e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 110.56 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 39 FNPAKGEILATV-------AKA---SREHAEKAVQAARHAfdhgkwrkypvgKRARVLNQIAAIMRERFQELVEIEVLNS 108
Cdd:PRK11903 24 FDPVTGEELVRVsatgldlAAAfafAREQGGAALRALTYA------------QRAALLAAIVKVLQANRDAYYDIATANS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 109 GKAISAAQPQINQAIEDFEFYA--GAIVGHRgtvNNVPNGFLNYTQKEPV-----------GVCAQIIPWNYPlmmaAW- 174
Cdd:PRK11903 92 GTTRNDSAVDIDGGIFTLGYYAklGAALGDA---RLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFP----AWg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 175 ---KVAPALAAGCSVVVKPASLTPITAILLNEICHEAGV-PEGVVNTVAGAGSVVGDYLvGHEDVnkVAFTGSTPIGKDI 250
Cdd:PRK11903 165 lweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL-QPFDV--VSFTGSAETAAVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 251 MEKASHTLKRVTLELGGKSPN--LVFADADMEAAvAGSLF------GIYFNTGQSCEARSRLFVHEEIYDEFIEEFITRA 322
Cdd:PRK11903 242 RSHPAVVQRSVRVNVEADSLNsaLLGPDAAPGSE-AFDLFvkevvrEMTVKSGQKCTAIRRIFVPEALYDAVAEALAARL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 323 KKLQLGDPFDKGTHVGSIISRDQLEiidsYVRSAEE---EGATIALGGKERRVEGFENGHWY--EPTVITNVTPD-MKAV 396
Cdd:PRK11903 321 AKTTVGNPRNDGVRMGPLVSRAQLA----AVRAGLAalrAQAEVLFDGGGFALVDADPAVAAcvGPTLLGASDPDaATAV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 397 QE-EIFGPVVVVETFQDEREVIKRANDTKFGLGSAIWTKDQGRATRVAHQLEA--GIVMVNCPFSA---------FPGTP 464
Cdd:PRK11903 397 HDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAalhtghgnvMPQSL 476
|
490
....*....|...
gi 4512364 465 FGGYKESGFGREL 477
Cdd:PRK11903 477 HGGPGRAGGGEEL 489
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-454 |
1.29e-23 |
|
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: 103.00 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 59 EKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSGKAISAAQPQINQAIEDFEFYAGAIVG--- 135
Cdd:cd07129 2 DAAAAAAAAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 136 HRGTVN-----------------NVPNGflnytqkePVGVCAqiiPWNYPLmmaAWKV-----APALAAGCSVVVKPASL 193
Cdd:cd07129 80 LDARIDpadpdrqplprpdlrrmLVPLG--------PVAVFG---ASNFPL---AFSVaggdtASALAAGCPVVVKAHPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 194 TPITAILLNEICHEA----GVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGSTPIGKDIMEKAShtlKR-----VTLE 264
Cdd:cd07129 146 HPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARpepipFYAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 265 LGGKSPNLVFADADME--AAVAGSLFG-IYFNTGQSCEARSRLFVHE-EIYDEFIEEFITRAKKLQLGDPFDKGthvgsi 340
Cdd:cd07129 223 LGSVNPVFILPGALAErgEAIAQGFVGsLTLGAGQFCTNPGLVLVPAgPAGDAFIAALAEALAAAPAQTMLTPG------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 341 isrdqleIIDSYVRSAEE----EGATIALGGKERrvegfENGHWYEPTVI-----TNVTPDmkAVQEEIFGPVVVVETFQ 411
Cdd:cd07129 297 -------IAEAYRQGVEAlaaaPGVRVLAGGAAA-----EGGNQAAPTLFkvdaaAFLADP--ALQEEVFGPASLVVRYD 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4512364 412 DEREVIKRANDTKFGLGSAIW--TKDQGRATRVAHQLE--AGIVMVN 454
Cdd:cd07129 363 DAAELLAVAEALEGQLTATIHgeEDDLALARELLPVLErkAGRLLFN 409
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
154-456 |
1.55e-13 |
|
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: 72.52 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 154 EPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP---ASLTPI-TAILLNEICHEAGVPEGVVNTVAGAGSVVGDYL 229
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIeAAKIMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 230 VGHEDVNKVAFTGSTPigkdiMEKASHTLKRVTLELG-GKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHE 308
Cdd:cd07122 174 MKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 309 EIYDEFIEEFITR-------AKKLQLGDPF--DKGTHVGSIISRDQLEIidsyvrsAEEEGATIAlggKERRVEGFEngh 379
Cdd:cd07122 249 EIYDEVRAELKRRgayflneEEKEKLEKALfdDGGTLNPDIVGKSAQKI-------AELAGIEVP---EDTKVLVAE--- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 380 wyeptvITNVTPDMKAVQEEIFgPVVVVETFQDEREVIKRAND-TKF-GLG--SAIWTKDQGRATRVAHQLEAGIVMVNC 455
Cdd:cd07122 316 ------ETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYgGAGhtAVIHSNDEEVIEEFALRMPVSRILVNT 388
|
.
gi 4512364 456 P 456
Cdd:cd07122 389 P 389
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
82-327 |
1.51e-12 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 69.17 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 82 RARVLNQIAAIMRERFQELVEIEVLNSGKAI-SAAQPQINQAIEDFEFYAGAIVGHRGTVNNV--------PNGFLNYTQ 152
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrSLIANWIAMMGCSESKLYKNIDTERGITASVghiqdvllPDNGETYVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 153 KEPVGVCAQIIPWNYPLMmAAWKVAPALAAGCSVVVKPASLTPITA---ILLNEICHEAGVPEGVVNTVAGAGSVVGDYL 229
Cdd:cd07077 98 AFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTNralALLFQAADAAHGPKILVLYVPHPSDELAEEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 230 VGHEDVNKVAFTGSTPIGKDIMEKASHtlKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNtGQSCEARSRLFVHEE 309
Cdd:cd07077 177 LSHPKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253
|
250
....*....|....*...
gi 4512364 310 IYDEFIEEFITRAKKLQL 327
Cdd:cd07077 254 VLDPLYEEFKLKLVVEGL 271
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
147-326 |
8.86e-12 |
|
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: 66.91 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 147 FLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP----ASLTPITAILLNEICHEAGVPEGVVNTVAGAG 222
Cdd:cd07081 87 GGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 223 SVVGDYLVGHEDVNKVAFTGstpiGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARS 302
Cdd:cd07081 167 IELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170 180
....*....|....*....|....*
gi 4512364 303 RLFVHEEIYDEFIEEFITR-AKKLQ 326
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQgAYKLT 267
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
155-415 |
2.51e-11 |
|
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: 65.59 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 155 PVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKPASLTPITAILLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEd 234
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 235 VNKVAFTGSTPIGkdimEKASHTLK-RVTLELGGKSPNLVFADADMEAAVA-GSLFGIYFNTGQSCEARSRLFVHEEIYD 312
Cdd:cd07126 221 PRMTLFTGSSKVA----ERLALELHgKVKLEDAGFDWKILGPDVSDVDYVAwQCDQDAYACSGQKCSAQSILFAHENWVQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 313 EFIEEFITR-AKKLQLGDpfdkgTHVGSIISRDQLEIIDSYVRSAEEEGATIALGGKErrvegFENGH------WYEPTV 385
Cdd:cd07126 297 AGILDKLKAlAEQRKLED-----LTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKP-----LTNHSipsiygAYEPTA 366
|
250 260 270
....*....|....*....|....*....|....*.
gi 4512364 386 I------TNVTPDMKAVQEEIFGPVVVVETFQDERE 415
Cdd:cd07126 367 VfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
61-330 |
4.33e-11 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 64.57 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 61 AVQAARHAFdhGKWRKYPVGKRARVLNQIAAIMRERFQELVEIEVLNSG---------KAISAAQpqINQAIEDFEfyAG 131
Cdd:cd07121 9 AVAAAKAAQ--KQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedkiaKNHLAAE--KTPGTEDLT--TT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 132 AIVGHRGtvnnvpngfLNYTQKEPVGVCAQIIPWNYPLMMAAWKVAPALAAGCSVVVKP---ASLTPITAI-LLNEICHE 207
Cdd:cd07121 83 AWSGDNG---------LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVeLINKAIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 208 AGVPEGVVNTVAGAGSVVGDYLVGHEDVNKVAFTGstpiGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSL 287
Cdd:cd07121 154 AGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 4512364 288 FGIYFNTGQSCEARSRLFVHEEIYDEFIEEFItRAKKLQLGDP 330
Cdd:cd07121 230 QGASFDNNLPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLNDE 271
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
159-463 |
6.39e-10 |
|
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: 61.34 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 159 CAQIIPWN-YPLMMAAwkvapaLAAGCSVVVKP--ASLTP--ITAILLNEICHEAGVPEGVVNTVA-GAGSVVGDYLVGH 232
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVKPhpAAILPlaITVQVAREVLAEAGFDPNLVTLAAdTPEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 233 EDVNKVAFTGSTPIGKDIMEKAshTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEE--- 309
Cdd:cd07127 276 PEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiq 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 310 ------IYDEFIEEFITRAKKLqLGDPFDKGTHVGSIISRDQLEIIDSYVRSAEeegatIALGGKERRVEGFENGHWYEP 383
Cdd:cd07127 354 tddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGE-----VLLASEAVAHPEFPDARVRTP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 384 TVITNVTPDMKAVQEEIFGPVVVVETFQDEREVIKRAND---TKFGLGSAIWTKDQGRATRVAH-QLEAGI--------- 450
Cdd:cd07127 428 LLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvrEHGAMTVGVYSTDPEVVERVQEaALDAGValsinltgg 507
|
330
....*....|....*
gi 4512364 451 VMVN--CPFSAFPGT 463
Cdd:cd07127 508 VFVNqsAAFSDFHGT 522
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
22-318 |
1.12e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 60.30 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 22 RMVINGERVDSDETFETFNPAKGeILATVakasrehaEKAVQAARHAFDhgKWRKYPVGKRARVLNQIAAIMRERFQELV 101
Cdd:PRK15398 11 KAVLAEMLSSQTVSPPAAVGEMG-VFASV--------DDAVAAAKVAQQ--RYQQKSLAMRQRIIDAIREALLPHAEELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 102 EIEVLNSG---------KAISAAQ--PqinqAIEDFEfyAGAIVGHRGtvnnvpngfLNYTQKEPVGVCAQIIPWNYP-- 168
Cdd:PRK15398 80 ELAVEETGmgrvedkiaKNVAAAEktP----GVEDLT--TEALTGDNG---------LTLIEYAPFGVIGAVTPSTNPte 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 169 ------LMMaawkvapaLAAGCSVVVKP---ASLTPITAI-LLNEICHEAGVPEGVVNTVAGAGSVVGDYLVGHEDVNKV 238
Cdd:PRK15398 145 tiinnaISM--------LAAGNSVVFSPhpgAKKVSLRAIeLLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4512364 239 AFTGstpiGKDIMEKASHTLKRVTLELGGKSPNLVFADADMEAAVAGSLFGIYFNTGQSCEARSRLFVHEEIYDEFIEEF 318
Cdd:PRK15398 217 VVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLM 292
|
|
| |
