|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
44-564 |
0e+00 |
|
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: 697.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 44 VANEKLLQYDEGSKERTELETALLGVLNRVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 123
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 124 AQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMLGQGKTLRQAEMDVA-ELVDFMRINPVFLRELANYEPIrDIQN 202
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPL-SSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 203 NCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 282
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 283 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 362
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 363 SCSMLYVPESLWQNhIREPLLEITASLVVRQDATYcDSFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKRRGYY 442
Cdd:cd07123 320 AASRAYVPESLWPE-VKERLLEELKEIKMGDPDDF-SNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 443 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKVAQIN-HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVND 521
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALRNAAGNFYIND 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 28571806 522 KSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESY 564
Cdd:cd07123 478 KPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
45-576 |
0e+00 |
|
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: 595.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 45 ANEKLLQYDEGSKERTELETALLGVLNRVEHVPIVINGQE-FQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 123
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEvYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 124 AQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMLGQGKTLRQAEMD-VAELVDFMRINPVFLRELANYEPIRDiqN 202
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDaVAELIDFFRFNVKYARELYAQQPISA--P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 203 NCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 282
Cdd:TIGR01236 159 GEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 283 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 362
Cdd:TIGR01236 239 SDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 363 SCSMLYVPESLWQnHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIDQSPSC-QILVGGSCDKRRGY 441
Cdd:TIGR01236 319 AASRLYVPHSKWP-EFKSDLLAELQSVKV-GDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 442 YVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKV-AQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVN 520
Cdd:TIGR01236 397 FVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVdSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYIN 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 521 DKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESYKTHRNIFYPYMQ 576
Cdd:TIGR01236 477 DKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
72-564 |
2.53e-138 |
|
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: 411.97 E-value: 2.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 72 RVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRY 151
Cdd:cd07083 15 FGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 152 RYNIIAATMLGqGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFT-GIAA 230
Cdd:cd07083 95 RELIATLTYEV-GKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGL-GAGVVISPWNFPvAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 231 NLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQL 310
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 311 VAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQnHIREPLLEITASLV 390
Cdd:cd07083 253 AARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE-PVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 391 VrQDATYCDSFCSAVINRRAYDRIYMWLRYIDQspSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVY 470
Cdd:cd07083 332 V-GPPEENGTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 471 VYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHS 550
Cdd:cd07083 409 RYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
490
....*....|....
gi 28571806 551 LLRWTSPQVIKESY 564
Cdd:cd07083 487 LRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
46-564 |
4.67e-99 |
|
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: 311.08 E-value: 4.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 46 NEKLLQYDEGSKeRTELETALLGVLNRV-EHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEA 124
Cdd:cd07124 3 NEPFTDFADEEN-RAAFRAALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 125 QVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANY--EPIRDIqn 202
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFpvEMVPGE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 203 ncRNSMRLRGLsGFVAAISPFNF-TGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETT 281
Cdd:cd07124 159 --DNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 282 FASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKC 361
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 362 SSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYIDQSPSCQILVGG---SCDKR 438
Cdd:cd07124 316 SACSRVIVHESVYDEFL-ERLVERTKALKV-GDPEDPEVYMGPVIDKGARDRI---RRYIEIGKSEGRLLLGgevLELAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 439 RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLN 518
Cdd:cd07124 391 EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDTEYGLTGGVFSRSPEHLERARREFE--VGNLY 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 28571806 519 VNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESY 564
Cdd:cd07124 467 ANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
74-564 |
4.44e-98 |
|
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: 307.44 E-value: 4.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 74 EHVPIVINGQEFQAK--EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRy 151
Cdd:COG1012 4 PEYPLFIGGEWVAAAsgETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 152 RYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAAN 231
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYG-ETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 232 LAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQL 310
Cdd:COG1012 160 WKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 311 VAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQnHIREPLLEITASLV 390
Cdd:COG1012 240 AAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD-EFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 391 V---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSC-DKRRGYYVDPTVVLVKDLDNIICREELLA 464
Cdd:COG1012 313 VgdpLDPGT----DMGPLISEAQLERV---LAYIEDAVAegAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 465 PILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTGlMVGQQPFGAGHMTGTSDK 544
Cdd:COG1012 386 PVLSVIPFDD--EEEAIALANDTEYGLAASVFTRDLARARRVAR--RLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGRE 460
|
490 500
....*....|....*....|
gi 28571806 545 LGtPHSLLRWTSPQVIKESY 564
Cdd:COG1012 461 GG-REGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
96-560 |
4.89e-87 |
|
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: 278.26 E-value: 4.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 96 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVA 175
Cdd:pfam00171 14 PAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEER-KDELAELETLENGKPLAEARGEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 176 ELVDFMRINPVFLRELanYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILS 254
Cdd:pfam00171 92 RAIDVLRYYAGLARRL--DGETLPSDPGRLAYTRREPL-GVVGAITPWNFPLLLPAWKIAPALAaGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 255 NYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFH 334
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 335 FVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRI 414
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIY-DEFVEKLVEAAKKLKV-GDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 415 ymwLRYIDQSPS--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLT 492
Cdd:pfam00171 321 ---LKYVEDAKEegAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKD--EEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 493 GSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVGqQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 560
Cdd:pfam00171 396 AGVFTSDLERALRV--ARRLEAGMVWINDYTTGDADG-LPFGGFKQSGFGREGG-PYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
117-560 |
5.15e-83 |
|
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: 266.77 E-value: 5.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRinpvFLRELA--NY 194
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEVARAADTFR----YYAGLArrLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 EPIRDIQNNCRNSMRLRGLSGFVAAISPFNFTG--IAANLAytPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGV 271
Cdd:cd07078 78 GEVIPSPDPGELAIVRREPLGVVGAITPWNFPLllAAWKLA--PALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 272 VNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIR 351
Cdd:cd07078 156 LNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 352 AAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQ--SPS 426
Cdd:cd07078 230 GAFGNAGQVCTAASRLLVHESIYDEFVER-LVERVKALKVgnpLDPDT----DMGPLISAAQLDRV---LAYIEDakAEG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 427 CQILVGGSCDKR-RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQDQNF 502
Cdd:cd07078 302 AKLLCGGKRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEE-----EAIELANDteyGLAAGVFTRDLER 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 503 IEEAydAFRVNVGNLNVNDKSTGlMVGQQPFGAGHMTGTSdKLGTPHSLLRWTSPQVI 560
Cdd:cd07078 377 ALRV--AERLEAGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
70-564 |
3.43e-78 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 256.79 E-value: 3.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 70 LNRVE-----HVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAA 144
Cdd:PRK03137 26 LKKVEkelgqDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 145 MLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELVDFMRinpVFLRE---LANYEPIRDIQNNcRNSMRLRGLsGFVAAI 220
Cdd:PRK03137 106 AII--RRRKHEFSAWLvKEAGKPWAEADADTAEAIDFLE---YYARQmlkLADGKPVESRPGE-HNRYFYIPL-GVGVVI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 221 SPFNF-TGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG 299
Cdd:PRK03137 179 SPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 300 TSTVLKVLWQLVAQnINFYQNY-PRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHI 378
Cdd:PRK03137 259 SREVGLRIYERAAK-VQPGQIWlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVY-DEV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 379 REPLLEITASLVVRQDATycDSFCSAVINRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRRGYYVDPTVVLVKDLDNII 457
Cdd:PRK03137 337 LEKVVELTKELTVGNPED--NAYMGPVINQASFDKI---MSYIEIGKEeGRLVLGGEGDDSKGYFIQPTIFADVDPKARI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 458 CREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNDKSTGLMVGQQPFGAGH 537
Cdd:PRK03137 412 MQEEIFGPVVAFIKAKD--FDHALEIANNTEYGLTGAVISNNREHLEKARREFH--VGNLYFNRGCTGAIVGYHPFGGFN 487
|
490 500
....*....|....*....|....*..
gi 28571806 538 MTGTSDKLGTPHSLLRWTSPQVIKESY 564
Cdd:PRK03137 488 MSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
74-564 |
6.98e-76 |
|
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: 250.55 E-value: 6.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 74 EHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMlIAGRYRY 153
Cdd:TIGR01237 31 KTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAA-IVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 154 NIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQNNCRNSMRLRglSGFVAAISPFNFT-GIAANL 232
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTP--TGVTVVISPWNFPfAIMVGM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 233 AYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVA 312
Cdd:TIGR01237 188 TVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 313 QNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVR 392
Cdd:TIGR01237 268 KVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVY-DEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 393 QDATyCDSFCSAVINRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRRGYYVDPTVvlVKDLD--NIICREELLAPILGV 469
Cdd:TIGR01237 347 PPDS-ADVYVGPVIDQKSFNKI---MEYIEIGKAeGRLVSGGCGDDSKGYFIGPTI--FADVDrkARLAQEEIFGPVVAF 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 470 YVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPH 549
Cdd:TIGR01237 421 IRASD--FDEALEIANNTEYGLTGGVISNNRDHINRAKAEF--EVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPD 496
|
490
....*....|....*
gi 28571806 550 SLLRWTSPQVIKESY 564
Cdd:TIGR01237 497 YLALFMQAKTVTEMF 511
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
71-553 |
7.08e-74 |
|
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: 245.57 E-value: 7.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 71 NRVEHVPIVINGQEfqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAG 149
Cdd:cd07125 29 KEWEAIPIINGEET--ETGEGAPVIdPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 150 RyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELaNYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNF---- 225
Cdd:cd07125 107 N-RGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQAREL-FSDPELPGPTGELNGLELHGR-GVFVCISPWNFplai 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 226 -TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG-TST 302
Cdd:cd07125 184 fTGqIAAALA-----AGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGsTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 303 vlkvlwqlvAQNINfyQNYP-------RLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQ 375
Cdd:cd07125 259 ---------AKLIN--RALAerdgpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 376 NhIREPLLEITASLVVrQDATYCDSFCSAVI------NRRAYDRIYM---WLryIDQSPScqilvggscDKRRGYYVDPT 446
Cdd:cd07125 328 R-FIEMLKGAMASLKV-GDPWDLSTDVGPLIdkpagkLLRAHTELMRgeaWL--IAPAPL---------DDGNGYFVAPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 vvlVKDLDNIIC-REELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTG 525
Cdd:cd07125 395 ---IIEIVGIFDlTTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRE--RVEAGNLYINRNITG 469
|
490 500
....*....|....*....|....*...
gi 28571806 526 LMVGQQPFGAGHMTGTSDKLGTPHSLLR 553
Cdd:cd07125 470 AIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
119-560 |
1.64e-60 |
|
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: 205.54 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 119 DKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELAnYEPIR 198
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLG-GPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 199 DIQNNCRNSMRLRGLsGFVAAISPFNFTG--IAANLAytPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFV 275
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFPLllAAWKLA--PALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 276 PAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFE 355
Cdd:cd06534 156 PGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 356 YAGQKCSSCSMLYVPESLWQnhirepllEITASLVvrqdatycdsfcsavinrraydriymwlryidqspscqilvggsc 435
Cdd:cd06534 230 NAGQICTAASRLLVHESIYD--------EFVEKLV--------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 436 dkrrgyyvdpTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETmekVAQINH---GLTGSVFAQDQNFIEEAydAFRV 512
Cdd:cd06534 257 ----------TVLVDVDPDMPIAQEEIFGPVLPVIRFKD--EEEA---IALANDteyGLTAGVFTRDLNRALRV--AERL 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571806 513 NVGNLNVNDKSTGLMVgQQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 560
Cdd:cd06534 320 RAGTVYINDSSIGVGP-EAPFGGVKNSGIGREGG-PYGLEEYTRTKTV 365
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
58-560 |
4.25e-53 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 196.31 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 58 ERTELETALLGVLNRVEHVPIVINGQEfqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDR 136
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAAPLIAGEA--ASGEARPVRnPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 137 IDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANyepirDIQNNCRNSMRLRGLsGF 216
Cdd:COG4230 618 AAILERAADLLEAH-RAELMALLVREAGKTLPDAIAEVREAVDF-------CRYYAA-----QARRLFAAPTVLRGR-GV 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 217 VAAISPFN-----FTG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHP 290
Cdd:COG4230 684 FVCISPWNfplaiFTGqVAAALA-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADP 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 291 KLAGINFTGtSTVlkvlwqlVAQNINfyqnypR-----------LVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 359
Cdd:COG4230 759 RIAGVAFTG-STE-------TARLIN------RtlaardgpivpLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQ 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 360 KCSSCSMLYVPEslwqnHIREPLLEI----TASLVV---RQDATycDsfCSAVINRRAYDRIymwLRYIDQ-----SPSC 427
Cdd:COG4230 825 RCSALRVLCVQE-----DIADRVLEMlkgaMAELRVgdpADLST--D--VGPVIDAEARANL---EAHIERmraegRLVH 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 428 QILVGGSCDKrrGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETmekVAQINH---GLTGSVFAQDQNFIE 504
Cdd:COG4230 893 QLPLPEECAN--GTFVAPTLIEIDSISDL--EREVFGPVLHVVRYKADELDKV---IDAINAtgyGLTLGVHSRIDETID 965
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 505 EAYDafRVNVGNLNVNDKSTGLMVGQQPFGaGH-MTGTSDKLGTPHSLLRWTSPQVI 560
Cdd:COG4230 966 RVAA--RARVGNVYVNRNIIGAVVGVQPFG-GEgLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
44-558 |
1.40e-50 |
|
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: 182.42 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 44 VANEKLLQydegskertELETALLGVLNRVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 123
Cdd:TIGR01238 15 LDNESELK---------PLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 124 AQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANyePIRDIQNN 203
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNAIAEVREAVDF-------CRYYAK--QVRDVLGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 204 crNSMRLRGLsgfVAAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPA 277
Cdd:TIGR01238 156 --FSVESRGV---FVCISPWNFplaifTGqISAALA-----AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 278 EETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYA 357
Cdd:TIGR01238 226 RGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED---APVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 358 GQKCSSCSMLYVPESLWQ---NHIREPLLEITASLVVRQDATycdsfCSAVINRRAYDRIymwLRYID-----QSPSCQI 429
Cdd:TIGR01238 303 GQRCSALRVLCVQEDVADrvlTMIQGAMQELKVGVPHLLTTD-----VGPVIDAEAKQNL---LAHIEhmsqtQKKIAQL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 430 LVGGSCDKRRGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQdqnfIEEAYDA 509
Cdd:TIGR01238 375 TLDDSRACQHGTFVAPTLFELDDIAEL--SEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSR----IETTYRW 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 28571806 510 F--RVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQ 558
Cdd:TIGR01238 449 IekHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
56-560 |
1.43e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 188.48 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 56 SKERTELETALLGVLNRVEHVPIVINGqefqaKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLS 134
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVsPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 135 DRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMR----------INPVFLR----Elanyepirdi 200
Cdd:PRK11904 608 ERAAILERAADLLEAN-RAELIALCVREAGKTLQDAIAEVREAVDFCRyyaaqarrlfGAPEKLPgptgE---------- 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 201 qnncRNSMRLRGLSGFVAaISPFNF-----TG-IAAnlaytpALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVN 273
Cdd:PRK11904 677 ----SNELRLHGRGVFVC-ISPWNFplaifLGqVAA------ALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQ 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 274 FVPAEETTFASVVTQHPKLAGINFTGtSTVlkvlwqlVAQNINfyqnypR-----------LVGEGGGKNFHFVHSSAEP 342
Cdd:PRK11904 746 LLPGDGATVGAALTADPRIAGVAFTG-STE-------TARIIN------RtlaardgpivpLIAETGGQNAMIVDSTALP 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 343 ETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEI----TASLVV---RQDATycDsfCSAVINRRAYDRIy 415
Cdd:PRK11904 812 EQVVDDVVTSAFRSAGQRCSALRVLFVQED-----IADRVIEMlkgaMAELKVgdpRLLST--D--VGPVIDAEAKANL- 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 416 mwLRYIDQSPS-----CQILVGGSCDKrrGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPdhklKETMEKV-AQINH 489
Cdd:PRK11904 882 --DAHIERMKRearllAQLPLPAGTEN--GHFVAPTAFEIDSISQL--EREVFGPILHVIRYK----ASDLDKViDAINA 951
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571806 490 ---GLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVI 560
Cdd:PRK11904 952 tgyGLTLGIHSRIEETADRIAD--RVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
79-534 |
6.16e-50 |
|
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: 180.14 E-value: 6.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 79 VINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYniIAA 158
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE--LAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 159 TM-LGQGKTLRQAEMDVAELVDFMRinpvFLRELANYEPIRDIQNNCRNSM--RLRGLSGFVAAISPFNF-TGIAA-NLA 233
Cdd:cd07097 82 LLtREEGKTLPEARGEVTRAGQIFR----YYAGEALRLSGETLPSTRPGVEveTTREPLGVVGLITPWNFpIAIPAwKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 234 ytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVA 312
Cdd:cd07097 158 --PALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 313 QNINFYQnyprlvGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwqnHIR--EPLLEITASLV 390
Cdd:cd07097 236 ARGARVQ------LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGI---HDRfvEALVERTKALK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 391 VrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKR--RGYYVDPTVVLVKDLDNIICREELLAPI 466
Cdd:cd07097 307 V-GDALDEGVDIGPVVSERQLEKD---LRYIEiaRSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPV 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571806 467 LGVYVYPDhkLKETMEKVAQINHGLTGSVFAQD----QNFIEeaydafRVNVGNLNVNDKSTGLMVgQQPFG 534
Cdd:cd07097 383 AAVIRVRD--YDEALAIANDTEFGLSAGIVTTSlkhaTHFKR------RVEAGVVMVNLPTAGVDY-HVPFG 445
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
60-557 |
2.77e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 163.88 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 60 TELETALLGVLNRVEHV-PIVINGQefqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRI 137
Cdd:PRK11905 539 AALDEALNAFAAKTWHAaPLLAGGD---VDGGTRPVLnPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERA 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 138 DIWERAAMLIAGRYRYnIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRdiqnnCRnsmrlrglsGFV 217
Cdd:PRK11905 616 AILERAADLMEAHMPE-LFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHK-----PL---------GPV 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 218 AAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 291
Cdd:PRK11905 681 VCISPWNFplaifTGqIAAALV-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 292 LAGINFTGTSTVLKVLWQLVAQNINfyQNYPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVpe 371
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSG--PPVP-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCL-- 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 372 slwQNHIREPLLEI----TASLVV-RQDATYCDSfcSAVINRRAYDRIymwLRYIDQSPSC-----QILVGGSCDKrrGY 441
Cdd:PRK11905 831 ---QEDVADRVLTMlkgaMDELRIgDPWRLSTDV--GPVIDAEAQANI---EAHIEAMRAAgrlvhQLPLPAETEK--GT 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 442 YVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETmekVAQIN---HGLTGSVFAQDQNFIEEAYDafRVNVGNLN 518
Cdd:PRK11905 901 FVAPTLIEIDSISDL--EREVFGPVLHVVRFKADELDRV---IDDINatgYGLTFGLHSRIDETIAHVTS--RIRAGNIY 973
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 28571806 519 VNDKSTGLMVGQQPFGaGH-MTGTSDKLGTPHSLLRWTSP 557
Cdd:PRK11905 974 VNRNIIGAVVGVQPFG-GEgLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
96-534 |
1.20e-40 |
|
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: 153.74 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 96 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYR--YNIIAATmlgQGKTLRQAEMD 173
Cdd:cd07094 6 PYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEefAKIIACE---GGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 174 VAELVDFMRINPVFLRELANYEPIRDIQ--NNCRNSMRLRGLSGFVAAISPFNF--TGIAANLAytPAL-MGNSVIWKPS 248
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATqgSDNRLAWTIREPVGVVLAITPFNFplNLVAHKLA--PAIaTGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 249 DSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTStvlKVLWQLVAQninfyQNYPRLVGEG 328
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSA---AVGEALRAN-----AGGKRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 329 GGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDSFCSAVINR 408
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELY-DEFIEAFVAAVKKLKV-GDPLDEDTDVGPLISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 409 RAYDRIYMWL-RYIDQspSCQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQI 487
Cdd:cd07094 310 EAAERVERWVeEAVEA--GARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDD--FEEAIRIANST 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571806 488 NHGLTGSVFAQDQNfieEAYDAF-RVNVGNLNVNDkSTGLMVGQQPFG 534
Cdd:cd07094 383 DYGLQAGIFTRDLN---VAFKAAeKLEVGGVMVND-SSAFRTDWMPFG 426
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
80-555 |
1.23e-40 |
|
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: 154.43 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQ--EFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYryNIIA 157
Cdd:cd07131 3 IGGEwvDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRK--EELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 158 ATMLGQ-GKTLRQAEMDVAELVDFMRIN---------PVFLRELANyepirdiqnncRNSMRLRGLSGFVAAISPFNFTG 227
Cdd:cd07131 81 RLVTREmGKPLAEGRGDVQEAIDMAQYAagegrrlfgETVPSELPN-----------KDAMTRRQPIGVVALITPWNFPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 228 IAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAE-ETTFASVVtQHPKLAGINFTGTSTVLK 305
Cdd:cd07131 150 AIPSWKIFPALVcGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRgEEVGEALV-EHPDVDVVSFTGSTEVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 306 VLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEI 385
Cdd:cd07131 229 RIGETCARPNK------RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKR-FVER 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 386 TASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICR 459
Cdd:cd07131 302 AKRLRV-GDGLDEETDMGPLINEAQLEKV---LNYNEigKEEGATLLLGGErltgGGYEKGYFVEPTVFTDVTPDMRIAQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 460 EELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNfieEAYDAFR-VNVGNLNVNDKSTGLMVgQQPFGAGHM 538
Cdd:cd07131 378 EEIFGPVVALIEVSS--LEEAIEIANDTEYGLSSAIYTEDVN---KAFRARRdLEAGITYVNAPTIGAEV-HLPFGGVKK 451
|
490
....*....|....*..
gi 28571806 539 TGTSDKLGTPHSLLRWT 555
Cdd:cd07131 452 SGNGHREAGTTALDAFT 468
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
109-542 |
4.05e-39 |
|
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: 149.42 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 109 AHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATMLGQ-GKTLRQAEMDVAELVDFMRINPVF 187
Cdd:cd07145 18 LSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELI--ERRKEELAKLLTIEvGKPIKQSRVEVERTIRLFKLAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 188 LREL-ANYEPIRDIQNNCRN-SMRLRGLSGFVAAISPFNFtgiAANL---AYTPAL-MGNSVIWKPSDSAILSNYFVFKA 261
Cdd:cd07145 96 AKVLrGETIPVDAYEYNERRiAFTVREPIGVVGAITPFNF---PANLfahKIAPAIaVGNSVVVKPSSNTPLTAIELAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 262 LREAGVPDGVVNFVPAE-ETTFASVVTqHPKLAGINFTGTSTVLKvlwQLVAQNINFYQnypRLVGEGGGKNFHFVHSSA 340
Cdd:cd07145 173 LEEAGLPPGVINVVTGYgSEVGDEIVT-NPKVNMISFTGSTAVGL---LIASKAGGTGK---KVALELGGSDPMIVLKDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 341 EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYmwlRY 420
Cdd:cd07145 246 DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKL-LVEKVKKLKV-GDPLDESTDLGPLISPEAVERME---NL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 421 IDQSPS--CQILVGGSCDKrrGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKETMEKVAQIN---HGLTGSV 495
Cdd:cd07145 321 VNDAVEkgGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIA-----KVKDDEEAVEIANsteYGLQASV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571806 496 FAQDqnfIEEAYD-AFRVNVGNLNVNDkSTGLMVGQQPFGAGHMTGTS 542
Cdd:cd07145 394 FTND---INRALKvARELEAGGVVIND-STRFRWDNLPFGGFKKSGIG 437
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
117-553 |
9.05e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 153.21 E-value: 9.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRyniiaaTMLG-----QGKTLRQAEMDVAELVDFmrinpvfLREL 191
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEAQMQ------TLMGllvreAGKTFSNAIAEVREAVDF-------LRYY 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 192 ANyePIRDIQNNCRNsmrlRGLsGFVAAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREA 265
Cdd:PRK11809 754 AG--QVRDDFDNDTH----RPL-GPVVCISPWNFplaifTGqVAAALA-----AGNSVLAKPAEQTPLIAAQAVRILLEA 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 266 GVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfYQNYP-RLVGEGGGKNFHFVHSSAEPET 344
Cdd:PRK11809 822 GVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLD-PQGRPiPLIAETGGQNAMIVDSSALTEQ 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 345 AVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITASLVV-RQDATYCDsfCSAVINRRAYDRIymwLRYIDQ 423
Cdd:PRK11809 901 VVADVLASAFDSAGQRCSALRVLCLQDDV-ADRTLKMLRGAMAECRMgNPDRLSTD--IGPVIDAEAKANI---ERHIQA 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 424 -----SPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETMEkvaQIN---HGLTGSV 495
Cdd:PRK11809 975 mrakgRPVFQAARENSEDWQSGTFVPPTLIELDSFDEL--KREVFGPVLHVVRYNRNQLDELIE---QINasgYGLTLGV 1049
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 496 FAQdqnfIEE--AYDAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLR 553
Cdd:PRK11809 1050 HTR----IDEtiAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
117-560 |
8.20e-38 |
|
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: 145.87 E-value: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAAT-MLGQGKTLRQAEMDVAELVDFMRinpvFLRELA--- 192
Cdd:cd07088 40 AVDAAEAAQKAWERLPAIERAAYLRKLADLI--RENADELAKLiVEEQGKTLSLARVEVEFTADYID----YMAEWArri 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 193 NYEPIR-DIQNncRNSMRLRGLSGFVAAISPFNFTG--IAANLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVP 268
Cdd:cd07088 114 EGEIIPsDRPN--ENIFIFKVPIGVVAGILPWNFPFflIARKLA--PALVtGNTIVIKPSEETPLNALEFAELVDEAGLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 269 DGVVNFVPAEETTFASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 347
Cdd:cd07088 190 AGVLNIVTGRGSVVGDALVAHPKVGMISLTGsTEAGQKIM-EAAAENIT------KVSLELGGKAPAIVMKDADLDLAVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 348 CTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIY-MWLRYIDQspS 426
Cdd:cd07088 263 AIVDSRIINCGQVCTCAERVYVHEDIYDEFM-EKLVEKMKAVKV-GDPFDAATDMGPLVNEAALDKVEeMVERAVEA--G 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 427 CQILVGGS-CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEE 505
Cdd:cd07088 339 ATLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSS--LDEAIELANDSEYGLTSYIYTENLNTAMR 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 506 AYDafRVNVGNLNVNDKSTGLMvgqQPFGAG-HMTGTSDKLGtPHSLLRWTSPQVI 560
Cdd:cd07088 417 ATN--ELEFGETYINRENFEAM---QGFHAGwKKSGLGGADG-KHGLEEYLQTKVV 466
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
96-541 |
1.96e-37 |
|
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: 144.66 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 96 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAEMDVA 175
Cdd:cd07149 6 PYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE-ERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 176 ELVDFMRINPVFLRELA----NYEPIRDIQNncRNSMRLRGLSGFVAAISPFNFtgiAANLA---YTPALM-GNSVIWKP 247
Cdd:cd07149 84 RAIETLRLSAEEAKRLAgetiPFDASPGGEG--RIGFTIREPIGVVAAITPFNF---PLNLVahkVGPAIAaGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 248 SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTV---------LKvlwqlvaqninfy 318
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVgeaiarkagLK------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 319 qnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVV---RQDA 395
Cdd:cd07149 226 ----KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIY-DEFLERFVAATKKLVVgdpLDED 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 396 TycdsFCSAVINRRAYDRIYMWLR-YIDQSPScqILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPIlgVYVYPD 474
Cdd:cd07149 301 T----DVGPMISEAEAERIEEWVEeAVEGGAR--LLTGG---KRDGAILEPTVLTDVPPDMKVVCEEVFAPV--VSLNPF 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 475 HKLKETMEKVAQINHGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTgLMVGQQPFGAGHMTGT 541
Cdd:cd07149 370 DTLDEAIAMANDSPYGLQAGVFTND---LQKALKAAReLEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
77-523 |
3.41e-36 |
|
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: 141.55 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 77 PIVINGQEFQAKEDFQQVL-PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDK-VRLSDRIDIWERAAMLIAgRYRYN 154
Cdd:cd07082 3 KYLINGEWKESSGKTIEVYsPID-GEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLK-ENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 155 IIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyEPIR-DIQNNCRNSMRL--RGLSGFVAAISPFNFtgiAAN 231
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDG-DSLPgDWFPGTKGKIAQvrREPLGVVLAIGPFNY---PLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 232 LAYT---PAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVL 307
Cdd:cd07082 157 LTVSkliPALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 308 WQLVAQNinfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITA 387
Cdd:cd07082 237 KKQHPMK--------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESV-ADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 388 SLVV---RQDATycdsFCSAVINRRAYDRIYmwlRYID--QSPSCQILVGGscdKRRGY-YVDPTVVLVKDLDNIICREE 461
Cdd:cd07082 308 KLKVgmpWDNGV----DITPLIDPKSADFVE---GLIDdaVAKGATVLNGG---GREGGnLIYPTLLDPVTPDMRLAWEE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571806 462 LLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKS 523
Cdd:cd07082 378 PFGPVLPIIRVND--IEEAIELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINSKC 435
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
117-534 |
7.46e-36 |
|
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: 140.78 E-value: 7.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagryRYNIIAatmLGQ------GKTLRQAEMDVAELVD---FM-----R 182
Cdd:cd07086 40 AVAAAREAFKEWRKVPAPRRGEIVRQIGEAL----RKKKEA---LGRlvslemGKILPEGLGEVQEMIDicdYAvglsrM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 183 IN-PVFLRELANYepirdiqnncRNSMRLRGLsGFVAAISPFNF-TGIAA-NLAytPALM-GNSVIWKPSDSAILSNY-- 256
Cdd:cd07086 113 LYgLTIPSERPGH----------RLMEQWNPL-GVVGVITAFNFpVAVPGwNAA--IALVcGNTVVWKPSETTPLTAIav 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 257 --FVFKALREAGVPDGVVNFVPAEeTTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFH 334
Cdd:cd07086 180 tkILAEVLEKNGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG------RVLLELGGNNAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 335 FVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRI 414
Cdd:cd07086 253 IVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDE-FLERLVKAYKQVRI-GDPLDEGTLVGPLINQAAVEKY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 415 ymwLRYID--QSPSCQILVGGSCDKRR--GYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQIN-- 488
Cdd:cd07086 331 ---LNAIEiaKSQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF------DSLEEAIAINnd 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571806 489 --HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVGqQPFG 534
Cdd:cd07086 402 vpQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIG-GAFG 448
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
117-556 |
1.77e-35 |
|
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: 139.00 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAelvdFMrinPVFLRELAN--Y 194
Cdd:cd07150 26 AIAAAYDAFPAWAATTPSERERILLKAAEIMERR-ADDLIDLLIDEGGSTYGKAWFETT----FT---PELLRAAAGecR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 EPIRDIQNNCRN---SMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDG 270
Cdd:cd07150 98 RVRGETLPSDSPgtvSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 271 VVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTI 350
Cdd:cd07150 178 VFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLK------KITLELGGKNPLIVLADADLDYAVRAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 351 RAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATycdsFCSAVINRRAYDRIYmwlRYIDQSPS- 426
Cdd:cd07150 252 FGAFMHQGQICMSASRIIVEEPVYDEFVKK-FVARASKLKVgdpRDPDT----VIGPLISPRQVERIK---RQVEDAVAk 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 427 -CQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEE 505
Cdd:cd07150 324 gAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD--AEEALELANDTEYGLSAAILTND---LQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 506 AYD-AFRVNVGNLNVNDkSTGLMVGQQPFGAGHMTGTSdKLGTPHSL-----LRWTS 556
Cdd:cd07150 396 AFKlAERLESGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
100-534 |
7.41e-35 |
|
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: 137.18 E-value: 7.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 100 QQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELV 178
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI--RERAEDLARLLtLEQGKPLAEARGEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 179 DFM--------RINPVFL-------RELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFTgiAANLAY--TPAL-MG 240
Cdd:cd07103 85 SFLewfaeearRIYGRTIpspapgkRILVIKQPV-----------------GVVAAITPWNFP--AAMITRkiAPALaAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 241 NSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqn 320
Cdd:cd07103 146 CTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 321 ypRLVGEGGGkNFHF-VHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCD 399
Cdd:cd07103 222 --RVSLELGG-NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEK-LVERVKKLKV-GNGLDEG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 400 SFCSAVINRRAYDRIymwLRYIDQSPSC--QILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhkl 477
Cdd:cd07103 297 TDMGPLINERAVEKV---EALVEDAVAKgaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPF----- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 478 kETMEKV-AQINH---GLTGSVFAQDQNfieeayDAFRV----NVGNLNVNdksTGLMVG-QQPFG 534
Cdd:cd07103 369 -DTEDEViARANDtpyGLAAYVFTRDLA------RAWRVaealEAGMVGIN---TGLISDaEAPFG 424
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
215-534 |
9.18e-35 |
|
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: 137.32 E-value: 9.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTqHPKLA 293
Cdd:cd07139 139 GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVR-HPGVD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07139 218 KVSFTGSTAAGRRIAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQnHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGscdKR-----RGYYVDPT 446
Cdd:cd07139 292 YD-EVVEALAAAVAALKV-GDPLDPATQIGPLASARQRERV---EGYIAkgRAEGARLVTGG---GRpagldRGWFVEPT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 VvlVKDLDN--IICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVN 520
Cdd:cd07139 364 L--FADVDNdmRIAQEEIFGPVLSVIPYDDED-----DAVRIANdsdYGLSGSVWTAD---VERGLAvARRIRTGTVGVN 433
|
330
....*....|....*
gi 28571806 521 dkstGLMVG-QQPFG 534
Cdd:cd07139 434 ----GFRLDfGAPFG 444
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
117-556 |
1.49e-34 |
|
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: 136.12 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyep 196
Cdd:cd07104 5 AYAAAAAAQKAWAATPPQERAAILRKAAEILEER-RDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 197 iRDIQNNC--RNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPS-DSAILSNYFVFKALREAGVPDGVV 272
Cdd:cd07104 81 -EILPSDVpgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 273 NFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRA 352
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLK------KVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 353 AFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--C 427
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFV-EKLVAKAKALPVgdpRDPDT----VIGPLINERQVDRV---HAIVEDAVAagA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 428 QILVGGscdKRRGYYVDPTVVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEA 506
Cdd:cd07104 306 RLLTGG---TYEGLFYQPTVLSdVTP-DMPIFREEIFGPVAPVIPFDD--DEEAVELANDTEYGLSAAVFTRD---LERA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 507 YD-AFRVNVGNLNVNDkSTGLMVGQQPFGAghmTGTS--DKLGTPHSL-----LRWTS 556
Cdd:cd07104 377 MAfAERLETGMVHIND-QTVNDEPHVPFGG---VKASggGRFGGPASLeefteWQWIT 430
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
117-534 |
2.54e-33 |
|
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: 132.40 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELVDfmRINpVFLRELANYE 195
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELL--KANKEELARLIsRETGKPLWEAQTEVAAMAG--KID-ISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 196 PIRDIQN-NCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVN 273
Cdd:cd07095 80 GERATPMaQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 274 FVPAEETTFASVVtQHPKLAGINFTGTSTVLKVLWQLVAqninfyqNYPR--LVGEGGGKNFHFVHSSAEPETAVACTIR 351
Cdd:cd07095 159 LVQGGRETGEALA-AHEGIDGLLFTGSAATGLLLHRQFA-------GRPGkiLALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 352 AAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVVRQ-DATycDSFCSAVINRRAYDRIYMwlryidqspSCQIL 430
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAKRLRIGApDAE--PPFMGPLIIAAAAARYLL---------AQQDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 431 VGGSCD-----KR---RGYYVDPTVVLVKDLDNIIcREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnf 502
Cdd:cd07095 300 LALGGEpllamERlvaGTAFLSPGIIDVTDAADVP-DEEIFGPLLQVYRYDD--FDEAIALANATRFGLSAGLLSDD--- 373
|
410 420 430
....*....|....*....|....*....|....
gi 28571806 503 iEEAYDAF--RVNVGNLNVNDKSTGlMVGQQPFG 534
Cdd:cd07095 374 -EALFERFlaRIRAGIVNWNRPTTG-ASSTAPFG 405
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
215-540 |
1.14e-32 |
|
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: 131.21 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTgIAANLA-YTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKL 292
Cdd:cd07089 125 GVVAAITPWNFP-FFLNLAkLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 293 AGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPES 372
Cdd:cd07089 204 DMVSFTGSTAVGRRIMAQAAATLK------RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 373 lwqnhIREPLLEITASLV--VRQ-DATYCDSFCSAVINRRAYDRIymwLRYIDQ--SPSCQILVGGscdKR-----RGYY 442
Cdd:cd07089 278 -----RYDEVVEALAAAFeaLPVgDPADPGTVMGPLISAAQRDRV---EGYIARgrDEGARLVTGG---GRpagldKGFY 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 443 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQnfiEEAYD-AFRVNVGNLN 518
Cdd:cd07089 347 VEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD-----EAVRIANdsdYGLSGGVWSADV---DRAYRvARRIRTGSVG 418
|
330 340
....*....|....*....|..
gi 28571806 519 VNdkSTGLMVGQQPFGAGHMTG 540
Cdd:cd07089 419 IN--GGGGYGPDAPFGGYKQSG 438
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
118-561 |
1.42e-32 |
|
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: 131.18 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 118 IDKSVEAQVK------WDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQ-AEMDVAELVDFMR-------- 182
Cdd:cd07091 43 VDAAVKAARAafetgwWRKMDPRERGRLLNKLADLIE-RDRDELAALESLDNGKPLEEsAKGDVALSIKCLRyyagwadk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 183 -------INPVFLrelaNY---EPIrdiqnncrnsmrlrglsGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSA 251
Cdd:cd07091 122 iqgktipIDGNFL----AYtrrEPI-----------------GVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 252 ILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGK 331
Cdd:cd07091 181 PLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS-----NLKKVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 332 NFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAY 411
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEK-FKARAEKRVV-GDPFDPDTFQGPQVSKAQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 412 DRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQIN 488
Cdd:cd07091 334 DKI---LSYIEsgKKEGATLLTGGERHGSKGYFIQPTVFTdVKD-DMKIAKEEIFGPVVTILKFKT--EDEVIERANDTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571806 489 HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdksTGLMVGQQ-PFGAGHMTGTSDKLGTpHSLLRWTSPQVIK 561
Cdd:cd07091 408 YGLAAGVFTKD---INKALRvSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFGRELGE-EGLEEYTQVKAVT 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
117-560 |
6.15e-31 |
|
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: 125.72 E-value: 6.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRidiweRAAML-IAGRYRYNI--IAA-TMLGQGKTLRQAEMDVAELVDFmrinpvfLRELA 192
Cdd:cd07106 24 AVAAAKAAFPGWSATPLEER-----RAALLaIADAIEANAeeLARlLTLEQGKPLAEAQFEVGGAVAW-------LRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 193 NYE-PIRDIQNN--CRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAgVP 268
Cdd:cd07106 92 SLDlPDEVIEDDdtRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLCTLKLGELAQEV-LP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 269 DGVVNFVPAEETtFASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 347
Cdd:cd07106 170 PGVLNVVSGGDE-LGPALTSHPDIRKISFTGsTATGKKVM-ASAAKTLK------RVTLELGGNDAAIVLPDVDIDAVAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 348 CTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSP 425
Cdd:cd07106 242 KLFWGAFINSGQVCAAIKRLYVHESIYDE-FCEALVALAKAAVV-GDGLDPGTTLGPVQNKMQYDKV---KELVEdaKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 426 SCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQnfiEE 505
Cdd:cd07106 317 GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSD--EDEVIARANDSEYGLGASVWSSDL---ER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 506 AYD-AFRVNVGNLNVNdKSTGLMVgQQPFGaGH-MTGTSDKLGtPHSLLRWTSPQVI 560
Cdd:cd07106 392 AEAvARRLEAGTVWIN-THGALDP-DAPFG-GHkQSGIGVEFG-IEGLKEYTQTQVI 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
96-520 |
7.86e-31 |
|
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: 125.44 E-value: 7.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 96 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERA-AMLIAgryRYNIIAATMLGQ-GKTLRQA--E 171
Cdd:cd07102 3 PID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAA---NTDEIAEELTWQmGRPIAQAggE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 172 MD-VAELVDFM-RINPVFLRELANYEPirdiqNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPS 248
Cdd:cd07102 79 IRgMLERARYMiSIAEEALADIRVPEK-----DGFERYIRREPL-GVVLIIAPWNYPYLTAVNAVIPALLaGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 249 DSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQhPKLAGINFTGTSTVLKVLWQLVAqninfyqnyPRLVG-- 326
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIAD-PRIDHVSFTGSVAGGRAIQRAAA---------GRFIKvg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 327 -EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAV 405
Cdd:cd07102 223 lELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFV-EAFVAVVKGYKL-GDPLDPSTTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 406 INRRAYDRIymwLRYIDQSPS--CQILVGG---SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKET 480
Cdd:cd07102 301 VSARAADFV---RAQIADAIAkgARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIM-----KVKSD 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 28571806 481 MEKVAQIN---HGLTGSVFAQD----QNFIEEaydafrVNVGNLNVN 520
Cdd:cd07102 373 AEAIALMNdseYGLTASVWTKDiaraEALGEQ------LETGTVFMN 413
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
215-534 |
1.20e-30 |
|
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: 124.97 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:cd07114 121 GVVAAITPWNSPLLLLAKKLAPALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07114 201 KIAFTGGTETGRHIARAAAENLA------PVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQNHIrEPLLEITASLVV---RQDATYCDSfcsaVINRRAYDRIymwLRYIDQSPS--CQILVGG----SCDKRRGYYVD 444
Cdd:cd07114 275 YDEFV-ERLVARARAIRVgdpLDPETQMGP----LATERQLEKV---ERYVARAREegARVLTGGerpsGADLGAGYFFE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 445 PTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQINH---GLTGSVFAQDQNfieeayDAFRV----NVGNL 517
Cdd:cd07114 347 PTILADVTNDMRIAQEEVFGPVLSV-----IPFDDEEEAIALANDseyGLAAGIWTRDLA------RAHRVaraiEAGTV 415
|
330
....*....|....*...
gi 28571806 518 NVND-KSTGLMVgqqPFG 534
Cdd:cd07114 416 WVNTyRALSPSS---PFG 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
96-534 |
2.38e-30 |
|
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: 124.28 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 96 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAqvkwdkVRLSDRIDIWERAAML--IAGRY--RYNIIAATM-LGQGKTLRQA 170
Cdd:cd07147 6 PYT-GEVVARVALAGPDDIEEAIAAAVKA------FRPMRALPAHRRAAILlhCVARLeeRFEELAETIvLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 171 EMDVAELVDFMRInpvflrelANYEPIR--------DI--QNNCRNSMRLRGLSGFVAAISPFNFtgiAANLA---YTPA 237
Cdd:cd07147 79 RGEVARAIDTFRI--------AAEEATRiygevlplDIsaRGEGRQGLVRRFPIGPVSAITPFNF---PLNLVahkVAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 238 L-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEeTTFASVVTQHPKLAGINFTGTStvlKVLWQLVAQnin 316
Cdd:cd07147 148 IaAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSP---AVGWDLKAR--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 317 fyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQ 393
Cdd:cd07147 221 --AGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSR-LVARVKALKTgdpKD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 394 DATycdsFCSAVINRRAYDRIYMWlryIDQSPS--CQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYV 471
Cdd:cd07147 298 DAT----DVGPMISESEAERVEGW---VNEAVDagAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEP 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 472 YPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTgLMVGQQPFG 534
Cdd:cd07147 368 YDDFD-----EALAAVNdskFGLQAGVFTRD---LEKALRAWDeLEVGGVVINDVPT-FRVDHMPYG 425
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
101-534 |
2.76e-30 |
|
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: 124.02 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 101 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSdridiwERAAML--IAGRYRYNiiaATMLGQ------GKTLRQAEM 172
Cdd:cd07107 8 QVLARVPAASAADVDRAVAAARAAFPEWRATTPL------ERARMLreLATRLREH---AEELALidaldcGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 173 DVAELVDFMRINPVFLRELANyepiRDIQNNCRN-SMRLRGLSGFVAAISPFN--FTGIAANLAyTPALMGNSVIWKPSD 249
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKG----ETIPVGGRNlHYTLREPYGVVARIVAFNhpLMFAAAKIA-APLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 250 SAILSNYFVFKALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGG 329
Cdd:cd07107 154 QAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 330 GKNFHFVHSSAEPETAVACTIRAA-FEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINR 408
Cdd:cd07107 227 GKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVL-ARVVERVAAIKV-GDPTDPATTMGPLVSR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 409 RAYDRIymwLRYID--QSPSCQILVGG----SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETME 482
Cdd:cd07107 305 QQYDRV---MHYIDsaKREGARLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 483 KVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKST---GLmvgqqPFG 534
Cdd:cd07107 380 QANGVEYGLTAAIWTND---ISQAHRtARRVEAGYVWINGSSRhflGA-----PFG 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
127-499 |
3.59e-30 |
|
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: 123.83 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 127 KWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAE-MDVAELVDFMRinpvFLRELANYEPIRDI--QNN 203
Cdd:cd07093 34 GWSRMSPAERARILHKVADLIEAR-ADELALLESLDTGKPITLARtRDIPRAAANFR----FFADYILQLDGESYpqDGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 204 CRNSMrLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 282
Cdd:cd07093 109 ALNYV-LRQPVGVAGLITPWNLPLMLLTWKIAPALaFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 283 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 362
Cdd:cd07093 188 GAALVAHPDVDLISFTGETATGRTIMRAAAPNLK------PVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 363 SCSMLYVPESLWQNHIrEPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDK 437
Cdd:cd07093 262 AGSRILVQRSIYDEFL-ERFVERAKALKVgdpLDPDT----EVGPLISKEHLEKV---LGYVELARAegATILTGGGRPE 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 438 ----RRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQD 499
Cdd:cd07093 334 lpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAYVWTRD 397
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
80-546 |
9.60e-30 |
|
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: 122.94 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQEFQAK-EDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEA-QVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIA 157
Cdd:cd07113 4 IDGRPVAGQsEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 158 ATMLGQGKTLRQAEM-DVAELVDFMR-------------INPVF-LRELANYepirdiqnncrNSMRLRGLSGFVAAISP 222
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRyfagwatkingetLAPSIpSMQGERY-----------TAFTRREPVGVVAGIVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 223 FNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTS 301
Cdd:cd07113 152 WNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 302 TVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREP 381
Cdd:cd07113 231 ATGKKIGRQAASDLT------RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKF-DELVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 382 LLEITASLVV---RQDATYCDSFCsaviNRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNI 456
Cdd:cd07113 304 LKQALSSFQVgspMDESVMFGPLA----NQPHFDKV---CSYLDdaRAEGDEIVRGGEALAGEGYFVQPTLVLARSADSR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 457 ICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKStgLMVGQQP 532
Cdd:cd07113 377 LMREETFGPVVSFVPYEDEE-----ELIQLINdtpFGLTASVWTNN---LSKALRyIPRIEAGTVWVNMHT--FLDPAVP 446
|
490
....*....|....
gi 28571806 533 FGAGHMTGTSDKLG 546
Cdd:cd07113 447 FGGMKQSGIGREFG 460
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
141-547 |
1.71e-29 |
|
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: 122.03 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 141 ERAAML--IAGRYRYNIIAATML---GQGKTLRQAEMDVAELVDFMRinpvFLRELAnyEPIRDIQNNCRN---SMRLRG 212
Cdd:cd07119 60 ERAALLfrIADKIREDAEELARLetlNTGKTLRESEIDIDDVANCFR----YYAGLA--TKETGEVYDVPPhviSRTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 213 LSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 291
Cdd:cd07119 134 PVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 292 LAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPE 371
Cdd:cd07119 214 VDLVSFTGGTATGRSIMRAAAGNVK------KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 372 SLWQNHIREpLLEITASLVVRQ--DAtycDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGscdKR-------RG 440
Cdd:cd07119 288 SIHDKFVAA-LAERAKKIKLGNglDA---DTEMGPLVSAEHREKV---LSYIQlgKEEGARLVCGG---KRptgdelaKG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 441 YYVDPTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQIN---HGLTGSVFAQDQNfieeayDAFRV----N 513
Cdd:cd07119 358 YFVEPTIFDDVDRTMRIVQEEIFGPVLTV-----ERFDTEEEAIRLANdtpYGLAGAVWTKDIA------RANRVarrlR 426
|
410 420 430
....*....|....*....|....*....|....
gi 28571806 514 VGNLNVNDksTGLMVGQQPFGAGHMTGTSDKLGT 547
Cdd:cd07119 427 AGTVWIND--YHPYFAEAPWGGYKQSGIGRELGP 458
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
114-562 |
2.85e-29 |
|
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: 120.88 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 114 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAE---MDVA--------ELVDFMR 182
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLER-RDELLDLIQLETGKARRHAFeevLDVAivaryyarRAERLLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 183 IN------PVFLRELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFtgiAANLAYT---PALM-GNSVIWKPSDSAI 252
Cdd:cd07101 99 PRrrrgaiPVLTRTTVNRRPK-----------------GVVGVISPWNY---PLTLAVSdaiPALLaGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 253 LSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKlaGINFTGTSTVLKVLWQLVAQninfyqnypRLVG---EGG 329
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGR---------RLIGcslELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 330 GKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVRQDATYCDSFCSaVINRR 409
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRR-FVARTRALRLGAALDYGPDMGS-LISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 410 AYDRIYmwlRYIDQSPS--CQILVGGSCDKRRG-YYVDPTVVLVKDLDNIICREELLAPIlgVYVYPDHKLKETMEKVAQ 486
Cdd:cd07101 306 QLDRVT---AHVDDAVAkgATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPV--VSIYRVADDDEAIELAND 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 487 INHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVND------KSTGL-MVGQQPFGAGHMTGtsdklgtPHSLLRWTSPQ 558
Cdd:cd07101 381 TDYGLNASVWTRD---GARGRRiAARLRAGTVNVNEgyaaawASIDApMGGMKDSGLGRRHG-------AEGLLKYTETQ 450
|
....
gi 28571806 559 VIKE 562
Cdd:cd07101 451 TVAV 454
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
117-501 |
2.65e-28 |
|
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: 117.68 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANY-- 194
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESR-RDEFIEAMMEETGATAAWAGFNVDLAAGM-------LREAASLit 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 ----EPI-RDIQNncRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVP 268
Cdd:cd07105 77 qiigGSIpSDKPG--TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 269 DGVVNFVPAEETTFASVVTQ---HPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETA 345
Cdd:cd07105 155 KGVLNVVTHSPEDAPEVVEAliaHPAVRKVNFTGSTRVGRIIAETAAKHLK------PVLLELGGKAPAIVLEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 346 VACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVRQDATycdsfcSAVINRRAYDRIymwLRYIDQSP 425
Cdd:cd07105 229 ANAALFGAFLNSGQICMSTERIIVHESIADE-FVEKLKAAAEKLFAGPVVL------GSLVSAAAADRV---KELVDDAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 426 SC--QILVGG-SCDKRRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYpdhklKETMEKVAQIN---HGLTGS 494
Cdd:cd07105 299 SKgaKLVVGGlADESPSGTSMPPTI-----LDNVtpdmdIYSEESFGPVVSIIRV-----KDEEEAVRIANdseYGLSAA 368
|
....*..
gi 28571806 495 VFAQDQN 501
Cdd:cd07105 369 VFTRDLA 375
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
101-474 |
2.68e-28 |
|
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: 118.31 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 101 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAE-MDVAELVD 179
Cdd:cd07115 8 ELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARrLDVPRAAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 180 FMR---------------INPVFLrelaNY---EPIrdiqnncrnsmrlrglsGFVAAISPFNFTGIAANLAYTPAL-MG 240
Cdd:cd07115 87 TFRyyagwadkiegevipVRGPFL----NYtvrEPV-----------------GVVGAIVPWNFPLMFAAWKVAPALaAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 241 NSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqn 320
Cdd:cd07115 146 NTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 321 ypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDS 400
Cdd:cd07115 222 --RVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIY-DEFLERFTSLARSLRP-GDPLDPKT 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571806 401 FCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPD 474
Cdd:cd07115 298 QMGPLVSQAQFDRV---LDYVDvgREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRD 370
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
215-546 |
3.43e-28 |
|
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: 118.22 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:cd07141 147 GVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDID 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07141 227 KVAFTGSTEVGKLIQQAAGKS-----NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQNHIREpLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPT 446
Cdd:cd07141 302 YDEFVKR-SVERAKKRVVG------NPFDPKTeqgpqIDEEQFKKI---LELIEsgKKEGAKLECGGKRHGDKGYFIQPT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEA-YDAFRVNVGNLNVNdkST 524
Cdd:cd07141 372 VFSdVTD-DMRIAKEEIFGPVQQIFKFKT--IDEVIERANNTTYGLAAAVFTKD---IDKAiTFSNALRAGTVWVN--CY 443
|
330 340
....*....|....*....|..
gi 28571806 525 GLMVGQQPFGAGHMTGTSDKLG 546
Cdd:cd07141 444 NVVSPQAPFGGYKMSGNGRELG 465
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
215-534 |
6.35e-28 |
|
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: 117.32 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAeettFASVVTQ----H 289
Cdd:cd07112 126 GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPG----FGHTAGEalglH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 290 PKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVAC-TIRAAFEYAGQKCSSCSMLY 368
Cdd:cd07112 202 MDVDALAFTGSTEVGRRFLEYSGQS-----NLKRVWLECGGKSPNIVFADAPDLDAAAEaAAAGIFWNQGEVCSAGSRLL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 369 VPESlwqnhIREPLLEitasLVVRQDATY-------CDSFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDKR- 438
Cdd:cd07112 277 VHES-----IKDEFLE----KVVAAAREWkpgdpldPATRMGALVSEAHFDKV---LGYIESGKAegARLVAGGKRVLTe 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 439 -RGYYVDPTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQIN---HGLTGSVFAQDQNfieeayDAFRV-- 512
Cdd:cd07112 345 tGGFFVEPTVFDGVTPDMRIAREEIFGPVLSV-----ITFDSEEEAVALANdsvYGLAASVWTSDLS------RAHRVar 413
|
330 340
....*....|....*....|....
gi 28571806 513 --NVGNLNVNDKSTGLMvgQQPFG 534
Cdd:cd07112 414 rlRAGTVWVNCFDEGDI--TTPFG 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
80-520 |
6.87e-28 |
|
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: 117.23 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQEFQAK-EDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAA 158
Cdd:cd07085 5 INGEWVESKtTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL--EENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 159 TM-LGQGKTLRQAEMDVA---ELVDFMRINPvflrELANYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAY 234
Cdd:cd07085 83 LItLEHGKTLADARGDVLrglEVVEFACSIP----HLLKGEYLENVARGIDTYSYRQPL-GVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 235 TPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQ 313
Cdd:cd07085 158 PMAIaCGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 314 NINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLyVPESLWQNHIREPLLEITASLVVRq 393
Cdd:cd07085 237 NGK------RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVA-VAVGDEADEWIPKLVERAKKLKVG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 394 DATYCDSFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDK----RRGYYVDPTVvlvkdLDNI-----ICREEL 462
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERI---EGLIESGVEegAKLVLDGRGVKvpgyENGNFVGPTI-----LDNVtpdmkIYKEEI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571806 463 LAPILGVyVYPDHkLKETMEKVAQINHGLTGSVFAQD----QNFIEEaydafrVNVGNLNVN 520
Cdd:cd07085 381 FGPVLSI-VRVDT-LDEAIAIINANPYGNGAAIFTRSgaaaRKFQRE------VDAGMVGIN 434
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
215-546 |
8.11e-28 |
|
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: 117.12 E-value: 8.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:cd07144 146 GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07144 226 KIAFTGSTATGRLVMKAAAQNLK------AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQNHIrEPLLEitaslVVRQDATYCDSFCS-----AVINRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKR---RGYYV 443
Cdd:cd07144 300 YDKFV-EKFVE-----HVKQNYKVGSPFDDdtvvgPQVSKTQYDRV---LSYIEKgkKEGAKLVYGGEKAPEglgKGYFI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 444 DPTVVL-VKDlDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNd 521
Cdd:cd07144 371 PPTIFTdVPQ-DMRIVKEEIFGPVVVISKFKTY--EEAIKKANDTTYGLAAAVFTKD---IRRAHRvARELEAGMVWIN- 443
|
330 340
....*....|....*....|....*
gi 28571806 522 kSTGLMVGQQPFGAGHMTGTSDKLG 546
Cdd:cd07144 444 -SSNDSDVGVPFGGFKMSGIGRELG 467
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
134-534 |
1.65e-27 |
|
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: 115.92 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 134 SDRIDIWERAAMLIAGRYRYniiAATMLGQ--GKTLRQAEMDVAELVDFMRInpvflrelANYEPIR--------DIQNN 203
Cdd:cd07146 40 YQRSAILNKAAALLEARREE---FARLITLesGLCLKDTRYEVGRAADVLRF--------AAAEALRddgesfscDLTAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 204 C--RNSMRLRGLSGFVAAISPFNF--TGIAANLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAE 278
Cdd:cd07146 109 GkaRKIFTLREPLGVVLAITPFNHplNQVAHKIA--PAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 279 ETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAqninfyqnYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAG 358
Cdd:cd07146 187 PGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 359 QKCSSCSMLYVPESLWQNhIREPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIY-MWLRYIDQSPScqILVGGS 434
Cdd:cd07146 259 QRCTAVKRILVHESVADE-FVDLLVEKSAALVVgdpMDPAT----DMGTVIDEEAAIQIEnRVEEAIAQGAR--VLLGNQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 435 cdkRRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDa 509
Cdd:cd07146 332 ---RQGALYAPTV-----LDHVppdaeLVTEETFGPVAPVIRVKD--LDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE- 400
|
410 420
....*....|....*....|....*
gi 28571806 510 fRVNVGNLNVNDkSTGLMVGQQPFG 534
Cdd:cd07146 401 -RLDVGTVNVNE-VPGFRSELSPFG 423
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
215-546 |
3.07e-27 |
|
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: 115.32 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:cd07143 146 GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDID 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07143 226 KVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVK 451
Cdd:cd07143 301 YDKFVKR-FKEKAKKLKV-GDPFAEDTFQGPQVSQIQYERI---MSYIEsgKAEGATVETGGKRHGNEGYFIEPTIFTDV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 452 DLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNdkSTGLMVGQQ 531
Cdd:cd07143 376 TEDMKIVKEEIFGPVVAVIKFKT--EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALK--AGTVWVN--CYNLLHHQV 449
|
330
....*....|....*
gi 28571806 532 PFGAGHMTGTSDKLG 546
Cdd:cd07143 450 PFGGYKQSGIGRELG 464
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
215-541 |
7.20e-27 |
|
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: 114.13 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:cd07142 143 GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:cd07142 223 KVAFTGSTEVGKIIMQLAAKS-----NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WQNHIrEPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKRRGYYVDPT 446
Cdd:cd07142 298 YDEFV-EKAKARALKRVVG------DPFRKGVeqgpqVDKEQFEKI---LSYIEHgkEEGATLITGGDRIGSKGYYIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNdkSTG 525
Cdd:cd07142 368 IFSdVKD-DMKIARDEIFGPVQSILKFKT--VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYD 440
|
330
....*....|....*.
gi 28571806 526 LMVGQQPFGAGHMTGT 541
Cdd:cd07142 441 VFDASIPFGGYKMSGI 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
80-534 |
8.16e-27 |
|
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: 113.75 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQ--EFQAKEDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERaamlIAGRY--RYNI 155
Cdd:cd07138 3 IDGAwvAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLER----IAEAYeaRADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 156 IAATM---LGQGKTLRQAeMDVAELVDFMRinpVFLRELANYEPIRDIQNncrnSMRLRGLSGFVAAISPFNFT--GIAA 230
Cdd:cd07138 78 LAQAItleMGAPITLARA-AQVGLGIGHLR---AAADALKDFEFEERRGN----SLVVREPIGVCGLITPWNWPlnQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 231 NLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG-TSTVLKVLw 308
Cdd:cd07138 150 KVA--PALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGsTRAGKRVA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 309 QLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITAS 388
Cdd:cd07138 227 EAAADTVK------RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSR-YAEAEEIAAAAAEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 389 LVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSpscqI-----LVGGSCDK----RRGYYVDPTVVLVKDLDNI 456
Cdd:cd07138 300 YVVgdpRDPAT----TLGPLASAAQFDRV---QGYIQKG----IeegarLVAGGPGRpeglERGYFVKPTVFADVTPDMT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 457 ICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQnfiEEAYD-AFRVNVGNLNVNDKSTGLmvgQQP 532
Cdd:cd07138 369 IAREEIFGPVLSIIPYDDED-----EAIAIANdtpYGLAGYVWSADP---ERARAvARRLRAGQVHINGAAFNP---GAP 437
|
..
gi 28571806 533 FG 534
Cdd:cd07138 438 FG 439
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
117-560 |
1.03e-26 |
|
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: 113.47 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFM----RINPVFLRELA 192
Cdd:cd07099 23 AVARARAAQRAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAETGKPRADAGLEVLLALEAIdwaaRNAPRVLAPRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 193 nyEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGV 271
Cdd:cd07099 102 --VPTGLLMPNKKATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 272 VNFVPAEETTFASVVTQHP-KLAginFTG-TSTVLKVLWQLVAQNInfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACT 349
Cdd:cd07099 179 LQVVTGDGATGAALIDAGVdKVA---FTGsVATGRKVMAAAAERLI------P-VVLELGGKDPMIVLADADLERAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 350 IRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV----RQDATYcdsfcSAVINRRAYDRIYmwlRYIDQSP 425
Cdd:cd07099 249 VWGAMVNAGQTCISVERVYVHESVYDEFVAR-LVAKARALRPgaddIGDADI-----GPMTTARQLDIVR---RHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 426 S--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhklkeTMEKVAQIN---HGLTGSVFAQDQ 500
Cdd:cd07099 320 AkgAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVAD-----EDEAIALANdsrYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 501 NFIEEAydAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 560
Cdd:cd07099 395 ARAEAI--ARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHG-AEGLREFCRPKAI 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
117-556 |
1.04e-26 |
|
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: 113.16 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLiAGRYRYNIIAATMLGQGKTLRQAEMDVAELVdfmrinpVFLRELANY-- 194
Cdd:cd07152 18 AAARAAAAQRAWAATPPRERAAVLRRAADL-LEEHADEIADWIVRESGSIRPKAGFEVGAAI-------GELHEAAGLpt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 EPIRDI--QNNCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPS-DSAILSNYFVFKALREAGVPDG 270
Cdd:cd07152 90 QPQGEIlpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFEEAGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 271 VVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTI 350
Cdd:cd07152 170 VLHVLPGGADAGEALVE-DPNVAMISFTGSTAVGRKVGEAAGRHLK------KVSLELGGKNALIVLDDADLDLAASNGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 351 RAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVRQDATYcDSFCSAVINRRAYDRIymwLRYIDQS--PSCQ 428
Cdd:cd07152 243 WGAFLHQGQICMAAGRHLVHESVADAYT-AKLAAKAKHLPVGDPATG-QVALGPLINARQLDRV---HAIVDDSvaAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 429 ILVGGScdkRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQDqnfIEE 505
Cdd:cd07152 318 LEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE-----EAVALANDteyGLSAGIISRD---VGR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 506 AYD-AFRVNVGNLNVNDKsTGLMVGQQPFGAGHMTGTSDKLGTPHSL-----LRWTS 556
Cdd:cd07152 387 AMAlADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGPANWeeftqWQWVT 442
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
101-540 |
1.26e-26 |
|
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: 113.17 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 101 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAA-TMLGQGKTLRQAEMDVAELVD 179
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLL--RERNDEIARlETIDNGKPIEEARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 180 FMRinpvFLRELAnyepirdiQNNCRNSMRLRGLS---------GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSD 249
Cdd:cd07090 86 CLE----YYAGLA--------PTLSGEHVPLPGGSfaytrreplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 250 SAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEG 328
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGsVPTGKKVM-SAAAKGIK------HVTLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 329 GGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINR 408
Cdd:cd07090 226 GGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDE-FTERLVERTKKIRI-GDPLDEDTQMGALISE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 409 RAYDRIymwLRYIDQSPS--CQILVGG-----SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETM 481
Cdd:cd07090 304 EHLEKV---LGYIESAKQegAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF------DTE 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571806 482 EKVAQI----NHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdkSTGLMVGQQPFGAGHMTG 540
Cdd:cd07090 375 EEVIRRandtTYGLAAGVFTRD---LQRAHRvIAQLQAGTCWIN--TYNISPVEVPFGGYKQSG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
94-551 |
1.98e-26 |
|
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: 112.45 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 94 VLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYryNIIAATM-LGQGKTLR-QAE 171
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARS--EELARLLaLETGNALRtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 172 MDVAELVDFMRINPVFLREL-ANYEPIRDIQNncrnSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSD 249
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELkGETLPFGPDVL----TYTVREPLGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 250 SAILSNYFVFKALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAqninfyqnyPRLVG--- 326
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 327 EGGGKNFHFVHSSAEPETAVACTIRAA-FEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAV 405
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFL-EKLVAKLSKLKI-GDPLDEATDIGAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 406 INRRAYDRIymwLRYID---QSPSCQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklK 478
Cdd:cd07108 303 ISEKQFAKV---CGYIDlglSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDE--D 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571806 479 ETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdKSTGLMVGQQpFGAGHMTGtsdkLGTPHSL 551
Cdd:cd07108 378 EVIAMANDSHYGLAAYVWTRD---LGRALRaAHALEAGWVQVN-QGGGQQPGQS-YGGFKQSG----LGREASL 442
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
118-534 |
6.98e-26 |
|
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: 110.79 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 118 IDKSVEA-----QVKWDKVRLSDRIDIWERAAMLIaGRYRYNIIAATMLGQGKTLRQAEMDVAELVdfmrinpvflRELA 192
Cdd:cd07109 21 VDRAVQAarrafESGWLRLSPAERGRLLLRIARLI-REHADELARLESLDTGKPLTQARADVEAAA----------RYFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 193 NYEPIRD--------IQNNCRNSMrLRGLSGFVAAISPFNFT------GIAANLAytpalMGNSVIWKPSDSAILSNYFV 258
Cdd:cd07109 90 YYGGAADklhgetipLGPGYFVYT-VREPHGVTGHIIPWNYPlqitgrSVAPALA-----AGNAVVVKPAEDAPLTALRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 259 FKALREAGVPDGVVNFVP--AEETTFAsvVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFV 336
Cdd:cd07109 164 AELAEEAGLPAGALNVVTglGAEAGAA--LVAHPGVDHISFTGSVETGIAVMRAAAENVV------PVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 337 HSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEITASLV--VRQDATYCDSFCSAVINRRAYDRI 414
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRS-----IYDEVLERLVERFraLRVGPGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 415 YMWLRYIDQSpSCQILVGG---SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN--- 488
Cdd:cd07109 311 EGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEA-----EAIALANgtd 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 28571806 489 HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKSTGLMVgQQPFG 534
Cdd:cd07109 385 YGLVAGVWTRD---GDRALRvARRLRAGQVFVNNYGAGGGI-ELPFG 427
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
118-546 |
8.73e-26 |
|
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: 110.50 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 118 IDKSVEAQVK------WDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLREL 191
Cdd:cd07118 21 VDAAVAAARKafdkgpWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQARGEIEGAADLWRYAASLARTL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 192 ANyepirDIQNNCRNSMR---LRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGV 267
Cdd:cd07118 100 HG-----DSYNNLGDDMLglvLREPIGVVGIITPWNFPFLILSQKLPFALaAGCTVVVKPSEFTSGTTLMLAELLIEAGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 268 PDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 347
Cdd:cd07118 175 PAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK------KVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 348 CTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREpllEITASLVVR-QDATYCDSF-----CSAVINRRAYDRIymwLRYI 421
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHES-----IAD---AFVAAVVARsRKVRVGDPLdpetkVGAIINEAQLAKI---TDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 422 D--QSPSCQILVGG-SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQI----NHGLTGS 494
Cdd:cd07118 318 DagRAEGATLLLGGeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF------DTVDEAIALandtVYGLSAG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571806 495 VFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTGlmVGQQPFGAGHMTGTSDKLG 546
Cdd:cd07118 392 VWSKD---IDTALTVARrIRAGTVWVNTFLDG--SPELPFGGFKQSGIGRELG 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
123-534 |
2.02e-25 |
|
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: 109.70 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 123 EAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRinpvflrELANYePIR---- 198
Cdd:cd07151 43 AAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRESGSTRIKANIEWGAAMAITR-------EAATF-PLRmegr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 199 DIQNNC--RNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKP-SDSAILSNYFVFKALREAGVPDGVVNF 274
Cdd:cd07151 114 ILPSDVpgKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 275 V--PAEETTFASVVTQHPKLagINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRA 352
Cdd:cd07151 194 VvgAGSEIGDAFVEHPVPRL--ISFTGSTPVGRHIGELAGRHLK------KVALELGGNNPFVVLEDADIDAAVNAAVFG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 353 AFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYIDQSPS--CQIL 430
Cdd:cd07151 266 KFLHQGQICMAINRIIVHEDVYDEFV-EKFVERVKALPY-GDPSDPDTVVGPLINESQVDGL---LDKIEQAVEegATLL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 431 VGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-A 509
Cdd:cd07151 341 VGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALELANDTEYGLSGAVFTSD---LERGVQfA 412
|
410 420
....*....|....*....|....*...
gi 28571806 510 FRVNVGNLNVNDKStglmVGQQP---FG 534
Cdd:cd07151 413 RRIDAGMTHINDQP----VNDEPhvpFG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
114-534 |
8.60e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 108.12 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 114 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAAtMLGQ--GKTLRQAEMDVAELvdfmrINPVFLREL 191
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALL--EENKEELAE-VIARetGKPLWEAATEVTAM-----INKIAISIQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 192 ANYE---PIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGV 267
Cdd:PRK09457 111 AYHErtgEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVKLWQQAGL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 268 PDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNinfyqnyPR--LVGEGGGKNFHFVHSSAEPETA 345
Cdd:PRK09457 190 PAGVLNLVQGGRETGKALAA-HPDIDGLLFTGSANTGYLLHRQFAGQ-------PEkiLALEMGGNNPLVIDEVADIDAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 346 VACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVVRQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSP 425
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQL-LAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 426 SCQILVGGSCDKRRGYYVDPTVVlvkDLDNIICR--EELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfi 503
Cdd:PRK09457 341 GGKSLLEMTQLQAGTGLLTPGII---DVTGVAELpdEEYFGPLLQVVRYDD--FDEAIRLANNTRFGLSAGLLSDD---- 411
|
410 420 430
....*....|....*....|....*....|...
gi 28571806 504 EEAYDAFRVNV--GNLNVNDKSTGlMVGQQPFG 534
Cdd:PRK09457 412 REDYDQFLLEIraGIVNWNKPLTG-ASSAAPFG 443
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
163-501 |
2.18e-24 |
|
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: 106.27 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 163 QGKTLRQAEMDVAELVDFMRinpvFLRELANYEPIRDIQNNCRN-SMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-G 240
Cdd:cd07120 70 NGKILGEARFEISGAISELR----YYAGLARTEAGRMIEPEPGSfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 241 NSVIWKPSDSAILSNYFVFKALREA-GVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyq 319
Cdd:cd07120 146 CTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 320 nypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCD 399
Cdd:cd07120 223 ---RLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE-VRDRLAARLAAVKV-GPGLDPA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 400 SFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKR--RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKl 477
Cdd:cd07120 298 SDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA- 376
|
330 340
....*....|....*....|....*..
gi 28571806 478 ketmEKVAQINH---GLTGSVFAQDQN 501
Cdd:cd07120 377 ----EAVALANDtdyGLAASVWTRDLA 399
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
141-512 |
2.47e-24 |
|
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: 106.28 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 141 ERAAML--IA---GRYRYNIIAATMLGQGKTLRQAEMDV----------AELVDFMRINpvflRELANYEPIRDIQNNCR 205
Cdd:cd07110 42 ERAKYLraIAegvRERREELAELEARDNGKPLDEAAWDVddvagcfeyyADLAEQLDAK----AERAVPLPSEDFKARVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 206 nsmrlRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFAS 284
Cdd:cd07110 118 -----REPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 285 VVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSC 364
Cdd:cd07110 193 PLAAHPGIDKISFTGSTATGSQVMQAAAQDIK------PVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 365 SMLYVPESlwqnhIREPLLEitaSLVVRQDAT-YCDSF-----CSAVINRRAYDRIymwLRYIDQSPS--CQILVGGS-- 434
Cdd:cd07110 267 SRLLVHES-----IADAFLE---RLATAAEAIrVGDPLeegvrLGPLVSQAQYEKV---LSFIARGKEegARLLCGGRrp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 435 CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQNFIEEAYDAFR 511
Cdd:cd07110 336 AHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-----EAIALANdseYGLAAAVISRDAERCDRVAEALE 410
|
.
gi 28571806 512 V 512
Cdd:cd07110 411 A 411
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
115-560 |
7.10e-24 |
|
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: 104.63 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 115 QMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMrinpvFLRELANY 194
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAENICGDQVQLR-----ARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 EPIRDIQNNCRN---SMRLRGL---SGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAG- 266
Cdd:cd07084 76 YRIPHEPGNHLGqglKQQSHGYrwpYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 267 VPDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNinfyqnypRLVGEGGGKNFHFVHSSAEPETAV 346
Cdd:cd07084 156 LPPEDVTLINGDGKTMQALLL-HPNPKMVLFTGSSRVAEKLALDAKQA--------RIYLELAGFNWKVLGPDAQAVDYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 347 ACTI-RAAFEYAGQKCSSCSMLYVPESlWQnhiREPLLEITASLVVRQ-------DATYCDSFCSAVINRRAYDRIYmwL 418
Cdd:cd07084 227 AWQCvQDMTACSGQKCTAQSMLFVPEN-WS---KTPLVEKLKALLARRkledlllGPVQTFTTLAMIAHMENLLGSV--L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 419 RYidqspSCQILVGGSCDKRRGYYVDPTVVLVKDLDN---IICREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSV 495
Cdd:cd07084 301 LF-----SGKELKNHSIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571806 496 FAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVI 560
Cdd:cd07084 376 YSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
215-546 |
2.80e-23 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 103.75 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:PLN02766 160 GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:PLN02766 240 KVSFTGSTEVGRKIMQAAATS-----NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WqNHIREPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPT 446
Cdd:PLN02766 315 Y-DEFVKKLVEKAKDWVVG------DPFDPRArqgpqVDKQQFEKI---LSYIEhgKREGATLLTGGKPCGDKGYYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 VVLVKDLDNIICREELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNV-----ND 521
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCyfafdPD 462
|
330 340
....*....|....*....|....*
gi 28571806 522 kstglmvgqQPFGAGHMTGTSDKLG 546
Cdd:PLN02766 463 ---------CPFGGYKMSGFGRDQG 478
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
215-520 |
7.75e-23 |
|
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: 101.90 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTgiAANLAYTPALM---GNSVIWKPSDS----AILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVt 287
Cdd:cd07130 134 GVVGVITAFNFP--VAVWGWNAAIAlvcGNVVVWKPSPTtpltAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALV- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 288 QHPKLAGINFTGTSTVLKvlwqLVAQNINfyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 367
Cdd:cd07130 211 KDPRVPLVSFTGSTAVGR----QVGQAVA--ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 368 YVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSPSCQILVGGSCDKRRGYYVDPTV 447
Cdd:cd07130 285 IVHESIYDE-VLERLKKAYKQVRI-GDPLDDGTLVGPLHTKAAVDNYLAAIEEA-KSQGGTVLFGGKVIDGPGNYVEPTI 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 448 VLVKDLDNIIcREELLAPILgvYVypdHKLKeTMEKVAQIN----HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVN 520
Cdd:cd07130 362 VEGLSDAPIV-KEETFAPIL--YV---LKFD-TLEEAIAWNnevpQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVN 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
103-501 |
3.52e-22 |
|
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: 99.84 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 103 IAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMlGQGKTLRQAE-MDVAELVDFM 181
Cdd:cd07117 29 LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL-DNGKPIRETRaVDIPLAADHF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 182 RINPVFLRelANYEPIRDIQNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFK 260
Cdd:cd07117 108 RYFAGVIR--AEEGSANMIDEDTL-SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 261 ALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnYPRLVgEGGGKNFHFVHSSA 340
Cdd:cd07117 185 IIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANIIFDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 341 EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVvrQDATYCDSFCSAVINRRAYDRIymwLRY 420
Cdd:cd07117 258 NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKV--GNPLDPDTQMGAQVNKDQLDKI---LSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 421 ID--QSPSCQILVGG------SCDKrrGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKETMEKVAQIN---H 489
Cdd:cd07117 333 VDiaKEEGAKILTGGhrltenGLDK--GFFIEPTLIVNVTNDMRVAQEEIFGPVATVI-----KFKTEDEVIDMANdseY 405
|
410
....*....|..
gi 28571806 490 GLTGSVFAQDQN 501
Cdd:cd07117 406 GLGGGVFTKDIN 417
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
80-560 |
5.04e-22 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 99.59 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQEFQAKED--FQQVLPYDiQQPIAHYGHAHRVLIQMAID--KSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNI 155
Cdd:PRK09847 24 INGEYTAAAENetFETVDPVT-QAPLAKIARGKSVDIDRAVSaaRGVFERGDWSLSSPAKRKAVLNKLADLME-AHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 156 IAATMLGQGKTLRQAEMD-----------VAELVD--FMRINPVFLRELAnyepirdiqnncrnsMRLRGLSGFVAAISP 222
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDdipgaarairwYAEAIDkvYGEVATTSSHELA---------------MIVREPVGVIAAIVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 223 FNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTS 301
Cdd:PRK09847 167 WNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGST 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 302 TVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSA-EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIRe 380
Cdd:PRK09847 247 RTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 381 pLLEITASLVVRQDATYCDSFCSAVINRRAYDRIYmwlRYIDQSPS-CQILVGGscdKRRGY--YVDPTVVLVKDLDNII 457
Cdd:PRK09847 321 -LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH---SFIREGESkGQLLLDG---RNAGLaaAIGPTIFVDVDPNASL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 458 CREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKSTGLMVgqQPFGAG 536
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSE--EQALQLANDSQYGLGAAVWTRD---LSRAHRmSRRLKAGSVFVNNYNDGDMT--VPFGGY 466
|
490 500
....*....|....*....|....*
gi 28571806 537 HMTGTS-DKlgTPHSLLRWTSPQVI 560
Cdd:PRK09847 467 KQSGNGrDK--SLHALEKFTELKTI 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
150-501 |
5.35e-22 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 98.65 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 150 RYRYNIIAATMLG-QGKTLRQAEMDVAELVDFMRinpvFLRELA-NYEPirDIQNNCR---NSMRLRGLSGFVAAISPFN 224
Cdd:PRK10090 9 RERASEISALIVEeGGKIQQLAEVEVAFTADYID----YMAEWArRYEG--EIIQSDRpgeNILLFKRALGVTTGILPWN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 225 FTG--IAANLAytPALM-GNSVIWKPSdSAILSNYFVF-KALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGT 300
Cdd:PRK10090 83 FPFflIARKMA--PALLtGNTIVIKPS-EFTPNNAIAFaKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 301 STVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrE 380
Cdd:PRK10090 160 VSAGEKIMAAAAKNIT------KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV-N 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 381 PLLEITASLVVRQDATYCDSFCSAVINRRAYDRIY-MWLRYIDQSPScqILVGGSCDKRRGYYVDPTVVLVKDLDNIICR 459
Cdd:PRK10090 233 RLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEqKVARAVEEGAR--VALGGKAVEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 28571806 460 EELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQN 501
Cdd:PRK10090 311 EETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLN 350
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
215-563 |
6.43e-22 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 99.57 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNF---TGIAANLaytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHP 290
Cdd:PRK09407 156 GVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 291 KlaGINFTGTSTVLKVLWQLVAQninfyqnypRLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 367
Cdd:PRK09407 233 D--YLMFTGSTATGRVLAEQAGR---------RLIGfslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 368 YVPESLWQNHIREpLLEITASLVVRQDATYCDSFCSaVINRRAYDRIYmwlRYIDQSPS--CQILVGGscdKRR---G-Y 441
Cdd:PRK09407 302 YVHESIYDEFVRA-FVAAVRAMRLGAGYDYSADMGS-LISEAQLETVS---AHVDDAVAkgATVLAGG---KARpdlGpL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 442 YVDPTVVLVKDLDNIICREELLAPIlgVYVYPDHKLKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVN 520
Cdd:PRK09407 374 FYEPTVLTGVTPDMELAREETFGPV--VSVYPVADVDEAVERANDTPYGLNASVWTGD---TARGRAiAARIRAGTVNVN 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 28571806 521 D------KSTGL-MVGQQPFGAGHMTGtsdklgtPHSLLRWTSPQVIKES 563
Cdd:PRK09407 449 EgyaaawGSVDApMGGMKDSGLGRRHG-------AEGLLKYTESQTIATQ 491
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
141-499 |
1.30e-21 |
|
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: 98.17 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 141 ERAAML--IAGRYRYN---IIAATMLGQGKTLR-QAEMDVAELVDFMRINPVFLREL-----ANYEPirdiqnnCRNSMR 209
Cdd:cd07092 42 ERSKALlkLADAIEENaeeLAALESRNTGKPLHlVRDDELPGAVDNFRFFAGAARTLegpaaGEYLP-------GHTSMI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 210 LRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNyFVFKALREAGVPDGVVNFVPAEETTFASVVTQ 288
Cdd:cd07092 115 RREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTT-LLLAELAAEVLPPGVVNVVCGGGASAGDALVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 289 HPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVAcTIR-AAFEYAGQKCSSCSM 366
Cdd:cd07092 194 HPRVRMVSLTGsVRTGKKVA-RAAADTLK------RVHLELGGKAPVIVFDDADLDAAVA-GIAtAGYYNAGQDCTAACR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 367 LYVPESLWQnhirepllEITASLVVRQDAT-YCDSFCSAV-----INRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRR 439
Cdd:cd07092 266 VYVHESVYD--------EFVAALVEAVSAIrVGDPDDEDTemgplNSAAQRERV---AGFVERAPAhARVLTGGRRAEGP 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571806 440 GYYVDPTVVL-VKDLDNIIcREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQD 499
Cdd:cd07092 335 GYFYEPTVVAgVAQDDEIV-QEEIFGPVVTVQPFDD--EDEAIELANDVEYGLASSVWTRD 392
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
136-551 |
1.42e-21 |
|
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: 97.87 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 136 RIDIWERAAMLIAGRYRYNIIAATMLGqGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQ--NNCRNSMRLRGL 213
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREG-GKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTpaSAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 214 SGFVAAISPFNFtgiAANLA---YTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQh 289
Cdd:cd07148 125 IGVVVAISAFNH---PLNLIvhqVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 290 PKLAGINFTGTStvlKVLWQLVAQNInfyqnyP--RLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 367
Cdd:cd07148 201 PRVAFFSFIGSA---RVGWMLRSKLA------PgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 368 YVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWlryIDQSPS--CQILVGGscdKRRGYYV-D 444
Cdd:cd07148 272 FVPAEIADD-FAQRLAAAAEKLVV-GDPTDPDTEVGPLIRPREVDRVEEW---VNEAVAagARLLCGG---KRLSDTTyA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 445 PTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKs 523
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDD--LDEAIAQANSLPVAFQAAVFTKD---LDVALKAVRrLDATAVMVNDH- 417
|
410 420 430
....*....|....*....|....*....|..
gi 28571806 524 TGLMVGQQPFG----AGHMTGtsdklGTPHSL 551
Cdd:cd07148 418 TAFRVDWMPFAgrrqSGYGTG-----GIPYTM 444
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
215-540 |
5.85e-21 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 96.80 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:PLN02466 277 KLAFTGSTDTGKIVLELAAKS-----NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WqnhirEPLLEITASLVVRQdaTYCDSFCSAV-----INRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKRRGYYVDPT 446
Cdd:PLN02466 352 Y-----DEFVEKAKARALKR--VVGDPFKKGVeqgpqIDSEQFEKI---LRYIKSgvESGATLECGGDRFGSKGYYIQPT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 447 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVN---VGNLNVNDK 522
Cdd:PLN02466 422 VFSnVQD-DMLIAQDEIFGPVQSILKFKD--LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGtvwVNCFDVFDA 498
|
330
....*....|....*...
gi 28571806 523 STglmvgqqPFGAGHMTG 540
Cdd:PLN02466 499 AI-------PFGGYKMSG 509
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
215-514 |
6.27e-21 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 96.34 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNInfyqnypRLVG-EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPES 372
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMV-------KPVSlELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHER 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 373 lwqnhIREPLLEitaSLVVRQDA-TYCDSF---C--SAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDK--RRGYY 442
Cdd:PLN02467 306 -----IASEFLE---KLVKWAKNiKISDPLeegCrlGPVVSEGQYEKV---LKFIStaKSEGATILCGGKRPEhlKKGFF 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571806 443 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNV 514
Cdd:PLN02467 375 IEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGI 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
215-542 |
1.35e-20 |
|
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: 94.59 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIaanLAYTPAL----MGNSVIWKPSD-----SAILSNyFVFKALREAGVpdGVVNFVPAEETTfasV 285
Cdd:cd07135 110 GVVLIIGPWNYPVL---LALSPLVgaiaAGCTVVLKPSEltphtAALLAE-LVPKYLDPDAF--QVVQGGVPETTA---L 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 286 VTQhpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCS 365
Cdd:cd07135 181 LEQ--KFDKIFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 366 MLYVPESLWQNHIREplLEITASLVVRQDATYCDSFcSAVINRRAYDRIymwLRYIDQSPScQILVGGSCDKRRgYYVDP 445
Cdd:cd07135 253 YVLVDPSVYDEFVEE--LKKVLDEFYPGGANASPDY-TRIVNPRHFNRL---KSLLDTTKG-KVVIGGEMDEAT-RFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 446 TVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTG 525
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDD--LDEAIKVINSRDTPLALYIFTDDKSEIDHILT--RTRSGGVVINDTLIH 400
|
330
....*....|....*..
gi 28571806 526 LMVGQQPFGAghmTGTS 542
Cdd:cd07135 401 VGVDNAPFGG---VGDS 414
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
80-499 |
4.04e-19 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 90.71 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGQEFQAK--EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIA 157
Cdd:PRK13252 11 IDGAYVEATsgETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL--RERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 158 AT-MLGQGKTLRQAEM-------DVAE----LVDFMRINPVFLRELANY----EPIrdiqnncrnsmrlrglsGFVAAIS 221
Cdd:PRK13252 88 ALeTLDTGKPIQETSVvdivtgaDVLEyyagLAPALEGEQIPLRGGSFVytrrEPL-----------------GVCAGIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 222 PFNF-TGIAANLAyTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFAsVVTQHPKLAGINFTG 299
Cdd:PRK13252 151 AWNYpIQIACWKS-APALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGA-WLTEHPDIAKVSFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 300 TSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIr 379
Cdd:PRK13252 229 GVPTGKKVMAAAAASLK------EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 380 EPLLEITASLVV---RQDATycdSFcSAVINRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKR----RGYYVDPTVVL- 449
Cdd:PRK13252 302 ARLLERVERIRIgdpMDPAT---NF-GPLVSFAHRDKV---LGYIEKgkAEGARLLCGGERLTEggfaNGAFVAPTVFTd 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571806 450 VKDlDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQD 499
Cdd:PRK13252 375 CTD-DMTIVREEIFGPVMSVLTFDDED-----EVIARANDteyGLAAGVFTAD 421
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
114-534 |
1.78e-18 |
|
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: 88.29 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 114 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLiagrYRYN------IIAATMlgqGKTLRQAEMDV---AELVDFMRIN 184
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADL----LRERkdelarLITLEM---GKPIAEARAEVekcAWICRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 185 -PVFL----RELA------NYEPIrdiqnncrnsmrlrglsGFVAAISPFNF-----TGIAAnlaytPALM-GNSVIWKP 247
Cdd:cd07100 74 aEAFLadepIETDagkayvRYEPL-----------------GVVLGIMPWNFpfwqvFRFAA-----PNLMaGNTVLLKH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 248 SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVtQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGE 327
Cdd:cd07100 132 ASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLK------KSVLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 328 GGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATYCDSFCSA 404
Cdd:cd07100 205 LGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEK-FVEAMAALKVgdpMDEDTDLGPLARK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 405 vinrRAYDRIymwLRYIDQSPS--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETME 482
Cdd:cd07100 284 ----DLRDEL---HEQVEEAVAagATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKD--EEEAIA 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 28571806 483 KVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDkstglMVGQQ---PFG 534
Cdd:cd07100 355 LANDSPFGLGGSVFTTDLERAERV--ARRLEAGMVFING-----MVKSDprlPFG 402
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
215-547 |
8.12e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 86.81 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDS----AILSNYFVFKALREAGVPDGVVNFVpAEETTFASVVTQH 289
Cdd:PLN02315 156 GIVGVITAFNFPCAVLGWNACIALVcGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLPGAIFTSF-CGGAEIGEAIAKD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 290 PKLAGINFTGTSTVlkvlWQLVAQNINfyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYV 369
Cdd:PLN02315 235 TRIPLVSFTGSSKV----GLMVQQTVN--ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 370 PESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSPSCQILVGGSCDKRRGYYVDPTVVL 449
Cdd:PLN02315 309 HESIYDDVL-EQLLTVYKQVKI-GDPLEKGTLLGPLHTPESKKNFEKGIEII-KSQGGKILTGGSAIESEGNFVQPTIVE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 450 VKDlDNIICREELLAPILgvYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVG 529
Cdd:PLN02315 386 ISP-DADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG 462
|
330
....*....|....*...
gi 28571806 530 qQPFGAGHMTGTSDKLGT 547
Cdd:PLN02315 463 -GAFGGEKATGGGREAGS 479
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
117-499 |
1.12e-17 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 86.28 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWER-AAMLIAGRyryNIIAATM-LGQGKTLRQAEMDVAELVDFMrinpvflrELANY 194
Cdd:PLN02278 67 AIASAHDAFPSWSKLTASERSKILRRwYDLIIANK---EDLAQLMtLEQGKPLKEAIGEVAYGASFL--------EYFAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 195 EPIR---DI----QNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAG 266
Cdd:PLN02278 136 EAKRvygDIipspFPDRR-LLVLKQPVGVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 267 VPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAV 346
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 347 ACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIYmwlRYI 421
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFA-EAFSKAVQKLVVG------DGFEEGVtqgplINEAAVQKVE---SHV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 422 DQ--SPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQI----NHGLTGSV 495
Cdd:PLN02278 359 QDavSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF------KTEEEAIAIandtEAGLAAYI 432
|
....
gi 28571806 496 FAQD 499
Cdd:PLN02278 433 FTRD 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
114-562 |
1.22e-17 |
|
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: 85.81 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 114 IQMAIDKSVEAQVKWDKVRLSDRidiweRAAMLIAGRYRYN----IIAATMLGQGKTLRQAE----MDVAELVDFM---- 181
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAER-----RKVLRSLLKYILEnqeeICRVACRDTGKTMVDASlgeiLVTCEKIRWTlkhg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 182 --------RINPVFL---RELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFT-------GIAANLAytpalmGNSV 243
Cdd:cd07098 95 ekalrpesRPGGLLMfykRARVEYEPL-----------------GVVGAIVSWNYPfhnllgpIIAALFA------GNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 244 IWKPSDSAILSNYF----VFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyq 319
Cdd:cd07098 152 VVKVSEQVAWSSGFflsiIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 320 nyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEITASLV--VRQDATY 397
Cdd:cd07098 228 --P-VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEK-----IYDKLLEILTDRVqaLRQGPPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 398 CDSF-CSAVINRRAYDRIYMWLRyiDQSPS-CQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYV 471
Cdd:cd07098 300 DGDVdVGAMISPARFDRLEELVA--DAVEKgARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 472 YPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGtSDKLGTPHSL 551
Cdd:cd07098 378 ASD--DEEAVEIANSTEYGLGASVFGKDIKRARRI--ASQLETGMVAINDFGVNYYVQQLPFGGVKGSG-FGRFAGEEGL 452
|
490
....*....|.
gi 28571806 552 LRWTSPQVIKE 562
Cdd:cd07098 453 RGLCNPKSVTE 463
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
215-534 |
3.18e-17 |
|
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: 84.11 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSDSA---------ILSNYFVFKALReagvpdgVVNfVPAEETT 281
Cdd:cd07087 102 GVVLIIGPWNY---PLQLALAPligAIAaGNTVVLKPSELApatsallakLIPKYFDPEAVA-------VVE-GGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 282 fasVVTQHPkLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKC 361
Cdd:cd07087 171 ---ALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 362 SSCSMLYVPESlwqnhIREPLLE-ITASLV------VRQDATYcdsfcSAVINRRAYDRIymwLRYIDQSpscQILVGGS 434
Cdd:cd07087 241 IAPDYVLVHES-----IKDELIEeLKKAIKefygedPKESPDY-----GRIINERHFDRL---ASLLDDG---KVVIGGQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 435 CDKRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNV 514
Cdd:cd07087 305 VDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDD--LDEAIEFINSRPKPLALYLFSEDKAVQERVLA--ETSS 379
|
330 340
....*....|....*....|
gi 28571806 515 GNLNVNDKSTGLMVGQQPFG 534
Cdd:cd07087 380 GGVCVNDVLLHAAIPNLPFG 399
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
207-499 |
4.13e-17 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 84.19 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 207 SMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAgVPDGVVNFVPAEETTFASV 285
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 286 VTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSC 364
Cdd:PRK13473 211 LVGHPKVRMVSLTGsIATGKHVL-SAAADSVK------RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 365 SMLYVPESLWQNHIrEPLLEITASLVV-RQDATycDSFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKRRGYYV 443
Cdd:PRK13473 284 CRIYAQRGIYDDLV-AKLAAAVATLKVgDPDDE--DTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYY 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28571806 444 DPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQD 499
Cdd:PRK13473 361 EPTLLAGARQDDEIVQREVFGPVVSVTPFDDED-----QAVRWANdsdYGLASSVWTRD 414
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
215-546 |
1.13e-16 |
|
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: 82.93 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFT------GIAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQ 288
Cdd:cd07140 149 GVCGIVIPWNYPlmmlawKMAACLA-----AGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 289 HPKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLY 368
Cdd:cd07140 224 HPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 369 VPESLWQNHIREPLLEItaslvvrQDATYCDSFCSAVI----NRRAY-DRIymwLRYIDQS--PSCQILVGGSCDKRRGY 441
Cdd:cd07140 299 VEESIHDEFVRRVVEEV-------KKMKIGDPLDRSTDhgpqNHKAHlDKL---VEYCERGvkEGATLVYGGKQVDRPGF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 442 YVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQN---FIEEAYDAFRVNVGNLN 518
Cdd:cd07140 369 FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINkalYVSDKLEAGTVFVNTYN 448
|
330 340
....*....|....*....|....*...
gi 28571806 519 VNDKSTglmvgqqPFGAGHMTGTSDKLG 546
Cdd:cd07140 449 KTDVAA-------PFGGFKQSGFGKDLG 469
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
215-534 |
2.38e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 82.00 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFtgiAANLAYTPAL----MGNSVIWKPSDSA---------ILSNYFVFKALR--EAGVPdgvvnfvpaeE 279
Cdd:PTZ00381 111 GVVLVIGAWNY---PLNLTLIPLAgaiaAGNTVVLKPSELSphtsklmakLLTKYLDPSYVRviEGGVE----------V 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 280 TTfasVVTQHPkLAGINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEY 356
Cdd:PTZ00381 178 TT---ELLKEP-FDHIFFTGSPRVGKLVMQAAAEN---------LTPctlELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 357 AGQKCSSCSMLYVPESlwqnhIREPLLEITASLVVRQ---DATYCDSFcSAVINRRAYDRIyMWLRYIDQSpscQILVGG 433
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRS-----IKDKFIEALKEAIKEFfgeDPKKSEDY-SRIVNEFHTKRL-AELIKDHGG---KVVYGG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 434 SCDKRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVN 513
Cdd:PTZ00381 315 EVDIEN-KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYEN--IDEVLEFINSRPKPLALYYFGEDKRHKELVLE--NTS 389
|
330 340
....*....|....*....|.
gi 28571806 514 VGNLNVNDKSTGLMVGQQPFG 534
Cdd:PTZ00381 390 SGAVVINDCVFHLLNPNLPFG 410
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
215-534 |
1.07e-14 |
|
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: 76.50 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETtfASVVTQHP 290
Cdd:cd07134 102 GVCLIISPWNY---PFNLAFGPlvsAIAaGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEV--AQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 291 kLAGINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 367
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAAKH---------LASvtlELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 368 YVPESlwqnhIREPLLEITASLVVRQ-----DATYCDSFCSaVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDKRRg 440
Cdd:cd07134 247 FVHES-----VKDAFVEHLKAEIEKFygkdaARKASPDLAR-IVNDRHFDRL---KGLLDDAVAkgAKVEFGGQFDAAQ- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 441 YYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKvaqINHG---LTGSVFAQDQNFIEEAYDafRVNVGNL 517
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYED--LDEVIEY---INAKpkpLALYVFSKDKANVNKVLA--RTSSGGV 389
|
330
....*....|....*..
gi 28571806 518 NVNDKSTGLMVGQQPFG 534
Cdd:cd07134 390 VVNDVVLHFLNPNLPFG 406
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
215-540 |
2.24e-14 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 75.71 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 293
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 294 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 373
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCAKDIK------KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 374 WqNHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYmwlRYIDQ--SPSCQILVGGSCDKRRGYYVDPTVVLVK 451
Cdd:PRK11241 302 Y-DRFAEKLQQAVSKLHI-GDGLEKGVTIGPLIDEKAVAKVE---EHIADalEKGARVVCGGKAHELGGNFFQPTILVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 452 DLDNIICREELLAPILgvyvyPDHKLKETMEKVAQINH---GLTGSVFAQDQNFIEEAYDAFRVNVGNLNvndksTGLMV 528
Cdd:PRK11241 377 PANAKVAKEETFGPLA-----PLFRFKDEADVIAQANDtefGLAAYFYARDLSRVFRVGEALEYGIVGIN-----TGIIS 446
|
330
....*....|...
gi 28571806 529 GQ-QPFGAGHMTG 540
Cdd:PRK11241 447 NEvAPFGGIKASG 459
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
117-501 |
2.67e-14 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 75.56 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 117 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATMLGQ-GKTLRQAEMDV---AELVDFMRINPVflRELA 192
Cdd:PLN00412 58 AMESAKAAQKAWAKTPLWKRAELLHKAAAIL--KEHKAPIAECLVKEiAKPAKDAVTEVvrsGDLISYTAEEGV--RILG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 193 NYEPIRD--IQNNCRNSMRLRGLS--GFVAAISPFNFtgiAANLAYT---PALM-GNSVIWKPSDSAILSNYFVFKALRE 264
Cdd:PLN00412 134 EGKFLVSdsFPGNERNKYCLTSKIplGVVLAIPPFNY---PVNLAVSkiaPALIaGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 265 AGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKvlwqlVAQNINFYQnyprLVGEGGGKNFHFVHSSAEPET 344
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIA-----ISKKAGMVP----LQMELGGKDACIVLEDADLDL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 345 AVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITASLVVRQDATYCDsfCSAVINRRAYDRIymwlryidqs 424
Cdd:PLN00412 282 AAANIIKGGFSYSGQRCTAVKVVLVMESV-ADALVEKVNAKVAKLTVGPPEDDCD--ITPVVSESSANFI---------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 425 pscQILVGGSCDK---------RRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYPDhkLKETMEKVAQINHG 490
Cdd:PLN00412 349 ---EGLVMDAKEKgatfcqewkREGNLIWPLL-----LDNVrpdmrIAWEEPFGPVLPVIRINS--VEEGIHHCNASNFG 418
|
410
....*....|.
gi 28571806 491 LTGSVFAQDQN 501
Cdd:PLN00412 419 LQGCVFTRDIN 429
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
80-511 |
2.11e-13 |
|
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: 72.87 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 80 INGqEFQAK---EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYNII 156
Cdd:cd07116 5 IGG-EWVAPvkgEYFDNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 157 AATmLGQGKTLRQA-EMDVAELVDFMRINPVFLRelANYEPIRDIQNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYT 235
Cdd:cd07116 83 AET-WDNGKPVRETlAADIPLAIDHFRYFAGCIR--AQEGSISEIDENTV-AYHFHEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 236 PALM-GNSVIWKPSDSAILSnYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQN 314
Cdd:cd07116 159 PALAaGNCVVLKPAEQTPAS-ILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 315 InfyqnYPRLVgEGGGK--NFHFVHSSAEPETAVACTIRAAFEYA---GQKCSSCSMLYVPESLWQNHIREPLLEITAsl 389
Cdd:cd07116 238 I-----IPVTL-ELGGKspNIFFADVMDADDAFFDKALEGFVMFAlnqGEVCTCPSRALIQESIYDRFMERALERVKA-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 390 vVRQ-----DATYCDSFCSAVinrrAYDRIymwLRYID--QSPSCQILVGG----SCDKRRGYYVDPTVVLvKDLDNIIC 458
Cdd:cd07116 310 -IKQgnpldTETMIGAQASLE----QLEKI---LSYIDigKEEGAEVLTGGerneLGGLLGGGYYVPTTFK-GGNKMRIF 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571806 459 REELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDQNfieEAYDAFR 511
Cdd:cd07116 381 QEEIFGPVLAVTTFKDE--EEALEIANDTLYGLGAGVWTRDGN---TAYRMGR 428
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
163-467 |
4.86e-12 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 68.62 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 163 QGKTLRQAEMDVAELVDFMRiNPVFLRELANYEPIRDIQNNCrNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GN 241
Cdd:PLN02419 201 QGKTLKDSHGDIFRGLEVVE-HACGMATLQMGEYLPNVSNGV-DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTcGN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 242 SVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTSTV-LKVLWQLVAQNinfyqn 320
Cdd:PLN02419 279 TFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDT-VNAICDDEDIRAVSFVGSNTAgMHIYARAAAKG------ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 321 yPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCS-MLYVPES-LWQNHI--REPLLEITAslvvrqdAT 396
Cdd:PLN02419 352 -KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALStVVFVGDAkSWEDKLveRAKALKVTC-------GS 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571806 397 YCDSFCSAVINRRAYDRIYMWLRY-IDQSPSC-----QILVGGScdkRRGYYVDPTVVLVKDLDNIICREELLAPIL 467
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSgVDDGAKLlldgrDIVVPGY---EKGNFIGPTILSGVTPDMECYKEEIFGPVL 497
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
215-504 |
1.53e-09 |
|
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: 60.60 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSD---------SAILSNYFvfkalreagvPDGVVNFVP--AEE 279
Cdd:cd07136 102 GVVLIIAPWNY---PFQLALAPligAIAaGNTAVLKPSEltpntskviAKIIEETF----------DEEYVAVVEggVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 280 TTFasvvTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 359
Cdd:cd07136 169 NQE----LLDQKFDYIFFTGSVRVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 360 KCSSCSMLYVPESlwqnhIREPLLEITASLVVRQ---DATYCDSFCSaVINRRAYDRIymwLRYIDQSpscQILVGGSCD 436
Cdd:cd07136 239 TCVAPDYVLVHES-----VKEKFIKELKEEIKKFygeDPLESPDYGR-IINEKHFDRL---AGLLDNG---KIVFGGNTD 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 437 KRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQNFIE 504
Cdd:cd07136 307 RET-LYIEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEK 371
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
215-574 |
2.34e-09 |
|
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: 59.82 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFT-GIAANLAYTPALMGNSVIWKpSDS--AILSNYFVfKALREAGVPDGVVNFVPAEETTFASVVTQ-HP 290
Cdd:cd07126 144 GPVAIITPFNFPlEIPALQLMGALFMGNKPLLK-VDSkvSVVMEQFL-RLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 291 KLagINFTGTSTVLKVLWQLVAQNINFyqnyprlvgEGGGKNFHFVHSSAEPETAVA--CTiRAAFEYAGQKCSSCSMLY 368
Cdd:cd07126 222 RM--TLFTGSSKVAERLALELHGKVKL---------EDAGFDWKILGPDVSDVDYVAwqCD-QDAYACSGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 369 VPEslwqNHIREPLLEITASLVVR---QDATYCDSFcsAVINRRAYDRIYMWLryidQSPSCQILVGG------SCDKRR 439
Cdd:cd07126 290 AHE----NWVQAGILDKLKALAEQrklEDLTIGPVL--TWTTERILDHVDKLL----AIPGAKVLFGGkpltnhSIPSIY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 440 GYYvDPTVVLVKdLDNIICRE-------ELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYdAFRV 512
Cdd:cd07126 360 GAY-EPTAVFVP-LEEIAIEEnfelvttEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVL-ANTV 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571806 513 N-VGNLNVNDKSTGlmvgqQP----FG-AGHMTGTSdkLGTphsllrwtsPQVIKESYKTHRNIFYPY 574
Cdd:cd07126 437 NgTTYAGIRARTTG-----APqnhwFGpAGDPRGAG--IGT---------PEAIRLVWSCHREIITDI 488
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
215-534 |
2.56e-09 |
|
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: 59.73 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFT----------GIAAnlaytpalmGNSVIWKPSD-----SAILSN----YFVFKALR--EAGVPDGvvn 273
Cdd:cd07137 103 GVVLVISAWNFPfllslepvigAIAA---------GNAVVLKPSElapatSALLAKlipeYLDTKAIKviEGGVPET--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 274 fvpaeettfaSVVTQHpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAA 353
Cdd:cd07137 171 ----------TALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRIAGGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 354 FEY-AGQKCSSCSMLYVPESLWQNHIRepLLEITASLVVRQDATYCDSFcSAVINRRAYDRIYMWLRyiDQSPSCQILVG 432
Cdd:cd07137 234 WGCnNGQACIAPDYVLVEESFAPTLID--ALKNTLEKFFGENPKESKDL-SRIVNSHHFQRLSRLLD--DPSVADKIVHG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 433 GSCDKRRgYYVDPTVVLVKDLDNIICREELLAPILgvyvyPDHKLKETMEKVAQIN---HGLTGSVFAQDQNFIEEAYDA 509
Cdd:cd07137 309 GERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLL-----PIITVKKIEESIEIINsrpKPLAAYVFTKNKELKRRIVAE 382
|
330 340
....*....|....*....|....*
gi 28571806 510 frVNVGNLNVNDKSTGLMVGQQPFG 534
Cdd:cd07137 383 --TSSGGVTFNDTVVQYAIDTLPFG 405
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
215-535 |
4.56e-07 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 52.74 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIaanLAYTPAL----MGNSVIWKPSDSAILSNYFVFKALrEAGVPDGVVNFVPAEETTFASVVTQhp 290
Cdd:PLN02174 114 GVVLVISAWNYPFL---LSIDPVIgaisAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 291 KLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFE-YAGQKCSSCSMLYV 369
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLT------PVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 370 PESLWQNHIREPLLEItASLVVRQDATYCDsfCSAVINRRAYDRIYMWLRyiDQSPSCQILVGGSCDkRRGYYVDPTVVL 449
Cdd:PLN02174 262 TKEYAPKVIDAMKKEL-ETFYGKNPMESKD--MSRIVNSTHFDRLSKLLD--EKEVSDKIVYGGEKD-RENLKIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 450 VKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVG 529
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNN--LEESFDVIRSRPKPLAAYLFTHNKKLKERF--AATVSAGGIVVNDIAVHLALH 411
|
....*.
gi 28571806 530 QQPFGA 535
Cdd:PLN02174 412 TLPFGG 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
258-557 |
2.20e-06 |
|
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: 50.23 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 258 VFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQN---INFYqnyprlvGEGGGKNFH 334
Cdd:cd07129 157 IRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepIPFY-------AELGSVNPV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 335 FVHSSAEPETAVActIRAAFEY-----AGQKCSSCSMLYVPESLWQnhirEPLLEITASLVVRQDAT------YCDSFCS 403
Cdd:cd07129 230 FILPGALAERGEA--IAQGFVGsltlgAGQFCTNPGLVLVPAGPAG----DAFIAALAEALAAAPAQtmltpgIAEAYRQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 404 AVINRRAydriymwlryidqSPSCQILVGGScDKRRGYYVDPTVVLVkDLDNIICREELLAPILG----VYVYPDHklkE 479
Cdd:cd07129 304 GVEALAA-------------APGVRVLAGGA-AAEGGNQAAPTLFKV-DAAAFLADPALQEEVFGpaslVVRYDDA---A 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 480 TMEKVAQINHG-LTGSVFA--QDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVG--QQ---PFGAghmtgTSDKLGT---P 548
Cdd:cd07129 366 ELLAVAEALEGqLTATIHGeeDDLALARELLPVLERKAGRLLFNGWPTGVEVCpaMVhggPYPA-----TTDPRFTsvgT 440
|
....*....
gi 28571806 549 HSLLRWTSP 557
Cdd:cd07129 441 AAIERFLRP 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
101-520 |
4.55e-06 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 49.47 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 101 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWER--AAMLIAGRYRYNIIAATMlgqGKTLRQAEMDVAE-- 176
Cdd:PRK13968 18 EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDigKALRARSEEMAQMITREM---GKPINQARAEVAKsa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 177 -LVD-FMRINPVFLrelaNYEPIrdIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAIL 253
Cdd:PRK13968 95 nLCDwYAEHGPAML----KAEPT--LVENQQAVIEYRPL-GTILAIMPWNFPLWQVMRGAVPILLaGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 254 SNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQhPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNF 333
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 334 HFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVV---RQDATYCDSFCSAVINRRA 410
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASA-FTERFVAAAAALKMgdpRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 411 YDRIYMWLryidqSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHG 490
Cdd:PRK13968 320 HHQVEATL-----AEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKD--AEHALELANDSEFG 392
|
410 420 430
....*....|....*....|....*....|
gi 28571806 491 LTGSVFAQDQNFIEEAydAFRVNVGNLNVN 520
Cdd:PRK13968 393 LSATIFTTDETQARQM--AARLECGGVFIN 420
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
215-373 |
2.53e-05 |
|
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: 46.83 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNY---FVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 291
Cdd:cd07077 102 GVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPFTNRalaLLFQAADAAHGPKILVLYVPHPSDELAEELLSHPK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 292 LAGINFTGTSTVLKVLWQlvaqninfYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYaGQKCSSCSMLYVPE 371
Cdd:cd07077 182 IDLIVATGGRDAVDAAVK--------HSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVD 252
|
..
gi 28571806 372 SL 373
Cdd:cd07077 253 DV 254
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
215-534 |
4.69e-04 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 43.18 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNFtgiAANLAYTPAL----MGNSVIWKPSD-----SAILSN----YFVFKALReagvpdgVVNFVPAeett 281
Cdd:PLN02203 110 GVVLIFSSWNF---PIGLSLEPLIgaiaAGNAVVLKPSElapatSAFLAAnipkYLDSKAVK-------VIEGGPA---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 282 FASVVTQHpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPRLVgEGGGKN---FHFVHSSAEPETAVACTIRAAFEY-A 357
Cdd:PLN02203 176 VGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLT-----PVAL-ELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 358 GQKCSSCSMLYVPESLWQNHIRepLLEITASLVVRQDATYCDSFCSaVINRRAYDRIYMWLRyiDQSPSCQILVGGSCDK 437
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIE--LLKSTIKKFFGENPRESKSMAR-ILNKKHFQRLSNLLK--DPRVAASIVHGGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 438 RRgYYVDPTVVLVKDLDNIICREELLAPILgvyvyPDHKLKETMEKVAQIN---HGLTGSVFAQDQNF----IEEAydaf 510
Cdd:PLN02203 324 KK-LFIEPTILLNPPLDSDIMTEEIFGPLL-----PIITVKKIEDSIAFINskpKPLAIYAFTNNEKLkrriLSET---- 393
|
330 340
....*....|....*....|....
gi 28571806 511 rvNVGNLNVNDKSTGLMVGQQPFG 534
Cdd:PLN02203 394 --SSGSVTFNDAIIQYACDSLPFG 415
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
215-534 |
6.19e-04 |
|
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: 42.47 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPFNF----------TGIAAnlaytpalmGNSVIWKPSDSAILSNYFVFKALREAGVPD--GVVNFVPAEETTF 282
Cdd:cd07133 103 GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAELLAEYFDEDevAVVTGGADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 283 ASVVTQHpklagINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 359
Cdd:cd07133 174 SSLPFDH-----LLFTGSTAVGRHVMRAAAEN---------LTPvtlELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 360 KCSSCSMLYVPESLwqnhiREPLLEITASLVVRQDATYCDSF-CSAVINRRAYDRIYMWL--------RYIDQSPSCQIL 430
Cdd:cd07133 240 TCVAPDYVLVPEDK-----LEEFVAAAKAAVAKMYPTLADNPdYTSIINERHYARLQGLLedarakgaRVIELNPAGEDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 431 VGGscdkRRgyyVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETmekVAQIN---HGLTGSVFAQD---QNFIE 504
Cdd:cd07133 315 AAT----RK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDS--LDEA---IDYINarpRPLALYYFGEDkaeQDRVL 382
|
330 340 350
....*....|....*....|....*....|..
gi 28571806 505 EaydafRVNVGNLNVNDksTGLMVGQ--QPFG 534
Cdd:cd07133 383 R-----RTHSGGVTIND--TLLHVAQddLPFG 407
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
215-380 |
3.65e-03 |
|
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: 39.94 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 215 GFVAAISPF-NFTGIAANLAYTPALMGNSVIWKP----SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQH 289
Cdd:cd07081 97 GVVASITPStNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571806 290 PKLAGINFTGTSTVLKVLwqlvaqninfYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYV 369
Cdd:cd07081 177 PGIGLLLATGGPAVVKAA----------YSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170
....*....|.
gi 28571806 370 PESLWQNHIRE 380
Cdd:cd07081 247 VDSVYDEVMRL 257
|
|
| |
