|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
14-502 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 858.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 14 KISLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKL 93
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 94 IEEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLA 173
Cdd:cd07144 81 VEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQ-GKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 174 MACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSV 253
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 254 LEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWDVA 333
Cdd:cd07144 240 MKAAAQ-NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 334 gkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKE-EKLDMFQTSEFPiGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVV 412
Cdd:cd07144 319 ---SPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEgAKLVYGGEKAPE-GLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 413 VVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNY 492
Cdd:cd07144 395 VISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETY 474
|
490
....*....|
gi 6323821 493 LQIKSVHVDL 502
Cdd:cd07144 475 TQTKAVHINL 484
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-500 |
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: 691.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 19 QPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWS-KTSSEQRGIYLSNLLKLIEEE 97
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWrKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 98 QDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACR 177
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQ-GKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 178 KMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEAS 257
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 258 GQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfD 337
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR--VVG--D 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 338 PFDEKCIVGPVISSTQYDRIKSYIERGKKeEKLDMFQTSEFPigGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKF 417
Cdd:cd07091 317 PFDPDTFQGPQVSKAQFDKILSYIESGKK-EGATLLTGGERH--GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 418 TNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKS 497
Cdd:cd07091 394 KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
...
gi 6323821 498 VHV 500
Cdd:cd07091 474 VTI 476
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
18-502 |
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: 610.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 18 KQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEE 97
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP-AWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 98 QDTLAALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMAC 176
Cdd:COG1012 82 REELAALLTLETGKPL-AEARGEVDRAADFLRYYAGEARRLY-GETIPSDApGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 177 RKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEA 256
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 257 SGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkf 336
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKAL--KVG-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKKE--------EKLDmfqtsefpigGAKGYFIPPTIFTDVPETSKLLRDEIF 408
Cdd:COG1012 315 DPLDPGTDMGPLISEAQLERVLAYIEDAVAEgaelltggRRPD----------GEGGYFVEPTVLADVTPDMRIAREEIF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 409 GPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQ-EEAKVPFGGFKMSGIGRESGDT 487
Cdd:COG1012 385 GPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGRE 464
|
490
....*....|....*
gi 6323821 488 GVDNYLQIKSVHVDL 502
Cdd:COG1012 465 GLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
32-498 |
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: 603.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 32 SSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGK 111
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP-AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 112 PFhSNAKQDLAQIIELTRYYAGAVDKFnMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVII 191
Cdd:pfam00171 82 PL-AEARGEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 192 KPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGG 271
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 272 KSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDEKCIVGPVISS 351
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVG---DPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 352 TQYDRIKSYIERGKKEekldmfqTSEFPIGG----AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLA 427
Cdd:pfam00171 315 AQLERVLKYVEDAKEE-------GAKLLTGGeaglDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323821 428 NDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQ--TNQEEAkVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:pfam00171 388 NDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDytTGDADG-LPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
23-500 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 589.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAF--DNVWSKTSSEQRGIYLSNLLKLIEEEQDT 100
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklGSPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 101 LAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKfNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQ 180
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADK-IHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 181 GALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQS 260
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 261 NLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFD 340
Cdd:cd07141 248 NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR--VVG--NPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 341 EKCIVGPVISSTQYDRIKSYIERGKKEekldmfqTSEFPIGGA----KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSK 416
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKE-------GAKLECGGKrhgdKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 417 FTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIK 496
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
....
gi 6323821 497 SVHV 500
Cdd:cd07141 477 TVTI 480
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-502 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 579.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 15 ISLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWS-KTSSEQRGIYLSNLLKL 93
Cdd:cd07143 1 GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGlKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 94 IEEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKfNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLA 173
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADK-IHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 174 MACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSV 253
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 254 LEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewDVA 333
Cdd:cd07143 240 MEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK--LKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 334 GkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEekldmfqTSEFPIGGA----KGYFIPPTIFTDVPETSKLLRDEIFG 409
Cdd:cd07143 318 G--DPFAEDTFQGPQVSQIQYERIMSYIESGKAE-------GATVETGGKrhgnEGYFIEPTIFTDVTEDMKIVKEEIFG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 410 PVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGV 489
Cdd:cd07143 389 PVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYAL 468
|
490
....*....|...
gi 6323821 490 DNYLQIKSVHVDL 502
Cdd:cd07143 469 ENYTQIKAVHINL 481
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-498 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 563.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 35 GKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAF-DNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPF 113
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 114 HSNAKQDLAQIIELTRYYAGAVDKFnMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKP 193
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKV-YGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 194 AENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSNLKDITLECGGKS 273
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 274 PALVFEDA-DLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAkKEWDVAgkfDPFDEKCIVGPVISST 352
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAA-REWKPG---DPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIERGKKEE-KLDMFQTSEFPIGGakGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:cd07112 316 HFDKVLGYIESGKAEGaRLVAGGKRVLTETG--GFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-498 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 537.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAK 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 119 QdLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENT 197
Cdd:cd07114 81 Q-VRYLAEWYRYYAGLADKIE-GAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 198 SLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALV 277
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 278 FEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRI 357
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAI--RVG--DPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 358 KSYIERGKKEEkldmfqtSEFPIGGA--------KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLAND 429
Cdd:cd07114 314 ERYVARAREEG-------ARVLTGGErpsgadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAND 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 430 TCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07114 387 SEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-500 |
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: 532.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 61 DKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnAKQDLAQIIELTRYYAGAVDKfNM 140
Cdd:cd07078 1 DAAVAAARAAFKA-WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE-ALGEVARAADTFRYYAGLARR-LH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 141 GETIPLTFNKF-AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVN 219
Cdd:cd07078 78 GEVIPSPDPGElAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 220 VIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSG 299
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 300 QICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEfp 379
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKAL--KVG--NPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKR-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 380 IGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVW 459
Cdd:cd07078 311 LEGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVW 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6323821 460 INQTN-QEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07078 391 INDYSvGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
19-498 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 524.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 19 QPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEE 97
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 98 QDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACR 177
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIH-GMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 178 KMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEAS 257
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 258 GQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfD 337
Cdd:cd07142 241 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALK-RVVG---D 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 338 PFDEKCIVGPVISSTQYDRIKSYIERGKKE-EKLdmfQTSEFPIgGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSK 416
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEgATL---ITGGDRI-GSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 417 FTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIK 496
Cdd:cd07142 393 FKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
..
gi 6323821 497 SV 498
Cdd:cd07142 473 AV 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-498 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 524.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 8 IEIPQLKISlkqplGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIY 86
Cdd:PLN02766 13 VKVPEIKFT-----KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgPWPRMSGFERGRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 87 LSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIV 166
Cdd:PLN02766 88 MMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIH-GETLKMSRQLQGYTLKEPIGVVGHII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 167 PWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGS 246
Cdd:PLN02766 167 PWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 247 TKVGGSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETA 326
Cdd:PLN02766 247 TEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 327 KKeWDVAgkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKldMFQTSEFPIgGAKGYFIPPTIFTDVPETSKLLRDE 406
Cdd:PLN02766 327 KD-WVVG---DPFDPRARQGPQVDKQQFEKILSYIEHGKREGA--TLLTGGKPC-GDKGYYIEPTIFTDVTEDMKIAQDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 407 IFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGD 486
Cdd:PLN02766 400 IFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGM 479
|
490
....*....|..
gi 6323821 487 TGVDNYLQIKSV 498
Cdd:PLN02766 480 DALDKYLQVKSV 491
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-503 |
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: 522.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKfNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:cd07119 81 RLETLNTGKTL-RESEIDIDDVANCFRYYAGLATK-ETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNL 262
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA-GNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEK 342
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKI--KLG--NGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 343 CIVGPVISSTQYDRIKSYIERGKKEEkldmfqtSEFPIGG--------AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVV 414
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEG-------ARLVCGGkrptgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 415 SKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQ 494
Cdd:cd07119 387 ERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQE 466
|
....*....
gi 6323821 495 IKSVHVDLS 503
Cdd:cd07119 467 TKHININLS 475
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
40-502 |
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: 518.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEqRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQ 119
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAE-RGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIE-GEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASgQSNLKDITLECGGKSPALVFE 279
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGA-AGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKS 359
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSL--RPG--DPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 360 YIERGKKE-EKLDMFQTSEfpigGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAV 438
Cdd:cd07115 314 YVDVGREEgARLLTGGKRP----GARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323821 439 FTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHVDL 502
Cdd:cd07115 390 WTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-500 |
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: 517.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQ 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG-WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07093 80 DIPRAAANFRFFADYILQLD-GESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALVFE 279
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDEKCIVGPVISSTQYDRIKS 359
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKA-LKVG---DPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 360 YIERGKKEEkldmfqtSEFPIGG--------AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:cd07093 314 YVELARAEG-------ATILTGGgrpelpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
41-498 |
5.79e-175 |
|
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: 499.84 E-value: 5.79e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQD 120
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPL-TQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKFnMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLS 200
Cdd:cd07109 81 VEAAARYFEYYGGAADKL-HGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 201 LLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFED 280
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 281 ADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKkewdvAGKFDPFDEKCIVGPVISSTQYDRIKSY 360
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFR-----ALRVGPGLEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 361 IERGKKEEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFT 440
Cdd:cd07109 314 VARARARGARIVAGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323821 441 KDVKKAHMFARDIKAGTVWINqtNQEEA---KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVN--NYGAGggiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-498 |
8.71e-169 |
|
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: 484.55 E-value: 8.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnAKQ 119
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDE-AAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKF--NMGETIPLTFNKF-AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAEN 196
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLdaKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 197 TSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPAL 276
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 277 VFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDEKCIVGPVISSTQYDR 356
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEA-IRVG---DPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 357 IKSYIERGkKEEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLAS 436
Cdd:cd07110 314 VLSFIARG-KEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323821 437 AVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07110 393 AVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
10-498 |
1.65e-168 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 486.62 E-value: 1.65e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 10 IPQLKISLKQplgLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLS 88
Cdd:PLN02466 50 TPPVQVSYTQ---LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgPWPKMTAYERSRILL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 89 NLLKLIEEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPW 168
Cdd:PLN02466 127 RFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIH-GLTVPADGPHHVQTLHEPIGVAGQIIPW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 169 NYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTK 248
Cdd:PLN02466 206 NFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 249 VGGSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKK 328
Cdd:PLN02466 286 TGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 329 EwdVAGkfDPFDEKCIVGPVISSTQYDRIKSYIERGkkeekldMFQTSEFPIGG----AKGYFIPPTIFTDVPETSKLLR 404
Cdd:PLN02466 366 R--VVG--DPFKKGVEQGPQIDSEQFEKILRYIKSG-------VESGATLECGGdrfgSKGYYIQPTVFSNVQDDMLIAQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 405 DEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRES 484
Cdd:PLN02466 435 DEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREK 514
|
490
....*....|....
gi 6323821 485 GDTGVDNYLQIKSV 498
Cdd:PLN02466 515 GIYSLNNYLQVKAV 528
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-502 |
2.19e-167 |
|
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: 481.84 E-value: 2.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 22 GLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT-WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVdKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVI-RAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsN 261
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDA-----DLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkf 336
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI--KVG-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKKEekldmfqTSEFPIGG--------AKGYFIPPTIFTDVPETSKLLRDEIF 408
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEE-------GAEVLTGGerltlgglDKGYFYEPTLIKGGNNDMRIFQEEIF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 409 GPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTG 488
Cdd:cd07559 387 GPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMM 466
|
490
....*....|....
gi 6323821 489 VDNYLQIKSVHVDL 502
Cdd:cd07559 467 LDHYQQTKNILVSY 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
23-503 |
4.37e-166 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 478.61 E-value: 4.37e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK-IWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFHSNAKQDL---AQIIEltrYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKM 179
Cdd:PRK13252 88 ALETLDTGKPIQETSVVDIvtgADVLE---YYAGLAPALE-GEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 180 QGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVLEASGQ 259
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 260 SnLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPF 339
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI--RIG--DPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 340 DEKCIVGPVISSTQYDRIKSYIERGKKE--------EKLDmfqtsefPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPV 411
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEgarllcggERLT-------EGGFANGAFVAPTVFTDCTDDMTIVREEIFGPV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 412 VVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDN 491
Cdd:PRK13252 391 MSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEH 470
|
490
....*....|..
gi 6323821 492 YLQIKSVHVDLS 503
Cdd:PRK13252 471 YTQIKSVQVEMG 482
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-499 |
2.53e-162 |
|
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: 468.14 E-value: 2.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA-WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFH-SNAKQDLAQIIELtRYYAGAVDKFNMGETIPLTFnkfayTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07138 80 QAITLEMGAPITlARAAQVGLGIGHL-RAAADALKDFEFEERRGNSL-----VVREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSn 261
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAkKEWDVAgkfDPFDE 341
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAA-EAYVVG---DPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKE---------EKldmfqtsefPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVV 412
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEgarlvaggpGR---------PEGLERGYFVKPTVFADVTPDMTIAREEIFGPVL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 413 VVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQeEAKVPFGGFKMSGIGRESGDTGVDNY 492
Cdd:cd07138 380 SIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF-NPGAPFGGYKQSGNGREWGRYGLEEF 458
|
....*..
gi 6323821 493 LQIKSVH 499
Cdd:cd07138 459 LEVKSIQ 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
23-503 |
3.60e-161 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 465.54 E-value: 3.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFcPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:PRK13473 5 LLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE-WSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFN---MGETIPltfnkfAYTLKV---PFGVVAQIVPWNYPLAMAC 176
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEgkaAGEYLE------GHTSMIrrdPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 177 RKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEA 256
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 257 SGqSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkf 336
Cdd:PRK13473 236 AA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL--KVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEFPigGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSK 416
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAP--DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 417 FTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIK 496
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
....*..
gi 6323821 497 SVHVDLS 503
Cdd:PRK13473 469 HVMVKHT 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-503 |
1.18e-159 |
|
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: 461.00 E-value: 1.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnAKQ 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ-KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEE-ARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLS-GEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAGFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALVFE 279
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKS 359
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKI--RIG--DPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 360 YIERGKKE--EKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASA 437
Cdd:cd07090 312 YIESAKQEgaKVLCGGERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323821 438 VFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHVDLS 503
Cdd:cd07090 392 VFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-496 |
3.94e-158 |
|
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: 457.73 E-value: 3.94e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ-GEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGAL 183
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPALN-GEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 184 AAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLK 263
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 264 DITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKC 343
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERI--KLG--DPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 344 IVGPVISSTQYDRIKSYIERGKKEekldmfqTSEFPIGGA--------KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVS 415
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAE-------GATLATGGGrpenvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 416 KFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQI 495
Cdd:TIGR01804 387 TFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEV 466
|
.
gi 6323821 496 K 496
Cdd:TIGR01804 467 K 467
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
41-500 |
3.79e-157 |
|
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: 454.58 E-value: 3.79e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQD 120
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK-TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPL-AEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKFnMGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07103 80 VDYAASFLEWFAEEARRI-YGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALVFE 279
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKS 359
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKL--KVG--NGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 360 YIE--RGKKEEKLdmfqtsefpIGG----AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYG 433
Cdd:cd07103 314 LVEdaVAKGAKVL---------TGGkrlgLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 434 LASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
41-500 |
4.03e-156 |
|
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: 451.78 E-value: 4.03e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQD 120
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS-WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGA---VDKFNMGETIPltfNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENT 197
Cdd:cd07092 81 LPGAVDNFRFFAGAartLEGPAAGEYLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 198 SLSLLYFATLIKKaGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALV 277
Cdd:cd07092 158 PLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 278 FEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRI 357
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAI--RVG--DPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 358 KSYIERGKKEEKLdmfqTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASA 437
Cdd:cd07092 312 AGFVERAPAHARV----LTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323821 438 VFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
43-500 |
6.08e-156 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 451.41 E-value: 6.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 43 PATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQDL 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPI-SQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 122 AQIIELTRYYAGAV-----DKF-NMGEtipltfNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE 195
Cdd:cd07118 83 EGAADLWRYAASLArtlhgDSYnNLGD------DMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 196 NTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPA 275
Cdd:cd07118 157 FTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 276 LVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdvagKF-DPFDEKCIVGPVISSTQY 354
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKV-----RVgDPLDPETKVGAIINEAQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 355 DRIKSYIERGKKEekldmfqTSEFPIGG-----AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLAND 429
Cdd:cd07118 311 AKITDYVDAGRAE-------GATLLLGGerlasAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALAND 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323821 430 TCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07118 384 TVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-500 |
4.13e-155 |
|
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: 450.10 E-value: 4.13e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsN 261
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDE 341
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL--KVG--DPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKEEKlDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYD 421
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGA-RLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 422 DALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAkVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-498 |
8.96e-155 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 450.34 E-value: 8.96e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 22 GLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN----VWSKTSSEQRGIYLSNLLKLIEEE 97
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 98 QDTLAALETLDAGKPFhSNAKQDLAQIIELTRYYAG---AVDKFNmGETIPLTFNKFA-YTLKVPFGVVAQIVPWNYPLA 173
Cdd:PLN02467 89 KSELAKLETLDCGKPL-DEAAWDMDDVAGCFEYYADlaeALDAKQ-KAPVSLPMETFKgYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 174 MACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSV 253
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 254 LEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVA 333
Cdd:PLN02467 247 MTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN-IKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 334 gkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEfPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVV 413
Cdd:PLN02467 325 ---DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR-PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 414 VSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYL 493
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
....*
gi 6323821 494 QIKSV 498
Cdd:PLN02467 481 SVKQV 485
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
41-500 |
4.37e-153 |
|
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: 443.89 E-value: 4.37e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNAKQD 120
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKP-LAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKfnmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLS 200
Cdd:cd07106 80 VGGAVAWLRYTASLDLP---DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 201 LLYFATLIKKAgFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALVFED 280
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 281 ADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKSY 360
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAA--VVG--DGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 361 IERGKKeekldmfQTSEFPIGGA----KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLAS 436
Cdd:cd07106 310 VEDAKA-------KGAKVLAGGEpldgPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323821 437 AVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07106 383 SVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
23-502 |
6.31e-152 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 442.80 E-value: 6.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFnMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKV-YGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSN 261
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDA-DLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAkKEWDVAgkfDPFD 340
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQA-QNWQPG---HPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 341 EKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTSEFPIGGAKGyfipPTIFTDVPETSKLLRDEIFGPVVVVSKFTNY 420
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQL-LLDGRNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 421 DDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:PRK09847 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
..
gi 6323821 501 DL 502
Cdd:PRK09847 492 SL 493
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-502 |
2.81e-151 |
|
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: 440.35 E-value: 2.81e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 22 GLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAF-KTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVdKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVI-RAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsN 261
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewdvAGKFDPFDE 341
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN----VKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKEEkldmfqtSEFPIGG--------AKGYFIPPTIFTDVPETSKLLRDEIFGPVVV 413
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEG-------AKILTGGhrltenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVAT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 414 VSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYL 493
Cdd:cd07117 387 VIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
....*....
gi 6323821 494 QIKSVHVDL 502
Cdd:cd07117 467 QMKNIYIDL 475
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-501 |
4.84e-151 |
|
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: 440.39 E-value: 4.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 16 SLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSKTSSEQRGIYLSNLLKLI 94
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 95 EEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLT----FNKFAYTLKVPFGVVAQIVPWNY 170
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQ-GKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 171 PLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVG 250
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 251 GSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEw 330
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 331 dvagKF-DPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEFPIggaKGYFIPPTIFTDVPETSKLLRDEIFG 409
Cdd:cd07140 319 ----KIgDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR---PGFFFEPTVFTDVEDHMFIAKEESFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 410 PVVVVSKFTN--YDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDT 487
Cdd:cd07140 392 PIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEE 471
|
490
....*....|....
gi 6323821 488 GVDNYLQIKSVHVD 501
Cdd:cd07140 472 ALNEYLKTKTVTIE 485
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-500 |
7.53e-151 |
|
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: 439.01 E-value: 7.53e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQ-KAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPfHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:cd07088 80 LIVEEQGKT-LSLARVEVEFTADYIDYMAEWARRIE-GEIIPSDRpNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNL 262
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdvagKF-DPFDE 341
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAV-----KVgDPFDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKE-EKLdmfQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNY 420
Cdd:cd07088 312 ATDMGPLVNEAALDKVEEMVERAVEAgATL---LTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 421 DDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07088 389 DEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-500 |
1.86e-150 |
|
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: 437.56 E-value: 1.86e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQ 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE-WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELK-GETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFE 279
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGI-FFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIK 358
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKL--KIG--DPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 359 SYIERGKKEEKLDMFQTSEFPIGG--AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLAS 436
Cdd:cd07108 313 GYIDLGLSTSGATVLRGGPLPGEGplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323821 437 AVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRE-SGDTGVDNYLQIKSVHV 500
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-500 |
1.59e-149 |
|
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: 432.04 E-value: 1.59e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 65 KAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNAKQDLAQIIELTRYYAGAVDKFnMGETI 144
Cdd:cd06534 1 AAARAAFKA-WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKL-GGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 145 PLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPG 223
Cdd:cd06534 78 PSPDpGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 224 YGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICT 303
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 304 ANSRVYVQSSIYDKFVEKFKetakkewdvagkfdpfdekcivgpvisstqydriksyiergkkeekldmfqtsefpigga 383
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 384 kgyfippTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQT 463
Cdd:cd06534 257 -------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDS 329
|
410 420 430
....*....|....*....|....*....|....*...
gi 6323821 464 N-QEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd06534 330 SiGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
41-500 |
1.07e-147 |
|
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: 430.90 E-value: 1.07e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDN-VWSkTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQ 119
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTgDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTL----KVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE 195
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 196 NTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPA 275
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 276 LVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDEKCIVGPVISSTQYD 355
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEA-LPVG---DPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 356 RIKSYIERGKKEE-KLdmFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGL 434
Cdd:cd07089 316 RVEGYIARGRDEGaRL--VTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323821 435 ASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-500 |
8.96e-147 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 428.98 E-value: 8.96e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKtiETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA-WRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFnMGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07097 81 RLLTREEGKTL-PEARGEVTRAGQIFRYYAGEALRL-SGETLPSTRpGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSN 261
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDE 341
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA-LKVG---DALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKE--------EKLDmfqtsefpiGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVV 413
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEgaklvyggERLK---------RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 414 VSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQ-TNQEEAKVPFGGFKMSGIG-RESGDTGVDN 491
Cdd:cd07097 385 VIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLpTAGVDYHVPFGGRKGSSYGpREQGEAALEF 464
|
....*....
gi 6323821 492 YLQIKSVHV 500
Cdd:cd07097 465 YTTIKTVYV 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
16-499 |
4.37e-146 |
|
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: 427.58 E-value: 4.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 16 SLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIE 95
Cdd:cd07111 17 AHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES-WSALPGHVRARHLYRIARHIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 96 EEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKfnMGETIPltfnkfAYTlkvPFGVVAQIVPWNYPLAMA 175
Cdd:cd07111 96 KHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL--LDTELA------GWK---PVGVVGQIVPWNFPLLML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 176 CRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVLE 255
Cdd:cd07111 165 AWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 256 ASGQSNlKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAkkewdvaGK 335
Cdd:cd07111 244 ATAGTG-KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERM-------SH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 336 F---DPFDEKCIVGPVISSTQYDRIKSYIERGKKEeKLDMFQTSEFPigGAKGYFIPPTIFTDVPETSKLLRDEIFGPVV 412
Cdd:cd07111 316 LrvgDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE-GADVFQPGADL--PSKGPFYPPTLFTNVPPASRIAQEEIFGPVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 413 VVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNY 492
Cdd:cd07111 393 VVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
....*..
gi 6323821 493 LQIKSVH 499
Cdd:cd07111 473 LRPSWEP 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-503 |
7.87e-145 |
|
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: 424.07 E-value: 7.87e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATG-EPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFP-EWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFnMGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07131 81 RLVTREMGKPL-AEGRGDVQEAIDMAQYAAGEGRRL-FGETVPSELpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSN 261
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 lKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDE 341
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRL--RVG--DGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEFPIGG-AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNY 420
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 421 DDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIG-RESGDTGVDNYLQIKSV 498
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
....*
gi 6323821 499 HVDLS 503
Cdd:cd07131 474 YVDYS 478
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
23-498 |
1.74e-143 |
|
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: 422.02 E-value: 1.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEfcPSSDGKTIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT-WRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKvPFGVVAQIVPWNYPLAMACRKMQG 181
Cdd:cd07124 112 AAWMVLEVGKNW-AEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEAS---- 257
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAakvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 258 -GQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkf 336
Cdd:cd07124 270 pGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKAL--KVG-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdmFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSK 416
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 417 FTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV---PFGGFKMSGIGRESGdtGVD--- 490
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANR-KITGALVgrqPFGGFKMSGTGSKAG--GPDyll 500
|
....*...
gi 6323821 491 NYLQIKSV 498
Cdd:cd07124 501 QFMQPKTV 508
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-500 |
8.72e-139 |
|
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: 408.75 E-value: 8.72e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 22 GLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTFNKF------AYTLKVPFGVVAQIVPWNYPLAMA 175
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKIN-GETLAPSIPSMqgerytAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 176 CRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVlE 255
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKI-G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 256 ASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKeTAKKEWDVAgk 335
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLK-QALSSFQVG-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 336 fDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEkldmfqtSEFPIGG----AKGYFIPPTIFTDVPETSKLLRDEIFGPV 411
Cdd:cd07113 315 -SPMDESVMFGPLANQPHFDKVCSYLDDARAEG-------DEIVRGGealaGEGYFVQPTLVLARSADSRLMREETFGPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 412 VVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDN 491
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDD 466
|
....*....
gi 6323821 492 YLQIKSVHV 500
Cdd:cd07113 467 YTELKSVMI 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-502 |
5.94e-137 |
|
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: 403.29 E-value: 5.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQ 119
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE-WRATTPLERARMLRELATRLREHAEELALIDALDCGNPV-SAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVDKFNmGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELK-GETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSnLKDITLECGGKSPALVFE 279
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 280 DADLDKAIEWVANGIFFN-SGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIK 358
Cdd:cd07107 236 DADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAI--KVG--DPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 359 SYIERGKKEEKLDMF-----QTSEFpiggAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYG 433
Cdd:cd07107 312 HYIDSAKREGARLVTgggrpEGPAL----EGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 434 LASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHVDL 502
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-483 |
1.11e-131 |
|
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: 389.65 E-value: 1.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNA 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK-EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIElTRYYAGAVDKFNMGETIPL-----TFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIK 192
Cdd:cd07149 79 RKEVDRAIE-TLRLSAEEAKRLAGETIPFdaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 PAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqsnLKDITLECGGK 272
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 273 SPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISST 352
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKL--VVG--DPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIergkkEEKLDmfqtsefpiGGAK--------GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDAL 424
Cdd:cd07149 311 EAERIEEWV-----EEAVE---------GGARlltggkrdGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 425 KLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKV-PFGGFKMSGIGRE 483
Cdd:cd07149 377 AMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGRE 436
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
42-500 |
3.12e-131 |
|
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: 388.61 E-value: 3.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 42 NPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQDL 121
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA-WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTY-GKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 122 AQIIELTRYYAGAVDKFNmGETIPLTFN-KFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLS 200
Cdd:cd07150 83 TFTPELLRAAAGECRRVR-GETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 201 LLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFED 280
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 281 ADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewdvAGKFDPFDEKCIVGPVISSTQYDRIKSY 360
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK----LKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 361 IERG-KKEEKLdmfqtsefpIGGAK--GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASA 437
Cdd:cd07150 317 VEDAvAKGAKL---------LTGGKydGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323821 438 VFTKDVKKAHMFARDIKAGTVWINQ-TNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDpTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-500 |
2.07e-130 |
|
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: 385.73 E-value: 2.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 59 DVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNAKQDLAQIIELTRYYAGAVDKF 138
Cdd:cd07104 1 DVDRAYAAAAAAQKA-WAATPPQERAAILRKAAEILEERRDEIADWLIRESGST-RPKAAFEVGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 139 NmGETIPLTFN-KFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSL-LYFATLIKKAGFPPG 216
Cdd:cd07104 79 E-GEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 217 VVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFF 296
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 297 NSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEekldmfqTS 376
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKAL--PVG--DPRDPDTVIGPLINERQVDRVHAIVEDAVAA-------GA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 377 EFPIGG-AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKA 455
Cdd:cd07104 306 RLLTGGtYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 6323821 456 GTVWIN-QTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07104 386 GMVHINdQTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-500 |
1.18e-129 |
|
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: 385.27 E-value: 1.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA-WGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFHSNAKQDLAQIIELTRYYAGAVdKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGAL 183
Cdd:cd07116 83 AETWDNGKPVRETLAADIPLAIDHFRYFAGCI-RAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 184 AAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLK 263
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 264 DITLECGGKSPALVFE------DADLDKAIEWVAngIF-FNSGQICTANSRVYVQSSIYDKFVEKFKETAKkewdVAGKF 336
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGFV--MFaLNQGEVCTCPSRALIQESIYDRFMERALERVK----AIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKKE--EKLDMFQTSEFPIGGAKGYFIPPTIFTDvpETSKLLRDEIFGPVVVV 414
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEgaEVLTGGERNELGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 415 SKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQ 494
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
....*.
gi 6323821 495 IKSVHV 500
Cdd:cd07116 472 TKNLLV 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-484 |
1.72e-127 |
|
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: 379.00 E-value: 1.72e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnA 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD-VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIELTRYYAGAVDKFNmGETIPL-----TFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIK 192
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLR-GETIPVdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 PAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGK 272
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 273 SPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPFDEKCIVGPVISST 352
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK-LKVG---DPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIERGKKEekldmfqTSEFPIGGAK--GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDT 430
Cdd:cd07145 313 AVERMENLVNDAVEK-------GGKILYGGKRdeGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANST 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 6323821 431 CYGLASAVFTKDVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRES 484
Cdd:cd07145 386 EYGLQASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-500 |
7.18e-126 |
|
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: 374.76 E-value: 7.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQ 119
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKIL-GEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYAGAVdKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSL 199
Cdd:cd07120 80 EISGAISELRYYAGLA-RTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 200 SLLYFATLIKKA-GFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEAsGQSNLKDITLECGGKSPALVF 278
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAA-AAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 279 EDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKkewdvAGKFDP-FDEKCIVGPVISSTQYDRI 357
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLA-----AVKVGPgLDPASDMGPLIDRANVDRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 358 KSYIERGKKEEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASA 437
Cdd:cd07120 313 DRMVERAIAAGAEVVLRGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323821 438 VFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
24-498 |
3.21e-124 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 372.10 E-value: 3.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF-PSWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:PLN02278 107 LMTLEQGKPL-KEAIGEVAYGASFLEYFAEEAKRVY-GDIIPSPFpDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSnL 262
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEK 342
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKL--VVG--DGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 343 CIVGPVISSTQYDRIKSYIERGkkeekldMFQTSEFPIGGAK----GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFT 418
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDA-------VSKGAKVLLGGKRhslgGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 419 NYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-500 |
4.97e-123 |
|
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: 367.78 E-value: 4.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 27 NEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALET 106
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 107 LDAGKPfHSNAKQDLAQIIELTRYYAGAVDKFNmGETIP-LTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAA 185
Cdd:cd07151 80 RESGST-RIKANIEWGAAMAITREAATFPLRME-GRILPsDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 186 GNTVIIKPAENTSLS--LLyFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLK 263
Cdd:cd07151 158 GNAVVLKPASDTPITggLL-LAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 264 DITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKC 343
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKAL--PYG--DPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 344 IVGPVISSTQYDRIKSYIERGKKEEKLDMFQtsefpiGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDA 423
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVG------GEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 424 LKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07151 386 LELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-503 |
9.96e-121 |
|
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: 362.65 E-value: 9.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSdGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK-EWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:cd07086 80 LVSLEMGKIL-PEGLGEVQEMIDICDYAVGLSRMLY-GLTIPSERpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKA----GFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVLEASG 258
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 259 QSNLKDItLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewdVA-GkfD 337
Cdd:cd07086 237 RRFGRVL-LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ---VRiG--D 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 338 PFDEKCIVGPVISSTQYDRIKSYIERGKKE--------EKLDmfqtsefpiGGAKGYFIPPTIFTDVPETSKLLRDEIFG 409
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQggtvltggKRID---------GGEPGNYVEPTIVTGVTDDARIVQEETFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 410 PVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARD--IKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRESGD 486
Cdd:cd07086 382 PILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGS 461
|
490
....*....|....*..
gi 6323821 487 TGVDNYLQIKSVHVDLS 503
Cdd:cd07086 462 DAWKQYMRRSTCTINYS 478
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
36-498 |
1.52e-117 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 355.40 E-value: 1.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 36 KTIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFh 114
Cdd:PRK03137 50 DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET-WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPW- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 115 SNAKQDLAQIIELTRYYAGAVDKFNMGETI---PLTFNKFAYTlkvPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVII 191
Cdd:PRK03137 128 AEADADTAEAIDFLEYYARQMLKLADGKPVesrPGEHNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 192 KPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEAS-----GQSNLKDIT 266
Cdd:PRK03137 205 KPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAakvqpGQIWLKRVI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 267 LECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPfDEKCIVG 346
Cdd:PRK03137 285 AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE-LTVG---NP-EDNAYMG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 347 PVISSTQYDRIKSYIERGKKEEKLDMFQTSefpiGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKL 426
Cdd:PRK03137 360 PVINQASFDKIMSYIEIGKEEGRLVLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEI 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 427 ANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV---PFGGFKMSGIGRESGdtGVD---NYLQIKSV 498
Cdd:PRK03137 436 ANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNR-GCTGAIVgyhPFGGFNMSGTDSKAG--GPDyllLFLQAKTV 510
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-498 |
3.78e-114 |
|
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: 344.80 E-value: 3.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNA 117
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAEN-RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPI-KDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIELTRYyAGAVDKFNMGETIPL-----TFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIK 192
Cdd:cd07094 79 RVEVDRAIDTLRL-AAEEAERIRGEEIPLdatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 PAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqsnLKDITLECGGK 272
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 273 SPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISST 352
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKL--KVG--DPLDEDTDVGPLISEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIERGKKEekldmfqTSEFPIGGA-KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:cd07094 311 AAERVERWVEEAVEA-------GARLLCGGErDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTD 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAK-VPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07094 384 YGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-498 |
1.20e-112 |
|
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: 340.74 E-value: 1.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnAKQD 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ-RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRAD-AGLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKFNMGETIP---LTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENT 197
Cdd:cd07099 79 VLLALEAIDWAARNAPRVLAPRKVPtglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 198 SLSLLYFATLIKKAGFPPGVVNVIPGYGSVvGKALGTHMdIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALV 277
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 278 FEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRI 357
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARAL--RPG--ADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 358 KSYIE----RGKKeekldmfqtseFPIGGA----KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLAND 429
Cdd:cd07099 312 RRHVDdavaKGAK-----------ALTGGArsngGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALAND 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323821 430 TCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07099 381 SRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-498 |
1.24e-112 |
|
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: 339.94 E-value: 1.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 59 DVDKAVKAARAAFdNVWSKTS-SEQRGIyLSNLLKLIEEEQDTLAALETLDAGKPFHSnAKQDLAQIIELTRYYAGAVDK 137
Cdd:cd07105 1 DADQAVEAAAAAF-PAWSKTPpSERRDI-LLKAADLLESRRDEFIEAMMEETGATAAW-AGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 138 FnMGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPG 216
Cdd:cd07105 78 I-IGGSIPSDKpGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 217 VVNVI---PGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANG 293
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 294 IFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdvagkfdpFDEKCIVGPVISSTQYDRIKSYIERG-KKEEKLDM 372
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL---------FAGPVVLGSLVSAAAADRVKELVDDAlSKGAKLVV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 373 FQTSEFPIGGAkgyFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARD 452
Cdd:cd07105 307 GGLADESPSGT---SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 6323821 453 IKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07105 384 IESGAVHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-500 |
5.44e-110 |
|
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: 333.27 E-value: 5.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 60 VDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhsnaKQDLAQI---IELTRYYAGAVD 136
Cdd:cd07100 1 IEAALDRAHAAFLA-WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPI----AEARAEVekcAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 137 KFNMGETIPlTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPG 216
Cdd:cd07100 76 AFLADEPIE-TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 217 VVNVIPGYGSVVGKALGtHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFF 296
Cdd:cd07100 155 VFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 297 NSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKE--------E 368
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAAL--KVG--DPMDEDTDLGPLARKDLRDELHEQVEEAVAAgatlllggK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 369 KLDmfqtsefpiggAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHM 448
Cdd:cd07100 309 RPD-----------GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAER 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6323821 449 FARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07100 378 VARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-498 |
1.77e-107 |
|
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: 328.32 E-value: 1.77e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 21 LGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDT 100
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA-WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 101 LAALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFnMGETIP-LTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKM 179
Cdd:cd07085 80 LARLITLEHGKTL-ADARGDVLRGLEVVEFACSIPHLL-KGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 180 QGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVgKALGTHMDIDKISFTGSTKVGGSVLEaSGQ 259
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYE-RAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 260 SNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAGKFDP- 338
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKK-LKVGAGDDPg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 339 FDekciVGPVISSTQYDRIKSYIERGKKE-EKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKF 417
Cdd:cd07085 315 AD----MGPVISPAAKERIEGLIESGVEEgAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 418 TNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINqtnqeeakVP---------FGGFKMS--GIGRESGD 486
Cdd:cd07085 391 DTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSffGDLHFYGK 462
|
490
....*....|..
gi 6323821 487 TGVDNYLQIKSV 498
Cdd:cd07085 463 DGVRFYTQTKTV 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
41-499 |
1.79e-105 |
|
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: 322.27 E-value: 1.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQD 120
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK-GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPI-AQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLS 200
Cdd:cd07102 79 IRGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 201 LLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHmDIDKISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALVFED 280
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 281 ADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKkewdvAGKF-DPFDEKCIVGPVISSTQYDRIKS 359
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVK-----GYKLgDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 360 YIERGKKEEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVF 439
Cdd:cd07102 312 QIADAIAKGARALIDGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 440 TKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVH 499
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYH 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
17-498 |
3.32e-105 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 323.74 E-value: 3.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 17 LKQPLG----LFINNEFCpSSDGKtIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLL 91
Cdd:TIGR01237 25 VKEQLGktypLVINGERV-ETENK-IVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA-WKKTDPEERAAILFKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 92 KLIEEEQDTLAALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNMGE---TIPLTFNKFAYTlkvPFGVVAQIVPW 168
Cdd:TIGR01237 102 AIVRRRRHEFSALLVKEVGKPW-NEADAEVAEAIDFMEYYARQMIELAKGKpvnSREGETNQYVYT---PTGVTVVISPW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 169 NYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTK 248
Cdd:TIGR01237 178 NFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSRE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 249 VGGSVLEAS-----GQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFK 323
Cdd:TIGR01237 258 VGTRIFERAakvqpGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 324 ETAKKEwdVAGKFDPFDEKciVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEfpigGAKGYFIPPTIFTDVPETSKLL 403
Cdd:TIGR01237 338 EITESL--KVGPPDSADVY--VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGD----DSKGYFIGPTIFADVDRKARLA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 404 RDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQ--TNQEEAKVPFGGFKMSGIG 481
Cdd:TIGR01237 410 QEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRniTGAIVGYQPFGGFKMSGTD 489
|
490 500
....*....|....*....|
gi 6323821 482 RESGdtGVD---NYLQIKSV 498
Cdd:TIGR01237 490 SKAG--GPDylaLFMQAKTV 507
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-498 |
8.47e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 322.98 E-value: 8.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 31 PSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFHSnAKQDLAQIIELTRYYAGAVDKF----NMGETIPLtFNKfAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAG 186
Cdd:PRK09407 106 KARRH-AFEEVLDVALTARYYARRAPKLlaprRRAGALPV-LTK-TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 187 NTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHmdIDKISFTGSTKVGGSVLEASGqSNLKDIT 266
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RRLIGFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 267 LECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKEtAKKEWDVAGKFDpFDEKciVG 346
Cdd:PRK09407 260 LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVA-AVRAMRLGAGYD-YSAD--MG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 347 PVISSTQYDRIKSYIERGKkeekldmfqtsefpiggAKG---------------YFIPPTIFTDVPETSKLLRDEIFGPV 411
Cdd:PRK09407 336 SLISEAQLETVSAHVDDAV-----------------AKGatvlaggkarpdlgpLFYEPTVLTGVTPDMELAREETFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 412 VVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINqtnqeEA--------KVPFGGFKMSGIGRE 483
Cdd:PRK09407 399 VSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN-----EGyaaawgsvDAPMGGMKDSGLGRR 473
|
490
....*....|....*
gi 6323821 484 SGDTGVDNYLQIKSV 498
Cdd:PRK09407 474 HGAEGLLKYTESQTI 488
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
24-487 |
3.65e-104 |
|
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: 319.90 E-value: 3.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCpSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:cd07082 5 LINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPfHSNAKQDLAQIIELTRYYAGAVDK----FNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKM 179
Cdd:cd07082 84 LLMWEIGKT-LKDALKEVDRTIDYIRDTIEELKRldgdSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 180 QGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGq 259
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 260 snLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWDVAgkfDPF 339
Cdd:cd07082 242 --MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAK-LKVG---MPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 340 DEKCIVGPVISSTQYDRIKSYIERGKKEEKldmfqTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTN 419
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGA-----TVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 420 YDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKV-PFGGFKMSGIGRES-GDT 487
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGiGDA 460
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
43-498 |
2.80e-101 |
|
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: 311.55 E-value: 2.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 43 PATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNAKQDLA 122
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRA-WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKA-RRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 123 QIIELTRYYAGAVDKF----NMGETIP-LTFNKFAYTlkvPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENT 197
Cdd:cd07101 81 DVAIVARYYARRAERLlkprRRRGAIPvLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 198 SLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIdkISFTGSTKVGGSVLEASGqSNLKDITLECGGKSPALV 277
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 278 FEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWDVAGkfdpFDEKCIVGPVISSTQYDRI 357
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAA----LDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 358 KSYIE--RGKKEEKLdmfqtsefpIGGAK----G-YFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDT 430
Cdd:cd07101 311 TAHVDdaVAKGATVL---------AGGRArpdlGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323821 431 CYGLASAVFTKDVKKAHMFARDIKAGTVWINQ---TNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07101 382 DYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyaAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-483 |
9.70e-101 |
|
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: 310.33 E-value: 9.70e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVwSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNA 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPM-RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPI-KDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIELTRYYAGAVDKFNmGETIPLTFN-----KFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIK 192
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIY-GEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 PAENTSLSLLYFATLIKKAGFPPGVVNVIPgYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsnlKDITLECGGK 272
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 273 SPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISST 352
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKAL--KTG--DPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIErgkkeEKLDmfQTSEFPIGGA-KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:cd07147 310 EAERVEGWVN-----EAVD--AGAKLLTGGKrDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEA-KVPFGGFKMSGIGRE 483
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGRE 435
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-501 |
1.11e-98 |
|
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: 305.38 E-value: 1.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 41 VNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQD 120
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE-WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 121 LAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKV---PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENT 197
Cdd:cd07098 80 ILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVeyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 198 SLSLLYFATLIKKA----GFPPGVVNVIPGYGSVvGKALGTHMDIDKISFTGSTKVGGSVLEASGQSnLKDITLECGGKS 273
Cdd:cd07098 160 AWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 274 PALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWDVAGKFDPFDekciVGPVISSTQ 353
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVD----VGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 354 YDRIKSYI-ERGKKEEKL----DMFQTSEFPiggaKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLAN 428
Cdd:cd07098 314 FDRLEELVaDAVEKGARLlaggKRYPHPEYP----QGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323821 429 DTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQ--TNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHVD 501
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDfgVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-496 |
1.45e-98 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 305.68 E-value: 1.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP-AWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFnMGETIP-LTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:PRK11241 93 LMTLEQGKPL-AEAKGEISYAASFIEWFAEEGKRI-YGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNL 262
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewdvAGKFDPFDEK 342
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK----LHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 343 CIVGPVISSTQYDRIKSYIErgkkeeklDMFQTSEFPIGGAK-----GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKF 417
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIA--------DALEKGARVVCGGKahelgGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 418 TNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIK 496
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
46-494 |
4.45e-94 |
|
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: 292.66 E-value: 4.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 46 GEPITSFQAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQDLAQII 125
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA-QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 126 ELtrYYAGAVDKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSL-LYF 204
Cdd:cd07152 80 EL--HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 205 ATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLD 284
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 285 KAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRI----KSY 360
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHL--PVG--DPATGQVALGPLINARQLDRVhaivDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 361 IERGKKEEkldmfqtsefpIGG-AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVF 439
Cdd:cd07152 312 VAAGARLE-----------AGGtYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGII 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 440 TKDVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIG-RESGDTGVDNYLQ 494
Cdd:cd07152 381 SRDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-500 |
2.32e-93 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 289.71 E-value: 2.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 87 LSNLLKLIEEEQDTLAALETLDAGKPfhsnakQDLAQI------------IELTRYYAGAV---DKFNmgETIpltfnkf 151
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKI------QQLAEVevaftadyidymAEWARRYEGEIiqsDRPG--ENI------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 152 aYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKA 231
Cdd:PRK10090 66 -LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 232 LGTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQ 311
Cdd:PRK10090 145 LAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 312 SSIYDKFVEKFKETAKkewdvAGKF-DPFDEKCI-VGPVISSTQYDRIKSYIERGKKeekldmfQTSEFPIGG----AKG 385
Cdd:PRK10090 224 KGIYDQFVNRLGEAMQ-----AVQFgNPAERNDIaMGPLINAAALERVEQKVARAVE-------EGARVALGGkaveGKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 386 YFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQ 465
Cdd:PRK10090 292 YYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENF 371
|
410 420 430
....*....|....*....|....*....|....*
gi 6323821 466 EEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:PRK10090 372 EAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYL 406
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
38-485 |
5.23e-93 |
|
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: 290.41 E-value: 5.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARaafdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfHSNA 117
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAA----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLC-LKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIELTRYYAGAVDKFNmGETIP--LTFN---KFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIK 192
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDD-GESFScdLTANgkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 PAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGqsnLKDITLECGGK 272
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 273 SPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKeWdVAGkfDPFDEKCIVGPVISST 352
Cdd:cd07146 232 DPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAA-L-VVG--DPMDPATDMGTVIDEE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 353 QYDRIKSYIERGKKeekldmfQTSEFPIGGAK-GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:cd07146 308 AAIQIENRVEEAIA-------QGARVLLGNQRqGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAK-VPFGGFKMSGIGRESG 485
Cdd:cd07146 381 YGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEG 435
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-498 |
6.84e-88 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 277.39 E-value: 6.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSnA 117
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRD-YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KQDLAQIIELTRYYAGAVDKFNMGET--IPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE 195
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEPadAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 196 NTSLSLLYFATLIKKAGFPPGV-VNVIPGYGSVvgKALGTHMDIDKISFTGSTKVGGSVLEASGQSnLKDITLECGGKSP 274
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCfQTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 275 ALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFkeTAKKEWDVAGkfDPFDEKCIVGPVISSTQY 354
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKF--VARMAALRVG--DPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 355 DRIKSYIERGKKeekldmfQTSEFPIGGAK----GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDT 430
Cdd:PRK09406 314 DEVEKQVDDAVA-------AGATILCGGKRpdgpGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANAT 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 431 CYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
24-494 |
1.11e-84 |
|
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: 270.61 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIetVNPATGE-PITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLA 102
Cdd:cd07125 36 IINGEETETGEGAPV--IDPADHErTIGEVSLADAEDVDAALAIAAAAFAG-WSATPVEERAEILEKAADLLEANRGELI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 103 ALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:cd07125 113 ALAAAEAGKTL-ADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSNL 262
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITL--ECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKEtAKKEWDVAgkfDPFD 340
Cdd:cd07125 272 PILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKG-AMASLKVG---DPWD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 341 EKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTsefPIGGAKGYFIPPTIFTDVpeTSKLLRDEIFGPVVVVSKF--T 418
Cdd:cd07125 348 LSTDVGPLIDKPAGKLLRAHTELMRGEAWL-IAPA---PLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFkaE 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 419 NYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV---PFGGFKMSGIGRESGdtGvDNYLQ 494
Cdd:cd07125 422 DLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NITGAIVgrqPFGGWGLSGTGPKAG--G-PNYLL 496
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
23-485 |
4.32e-82 |
|
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: 263.67 E-value: 4.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 23 LFINNEFCPSSDGKTIetVNP-ATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:cd07083 21 LVIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKT-WKDWPQEDRARLLLKAADLLRRRRREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNMGETI----PLTFNKFAYtlkVPFGVVAQIVPWNYPLAMACR 177
Cdd:cd07083 98 IATLTYEVGKNW-VEAIDDVAEAIDFIRYYARAALRLRYPAVEvvpyPGEDNESFY---VGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 178 KMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEA- 256
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 257 ----SGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdV 332
Cdd:cd07083 254 arlaPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL--S 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 333 AGkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdmfqtsefpIGGAK-----GYFIPPTIFTDVPETSKLLRDEI 407
Cdd:cd07083 332 VG--PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQL---------VLGGKrlegeGYFVAPTVVEEVPPKARIAQEEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 408 FGPV--VVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV---PFGGFKMSGIGR 482
Cdd:cd07083 401 FGPVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR-KITGALVgvqPFGGFKLSGTNA 479
|
...
gi 6323821 483 ESG 485
Cdd:cd07083 480 KTG 482
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
63-500 |
1.22e-75 |
|
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: 244.36 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 63 AVKAARAAFDNvwSKTSS-EQRGIYLSNLLKLIEE-EQDTLAALETlDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNM 140
Cdd:cd07087 3 LVARLRETFLT--GKTRSlEWRKAQLKALKRMLTEnEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 141 GETIPLTFNKF---AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE---NTSlSLLyfATLIKKAgFP 214
Cdd:cd07087 80 PRRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSElapATS-ALL--AKLIPKY-FD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 215 PGVVNVIPGyGSVVGKALGTHmDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGI 294
Cdd:cd07087 156 PEAVAVVEG-GVEVATALLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 295 FFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWdvaGKfDPFDEKCIvGPVISSTQYDRIKSYIERGKkeekldmfq 374
Cdd:cd07087 233 FLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFY---GE-DPKESPDY-GRIINERHFDRLASLLDDGK--------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 375 tseFPIGG---AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFAR 451
Cdd:cd07087 299 ---VVIGGqvdKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 6323821 452 DIKAGTVWINQT-----NQEeakVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV 500
Cdd:cd07087 376 ETSSGGVCVNDVllhaaIPN---LPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-498 |
1.76e-72 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 237.45 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 40 TVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNAKQ 119
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD-WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPI-NQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 120 DLAQIIELTRYYA--GAVdkfnMGETIP-LTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAEN 196
Cdd:PRK13968 89 EVAKSANLCDWYAehGPA----MLKAEPtLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 197 TSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMdIDKISFTGSTKVGGSVLEASGQSnLKDITLECGGKSPAL 276
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 277 VFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKkewdvAGKF-DPFDEKCIVGPVISSTQYD 355
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAA-----ALKMgDPRDEENALGPMARFDLRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 356 RIKSYIERGKKEekldmfqTSEFPIGGAK----GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTC 431
Cdd:PRK13968 318 ELHHQVEATLAE-------GARLLLGGEKiagaGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 432 YGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
24-503 |
1.36e-68 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 228.10 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPfHSNAKQDLAQIIELTRYYAG------AVDKFNMGETIPLT-FNKFAYTLKVPFGVVAQIVPWNYPLAMAC 176
Cdd:PLN00412 98 CLVKEIAKP-AKDAVTEVVRSGDLISYTAEegvrilGEGKFLVSDSFPGNeRNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 177 RKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGstkvGGSVLEA 256
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG----GDTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 257 SGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdvagKF 336
Cdd:PLN00412 253 SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL-----TV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 DPFDEKCIVGPVISSTQYDRIKSYIERGKkeEKLDMFQTSEfpigGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSK 416
Cdd:PLN00412 328 GPPEDDCDITPVVSESSANFIEGLVMDAK--EKGATFCQEW----KREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 417 FTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVwinQTNQEEAK----VPFGGFKMSGIGRESGDTGVDNY 492
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTV---QINSAPARgpdhFPFQGLKDSGIGSQGITNSINMM 478
|
490
....*....|.
gi 6323821 493 LQIKSVHVDLS 503
Cdd:PLN00412 479 TKVKSTVINLP 489
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-481 |
4.26e-68 |
|
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: 225.76 E-value: 4.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 38 IETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFhSNA 117
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPL-VDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 118 KqdlaqiIELTRYYAG---AVDKFNM--GETIPLTF-----NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGN 187
Cdd:cd07148 80 K------VEVTRAIDGvelAADELGQlgGREIPMGLtpasaGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 188 TVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVleasgQSNLKDIT- 266
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLAPGTr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 267 --LECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCI 344
Cdd:cd07148 228 caLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKL--VVG--DPTDPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 345 VGPVISSTQYDRIKSYIErgkkeekldmfqtsEFPIGGAK----GYFI-----PPTIFTDVPETSKLLRDEIFGPVVVVS 415
Cdd:cd07148 304 VGPLIRPREVDRVEEWVN--------------EAVAAGARllcgGKRLsdttyAPTVLLDPPRDAKVSTQEIFGPVVCVY 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 416 KFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIG 481
Cdd:cd07148 370 SYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
35-485 |
5.36e-68 |
|
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: 225.93 E-value: 5.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 35 GKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGiylsNLLKLIEEE----QDTLAALETLDAG 110
Cdd:cd07130 11 GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAF-KEWRDVPAPKRG----EIVRQIGDAlrkkKEALGKLVSLEMG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFhSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTV 189
Cdd:cd07130 86 KIL-PEGLGEVQEMIDICDFAVGLSRQLY-GLTIPSERpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 190 IIKPAENTSLSLL----YFATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASgQSNLKDI 265
Cdd:cd07130 164 VWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV-AARFGRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 266 TLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKeTAKKEWDVAgkfDPFDEKCIV 345
Cdd:cd07130 242 LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLK-KAYKQVRIG---DPLDDGTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 346 GPVISSTQYDRIKSYIERGKKeekldmfQTSEFPIGG----AKGYFIPPTIFTdVPETSKLLRDEIFGPVVVVSKFTNYD 421
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKS-------QGGTVLFGGkvidGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323821 422 DALKLANDTCYGLASAVFTKDVKKAHMF--ARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRESG 485
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNiGTSGAEIGGAFGGEKETGGGRESG 456
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
58-498 |
1.41e-65 |
|
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: 218.24 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 58 KDVDKAVKAARAAFDNvwSKTSS-EQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFH-------SNAKQDLAQIIEltr 129
Cdd:cd07135 5 DEIDSIHSRLRATFRS--GKTKDlEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFetlltevSGVKNDILHMLK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 130 yyagAVDKFNMGETI--PLTFNKF--AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFA 205
Cdd:cd07135 80 ----NLKKWAKDEKVkdGPLAFMFgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 206 TLIKKAgFPPGVVNVIPGYGSVVGKALGTHMDidKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDK 285
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 286 AIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWdvAGKFDPFDEkciVGPVISSTQYDRIKSYIE--R 363
Cdd:cd07135 232 AAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFY--PGGANASPD---YTRIVNPRHFNRLKSLLDttK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 364 GKKEekldmfqtsefpIGG---AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFT 440
Cdd:cd07135 307 GKVV------------IGGemdEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323821 441 KDVK-KAHMFARdIKAGTVWINQTNQEEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07135 375 DDKSeIDHILTR-TRSGGVVINDTLIHVGvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-484 |
1.95e-63 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 214.05 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 22 GLFINNEFCPSSdGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTL 101
Cdd:PRK09457 2 TLWINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA-WARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 102 AALETLDAGKPFHSNAKQDLAQI----IELTRYYA--GAVDKFNMGETIPLTFNkfaytlkvPFGVVAQIVPWNYPLAMA 175
Cdd:PRK09457 80 AEVIARETGKPLWEAATEVTAMInkiaISIQAYHErtGEKRSEMADGAAVLRHR--------PHGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 176 CRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKvGGSVL- 254
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSAN-TGYLLh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 255 -EASGQSNlKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIY-DKFVEKFKETAKKEwdV 332
Cdd:PRK09457 230 rQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL--T 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 333 AGKFD----PFdekciVGPVISSTQYDRI---KSYIERGKKEEKLDMFQTSEfpiGGAkgyFIPPTIFtDVPETSKLLRD 405
Cdd:PRK09457 307 VGRWDaepqPF-----MGAVISEQAAQGLvaaQAQLLALGGKSLLEMTQLQA---GTG---LLTPGII-DVTGVAELPDE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 406 EIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTV-WINQTNQEEAKVPFGGFKMSGIGRES 484
Cdd:PRK09457 375 EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-499 |
2.26e-63 |
|
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: 213.13 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 152 AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE---NTSlSLLyfATLIKKAgFPPGVVNVIPGyGSVV 228
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSEltpNTS-KVI--AKIIEET-FDEEYVAVVEG-GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 229 GKALgTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRV 308
Cdd:cd07136 169 NQEL-LDQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 309 YVQSSIYDKFVEKFKETAKKEWdvaGKfDPFDEKcIVGPVISSTQYDRIKSYIERGKKEekldmfqtsefpIGG---AKG 385
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFY---GE-DPLESP-DYGRIINEKHFDRLAGLLDNGKIV------------FGGntdRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 386 YFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQ 465
Cdd:cd07136 310 LYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIM 389
|
330 340 350
....*....|....*....|....*....|....*.
gi 6323821 466 EEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSVH 499
Cdd:cd07136 390 HLAnpYLPFGGVGNSGMGSYHGKYSFDTFSHKKSIL 425
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
59-485 |
5.39e-63 |
|
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: 211.36 E-value: 5.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 59 DVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPF---HSNAKQDLAQI-IELTRY--YA 132
Cdd:cd07095 1 QVDAAVAAARAAFPG-WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaQTEVAAMAGKIdISIKAYheRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 133 GAVDKfNMGETIPLTFNKfaytlkvPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAG 212
Cdd:cd07095 80 GERAT-PMAQGRAVLRHR-------PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 213 FPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVAN 292
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 293 GIFFNSGQICTANSRVYV-QSSIYDKFVEKFKETAKKEwdVAGkfDPFDEKCIVGPVISSTQYDRIKSYIER-----GKK 366
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRL--RIG--APDAEPPFMGPLIIAAAAARYLLAQQDllalgGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 367 EEKLDMFQtsefpiggAKGYFIPPTIFtDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKA 446
Cdd:cd07095 307 LLAMERLV--------AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALF 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 6323821 447 HMFARDIKAGTV-WINQTNQEEAKVPFGGFKMSGIGRESG 485
Cdd:cd07095 378 ERFLARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHRPSA 417
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
75-488 |
1.54e-62 |
|
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: 210.16 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 75 WSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfhsNAKQDLAQIIELTRYYAGAVDKFN--MG----ETIPLTF 148
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP---AAEVDLTEILPVLSEINHAIKHLKkwMKpkrvRTPLLLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 149 NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGyGSVV 228
Cdd:cd07134 91 GTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 229 GKALgTHMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRV 308
Cdd:cd07134 169 AQAL-LELPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 309 YVQSSIYDKFVEKFKETAKKewdVAGKFDPFDEKCIVGPVISSTQYDRIKSYIERGKKeekldmfQTSEFPIGG---AKG 385
Cdd:cd07134 247 FVHESVKDAFVEHLKAEIEK---FYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVA-------KGAKVEFGGqfdAAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 386 YFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQ 465
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL 396
|
410 420
....*....|....*....|....*
gi 6323821 466 EEA--KVPFGGFKMSGIGRESGDTG 488
Cdd:cd07134 397 HFLnpNLPFGGVNNSGIGSYHGVYG 421
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
54-498 |
3.24e-61 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 208.34 E-value: 3.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 54 AANEKDVDKAVKAARAAFDNVWSKtSSEQRGIYLSNLLKLIEE-EQDTLAALEtLDAGKPFHSNAKQDLAQIIELTRYYA 132
Cdd:PTZ00381 3 PDNPEIIPPIVKKLKESFLTGKTR-PLEFRKQQLRNLLRMLEEnKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIEHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 133 GAVDKFNMGETIPLTF-NKFA--YTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE---NTSlSLLYfaT 206
Cdd:PTZ00381 81 KHLDEYLKPEKVDTVGvFGPGksYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSElspHTS-KLMA--K 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 207 LIKKAgFPPGVVNVIPGyGSVVGKALGTHmDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKA 286
Cdd:PTZ00381 158 LLTKY-LDPSYVRVIEG-GVEVTTELLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 287 IEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWdvaGKfDPFDEKCiVGPVISSTQYDRIKSYIERGKk 366
Cdd:PTZ00381 234 ARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFF---GE-DPKKSED-YSRIVNEFHTKRLAELIKDHG- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 367 eekldmfqtSEFPIGG---AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDV 443
Cdd:PTZ00381 308 ---------GKVVYGGevdIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDK 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 444 KKAHMFARDIKAGTVWINQ-----TNQEeakVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PTZ00381 379 RHKELVLENTSSGAVVINDcvfhlLNPN---LPFGGVGNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
158-482 |
4.10e-61 |
|
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: 206.57 E-value: 4.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 158 PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTS-LSLLyFATLIKKAgFPPGVVNVIPGyGSVVGKALgTHM 236
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-GADVAAAF-SSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 237 DIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYD 316
Cdd:cd07133 177 PFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 317 KFVEKFKETAKKEW-DVAGKFDpfdekciVGPVISSTQYDRIKSYIE--RGKKEEKLDMFQTSEFPIGGAKgyfIPPTIF 393
Cdd:cd07133 256 EFVAAAKAAVAKMYpTLADNPD-------YTSIINERHYARLQGLLEdaRAKGARVIELNPAGEDFAATRK---LPPTLV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 394 TDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQT----NQEEAk 469
Cdd:cd07133 326 LNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTllhvAQDDL- 404
|
330
....*....|...
gi 6323821 470 vPFGGFKMSGIGR 482
Cdd:cd07133 405 -PFGGVGASGMGA 416
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
32-481 |
1.10e-58 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 209.67 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 32 SSDGKTIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAF-PAWSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFhsnakQD-LAQI---IELTRYYAG-AVDKFNMGETIP--------LTFNkfaytlkvPFGVVAQIVPWNYPLAMACR 177
Cdd:PRK11904 637 KTL-----QDaIAEVreaVDFCRYYAAqARRLFGAPEKLPgptgesneLRLH--------GRGVFVCISPWNFPLAIFLG 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 178 KMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGS---VL 254
Cdd:PRK11904 704 QVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIinrTL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 255 EAsgqsnlKD---ITL--ECGGK------SPALvfedadldkaIEWVANGI----FFNSGQICTAnSRV-YVQSSIYDKF 318
Cdd:PRK11904 784 AA------RDgpiVPLiaETGGQnamivdSTAL----------PEQVVDDVvtsaFRSAGQRCSA-LRVlFVQEDIADRV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 319 VEKFKeTAKKEWDVAgkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTsEFPIGGAKGYFIPPTIFtdvpE 398
Cdd:PRK11904 847 IEMLK-GAMAELKVG---DPRLLSTDVGPVIDAEAKANLDAHIERMKREARL-LAQL-PLPAGTENGHFVAPTAF----E 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 399 TSKL--LRDEIFGPVVVVSKFTNYD-----DALklaNDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV- 470
Cdd:PRK11904 917 IDSIsqLEREVFGPILHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQIGAVVg 992
|
490
....*....|...
gi 6323821 471 --PFGGFKMSGIG 481
Cdd:PRK11904 993 vqPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-481 |
5.57e-58 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 207.80 E-value: 5.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 32 SSDGKTIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE-WSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFhSNAKQDLAQIIELTRYYA-GAVDKFNMGETIPLtfnkfaytlkvpfGVVAQIVPWNYPLAMACRKMQGALAAGNTV 189
Cdd:PRK11905 642 KTL-ANAIAEVREAVDFLRYYAaQARRLLNGPGHKPL-------------GPVVCISPWNFPLAIFTGQIAAALVAGNTV 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 190 IIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGsVLEASGQSNLKDITL-- 267
Cdd:PRK11905 708 LAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVAR-LIQRTLAKRSGPPVPli 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 268 -ECGGK------SPALVfEDADLDkaiewVANGIFFNSGQICTAnSRV-YVQSSIYDKFVEKFKeTAKKEWDVAgkfDPF 339
Cdd:PRK11905 787 aETGGQnamivdSSALP-EQVVAD-----VIASAFDSAGQRCSA-LRVlCLQEDVADRVLTMLK-GAMDELRIG---DPW 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 340 DEKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQtSEFPIGGAKGYFIPPTIFtdvpETSKL--LRDEIFGPVVVVSKF 417
Cdd:PRK11905 856 RLSTDVGPVIDAEAQANIEAHIEAMRAAGRL-VHQ-LPLPAETEKGTFVAPTLI----EIDSIsdLEREVFGPVLHVVRF 929
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 418 --TNYDDALKLANDTCYGLASAVFTK-DVKKAHMFARdIKAGTVWINQtNQEEAKV---PFGGFKMSGIG 481
Cdd:PRK11905 930 kaDELDRVIDDINATGYGLTFGLHSRiDETIAHVTSR-IRAGNIYVNR-NIIGAVVgvqPFGGEGLSGTG 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
31-485 |
1.12e-57 |
|
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: 199.37 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 31 PSSDGKTIETVNPATGEPITSF-QAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDA 109
Cdd:TIGR01238 46 YKADGEAQPVTNPADRRDIVGQvFHANLAHVQAAIDSAQQAFP-TWNATPAKERAAKLDRLADLLELHMPELMALCVREA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 110 GKPFHsNAKQDLAQIIELTRYYAGAVDKfnmgetiplTFNKFAYTlkvPFGVVAQIVPWNYPLAMACRKMQGALAAGNTV 189
Cdd:TIGR01238 125 GKTIH-NAIAEVREAVDFCRYYAKQVRD---------VLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAALAAGNTV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 190 IIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSNLKDITL-- 267
Cdd:TIGR01238 192 IAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLia 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 268 ECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKeTAKKEWDVAgkfDPFDEKCIVGP 347
Cdd:TIGR01238 272 ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQ-GAMQELKVG---VPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 348 VISSTQYDRIKSYIERGKKEEKLDMFQTSEFPIGGAKGYFIPPTIF--TDVPEtsklLRDEIFGPVVVVSKFT--NYDDA 423
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFelDDIAE----LSEEVFGPVLHVVRYKarELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323821 424 LKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQtNQEEAKV---PFGGFKMSGIGRESG 485
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQVGAVVgvqPFGGQGLSGTGPKAG 487
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-506 |
1.62e-55 |
|
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: 192.05 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 62 KAVKAARAAFDNvwSKTSS-EQRGIYLSNLLKLIEE-EQDTLAALEtLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFN 139
Cdd:cd07132 2 EAVRRAREAFSS--GKTRPlEFRIQQLEALLRMLEEnEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYAISNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 140 MGETIPLTF-NKF--AYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSlsllYFATLIKKagfppg 216
Cdd:cd07132 79 KPEPVKKNLaTLLddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----ATAKLLAE------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 217 vvnVIPGY------GSVVGKALGT----HMDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKA 286
Cdd:cd07132 149 ---LIPKYldkecyPVVLGGVEETtellKQRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 287 IEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAkKEW--DVAGKFDPFdekcivGPVISSTQYDRIKSYIERG 364
Cdd:cd07132 225 ARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTL-KEFygEDPKESPDY------GRIINDRHFQRLKKLLSGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 365 KkeekldmfqtseFPIGG---AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTK 441
Cdd:cd07132 298 K------------VAIGGqtdEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSN 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 442 DVKKAHMFARDIKAGTVWINQTNQEEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSVHV-DLSLDK 506
Cdd:cd07132 366 NKKVINKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVkSLNMEK 433
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
32-481 |
1.79e-55 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 200.55 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 32 SSDGKTIETVNPA-TGEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:COG4230 566 AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA-WSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFhSNAKQDLAQIIELTRYYAG-AVDKFNMGetipltfnkfayTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTV 189
Cdd:COG4230 645 KTL-PDAIAEVREAVDFCRYYAAqARRLFAAP------------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTV 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 190 IIKPAENTSLsLLYFAT-LIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVleasgQSNL-----K 263
Cdd:COG4230 712 LAKPAEQTPL-IAARAVrLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI-----NRTLaardgP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 264 DITL--ECGGK------SPALvfedadldkaIEWVANGIF---FNS-GQICTAnSRV-YVQSSIYDKFVEKFKEtAKKEW 330
Cdd:COG4230 786 IVPLiaETGGQnamivdSSAL----------PEQVVDDVLasaFDSaGQRCSA-LRVlCVQEDIADRVLEMLKG-AMAEL 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 331 DVAgkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTsEFPIGGAKGYFIPPTIFtdvpETSKL--LRDEIF 408
Cdd:COG4230 854 RVG---DPADLSTDVGPVIDAEARANLEAHIERMRAEGRL-VHQL-PLPEECANGTFVAPTLI----EIDSIsdLEREVF 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 409 GPVVVVSKFTNYD-----DALklaNDTCYGLASAVFTK-DVKKAHMFARdIKAGTVWINQtNQEEAKV---PFGGFKMSG 479
Cdd:COG4230 925 GPVLHVVRYKADEldkviDAI---NATGYGLTLGVHSRiDETIDRVAAR-ARVGNVYVNR-NIIGAVVgvqPFGGEGLSG 999
|
..
gi 6323821 480 IG 481
Cdd:COG4230 1000 TG 1001
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
35-479 |
4.29e-54 |
|
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: 190.11 E-value: 4.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 35 GKTIETVNPAT-GEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRG-IYLSNLLKLIEEEQDTLAALETLDAGKP 112
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARK-EWARMPFEDRAaIFLKAADLLSGKYRYELNAATMLGQGKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 113 FHsNAKQDLA-QIIELTRYYAGAVDKFNMGETI---PLTFNKFAYTlkvPF-GVVAQIVPWNYPlAMAcrkmqGALAA-- 185
Cdd:cd07123 124 VW-QAEIDAAcELIDFLRFNVKYAEELYAQQPLsspAGVWNRLEYR---PLeGFVYAVSPFNFT-AIG-----GNLAGap 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 186 ---GNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQS-- 260
Cdd:cd07123 194 almGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENld 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 261 ---NLKDITLECGGKSPALVFEDADldkaIEWVANGI----FFNSGQICTANSRVYVQSSIYDKFVEKFKETAK--KEWD 331
Cdd:cd07123 274 ryrTYPRIVGETGGKNFHLVHPSAD----VDSLVTATvrgaFEYQGQKCSAASRAYVPESLWPEVKERLLEELKeiKMGD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 332 VAgKFDPFdekciVGPVISSTQYDRIKSYIERGKKEEKLdmfqtsEFPIGG----AKGYFIPPTIF-TDVPeTSKLLRDE 406
Cdd:cd07123 350 PD-DFSNF-----MGAVIDEKAFDRIKGYIDHAKSDPEA------EIIAGGkcddSVGYFVEPTVIeTTDP-KHKLMTEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 407 IFGPVVVVSKF--TNYDDALKLANDTC-YGLASAVFTKD---VKKAHMFARDiKAGTVWINQ--TNQEEAKVPFGGFKMS 478
Cdd:cd07123 417 IFGPVLTVYVYpdSDFEETLELVDTTSpYALTGAIFAQDrkaIREATDALRN-AAGNFYINDkpTGAVVGQQPFGGARAS 495
|
.
gi 6323821 479 G 479
Cdd:cd07123 496 G 496
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-498 |
2.21e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 189.96 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 24 FINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAA 103
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP-LWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 104 LETLDAGKPFhSNAKQDLAQIIELTRYYAGaVDKFNMGETIPLTFNKF-AYTLKVPFGVVAQIVPWNYPLAMACRKMQGA 182
Cdd:PLN02419 196 NITTEQGKTL-KDSHGDIFRGLEVVEHACG-MATLQMGEYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 183 LAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVgKALGTHMDIDKISFTGSTKVGGSVLeASGQSNL 262
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIY-ARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 263 KDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYV---QSSIYDKFVEK---FKETAKKEWDVAgkf 336
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERakaLKVTCGSEPDAD--- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 337 dpfdekciVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEFPIGG-AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVS 415
Cdd:PLN02419 429 --------LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCM 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 416 KFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTnqeeAKVP-----FGGFKMSGIGRES--GDTG 488
Cdd:PLN02419 501 QANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVP----IPVPlpffsFTGNKASFAGDLNfyGKAG 576
|
490
....*....|
gi 6323821 489 VDNYLQIKSV 498
Cdd:PLN02419 577 VDFFTQIKLV 586
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-485 |
6.64e-53 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 187.30 E-value: 6.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 33 SDGKTIETVNPAT-GEPITSFQAANEKDVDKAVKAARAAFDNvWSKTSSEQRG-IYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:TIGR01236 43 DSNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKKD-WSNLPFYDRAaIFLKAADLLSGPYRYEILAATMLGQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFHSNAKQDLAQIIELTRYYAG-AVDKF-NMGETIPLTFNKFAYTlkvPF-GVVAQIVPWNYpLAMACrKMQGALA-AG 186
Cdd:TIGR01236 122 KTVYQAEIDAVAELIDFFRFNVKyARELYaQQPISAPGEWNRTEYR---PLeGFVYAISPFNF-TAIAG-NLAGAPAlMG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 187 NTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQS-----N 261
Cdd:TIGR01236 197 NTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNldryhN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 262 LKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYdkfvEKFKETAKKEWDVAGKFDPFDE 341
Cdd:TIGR01236 277 FPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKW----PEFKSDLLAELQSVKVGDPDDF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 342 KCIVGPVISSTQYDRIKSYIERGKKEekldmfqTSEFPI--GG----AKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVS 415
Cdd:TIGR01236 353 RGFMGAVIDEQSFDKIVKYIEDAKKD-------PEALTIlyGGkyddSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVY 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323821 416 KF--TNYDDALKLANDTC-YGLASAVFTKDvKKAHMFARDI---KAGTVWINQ--TNQEEAKVPFGGFKMSGIGRESG 485
Cdd:TIGR01236 426 VYpdDKYKEILDLVDSTSqYGLTGAVFAKD-RKAILEADKKlrfAAGNFYINDkcTGAVVGQQPFGGARMSGTNDKAG 502
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-498 |
2.00e-49 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 175.29 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 64 VKAARAAFDNVWSKtSSEQRGIYLSNLLKLI-EEEQDTLAALETlDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNMGE 142
Cdd:cd07137 5 VRELRETFRSGRTR-SAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 143 TIPLTFNKFAYTLKV---PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAE---NTSlSLLyfATLIKKAgFPPG 216
Cdd:cd07137 83 KVKTPLTTFPAKAEIvsePLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSElapATS-ALL--AKLIPEY-LDTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 217 VVNVIPGyGSVVGKALGTHmDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPALVFEDADLDKAIEWVANGIF- 295
Cdd:cd07137 159 AIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 296 FNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWdvaGKfDPFDEKCIvGPVISSTQYDRIKSYIERGKKEEKLDMfqt 375
Cdd:cd07137 236 CNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFF---GE-NPKESKDL-SRIVNSHHFQRLSRLLDDPSVADKIVH--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 376 sefpiGGA---KGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARD 452
Cdd:cd07137 308 -----GGErdeKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 6323821 453 IKAGTVWINQTNQEEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:cd07137 383 TSSGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
30-485 |
8.72e-44 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 166.30 E-value: 8.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 30 CPSSDGKTIETVNPATGEPITSF-QAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLD 108
Cdd:PRK11809 653 DPVAAGEMSPVINPADPRDIVGYvREATPAEVEQALESAVNA-APIWFATPPAERAAILERAADLMEAQMQTLMGLLVRE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 109 AGKPFhSNAKQDLAQIIELTRYYAGAV-DKFNMGETIPLtfnkfaytlkvpfGVVAQIVPWNYPLAMACRKMQGALAAGN 187
Cdd:PRK11809 732 AGKTF-SNAIAEVREAVDFLRYYAGQVrDDFDNDTHRPL-------------GPVVCISPWNFPLAIFTGQVAAALAAGN 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 188 TVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGG-------SVLEASGQS 260
Cdd:PRK11809 798 SVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARllqrnlaGRLDPQGRP 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 261 nlkdITL--ECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKEtAKKEWDVAgkfDP 338
Cdd:PRK11809 878 ----IPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRG-AMAECRMG---NP 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 339 FDEKCIVGPVISSTQYDRIKSYIE----RGKKEEKLDMFQTSEFpiggAKGYFIPPTI--FTDVPEtsklLRDEIFGPVV 412
Cdd:PRK11809 950 DRLSTDIGPVIDAEAKANIERHIQamraKGRPVFQAARENSEDW----QSGTFVPPTLieLDSFDE----LKREVFGPVL 1021
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323821 413 VVSKF--TNYDDALKLANDTCYGLASAVFTK-DVKKAHMFARdIKAGTVWINQtNQEEAKV---PFGGFKMSGIGRESG 485
Cdd:PRK11809 1022 HVVRYnrNQLDELIEQINASGYGLTLGVHTRiDETIAQVTGS-AHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAG 1098
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
21-494 |
1.85e-42 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 158.07 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 21 LGLFINNEFcpSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAfDNVWSKTSSEQRGIYLSNLLKLIEEEQDT 100
Cdd:PLN02315 21 LGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA-AKIWMQVPAPKRGEIVRQIGDALRAKLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 101 LAALETLDAGKPFhSNAKQDLAQIIELTRYYAGAVDKFNmGETIPLTF-NKFAYTLKVPFGVVAQIVPWNYPLAMACRKM 179
Cdd:PLN02315 98 LGRLVSLEMGKIL-AEGIGEVQEIIDMCDFAVGLSRQLN-GSIIPSERpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 180 QGALAAGNTVIIKPAENTSLSLL----YFATLIKKAGFPPGVVNVIPGyGSVVGKALGTHMDIDKISFTGSTKVGGSVLE 255
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 256 ASGQSNLKDItLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKewdvAGK 335
Cdd:PLN02315 255 TVNARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ----VKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 336 FDPFDEKCIVGPVISSTQYDRIKSYIERGKkeekldmFQTSEFPIGGA----KGYFIPPTIfTDVPETSKLLRDEIFGPV 411
Cdd:PLN02315 330 GDPLEKGTLLGPLHTPESKKNFEKGIEIIK-------SQGGKILTGGSaiesEGNFVQPTI-VEISPDADVVKEELFGPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 412 VVVSKFTNYDDALKLANDTCYGLASAVFTK--DVKKAHMFARDIKAGTVWIN-QTNQEEAKVPFGGFKMSGIGRESGDTG 488
Cdd:PLN02315 402 LYVMKFKTLEEAIEINNSVPQGLSSSIFTRnpETIFKWIGPLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDS 481
|
....*.
gi 6323821 489 VDNYLQ 494
Cdd:PLN02315 482 WKQYMR 487
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
147-498 |
4.45e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 134.40 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 147 TFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPgyGS 226
Cdd:PLN02174 101 TFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVE--GA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 227 VVGKALGTHMDIDKISFTGSTKVgGSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIF-FNSGQICTAN 305
Cdd:PLN02174 178 VTETTALLEQKWDKIFYTGSSKI-GRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 306 SRVYVQSSIYDKFVEKFKETAKKEWdvaGKfDPFDEKCIvGPVISSTQYDRIKSYIERGKKEEKLdmfqtsefPIGGAK- 384
Cdd:PLN02174 257 DYILTTKEYAPKVIDAMKKELETFY---GK-NPMESKDM-SRIVNSTHFDRLSKLLDEKEVSDKI--------VYGGEKd 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 385 --GYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQ 462
Cdd:PLN02174 324 reNLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVND 403
|
330 340 350
....*....|....*....|....*....|....*...
gi 6323821 463 TNQEEA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PLN02174 404 IAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
79-498 |
1.33e-33 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 132.93 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 79 SSEQRGIYLSNLLKLI-EEEQDTLAALETlDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKV 157
Cdd:PLN02203 26 SLEWRKSQLKGLLRLLkDNEEAIFKALHQ-DLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKAKLPLVAFPATAEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 158 ---PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAgFPPGVVNVIPGyGSVVGKALGT 234
Cdd:PLN02203 105 vpePLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 235 HmDIDKISFTGSTKVGGSVLEASGQsNLKDITLECGGKSPAlVFEDADLDKAIEWVANGIFFN-----SGQICTANSRVY 309
Cdd:PLN02203 183 H-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPC-IVDSLSSSRDTKVAVNRIVGGkwgscAGQACIAIDYVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 310 VQSSIYDKFVEKFKETAKKEWDVagkfDPFDEKCIvGPVISSTQYDRIKSYIErgkkeeklDMFQTSEFPIGG---AKGY 386
Cdd:PLN02203 260 VEERFAPILIELLKSTIKKFFGE----NPRESKSM-ARILNKKHFQRLSNLLK--------DPRVAASIVHGGsidEKKL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 387 FIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQE 466
Cdd:PLN02203 327 FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQ 406
|
410 420 430
....*....|....*....|....*....|....
gi 6323821 467 EA--KVPFGGFKMSGIGRESGDTGVDNYLQIKSV 498
Cdd:PLN02203 407 YAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-485 |
6.75e-33 |
|
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: 130.05 E-value: 6.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 60 VDKAVKAARAAFDNvWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKP--FHSNAKQDLAQIieltRYYAGAVDK 137
Cdd:cd07084 1 PERALLAADISTKA-ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmFAENICGDQVQL----RARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 138 FNM----GETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAG- 212
Cdd:cd07084 76 YRIphepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 213 FPPGVVNVIPGYGSvVGKALGTHMDIDKISFTGSTKVGGSVLeasgqSNLKD--ITLECGGKSPALVFEDADLDKAIEW- 289
Cdd:cd07084 156 LPPEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLA-----LDAKQarIYLELAGFNWKVLGPDAQAVDYVAWq 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 290 VANGIFFNSGQICTANSRVYV-QSSIYDKFVEKFKETAKKEwdvagkfdpFDEKCIVGPVISSTQYDRIksyIERGKKEE 368
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARR---------KLEDLLLGPVQTFTTLAMI---AHMENLLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 369 KLDMFQTSEFPIGGAK---GYFIPPTIFTDVPE---TSKLLRDEIFGPVVVVSKFTNYD--DALKLANDTCYGLASAVF- 439
Cdd:cd07084 298 SVLLFSGKELKNHSIPsiyGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQlaLVLELLERMHGSLTAAIYs 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6323821 440 TKDVKKAHMFARDIKAGTVWIN---QTNQEEAKVPFGGFKMSGIGRESG 485
Cdd:cd07084 378 NDPIFLQELIGNLWVAGRTYAIlrgRTGVAPNQNHGGGPAADPRGAGIG 426
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
35-442 |
3.23e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.86 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 35 GKTIETVNPATGEPITSFQAANeKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGkpfh 114
Cdd:PRK11903 18 GAGTPLFDPVTGEELVRVSATG-LDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 115 sNAKQDLAQIIE----LTRYYA------GAVDKFNMGETIPLTFNK--FAYTLKVPF-GVVAQIVPWNYPLAMACRKMQG 181
Cdd:PRK11903 93 -TTRNDSAVDIDggifTLGYYAklgaalGDARLLRDGEAVQLGKDPafQGQHVLVPTrGVALFINAFNFPAWGLWEKAAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 182 ALAAGNTVIIKPAENTSLSLLYFATLIKKAG-FPPGVVNVIPGYGSVVGKALGThmdIDKISFTGSTKVG------GSVL 254
Cdd:PRK11903 172 ALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQP---FDVVSFTGSAETAavlrshPAVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 255 EASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVAG 334
Cdd:PRK11903 249 QRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKT--TVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 335 kfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTSEFPIGGA---KGYFIPPTIF-TDVPETSKLLRD-EIFG 409
Cdd:PRK11903 327 --NPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEV-LFDGGGFALVDAdpaVAACVGPTLLgASDPDAATAVHDvEVFG 403
|
410 420 430
....*....|....*....|....*....|...
gi 6323821 410 PVVVVSKFTNYDDALKLANDTCYGLASAVFTKD 442
Cdd:PRK11903 404 PVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
31-494 |
1.54e-20 |
|
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: 94.64 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 31 PSSDGKTIetVNPATGEPITSFQAAnEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAG 110
Cdd:cd07128 12 GTGDGRTL--HDAVTGEVVARVSSE-GLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAATGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KpfHSNAKQDLAQIIELTRYYAGAVDKF-------NMGETIPLTFN-KFAYT-LKVPF-GVVAQIVPWNYPLAMACRKMQ 180
Cdd:cd07128 89 T--RRDSWIDIDGGIGTLFAYASLGRRElpnahflVEGDVEPLSKDgTFVGQhILTPRrGVAVHINAFNFPVWGMLEKFA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 181 GALAAGNTVIIKPAENTSLSLLYFATLIKKAG-FPPGVVNVIPGygsVVGKALGTHMDIDKISFTGSTKVGG------SV 253
Cdd:cd07128 167 PALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDVVAFTGSAATAAklrahpNI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 254 LEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEwdVA 333
Cdd:cd07128 244 VARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKV--VV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 334 GkfDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLdMFQTSEFP----IGGAKGYFIPPTIFT-DVPETSKLLRD-EI 407
Cdd:cd07128 322 G--DPRLEGVRMGPLVSREQREDVRAAVATLLAEAEV-VFGGPDRFevvgADAEKGAFFPPTLLLcDDPDAATAVHDvEA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 408 FGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKA--GTVWINqtNQEEAK------VPFGGFKMSG 479
Cdd:cd07128 399 FGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL--NRDSAKestghgSPLPQLVHGG 476
|
490 500
....*....|....*....|.
gi 6323821 480 IGRESGDT------GVDNYLQ 494
Cdd:cd07128 477 PGRAGGGEelgglrGVKHYMQ 497
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
158-458 |
1.93e-17 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 84.85 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 158 PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALgTHMD 237
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-LEAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 238 IDKISFTGSTKVGGSV-LEASGQSNLKDITLECGGKSPALVFEDadldkAIEWVAN-GIFFNSGQICTANSRVYVQSSIY 315
Cdd:cd07126 221 PRMTLFTGSSKVAERLaLELHGKVKLEDAGFDWKILGPDVSDVD-----YVAWQCDqDAYACSGQKCSAQSILFAHENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 316 DK-FVEKFKETAKKEwdvagKFdpfdEKCIVGPVISSTQyDRIKSYIergkkeEKLDMFQTSEFPIGGAK---------- 384
Cdd:cd07126 296 QAgILDKLKALAEQR-----KL----EDLTIGPVLTWTT-ERILDHV------DKLLAIPGAKVLFGGKPltnhsipsiy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 385 GYFIPPTIF-----TDVPETSKLLRDEIFGPVVVVSKFTnyDDALKLANDTC----YGLASAVFTKDVkkahMFARDIKA 455
Cdd:cd07126 360 GAYEPTAVFvpleeIAIEENFELVTTEVFGPFQVVTEYK--DEQLPLVLEALermhAHLTAAVVSNDI----RFLQEVLA 433
|
...
gi 6323821 456 GTV 458
Cdd:cd07126 434 NTV 436
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
60-428 |
2.81e-15 |
|
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: 77.97 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 60 VDKAVKAARAAFDnVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPfhsnakqdLAQII-ELTR--------- 129
Cdd:cd07129 1 VDAAAAAAAAAFE-SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP--------EARLQgELGRttgqlrlfa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 130 ------YYAGAV--DKFNMGETIP---LTFnkfaytLKVPFGVVAQIVPWNYPLAMAcrkMQG-----ALAAGNTVIIK- 192
Cdd:cd07129 72 dlvregSWLDARidPADPDRQPLPrpdLRR------MLVPLGPVAVFGASNFPLAFS---VAGgdtasALAAGCPVVVKa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 193 ----PAentsLSLLyFATLIKKA----GFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKvGGSVLEASGQSNLKD 264
Cdd:cd07129 143 hpahPG----TSEL-VARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRR-GGRALFDAAAARPEP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 265 IT--LECGGKSPALVFEDADLDKAIEWV---ANGIFFNSGQICTANSRVYV-QSSIYDKFVEKFKETAKKewdvagkfdp 338
Cdd:cd07129 217 IPfyAELGSVNPVFILPGALAERGEAIAqgfVGSLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAA---------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 339 FDEKCIVGPVISSTQYDRiksyIERGKKEEKLDMFQTSEFPIGGAKGyfiPPTIFT---DVPETSKLLRDEIFGPVVVVS 415
Cdd:cd07129 287 APAQTMLTPGIAEAYRQG----VEALAAAPGVRVLAGGAAAEGGNQA---APTLFKvdaAAFLADPALQEEVFGPASLVV 359
|
410
....*....|...
gi 6323821 416 KFTNYDDALKLAN 428
Cdd:cd07129 360 RYDDAAELLAVAE 372
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
79-323 |
4.61e-15 |
|
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: 76.88 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 79 SSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNA----------KQDLAQIIELTRYYAGAVDKfNMGETIPLTF 148
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIanwiammgcsESKLYKNIDTERGITASVGH-IQDVLLPDNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 149 NkfAYTLKVPFGVVAQIVPWNYPLAmACRKMQGALAAGNTVIIKP-----AENTSLSLLYFATLikKAGFPPGVVNVIPG 223
Cdd:cd07077 93 E--TYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPhpsapFTNRALALLFQAAD--AAHGPKILVLYVPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 224 YGSVVGKALGTHMDIDKISFTGSTKVggsVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNsGQICT 303
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACA 243
|
250 260
....*....|....*....|
gi 6323821 304 ANSRVYVQSSIYDKFVEKFK 323
Cdd:cd07077 244 SEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
158-461 |
3.69e-13 |
|
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: 71.14 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 158 PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIK----KAGFPPGVVNVIPGYGSVVGKALG 233
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLqaavAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 234 THMDIDKISFTGstkvGGSVLEASGQSNLKDITLEcGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSS 313
Cdd:cd07081 175 KFPGIGLLLATG----GPAVVKAAYSSGKPAIGVG-AGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 314 IYDKFVEKFKETAkkewdvagkfdpfdekcivGPVISSTQYDRIKSYIERGKKEEKlDMFQTSEFPIGGAKGYFIPPTIF 393
Cdd:cd07081 250 VYDEVMRLFEGQG-------------------AYKLTAEELQQVQPVILKNGDVNR-DIVGQDAYKIAAAAGLKVPQETR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 394 TDVPETSKLLRDEIFG-----PVVVVSKFTNYDDALKLA----NDTCYGLASAVFTKDVK---KAHMFARDIKAGTVWIN 461
Cdd:cd07081 310 ILIGEVTSLAEHEPFAheklsPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKN 389
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
36-324 |
6.45e-12 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 67.62 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 36 KTIETVNPATGEPITSFQAANE--KDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAAL---ETlDAG 110
Cdd:PRK15398 12 AVLAEMLSSQTVSPPAAVGEMGvfASVDDAVAAAKVAQ-QRYQQKSLAMRQRIIDAIREALLPHAEELAELaveET-GMG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 111 KPFHSNAKQDLAqiIELTryyAGAVDKFNMGETIP--LTFNKFAytlkvPFGVVAQIVPWNYPLA-MACRKMqGALAAGN 187
Cdd:PRK15398 90 RVEDKIAKNVAA--AEKT---PGVEDLTTEALTGDngLTLIEYA-----PFGVIGAVTPSTNPTEtIINNAI-SMLAAGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 188 TVIIKP---AENTSLSLL-YFATLIKKAGFPPGVVNVI--PGYGSVvgKALGTHMDIDKISFTGstkvGGSVLEASGQSN 261
Cdd:PRK15398 159 SVVFSPhpgAKKVSLRAIeLLNEAIVAAGGPENLVVTVaePTIETA--QRLMKHPGIALLVVTG----GPAVVKAAMKSG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323821 262 LKDItlecG---GKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKE 324
Cdd:PRK15398 233 KKAI----GagaGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEK 294
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
58-453 |
9.48e-12 |
|
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: 66.88 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 58 KDVDKAVKAARAAFdNVWSKTSSEQRGIYLSNLLKLIEEEQDTLA--ALETLDAGKPFHSNAKQDLAqiIELTRyyagav 135
Cdd:cd07121 4 ATVDDAVAAAKAAQ-KQYRKCTLADREKIIEAIREALLSNAEELAemAVEETGMGRVEDKIAKNHLA--AEKTP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 136 dkfnmGETIPLTF-----NKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKP---AENTSLSLL-YFAT 206
Cdd:cd07121 75 -----GTEDLTTTawsgdNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVeLINK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 207 LIKKAGFPPGVVNVI--PGYGSVvgKALGTHMDIDKISFTGstkvGGSVLEASGQSNLKDItlecG---GKSPALVFEDA 281
Cdd:cd07121 150 AIAEAGGPDNLVVTVeePTIETT--NELMAHPDINLLVVTG----GPAVVKAALSSGKKAI----GagaGNPPVVVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 282 DLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKEtakkewdvAGKFdpfdekcivgpVISSTQYDRIKSYI 361
Cdd:cd07121 220 DIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR--------NGAY-----------VLNDEQAEQLLEVV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 362 ERGKKEEKL--DMFQTSEFPIGGAKGYFIPPT---IFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGL-- 434
Cdd:cd07121 281 LLTNKGATPnkKWVGKDASKILKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrh 360
|
410
....*....|....*....
gi 6323821 435 ASAVFTKDVKKAHMFARDI 453
Cdd:cd07121 361 TAIIHSKNVENLTKMARAM 379
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
157-462 |
1.27e-11 |
|
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: 66.36 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 157 VPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKP---AENTS---LSLLYFAtlIKKAGFPPGVVNVIPGYGSVVGK 230
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSieaAKIMREA--AVAAGAPEGLIQWIEEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 231 ALGTHMDIDKISFTGstkvGGSVLEA---SGQSNLkditlecG---GKSPALVFEDADLDKAIEWVANGIFFNSGQICTA 304
Cdd:cd07122 172 ELMKHPDVDLILATG----GPGMVKAaysSGKPAI-------GvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 305 NSRVYVQSSIYDKFVEKFK----------ETAKKE---WDVAGKFDPfdekcivgPVIsstqydriksyierGKKEEKld 371
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKrrgayflneeEKEKLEkalFDDGGTLNP--------DIV--------------GKSAQK-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 372 mfqtsefpIGGAKGYFIPPTI------FTDVPETSKLLRdEIFGPVVVVSKFTNYDDALKLAND-TCYGLA---SAVFTK 441
Cdd:cd07122 297 --------IAELAGIEVPEDTkvlvaeETGVGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSN 367
|
330 340
....*....|....*....|.
gi 6323821 442 DVKKAHMFARDIKAGTVWINQ 462
Cdd:cd07122 368 DEEVIEEFALRMPVSRILVNT 388
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
158-462 |
2.32e-08 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 56.73 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 158 PFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKP---AENTSLS---LLYFATLikKAGFPPGVVNVIPgYGSV-VGK 230
Cdd:PRK13805 108 PVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFhprAQKSSIAaakIVLDAAV--AAGAPKDIIQWIE-EPSVeLTN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 231 ALGTHMDIDKISFTGstkvGGSVLEA---SGQSNLkditlecG---GKSPALVFEDADLDKAIewvaNGIF----FNSGQ 300
Cdd:PRK13805 185 ALMNHPGIALILATG----GPGMVKAaysSGKPAL-------GvgaGNVPAYIDKTADIKRAV----NDILlsktFDNGM 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 301 ICTANSRVYVQSSIYDKFVEKFKETakkewdvagkfdpfdekcivgpvisstqydriKSYIERGKKEEKLD--MFQTSEF 378
Cdd:PRK13805 250 ICASEQAVIVDDEIYDEVKEEFASH--------------------------------GAYFLNKKELKKLEkfIFGKENG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 379 ----PIGGAKGYFIPPTIFTDVPETSKLLRDEIFG-------------PVVVVSKFTNYDDALKLA----NDTCYGLASA 437
Cdd:PRK13805 298 alnaDIVGQSAYKIAEMAGFKVPEDTKILIAEVKGvgeseplsheklsPVLAMYKAKDFEDAVEKAeklvEFGGLGHTAV 377
|
330 340
....*....|....*....|....*
gi 6323821 438 VFTKDVKKAHMFARDIKAGTVWINQ 462
Cdd:PRK13805 378 IYTNDDELIKEFGLRMKACRILVNT 402
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
141-463 |
4.51e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 55.56 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 141 GETIPLTFNKfAYTLkVPFGV-----VAQIVPWN-YPLAMAcrkmqgALAAGNTVIIKPAENTSLSLlyfATLIK----- 209
Cdd:cd07127 178 GKHDPLAMEK-TFTV-VPRGValvigCSTFPTWNgYPGLFA------SLATGNPVIVKPHPAAILPL---AITVQvarev 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 210 --KAGFPPGVVNVI---PGYGsvVGKALGTHMDIDKISFTGSTKVGGSVLEASGQsnlKDITLECGGKSPALVFEDADLD 284
Cdd:cd07127 247 laEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVVDSTDDLK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 285 KAIEWVANGIFFNSGQICTANSRVYV-QSSI-YDKFVEKFKETAKKEWDVAGKF--DPFDEKCIVGPVISSTQYDRIKSY 360
Cdd:cd07127 322 AMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqTDDGRKSFDEVAADLAAAIDGLlaDPARAAALLGAIQSPDTLARIAEA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323821 361 IERGKKEEKLDMFQTSEFPiggaKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCY---GLASA 437
Cdd:cd07127 402 RQLGEVLLASEAVAHPEFP----DARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVG 477
|
330 340 350
....*....|....*....|....*....|....*.
gi 6323821 438 VFTKD---VKKAHMFARDIKA-------GTVWINQT 463
Cdd:cd07127 478 VYSTDpevVERVQEAALDAGValsinltGGVFVNQS 513
|
|
| |
