|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
45-565 |
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 28571800 45 VANEKLLQYDEGSKERTELETALLGVLNRVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 124
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 125 AQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMLGQGKTLRQAEMDVA-ELVDFMRINPVFLRELANYEPIrDIQN 203
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPL-SSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 204 NCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 283
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 284 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 363
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 364 SCSMLYVPESLWQNhIREPLLEITASLVVRQDATYcDSFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKRRGYY 443
Cdd:cd07123 320 AASRAYVPESLWPE-VKERLLEELKEIKMGDPDDF-SNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 444 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKVAQIN-HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVND 522
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALRNAAGNFYIND 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 28571800 523 KSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESY 565
Cdd:cd07123 478 KPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
46-577 |
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 28571800 46 ANEKLLQYDEGSKERTELETALLGVLNRVEHVPIVINGQE-FQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 124
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEvYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 125 AQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMLGQGKTLRQAEMD-VAELVDFMRINPVFLRELANYEPIRDiqN 203
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDaVAELIDFFRFNVKYARELYAQQPISA--P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 204 NCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 283
Cdd:TIGR01236 159 GEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 284 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 363
Cdd:TIGR01236 239 SDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 364 SCSMLYVPESLWQnHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIDQSPSC-QILVGGSCDKRRGY 442
Cdd:TIGR01236 319 AASRLYVPHSKWP-EFKSDLLAELQSVKV-GDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 443 YVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKV-AQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVN 521
Cdd:TIGR01236 397 FVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVdSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYIN 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 522 DKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESYKTHRNIFYPYMQ 577
Cdd:TIGR01236 477 DKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
73-565 |
2.61e-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: 2.61e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 73 RVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRY 152
Cdd:cd07083 15 FGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 153 RYNIIAATMLGqGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFT-GIAA 231
Cdd:cd07083 95 RELIATLTYEV-GKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGL-GAGVVISPWNFPvAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 232 NLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQL 311
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 312 VAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQnHIREPLLEITASLV 391
Cdd:cd07083 253 AARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE-PVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 392 VrQDATYCDSFCSAVINRRAYDRIYMWLRYIDQspSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVY 471
Cdd:cd07083 332 V-GPPEENGTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 472 VYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHS 551
Cdd:cd07083 409 RYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
490
....*....|....
gi 28571800 552 LLRWTSPQVIKESY 565
Cdd:cd07083 487 LRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
47-565 |
4.80e-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: 4.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 47 NEKLLQYDEGSKeRTELETALLGVLNRV-EHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEA 125
Cdd:cd07124 3 NEPFTDFADEEN-RAAFRAALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 126 QVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANY--EPIRDIqn 203
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFpvEMVPGE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 204 ncRNSMRLRGLsGFVAAISPFNF-TGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETT 282
Cdd:cd07124 159 --DNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 283 FASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKC 362
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 363 SSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYIDQSPSCQILVGG---SCDKR 439
Cdd:cd07124 316 SACSRVIVHESVYDEFL-ERLVERTKALKV-GDPEDPEVYMGPVIDKGARDRI---RRYIEIGKSEGRLLLGgevLELAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 440 RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLN 519
Cdd:cd07124 391 EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDTEYGLTGGVFSRSPEHLERARREFE--VGNLY 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 28571800 520 VNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVIKESY 565
Cdd:cd07124 467 ANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
75-565 |
4.56e-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: 4.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 75 EHVPIVINGQEFQAK--EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRy 152
Cdd:COG1012 4 PEYPLFIGGEWVAAAsgETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 153 RYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAAN 232
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYG-ETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 233 LAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQL 311
Cdd:COG1012 160 WKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 312 VAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQnHIREPLLEITASLV 391
Cdd:COG1012 240 AAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD-EFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 392 V---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSC-DKRRGYYVDPTVVLVKDLDNIICREELLA 465
Cdd:COG1012 313 VgdpLDPGT----DMGPLISEAQLERV---LAYIEDAVAegAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 466 PILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTGlMVGQQPFGAGHMTGTSDK 545
Cdd:COG1012 386 PVLSVIPFDD--EEEAIALANDTEYGLAASVFTRDLARARRVAR--RLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGRE 460
|
490 500
....*....|....*....|
gi 28571800 546 LGtPHSLLRWTSPQVIKESY 565
Cdd:COG1012 461 GG-REGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
97-561 |
5.02e-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: 5.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 97 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVA 176
Cdd:pfam00171 14 PAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEER-KDELAELETLENGKPLAEARGEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 177 ELVDFMRINPVFLRELanYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILS 255
Cdd:pfam00171 92 RAIDVLRYYAGLARRL--DGETLPSDPGRLAYTRREPL-GVVGAITPWNFPLLLPAWKIAPALAaGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 256 NYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFH 335
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 336 FVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRI 415
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIY-DEFVEKLVEAAKKLKV-GDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 416 ymwLRYIDQSPS--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLT 493
Cdd:pfam00171 321 ---LKYVEDAKEegAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKD--EEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 494 GSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVGqQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 561
Cdd:pfam00171 396 AGVFTSDLERALRV--ARRLEAGMVWINDYTTGDADG-LPFGGFKQSGFGREGG-PYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
118-561 |
5.28e-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: 5.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRinpvFLRELA--NY 195
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEVARAADTFR----YYAGLArrLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 EPIRDIQNNCRNSMRLRGLSGFVAAISPFNFTG--IAANLAytPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGV 272
Cdd:cd07078 78 GEVIPSPDPGELAIVRREPLGVVGAITPWNFPLllAAWKLA--PALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 273 VNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIR 352
Cdd:cd07078 156 LNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 353 AAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQ--SPS 427
Cdd:cd07078 230 GAFGNAGQVCTAASRLLVHESIYDEFVER-LVERVKALKVgnpLDPDT----DMGPLISAAQLDRV---LAYIEDakAEG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 428 CQILVGGSCDKR-RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQDQNF 503
Cdd:cd07078 302 AKLLCGGKRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEE-----EAIELANDteyGLAAGVFTRDLER 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 504 IEEAydAFRVNVGNLNVNDKSTGlMVGQQPFGAGHMTGTSdKLGTPHSLLRWTSPQVI 561
Cdd:cd07078 377 ALRV--AERLEAGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
71-565 |
3.51e-78 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 256.79 E-value: 3.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 71 LNRVE-----HVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAA 145
Cdd:PRK03137 26 LKKVEkelgqDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 146 MLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELVDFMRinpVFLRE---LANYEPIRDIQNNcRNSMRLRGLsGFVAAI 221
Cdd:PRK03137 106 AII--RRRKHEFSAWLvKEAGKPWAEADADTAEAIDFLE---YYARQmlkLADGKPVESRPGE-HNRYFYIPL-GVGVVI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 222 SPFNF-TGIAANLAYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG 300
Cdd:PRK03137 179 SPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 301 TSTVLKVLWQLVAQnINFYQNY-PRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHI 379
Cdd:PRK03137 259 SREVGLRIYERAAK-VQPGQIWlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVY-DEV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 380 REPLLEITASLVVRQDATycDSFCSAVINRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRRGYYVDPTVVLVKDLDNII 458
Cdd:PRK03137 337 LEKVVELTKELTVGNPED--NAYMGPVINQASFDKI---MSYIEIGKEeGRLVLGGEGDDSKGYFIQPTIFADVDPKARI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 459 CREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNDKSTGLMVGQQPFGAGH 538
Cdd:PRK03137 412 MQEEIFGPVVAFIKAKD--FDHALEIANNTEYGLTGAVISNNREHLEKARREFH--VGNLYFNRGCTGAIVGYHPFGGFN 487
|
490 500
....*....|....*....|....*..
gi 28571800 539 MTGTSDKLGTPHSLLRWTSPQVIKESY 565
Cdd:PRK03137 488 MSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
75-565 |
7.15e-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: 7.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 75 EHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMlIAGRYRY 154
Cdd:TIGR01237 31 KTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAA-IVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 155 NIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQNNCRNSMRLRglSGFVAAISPFNFT-GIAANL 233
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTP--TGVTVVISPWNFPfAIMVGM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 234 AYTPALMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVA 313
Cdd:TIGR01237 188 TVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 314 QNINFYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVR 393
Cdd:TIGR01237 268 KVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVY-DEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 394 QDATyCDSFCSAVINRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRRGYYVDPTVvlVKDLD--NIICREELLAPILGV 470
Cdd:TIGR01237 347 PPDS-ADVYVGPVIDQKSFNKI---MEYIEIGKAeGRLVSGGCGDDSKGYFIGPTI--FADVDrkARLAQEEIFGPVVAF 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 471 YVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPH 550
Cdd:TIGR01237 421 IRASD--FDEALEIANNTEYGLTGGVISNNRDHINRAKAEF--EVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPD 496
|
490
....*....|....*
gi 28571800 551 SLLRWTSPQVIKESY 565
Cdd:TIGR01237 497 YLALFMQAKTVTEMF 511
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
72-554 |
7.24e-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: 7.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 72 NRVEHVPIVINGQEfqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAG 150
Cdd:cd07125 29 KEWEAIPIINGEET--ETGEGAPVIdPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 151 RyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELaNYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNF---- 226
Cdd:cd07125 107 N-RGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQAREL-FSDPELPGPTGELNGLELHGR-GVFVCISPWNFplai 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 227 -TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG-TST 303
Cdd:cd07125 184 fTGqIAAALA-----AGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGsTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 304 vlkvlwqlvAQNINfyQNYP-------RLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQ 376
Cdd:cd07125 259 ---------AKLIN--RALAerdgpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 377 NhIREPLLEITASLVVrQDATYCDSFCSAVI------NRRAYDRIYM---WLryIDQSPScqilvggscDKRRGYYVDPT 447
Cdd:cd07125 328 R-FIEMLKGAMASLKV-GDPWDLSTDVGPLIdkpagkLLRAHTELMRgeaWL--IAPAPL---------DDGNGYFVAPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 vvlVKDLDNIIC-REELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTG 526
Cdd:cd07125 395 ---IIEIVGIFDlTTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRE--RVEAGNLYINRNITG 469
|
490 500
....*....|....*....|....*...
gi 28571800 527 LMVGQQPFGAGHMTGTSDKLGTPHSLLR 554
Cdd:cd07125 470 AIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
120-561 |
1.55e-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: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 120 DKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELAnYEPIR 199
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLG-GPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 200 DIQNNCRNSMRLRGLsGFVAAISPFNFTG--IAANLAytPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFV 276
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFPLllAAWKLA--PALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 277 PAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnyPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFE 356
Cdd:cd06534 156 PGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 357 YAGQKCSSCSMLYVPESLWQnhirepllEITASLVvrqdatycdsfcsavinrraydriymwlryidqspscqilvggsc 436
Cdd:cd06534 230 NAGQICTAASRLLVHESIYD--------EFVEKLV--------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 437 dkrrgyyvdpTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETmekVAQINH---GLTGSVFAQDQNFIEEAydAFRV 513
Cdd:cd06534 257 ----------TVLVDVDPDMPIAQEEIFGPVLPVIRFKD--EEEA---IALANDteyGLTAGVFTRDLNRALRV--AERL 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571800 514 NVGNLNVNDKSTGLMVgQQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 561
Cdd:cd06534 320 RAGTVYINDSSIGVGP-EAPFGGVKNSGIGREGG-PYGLEEYTRTKTV 365
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
59-561 |
4.33e-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: 4.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 59 ERTELETALLGVLNRVEHVPIVINGQEfqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDR 137
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAAPLIAGEA--ASGEARPVRnPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 138 IDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANyepirDIQNNCRNSMRLRGLsGF 217
Cdd:COG4230 618 AAILERAADLLEAH-RAELMALLVREAGKTLPDAIAEVREAVDF-------CRYYAA-----QARRLFAAPTVLRGR-GV 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 218 VAAISPFN-----FTG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHP 291
Cdd:COG4230 684 FVCISPWNfplaiFTGqVAAALA-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADP 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 292 KLAGINFTGtSTVlkvlwqlVAQNINfyqnypR-----------LVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 360
Cdd:COG4230 759 RIAGVAFTG-STE-------TARLIN------RtlaardgpivpLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQ 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 361 KCSSCSMLYVPEslwqnHIREPLLEI----TASLVV---RQDATycDsfCSAVINRRAYDRIymwLRYIDQ-----SPSC 428
Cdd:COG4230 825 RCSALRVLCVQE-----DIADRVLEMlkgaMAELRVgdpADLST--D--VGPVIDAEARANL---EAHIERmraegRLVH 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 429 QILVGGSCDKrrGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETmekVAQINH---GLTGSVFAQDQNFIE 505
Cdd:COG4230 893 QLPLPEECAN--GTFVAPTLIEIDSISDL--EREVFGPVLHVVRYKADELDKV---IDAINAtgyGLTLGVHSRIDETID 965
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 506 EAYDafRVNVGNLNVNDKSTGLMVGQQPFGaGH-MTGTSDKLGTPHSLLRWTSPQVI 561
Cdd:COG4230 966 RVAA--RARVGNVYVNRNIIGAVVGVQPFG-GEgLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
45-559 |
1.43e-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: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 45 VANEKLLQydegskertELETALLGVLNRVEHVPIVINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVE 124
Cdd:TIGR01238 15 LDNESELK---------PLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 125 AQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANyePIRDIQNN 204
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNAIAEVREAVDF-------CRYYAK--QVRDVLGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 205 crNSMRLRGLsgfVAAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPA 278
Cdd:TIGR01238 156 --FSVESRGV---FVCISPWNFplaifTGqISAALA-----AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 279 EETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYA 358
Cdd:TIGR01238 226 RGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED---APVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 359 GQKCSSCSMLYVPESLWQ---NHIREPLLEITASLVVRQDATycdsfCSAVINRRAYDRIymwLRYID-----QSPSCQI 430
Cdd:TIGR01238 303 GQRCSALRVLCVQEDVADrvlTMIQGAMQELKVGVPHLLTTD-----VGPVIDAEAKQNL---LAHIEhmsqtQKKIAQL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 431 LVGGSCDKRRGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQdqnfIEEAYDA 510
Cdd:TIGR01238 375 TLDDSRACQHGTFVAPTLFELDDIAEL--SEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSR----IETTYRW 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 28571800 511 F--RVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQ 559
Cdd:TIGR01238 449 IekHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
57-561 |
1.45e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 188.48 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 57 SKERTELETALLGVLNRVEHVPIVINGqefqaKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLS 135
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVsPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 136 DRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMR----------INPVFLR----Elanyepirdi 201
Cdd:PRK11904 608 ERAAILERAADLLEAN-RAELIALCVREAGKTLQDAIAEVREAVDFCRyyaaqarrlfGAPEKLPgptgE---------- 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 202 qnncRNSMRLRGLSGFVAaISPFNF-----TG-IAAnlaytpALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVN 274
Cdd:PRK11904 677 ----SNELRLHGRGVFVC-ISPWNFplaifLGqVAA------ALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQ 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 275 FVPAEETTFASVVTQHPKLAGINFTGtSTVlkvlwqlVAQNINfyqnypR-----------LVGEGGGKNFHFVHSSAEP 343
Cdd:PRK11904 746 LLPGDGATVGAALTADPRIAGVAFTG-STE-------TARIIN------RtlaardgpivpLIAETGGQNAMIVDSTALP 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 344 ETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEI----TASLVV---RQDATycDsfCSAVINRRAYDRIy 416
Cdd:PRK11904 812 EQVVDDVVTSAFRSAGQRCSALRVLFVQED-----IADRVIEMlkgaMAELKVgdpRLLST--D--VGPVIDAEAKANL- 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 417 mwLRYIDQSPS-----CQILVGGSCDKrrGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPdhklKETMEKV-AQINH 490
Cdd:PRK11904 882 --DAHIERMKRearllAQLPLPAGTEN--GHFVAPTAFEIDSISQL--EREVFGPILHVIRYK----ASDLDKViDAINA 951
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571800 491 ---GLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVI 561
Cdd:PRK11904 952 tgyGLTLGIHSRIEETADRIAD--RVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
80-535 |
6.26e-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: 6.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 80 VINGQEFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYniIAA 159
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE--LAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 160 TM-LGQGKTLRQAEMDVAELVDFMRinpvFLRELANYEPIRDIQNNCRNSM--RLRGLSGFVAAISPFNF-TGIAA-NLA 234
Cdd:cd07097 82 LLtREEGKTLPEARGEVTRAGQIFR----YYAGEALRLSGETLPSTRPGVEveTTREPLGVVGLITPWNFpIAIPAwKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 235 ytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVA 313
Cdd:cd07097 158 --PALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 314 QNINFYQnyprlvGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwqnHIR--EPLLEITASLV 391
Cdd:cd07097 236 ARGARVQ------LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGI---HDRfvEALVERTKALK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 392 VrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKR--RGYYVDPTVVLVKDLDNIICREELLAPI 467
Cdd:cd07097 307 V-GDALDEGVDIGPVVSERQLEKD---LRYIEiaRSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPV 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571800 468 LGVYVYPDhkLKETMEKVAQINHGLTGSVFAQD----QNFIEeaydafRVNVGNLNVNDKSTGLMVgQQPFG 535
Cdd:cd07097 383 AAVIRVRD--YDEALAIANDTEFGLSAGIVTTSlkhaTHFKR------RVEAGVVMVNLPTAGVDY-HVPFG 445
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
61-558 |
2.81e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 163.88 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 61 TELETALLGVLNRVEHV-PIVINGQefqAKEDFQQVL-PYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRI 138
Cdd:PRK11905 539 AALDEALNAFAAKTWHAaPLLAGGD---VDGGTRPVLnPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERA 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 139 DIWERAAMLIAGRYRYnIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRdiqnnCRnsmrlrglsGFV 218
Cdd:PRK11905 616 AILERAADLMEAHMPE-LFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHK-----PL---------GPV 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 219 AAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 292
Cdd:PRK11905 681 VCISPWNFplaifTGqIAAALV-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 293 LAGINFTGTSTVLKVLWQLVAQNINfyQNYPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVpe 372
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSG--PPVP-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCL-- 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 373 slwQNHIREPLLEI----TASLVV-RQDATYCDSfcSAVINRRAYDRIymwLRYIDQSPSC-----QILVGGSCDKrrGY 442
Cdd:PRK11905 831 ---QEDVADRVLTMlkgaMDELRIgDPWRLSTDV--GPVIDAEAQANI---EAHIEAMRAAgrlvhQLPLPAETEK--GT 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 443 YVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETmekVAQIN---HGLTGSVFAQDQNFIEEAYDafRVNVGNLN 519
Cdd:PRK11905 901 FVAPTLIEIDSISDL--EREVFGPVLHVVRFKADELDRV---IDDINatgYGLTFGLHSRIDETIAHVTS--RIRAGNIY 973
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 28571800 520 VNDKSTGLMVGQQPFGaGH-MTGTSDKLGTPHSLLRWTSP 558
Cdd:PRK11905 974 VNRNIIGAVVGVQPFG-GEgLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
97-535 |
1.21e-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: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 97 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYR--YNIIAATmlgQGKTLRQAEMD 174
Cdd:cd07094 6 PYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEefAKIIACE---GGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 175 VAELVDFMRINPVFLRELANYEPIRDIQ--NNCRNSMRLRGLSGFVAAISPFNF--TGIAANLAytPAL-MGNSVIWKPS 249
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATqgSDNRLAWTIREPVGVVLAITPFNFplNLVAHKLA--PAIaTGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 250 DSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTStvlKVLWQLVAQninfyQNYPRLVGEG 329
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSA---AVGEALRAN-----AGGKRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 330 GGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDSFCSAVINR 409
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELY-DEFIEAFVAAVKKLKV-GDPLDEDTDVGPLISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 410 RAYDRIYMWL-RYIDQspSCQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQI 488
Cdd:cd07094 310 EAAERVERWVeEAVEA--GARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDD--FEEAIRIANST 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571800 489 NHGLTGSVFAQDQNfieEAYDAF-RVNVGNLNVNDkSTGLMVGQQPFG 535
Cdd:cd07094 383 DYGLQAGIFTRDLN---VAFKAAeKLEVGGVMVND-SSAFRTDWMPFG 426
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
81-556 |
1.24e-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: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQ--EFQAKEDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYryNIIA 158
Cdd:cd07131 3 IGGEwvDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRK--EELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 159 ATMLGQ-GKTLRQAEMDVAELVDFMRIN---------PVFLRELANyepirdiqnncRNSMRLRGLSGFVAAISPFNFTG 228
Cdd:cd07131 81 RLVTREmGKPLAEGRGDVQEAIDMAQYAagegrrlfgETVPSELPN-----------KDAMTRRQPIGVVALITPWNFPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 229 IAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAE-ETTFASVVtQHPKLAGINFTGTSTVLK 306
Cdd:cd07131 150 AIPSWKIFPALVcGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRgEEVGEALV-EHPDVDVVSFTGSTEVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 307 VLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEI 386
Cdd:cd07131 229 RIGETCARPNK------RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKR-FVER 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 387 TASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICR 460
Cdd:cd07131 302 AKRLRV-GDGLDEETDMGPLINEAQLEKV---LNYNEigKEEGATLLLGGErltgGGYEKGYFVEPTVFTDVTPDMRIAQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 461 EELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNfieEAYDAFR-VNVGNLNVNDKSTGLMVgQQPFGAGHM 539
Cdd:cd07131 378 EEIFGPVVALIEVSS--LEEAIEIANDTEYGLSSAIYTEDVN---KAFRARRdLEAGITYVNAPTIGAEV-HLPFGGVKK 451
|
490
....*....|....*..
gi 28571800 540 TGTSDKLGTPHSLLRWT 556
Cdd:cd07131 452 SGNGHREAGTTALDAFT 468
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
110-543 |
4.09e-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: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 110 AHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATMLGQ-GKTLRQAEMDVAELVDFMRINPVF 188
Cdd:cd07145 18 LSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELI--ERRKEELAKLLTIEvGKPIKQSRVEVERTIRLFKLAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 189 LREL-ANYEPIRDIQNNCRN-SMRLRGLSGFVAAISPFNFtgiAANL---AYTPAL-MGNSVIWKPSDSAILSNYFVFKA 262
Cdd:cd07145 96 AKVLrGETIPVDAYEYNERRiAFTVREPIGVVGAITPFNF---PANLfahKIAPAIaVGNSVVVKPSSNTPLTAIELAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 263 LREAGVPDGVVNFVPAE-ETTFASVVTqHPKLAGINFTGTSTVLKvlwQLVAQNINFYQnypRLVGEGGGKNFHFVHSSA 341
Cdd:cd07145 173 LEEAGLPPGVINVVTGYgSEVGDEIVT-NPKVNMISFTGSTAVGL---LIASKAGGTGK---KVALELGGSDPMIVLKDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 342 EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYmwlRY 421
Cdd:cd07145 246 DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKL-LVEKVKKLKV-GDPLDESTDLGPLISPEAVERME---NL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 422 IDQSPS--CQILVGGSCDKrrGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKETMEKVAQIN---HGLTGSV 496
Cdd:cd07145 321 VNDAVEkgGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIA-----KVKDDEEAVEIANsteYGLQASV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571800 497 FAQDqnfIEEAYD-AFRVNVGNLNVNDkSTGLMVGQQPFGAGHMTGTS 543
Cdd:cd07145 394 FTND---INRALKvARELEAGGVVIND-STRFRWDNLPFGGFKKSGIG 437
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
118-554 |
9.18e-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: 9.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRyniiaaTMLG-----QGKTLRQAEMDVAELVDFmrinpvfLREL 192
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEAQMQ------TLMGllvreAGKTFSNAIAEVREAVDF-------LRYY 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 193 ANyePIRDIQNNCRNsmrlRGLsGFVAAISPFNF-----TG-IAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREA 266
Cdd:PRK11809 754 AG--QVRDDFDNDTH----RPL-GPVVCISPWNFplaifTGqVAAALA-----AGNSVLAKPAEQTPLIAAQAVRILLEA 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 267 GVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfYQNYP-RLVGEGGGKNFHFVHSSAEPET 345
Cdd:PRK11809 822 GVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLD-PQGRPiPLIAETGGQNAMIVDSSALTEQ 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 346 AVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITASLVV-RQDATYCDsfCSAVINRRAYDRIymwLRYIDQ 424
Cdd:PRK11809 901 VVADVLASAFDSAGQRCSALRVLCLQDDV-ADRTLKMLRGAMAECRMgNPDRLSTD--IGPVIDAEAKANI---ERHIQA 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 425 -----SPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIicREELLAPILGVYVYPDHKLKETMEkvaQIN---HGLTGSV 496
Cdd:PRK11809 975 mrakgRPVFQAARENSEDWQSGTFVPPTLIELDSFDEL--KREVFGPVLHVVRYNRNQLDELIE---QINasgYGLTLGV 1049
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 497 FAQdqnfIEE--AYDAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLR 554
Cdd:PRK11809 1050 HTR----IDEtiAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
118-561 |
8.13e-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: 8.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAAT-MLGQGKTLRQAEMDVAELVDFMRinpvFLRELA--- 193
Cdd:cd07088 40 AVDAAEAAQKAWERLPAIERAAYLRKLADLI--RENADELAKLiVEEQGKTLSLARVEVEFTADYID----YMAEWArri 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 194 NYEPIR-DIQNncRNSMRLRGLSGFVAAISPFNFTG--IAANLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVP 269
Cdd:cd07088 114 EGEIIPsDRPN--ENIFIFKVPIGVVAGILPWNFPFflIARKLA--PALVtGNTIVIKPSEETPLNALEFAELVDEAGLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 270 DGVVNFVPAEETTFASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 348
Cdd:cd07088 190 AGVLNIVTGRGSVVGDALVAHPKVGMISLTGsTEAGQKIM-EAAAENIT------KVSLELGGKAPAIVMKDADLDLAVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 349 CTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIY-MWLRYIDQspS 427
Cdd:cd07088 263 AIVDSRIINCGQVCTCAERVYVHEDIYDEFM-EKLVEKMKAVKV-GDPFDAATDMGPLVNEAALDKVEeMVERAVEA--G 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 428 CQILVGGS-CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEE 506
Cdd:cd07088 339 ATLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSS--LDEAIELANDSEYGLTSYIYTENLNTAMR 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 507 AYDafRVNVGNLNVNDKSTGLMvgqQPFGAG-HMTGTSDKLGtPHSLLRWTSPQVI 561
Cdd:cd07088 417 ATN--ELEFGETYINRENFEAM---QGFHAGwKKSGLGGADG-KHGLEEYLQTKVV 466
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
97-542 |
1.97e-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: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 97 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAEMDVA 176
Cdd:cd07149 6 PYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE-ERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 177 ELVDFMRINPVFLRELA----NYEPIRDIQNncRNSMRLRGLSGFVAAISPFNFtgiAANLA---YTPALM-GNSVIWKP 248
Cdd:cd07149 84 RAIETLRLSAEEAKRLAgetiPFDASPGGEG--RIGFTIREPIGVVAAITPFNF---PLNLVahkVGPAIAaGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 249 SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTV---------LKvlwqlvaqninfy 319
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVgeaiarkagLK------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 320 qnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVV---RQDA 396
Cdd:cd07149 226 ----KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIY-DEFLERFVAATKKLVVgdpLDED 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 397 TycdsFCSAVINRRAYDRIYMWLR-YIDQSPScqILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPIlgVYVYPD 475
Cdd:cd07149 301 T----DVGPMISEAEAERIEEWVEeAVEGGAR--LLTGG---KRDGAILEPTVLTDVPPDMKVVCEEVFAPV--VSLNPF 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 476 HKLKETMEKVAQINHGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTgLMVGQQPFGAGHMTGT 542
Cdd:cd07149 370 DTLDEAIAMANDSPYGLQAGVFTND---LQKALKAAReLEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
78-524 |
3.45e-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: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 78 PIVINGQEFQAKEDFQQVL-PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDK-VRLSDRIDIWERAAMLIAgRYRYN 155
Cdd:cd07082 3 KYLINGEWKESSGKTIEVYsPID-GEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLK-ENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 156 IIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyEPIR-DIQNNCRNSMRL--RGLSGFVAAISPFNFtgiAAN 232
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDG-DSLPgDWFPGTKGKIAQvrREPLGVVLAIGPFNY---PLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 233 LAYT---PAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVL 308
Cdd:cd07082 157 LTVSkliPALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 309 WQLVAQNinfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITA 388
Cdd:cd07082 237 KKQHPMK--------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESV-ADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 389 SLVV---RQDATycdsFCSAVINRRAYDRIYmwlRYID--QSPSCQILVGGscdKRRGY-YVDPTVVLVKDLDNIICREE 462
Cdd:cd07082 308 KLKVgmpWDNGV----DITPLIDPKSADFVE---GLIDdaVAKGATVLNGG---GREGGnLIYPTLLDPVTPDMRLAWEE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571800 463 LLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFrvNVGNLNVNDKS 524
Cdd:cd07082 378 PFGPVLPIIRVND--IEEAIELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINSKC 435
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
118-535 |
7.53e-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: 7.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagryRYNIIAatmLGQ------GKTLRQAEMDVAELVD---FM-----R 183
Cdd:cd07086 40 AVAAAREAFKEWRKVPAPRRGEIVRQIGEAL----RKKKEA---LGRlvslemGKILPEGLGEVQEMIDicdYAvglsrM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 184 IN-PVFLRELANYepirdiqnncRNSMRLRGLsGFVAAISPFNF-TGIAA-NLAytPALM-GNSVIWKPSDSAILSNY-- 257
Cdd:cd07086 113 LYgLTIPSERPGH----------RLMEQWNPL-GVVGVITAFNFpVAVPGwNAA--IALVcGNTVVWKPSETTPLTAIav 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 258 --FVFKALREAGVPDGVVNFVPAEeTTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFH 335
Cdd:cd07086 180 tkILAEVLEKNGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG------RVLLELGGNNAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 336 FVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRI 415
Cdd:cd07086 253 IVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDE-FLERLVKAYKQVRI-GDPLDEGTLVGPLINQAAVEKY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 416 ymwLRYID--QSPSCQILVGGSCDKRR--GYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQIN-- 489
Cdd:cd07086 331 ---LNAIEiaKSQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF------DSLEEAIAINnd 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 28571800 490 --HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVGqQPFG 535
Cdd:cd07086 402 vpQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIG-GAFG 448
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
118-557 |
1.79e-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: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAelvdFMrinPVFLRELAN--Y 195
Cdd:cd07150 26 AIAAAYDAFPAWAATTPSERERILLKAAEIMERR-ADDLIDLLIDEGGSTYGKAWFETT----FT---PELLRAAAGecR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 EPIRDIQNNCRN---SMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDG 271
Cdd:cd07150 98 RVRGETLPSDSPgtvSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 272 VVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTI 351
Cdd:cd07150 178 VFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLK------KITLELGGKNPLIVLADADLDYAVRAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 352 RAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATycdsFCSAVINRRAYDRIYmwlRYIDQSPS- 427
Cdd:cd07150 252 FGAFMHQGQICMSASRIIVEEPVYDEFVKK-FVARASKLKVgdpRDPDT----VIGPLISPRQVERIK---RQVEDAVAk 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 428 -CQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEE 506
Cdd:cd07150 324 gAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD--AEEALELANDTEYGLSAAILTND---LQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 507 AYD-AFRVNVGNLNVNDkSTGLMVGQQPFGAGHMTGTSdKLGTPHSL-----LRWTS 557
Cdd:cd07150 396 AFKlAERLESGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
101-535 |
7.48e-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: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 101 QQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELV 179
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI--RERAEDLARLLtLEQGKPLAEARGEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 180 DFM--------RINPVFL-------RELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFTgiAANLAY--TPAL-MG 241
Cdd:cd07103 85 SFLewfaeearRIYGRTIpspapgkRILVIKQPV-----------------GVVAAITPWNFP--AAMITRkiAPALaAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 242 NSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqn 321
Cdd:cd07103 146 CTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 322 ypRLVGEGGGkNFHF-VHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCD 400
Cdd:cd07103 222 --RVSLELGG-NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEK-LVERVKKLKV-GNGLDEG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 401 SFCSAVINRRAYDRIymwLRYIDQSPSC--QILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhkl 478
Cdd:cd07103 297 TDMGPLINERAVEKV---EALVEDAVAKgaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPF----- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 479 kETMEKV-AQINH---GLTGSVFAQDQNfieeayDAFRV----NVGNLNVNdksTGLMVG-QQPFG 535
Cdd:cd07103 369 -DTEDEViARANDtpyGLAAYVFTRDLA------RAWRVaealEAGMVGIN---TGLISDaEAPFG 424
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
216-535 |
9.26e-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: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTqHPKLA 294
Cdd:cd07139 139 GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVR-HPGVD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07139 218 KVSFTGSTAAGRRIAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQnHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGscdKR-----RGYYVDPT 447
Cdd:cd07139 292 YD-EVVEALAAAVAALKV-GDPLDPATQIGPLASARQRERV---EGYIAkgRAEGARLVTGG---GRpagldRGWFVEPT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 VvlVKDLDN--IICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVN 521
Cdd:cd07139 364 L--FADVDNdmRIAQEEIFGPVLSVIPYDDED-----DAVRIANdsdYGLSGSVWTAD---VERGLAvARRIRTGTVGVN 433
|
330
....*....|....*
gi 28571800 522 dkstGLMVG-QQPFG 535
Cdd:cd07139 434 ----GFRLDfGAPFG 444
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
118-557 |
1.51e-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: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLRELANyep 197
Cdd:cd07104 5 AYAAAAAAQKAWAATPPQERAAILRKAAEILEER-RDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 198 iRDIQNNC--RNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPS-DSAILSNYFVFKALREAGVPDGVV 273
Cdd:cd07104 81 -EILPSDVpgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 274 NFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRA 353
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLK------KVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 354 AFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--C 428
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFV-EKLVAKAKALPVgdpRDPDT----VIGPLINERQVDRV---HAIVEDAVAagA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 429 QILVGGscdKRRGYYVDPTVVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEA 507
Cdd:cd07104 306 RLLTGG---TYEGLFYQPTVLSdVTP-DMPIFREEIFGPVAPVIPFDD--DEEAVELANDTEYGLSAAVFTRD---LERA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 508 YD-AFRVNVGNLNVNDkSTGLMVGQQPFGAghmTGTS--DKLGTPHSL-----LRWTS 557
Cdd:cd07104 377 MAfAERLETGMVHIND-QTVNDEPHVPFGG---VKASggGRFGGPASLeefteWQWIT 430
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
118-535 |
2.56e-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: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATM-LGQGKTLRQAEMDVAELVDfmRINpVFLRELANYE 196
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELL--KANKEELARLIsRETGKPLWEAQTEVAAMAG--KID-ISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 197 PIRDIQN-NCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVN 274
Cdd:cd07095 80 GERATPMaQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 275 FVPAEETTFASVVtQHPKLAGINFTGTSTVLKVLWQLVAqninfyqNYPR--LVGEGGGKNFHFVHSSAEPETAVACTIR 352
Cdd:cd07095 159 LVQGGRETGEALA-AHEGIDGLLFTGSAATGLLLHRQFA-------GRPGkiLALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 353 AAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVVRQ-DATycDSFCSAVINRRAYDRIYMwlryidqspSCQIL 431
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAKRLRIGApDAE--PPFMGPLIIAAAAARYLL---------AQQDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 432 VGGSCD-----KR---RGYYVDPTVVLVKDLDNIIcREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnf 503
Cdd:cd07095 300 LALGGEpllamERlvaGTAFLSPGIIDVTDAADVP-DEEIFGPLLQVYRYDD--FDEAIALANATRFGLSAGLLSDD--- 373
|
410 420 430
....*....|....*....|....*....|....
gi 28571800 504 iEEAYDAF--RVNVGNLNVNDKSTGlMVGQQPFG 535
Cdd:cd07095 374 -EALFERFlaRIRAGIVNWNRPTTG-ASSTAPFG 405
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
216-541 |
1.15e-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: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTgIAANLA-YTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKL 293
Cdd:cd07089 125 GVVAAITPWNFP-FFLNLAkLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 294 AGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPES 373
Cdd:cd07089 204 DMVSFTGSTAVGRRIMAQAAATLK------RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 374 lwqnhIREPLLEITASLV--VRQ-DATYCDSFCSAVINRRAYDRIymwLRYIDQ--SPSCQILVGGscdKR-----RGYY 443
Cdd:cd07089 278 -----RYDEVVEALAAAFeaLPVgDPADPGTVMGPLISAAQRDRV---EGYIARgrDEGARLVTGG---GRpagldKGFY 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 444 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQnfiEEAYD-AFRVNVGNLN 519
Cdd:cd07089 347 VEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD-----EAVRIANdsdYGLSGGVWSADV---DRAYRvARRIRTGSVG 418
|
330 340
....*....|....*....|..
gi 28571800 520 VNdkSTGLMVGQQPFGAGHMTG 541
Cdd:cd07089 419 IN--GGGGYGPDAPFGGYKQSG 438
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
119-562 |
1.31e-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: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 119 IDKSVEAQVK------WDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQ-AEMDVAELVDFMR-------- 183
Cdd:cd07091 43 VDAAVKAARAafetgwWRKMDPRERGRLLNKLADLIE-RDRDELAALESLDNGKPLEEsAKGDVALSIKCLRyyagwadk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 184 -------INPVFLrelaNY---EPIrdiqnncrnsmrlrglsGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSA 252
Cdd:cd07091 122 iqgktipIDGNFL----AYtrrEPI-----------------GVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 253 ILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGK 332
Cdd:cd07091 181 PLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS-----NLKKVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 333 NFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAY 412
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEK-FKARAEKRVV-GDPFDPDTFQGPQVSKAQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 413 DRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQIN 489
Cdd:cd07091 334 DKI---LSYIEsgKKEGATLLTGGERHGSKGYFIQPTVFTdVKD-DMKIAKEEIFGPVVTILKFKT--EDEVIERANDTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571800 490 HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdksTGLMVGQQ-PFGAGHMTGTSDKLGTpHSLLRWTSPQVIK 562
Cdd:cd07091 408 YGLAAGVFTKD---INKALRvSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFGRELGE-EGLEEYTQVKAVT 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
118-561 |
6.19e-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: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRidiweRAAML-IAGRYRYNI--IAA-TMLGQGKTLRQAEMDVAELVDFmrinpvfLRELA 193
Cdd:cd07106 24 AVAAAKAAFPGWSATPLEER-----RAALLaIADAIEANAeeLARlLTLEQGKPLAEAQFEVGGAVAW-------LRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 194 NYE-PIRDIQNN--CRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAgVP 269
Cdd:cd07106 92 SLDlPDEVIEDDdtRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLCTLKLGELAQEV-LP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 270 DGVVNFVPAEETtFASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 348
Cdd:cd07106 170 PGVLNVVSGGDE-LGPALTSHPDIRKISFTGsTATGKKVM-ASAAKTLK------RVTLELGGNDAAIVLPDVDIDAVAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 349 CTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSP 426
Cdd:cd07106 242 KLFWGAFINSGQVCAAIKRLYVHESIYDE-FCEALVALAKAAVV-GDGLDPGTTLGPVQNKMQYDKV---KELVEdaKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 427 SCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQnfiEE 506
Cdd:cd07106 317 GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSD--EDEVIARANDSEYGLGASVWSSDL---ER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 507 AYD-AFRVNVGNLNVNdKSTGLMVgQQPFGaGH-MTGTSDKLGtPHSLLRWTSPQVI 561
Cdd:cd07106 392 AEAvARRLEAGTVWIN-THGALDP-DAPFG-GHkQSGIGVEFG-IEGLKEYTQTQVI 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
97-521 |
7.55e-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: 125.82 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 97 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERA-AMLIAgryRYNIIAATMLGQ-GKTLRQA--E 172
Cdd:cd07102 3 PID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAA---NTDEIAEELTWQmGRPIAQAggE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 173 MD-VAELVDFM-RINPVFLRELANYEPirdiqNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPS 249
Cdd:cd07102 79 IRgMLERARYMiSIAEEALADIRVPEK-----DGFERYIRREPL-GVVLIIAPWNYPYLTAVNAVIPALLaGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 250 DSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQhPKLAGINFTGTSTVLKVLWQLVAqninfyqnyPRLVG-- 327
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIAD-PRIDHVSFTGSVAGGRAIQRAAA---------GRFIKvg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 328 -EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAV 406
Cdd:cd07102 223 lELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFV-EAFVAVVKGYKL-GDPLDPSTTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 407 INRRAYDRIymwLRYIDQSPS--CQILVGG---SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKET 481
Cdd:cd07102 301 VSARAADFV---RAQIADAIAkgARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIM-----KVKSD 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 28571800 482 MEKVAQIN---HGLTGSVFAQD----QNFIEEaydafrVNVGNLNVN 521
Cdd:cd07102 373 AEAIALMNdseYGLTASVWTKDiaraEALGEQ------LETGTVFMN 413
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
216-535 |
1.21e-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: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:cd07114 121 GVVAAITPWNSPLLLLAKKLAPALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07114 201 KIAFTGGTETGRHIARAAAENLA------PVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQNHIrEPLLEITASLVV---RQDATYCDSfcsaVINRRAYDRIymwLRYIDQSPS--CQILVGG----SCDKRRGYYVD 445
Cdd:cd07114 275 YDEFV-ERLVARARAIRVgdpLDPETQMGP----LATERQLEKV---ERYVARAREegARVLTGGerpsGADLGAGYFFE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 446 PTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQINH---GLTGSVFAQDQNfieeayDAFRV----NVGNL 518
Cdd:cd07114 347 PTILADVTNDMRIAQEEVFGPVLSV-----IPFDDEEEAIALANDseyGLAAGIWTRDLA------RAHRVaraiEAGTV 415
|
330
....*....|....*...
gi 28571800 519 NVND-KSTGLMVgqqPFG 535
Cdd:cd07114 416 WVNTyRALSPSS---PFG 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
97-535 |
2.39e-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: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 97 PYDiQQPIAHYGHAHRVLIQMAIDKSVEAqvkwdkVRLSDRIDIWERAAML--IAGRY--RYNIIAATM-LGQGKTLRQA 171
Cdd:cd07147 6 PYT-GEVVARVALAGPDDIEEAIAAAVKA------FRPMRALPAHRRAAILlhCVARLeeRFEELAETIvLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 172 EMDVAELVDFMRInpvflrelANYEPIR--------DI--QNNCRNSMRLRGLSGFVAAISPFNFtgiAANLA---YTPA 238
Cdd:cd07147 79 RGEVARAIDTFRI--------AAEEATRiygevlplDIsaRGEGRQGLVRRFPIGPVSAITPFNF---PLNLVahkVAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 239 L-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEeTTFASVVTQHPKLAGINFTGTStvlKVLWQLVAQnin 317
Cdd:cd07147 148 IaAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSP---AVGWDLKAR--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 318 fyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQ 394
Cdd:cd07147 221 --AGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSR-LVARVKALKTgdpKD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 395 DATycdsFCSAVINRRAYDRIYMWlryIDQSPS--CQILVGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYV 472
Cdd:cd07147 298 DAT----DVGPMISESEAERVEGW---VNEAVDagAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEP 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 473 YPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTgLMVGQQPFG 535
Cdd:cd07147 368 YDDFD-----EALAAVNdskFGLQAGVFTRD---LEKALRAWDeLEVGGVVINDVPT-FRVDHMPYG 425
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
102-535 |
2.78e-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: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 102 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSdridiwERAAML--IAGRYRYNiiaATMLGQ------GKTLRQAEM 173
Cdd:cd07107 8 QVLARVPAASAADVDRAVAAARAAFPEWRATTPL------ERARMLreLATRLREH---AEELALidaldcGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 174 DVAELVDFMRINPVFLRELANyepiRDIQNNCRN-SMRLRGLSGFVAAISPFN--FTGIAANLAyTPALMGNSVIWKPSD 250
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKG----ETIPVGGRNlHYTLREPYGVVARIVAFNhpLMFAAAKIA-APLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 251 SAILSNYFVFKALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGG 330
Cdd:cd07107 154 QAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 331 GKNFHFVHSSAEPETAVACTIRAA-FEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINR 409
Cdd:cd07107 227 GKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVL-ARVVERVAAIKV-GDPTDPATTMGPLVSR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 410 RAYDRIymwLRYID--QSPSCQILVGG----SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETME 483
Cdd:cd07107 305 QQYDRV---MHYIDsaKREGARLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 484 KVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKST---GLmvgqqPFG 535
Cdd:cd07107 380 QANGVEYGLTAAIWTND---ISQAHRtARRVEAGYVWINGSSRhflGA-----PFG 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
128-500 |
3.62e-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: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 128 KWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAE-MDVAELVDFMRinpvFLRELANYEPIRDI--QNN 204
Cdd:cd07093 34 GWSRMSPAERARILHKVADLIEAR-ADELALLESLDTGKPITLARtRDIPRAAANFR----FFADYILQLDGESYpqDGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 205 CRNSMrLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTF 283
Cdd:cd07093 109 ALNYV-LRQPVGVAGLITPWNLPLMLLTWKIAPALaFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 284 ASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCS 363
Cdd:cd07093 188 GAALVAHPDVDLISFTGETATGRTIMRAAAPNLK------PVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 364 SCSMLYVPESLWQNHIrEPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDK 438
Cdd:cd07093 262 AGSRILVQRSIYDEFL-ERFVERAKALKVgdpLDPDT----EVGPLISKEHLEKV---LGYVELARAegATILTGGGRPE 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 439 ----RRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQD 500
Cdd:cd07093 334 lpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAYVWTRD 397
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
81-547 |
9.66e-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: 9.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQEFQAK-EDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEA-QVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIA 158
Cdd:cd07113 4 IDGRPVAGQsEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 159 ATMLGQGKTLRQAEM-DVAELVDFMR-------------INPVF-LRELANYepirdiqnncrNSMRLRGLSGFVAAISP 223
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRyfagwatkingetLAPSIpSMQGERY-----------TAFTRREPVGVVAGIVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 224 FNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTS 302
Cdd:cd07113 152 WNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 303 TVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREP 382
Cdd:cd07113 231 ATGKKIGRQAASDLT------RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKF-DELVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 383 LLEITASLVV---RQDATYCDSFCsaviNRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNI 457
Cdd:cd07113 304 LKQALSSFQVgspMDESVMFGPLA----NQPHFDKV---CSYLDdaRAEGDEIVRGGEALAGEGYFVQPTLVLARSADSR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 458 ICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKStgLMVGQQP 533
Cdd:cd07113 377 LMREETFGPVVSFVPYEDEE-----ELIQLINdtpFGLTASVWTNN---LSKALRyIPRIEAGTVWVNMHT--FLDPAVP 446
|
490
....*....|....
gi 28571800 534 FGAGHMTGTSDKLG 547
Cdd:cd07113 447 FGGMKQSGIGREFG 460
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
142-548 |
1.72e-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: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 142 ERAAML--IAGRYRYNIIAATML---GQGKTLRQAEMDVAELVDFMRinpvFLRELAnyEPIRDIQNNCRN---SMRLRG 213
Cdd:cd07119 60 ERAALLfrIADKIREDAEELARLetlNTGKTLRESEIDIDDVANCFR----YYAGLA--TKETGEVYDVPPhviSRTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 214 LSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 292
Cdd:cd07119 134 PVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 293 LAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPE 372
Cdd:cd07119 214 VDLVSFTGGTATGRSIMRAAAGNVK------KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 373 SLWQNHIREpLLEITASLVVRQ--DAtycDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGscdKR-------RG 441
Cdd:cd07119 288 SIHDKFVAA-LAERAKKIKLGNglDA---DTEMGPLVSAEHREKV---LSYIQlgKEEGARLVCGG---KRptgdelaKG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 442 YYVDPTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQIN---HGLTGSVFAQDQNfieeayDAFRV----N 514
Cdd:cd07119 358 YFVEPTIFDDVDRTMRIVQEEIFGPVLTV-----ERFDTEEEAIRLANdtpYGLAGAVWTKDIA------RANRVarrlR 426
|
410 420 430
....*....|....*....|....*....|....
gi 28571800 515 VGNLNVNDksTGLMVGQQPFGAGHMTGTSDKLGT 548
Cdd:cd07119 427 AGTVWIND--YHPYFAEAPWGGYKQSGIGRELGP 458
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
115-563 |
2.87e-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: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 115 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAE---MDVA--------ELVDFMR 183
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLER-RDELLDLIQLETGKARRHAFeevLDVAivaryyarRAERLLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 184 IN------PVFLRELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFtgiAANLAYT---PALM-GNSVIWKPSDSAI 253
Cdd:cd07101 99 PRrrrgaiPVLTRTTVNRRPK-----------------GVVGVISPWNY---PLTLAVSdaiPALLaGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 254 LSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKlaGINFTGTSTVLKVLWQLVAQninfyqnypRLVG---EGG 330
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGR---------RLIGcslELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 331 GKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVVRQDATYCDSFCSaVINRR 410
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRR-FVARTRALRLGAALDYGPDMGS-LISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 411 AYDRIYmwlRYIDQSPS--CQILVGGSCDKRRG-YYVDPTVVLVKDLDNIICREELLAPIlgVYVYPDHKLKETMEKVAQ 487
Cdd:cd07101 306 QLDRVT---AHVDDAVAkgATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPV--VSIYRVADDDEAIELAND 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 488 INHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVND------KSTGL-MVGQQPFGAGHMTGtsdklgtPHSLLRWTSPQ 559
Cdd:cd07101 381 TDYGLNASVWTRD---GARGRRiAARLRAGTVNVNEgyaaawASIDApMGGMKDSGLGRRHG-------AEGLLKYTETQ 450
|
....
gi 28571800 560 VIKE 563
Cdd:cd07101 451 TVAV 454
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
118-502 |
2.67e-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: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFmrinpvfLRELANY-- 195
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESR-RDEFIEAMMEETGATAAWAGFNVDLAAGM-------LREAASLit 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 ----EPI-RDIQNncRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVP 269
Cdd:cd07105 77 qiigGSIpSDKPG--TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 270 DGVVNFVPAEETTFASVVTQ---HPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETA 346
Cdd:cd07105 155 KGVLNVVTHSPEDAPEVVEAliaHPAVRKVNFTGSTRVGRIIAETAAKHLK------PVLLELGGKAPAIVLEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 347 VACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVRQDATycdsfcSAVINRRAYDRIymwLRYIDQSP 426
Cdd:cd07105 229 ANAALFGAFLNSGQICMSTERIIVHESIADE-FVEKLKAAAEKLFAGPVVL------GSLVSAAAADRV---KELVDDAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 427 SC--QILVGG-SCDKRRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYpdhklKETMEKVAQIN---HGLTGS 495
Cdd:cd07105 299 SKgaKLVVGGlADESPSGTSMPPTI-----LDNVtpdmdIYSEESFGPVVSIIRV-----KDEEEAVRIANdseYGLSAA 368
|
....*..
gi 28571800 496 VFAQDQN 502
Cdd:cd07105 369 VFTRDLA 375
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
102-475 |
2.70e-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: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 102 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNIIAATMLGQGKTLRQAE-MDVAELVD 180
Cdd:cd07115 8 ELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARrLDVPRAAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 181 FMR---------------INPVFLrelaNY---EPIrdiqnncrnsmrlrglsGFVAAISPFNFTGIAANLAYTPAL-MG 241
Cdd:cd07115 87 TFRyyagwadkiegevipVRGPFL----NYtvrEPV-----------------GVVGAIVPWNFPLMFAAWKVAPALaAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 242 NSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqn 321
Cdd:cd07115 146 NTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 322 ypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWqNHIREPLLEITASLVVrQDATYCDS 401
Cdd:cd07115 222 --RVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIY-DEFLERFTSLARSLRP-GDPLDPKT 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571800 402 FCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPD 475
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 ... |
216-547 |
3.45e-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: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:cd07141 147 GVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDID 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07141 227 KVAFTGSTEVGKLIQQAAGKS-----NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQNHIREpLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPT 447
Cdd:cd07141 302 YDEFVKR-SVERAKKRVVG------NPFDPKTeqgpqIDEEQFKKI---LELIEsgKKEGAKLECGGKRHGDKGYFIQPT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEA-YDAFRVNVGNLNVNdkST 525
Cdd:cd07141 372 VFSdVTD-DMRIAKEEIFGPVQQIFKFKT--IDEVIERANNTTYGLAAAVFTKD---IDKAiTFSNALRAGTVWVN--CY 443
|
330 340
....*....|....*....|..
gi 28571800 526 GLMVGQQPFGAGHMTGTSDKLG 547
Cdd:cd07141 444 NVVSPQAPFGGYKMSGNGRELG 465
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
216-535 |
6.38e-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: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAeettFASVVTQ----H 290
Cdd:cd07112 126 GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPG----FGHTAGEalglH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 291 PKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVAC-TIRAAFEYAGQKCSSCSMLY 369
Cdd:cd07112 202 MDVDALAFTGSTEVGRRFLEYSGQS-----NLKRVWLECGGKSPNIVFADAPDLDAAAEaAAAGIFWNQGEVCSAGSRLL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 370 VPESlwqnhIREPLLEitasLVVRQDATY-------CDSFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDKR- 439
Cdd:cd07112 277 VHES-----IKDEFLE----KVVAAAREWkpgdpldPATRMGALVSEAHFDKV---LGYIESGKAegARLVAGGKRVLTe 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 440 -RGYYVDPTVVLVKDLDNIICREELLAPILGVyvypdHKLKETMEKVAQIN---HGLTGSVFAQDQNfieeayDAFRV-- 513
Cdd:cd07112 345 tGGFFVEPTVFDGVTPDMRIAREEIFGPVLSV-----ITFDSEEEAVALANdsvYGLAASVWTSDLS------RAHRVar 413
|
330 340
....*....|....*....|....
gi 28571800 514 --NVGNLNVNDKSTGLMvgQQPFG 535
Cdd:cd07112 414 rlRAGTVWVNCFDEGDI--TTPFG 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
81-521 |
6.54e-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: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQEFQAK-EDFQQVLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAA 159
Cdd:cd07085 5 INGEWVESKtTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL--EENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 160 TM-LGQGKTLRQAEMDVA---ELVDFMRINPvflrELANYEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAY 235
Cdd:cd07085 83 LItLEHGKTLADARGDVLrglEVVEFACSIP----HLLKGEYLENVARGIDTYSYRQPL-GVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 236 TPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQ 314
Cdd:cd07085 158 PMAIaCGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 315 NINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLyVPESLWQNHIREPLLEITASLVVRq 394
Cdd:cd07085 237 NGK------RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVA-VAVGDEADEWIPKLVERAKKLKVG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 395 DATYCDSFCSAVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDK----RRGYYVDPTVvlvkdLDNI-----ICREEL 463
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERI---EGLIESGVEegAKLVLDGRGVKvpgyENGNFVGPTI-----LDNVtpdmkIYKEEI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571800 464 LAPILGVyVYPDHkLKETMEKVAQINHGLTGSVFAQD----QNFIEEaydafrVNVGNLNVN 521
Cdd:cd07085 381 FGPVLSI-VRVDT-LDEAIAIINANPYGNGAAIFTRSgaaaRKFQRE------VDAGMVGIN 434
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
216-547 |
8.15e-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: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:cd07144 146 GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07144 226 KIAFTGSTATGRLVMKAAAQNLK------AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQNHIrEPLLEitaslVVRQDATYCDSFCS-----AVINRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKR---RGYYV 444
Cdd:cd07144 300 YDKFV-EKFVE-----HVKQNYKVGSPFDDdtvvgPQVSKTQYDRV---LSYIEKgkKEGAKLVYGGEKAPEglgKGYFI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 445 DPTVVL-VKDlDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNd 522
Cdd:cd07144 371 PPTIFTdVPQ-DMRIVKEEIFGPVVVISKFKTY--EEAIKKANDTTYGLAAAVFTKD---IRRAHRvARELEAGMVWIN- 443
|
330 340
....*....|....*....|....*
gi 28571800 523 kSTGLMVGQQPFGAGHMTGTSDKLG 547
Cdd:cd07144 444 -SSNDSDVGVPFGGFKMSGIGRELG 467
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
135-535 |
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 28571800 135 SDRIDIWERAAMLIAGRYRYniiAATMLGQ--GKTLRQAEMDVAELVDFMRInpvflrelANYEPIR--------DIQNN 204
Cdd:cd07146 40 YQRSAILNKAAALLEARREE---FARLITLesGLCLKDTRYEVGRAADVLRF--------AAAEALRddgesfscDLTAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 205 C--RNSMRLRGLSGFVAAISPFNF--TGIAANLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAE 279
Cdd:cd07146 109 GkaRKIFTLREPLGVVLAITPFNHplNQVAHKIA--PAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 280 ETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAqninfyqnYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAG 359
Cdd:cd07146 187 PGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 360 QKCSSCSMLYVPESLWQNhIREPLLEITASLVV---RQDATycdsFCSAVINRRAYDRIY-MWLRYIDQSPScqILVGGS 435
Cdd:cd07146 259 QRCTAVKRILVHESVADE-FVDLLVEKSAALVVgdpMDPAT----DMGTVIDEEAAIQIEnRVEEAIAQGAR--VLLGNQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 436 cdkRRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDa 510
Cdd:cd07146 332 ---RQGALYAPTV-----LDHVppdaeLVTEETFGPVAPVIRVKD--LDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE- 400
|
410 420
....*....|....*....|....*
gi 28571800 511 fRVNVGNLNVNDkSTGLMVGQQPFG 535
Cdd:cd07146 401 -RLDVGTVNVNE-VPGFRSELSPFG 423
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
216-547 |
3.08e-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: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:cd07143 146 GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDID 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07143 226 KVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQNHIREpLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPTVVLVK 452
Cdd:cd07143 301 YDKFVKR-FKEKAKKLKV-GDPFAEDTFQGPQVSQIQYERI---MSYIEsgKAEGATVETGGKRHGNEGYFIEPTIFTDV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 453 DLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNdkSTGLMVGQQ 532
Cdd:cd07143 376 TEDMKIVKEEIFGPVVAVIKFKT--EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALK--AGTVWVN--CYNLLHHQV 449
|
330
....*....|....*
gi 28571800 533 PFGAGHMTGTSDKLG 547
Cdd:cd07143 450 PFGGYKQSGIGRELG 464
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
216-542 |
7.24e-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: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:cd07142 143 GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:cd07142 223 KVAFTGSTEVGKIIMQLAAKS-----NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WQNHIrEPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKRRGYYVDPT 447
Cdd:cd07142 298 YDEFV-EKAKARALKRVVG------DPFRKGVeqgpqVDKEQFEKI---LSYIEHgkEEGATLITGGDRIGSKGYYIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRvnVGNLNVNdkSTG 526
Cdd:cd07142 368 IFSdVKD-DMKIARDEIFGPVQSILKFKT--VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYD 440
|
330
....*....|....*.
gi 28571800 527 LMVGQQPFGAGHMTGT 542
Cdd:cd07142 441 VFDASIPFGGYKMSGI 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
81-535 |
8.20e-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: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQ--EFQAKEDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERaamlIAGRY--RYNI 156
Cdd:cd07138 3 IDGAwvAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLER----IAEAYeaRADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 157 IAATM---LGQGKTLRQAeMDVAELVDFMRinpVFLRELANYEPIRDIQNncrnSMRLRGLSGFVAAISPFNFT--GIAA 231
Cdd:cd07138 78 LAQAItleMGAPITLARA-AQVGLGIGHLR---AAADALKDFEFEERRGN----SLVVREPIGVCGLITPWNWPlnQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 232 NLAytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTG-TSTVLKVLw 309
Cdd:cd07138 150 KVA--PALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGsTRAGKRVA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 310 QLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITAS 389
Cdd:cd07138 227 EAAADTVK------RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSR-YAEAEEIAAAAAEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 390 LVV---RQDATycdsFCSAVINRRAYDRIymwLRYIDQSpscqI-----LVGGSCDK----RRGYYVDPTVVLVKDLDNI 457
Cdd:cd07138 300 YVVgdpRDPAT----TLGPLASAAQFDRV---QGYIQKG----IeegarLVAGGPGRpeglERGYFVKPTVFADVTPDMT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 458 ICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQnfiEEAYD-AFRVNVGNLNVNDKSTGLmvgQQP 533
Cdd:cd07138 369 IAREEIFGPVLSIIPYDDED-----EAIAIANdtpYGLAGYVWSADP---ERARAvARRLRAGQVHINGAAFNP---GAP 437
|
..
gi 28571800 534 FG 535
Cdd:cd07138 438 FG 439
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
118-561 |
1.04e-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: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFM----RINPVFLRELA 193
Cdd:cd07099 23 AVARARAAQRAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAETGKPRADAGLEVLLALEAIdwaaRNAPRVLAPRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 194 nyEPIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGV 272
Cdd:cd07099 102 --VPTGLLMPNKKATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 273 VNFVPAEETTFASVVTQHP-KLAginFTG-TSTVLKVLWQLVAQNInfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACT 350
Cdd:cd07099 179 LQVVTGDGATGAALIDAGVdKVA---FTGsVATGRKVMAAAAERLI------P-VVLELGGKDPMIVLADADLERAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 351 IRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV----RQDATYcdsfcSAVINRRAYDRIYmwlRYIDQSP 426
Cdd:cd07099 249 VWGAMVNAGQTCISVERVYVHESVYDEFVAR-LVAKARALRPgaddIGDADI-----GPMTTARQLDIVR---RHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 427 S--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhklkeTMEKVAQIN---HGLTGSVFAQDQ 501
Cdd:cd07099 320 AkgAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVAD-----EDEAIALANdsrYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 502 NFIEEAydAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGtPHSLLRWTSPQVI 561
Cdd:cd07099 395 ARAEAI--ARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHG-AEGLREFCRPKAI 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
118-557 |
1.05e-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: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLiAGRYRYNIIAATMLGQGKTLRQAEMDVAELVdfmrinpVFLRELANY-- 195
Cdd:cd07152 18 AAARAAAAQRAWAATPPRERAAVLRRAADL-LEEHADEIADWIVRESGSIRPKAGFEVGAAI-------GELHEAAGLpt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 EPIRDI--QNNCRNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPS-DSAILSNYFVFKALREAGVPDG 271
Cdd:cd07152 90 QPQGEIlpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFEEAGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 272 VVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTI 351
Cdd:cd07152 170 VLHVLPGGADAGEALVE-DPNVAMISFTGSTAVGRKVGEAAGRHLK------KVSLELGGKNALIVLDDADLDLAASNGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 352 RAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVRQDATYcDSFCSAVINRRAYDRIymwLRYIDQS--PSCQ 429
Cdd:cd07152 243 WGAFLHQGQICMAAGRHLVHESVADAYT-AKLAAKAKHLPVGDPATG-QVALGPLINARQLDRV---HAIVDDSvaAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 430 ILVGGScdkRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQDqnfIEE 506
Cdd:cd07152 318 LEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE-----EAVALANDteyGLSAGIISRD---VGR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 507 AYD-AFRVNVGNLNVNDKsTGLMVGQQPFGAGHMTGTSDKLGTPHSL-----LRWTS 557
Cdd:cd07152 387 AMAlADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGPANWeeftqWQWVT 442
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
102-541 |
1.27e-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: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 102 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAA-TMLGQGKTLRQAEMDVAELVD 180
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLL--RERNDEIARlETIDNGKPIEEARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 181 FMRinpvFLRELAnyepirdiQNNCRNSMRLRGLS---------GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSD 250
Cdd:cd07090 86 CLE----YYAGLA--------PTLSGEHVPLPGGSfaytrreplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 251 SAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEG 329
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGsVPTGKKVM-SAAAKGIK------HVTLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 330 GGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINR 409
Cdd:cd07090 226 GGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDE-FTERLVERTKKIRI-GDPLDEDTQMGALISE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 410 RAYDRIymwLRYIDQSPS--CQILVGG-----SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETM 482
Cdd:cd07090 304 EHLEKV---LGYIESAKQegAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF------DTE 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571800 483 EKVAQI----NHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdkSTGLMVGQQPFGAGHMTG 541
Cdd:cd07090 375 EEVIRRandtTYGLAAGVFTRD---LQRAHRvIAQLQAGTCWIN--TYNISPVEVPFGGYKQSG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
95-552 |
1.99e-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: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 95 VLPYDIQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYryNIIAATM-LGQGKTLR-QAE 172
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARS--EELARLLaLETGNALRtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 173 MDVAELVDFMRINPVFLREL-ANYEPIRDIQNncrnSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSD 250
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELkGETLPFGPDVL----TYTVREPLGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 251 SAILSNYFVFKALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAqninfyqnyPRLVG--- 327
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 328 EGGGKNFHFVHSSAEPETAVACTIRAA-FEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAV 406
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFL-EKLVAKLSKLKI-GDPLDEATDIGAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 407 INRRAYDRIymwLRYID---QSPSCQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklK 479
Cdd:cd07108 303 ISEKQFAKV---CGYIDlglSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDE--D 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571800 480 ETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNdKSTGLMVGQQpFGAGHMTGtsdkLGTPHSL 552
Cdd:cd07108 378 EVIAMANDSHYGLAAYVWTRD---LGRALRaAHALEAGWVQVN-QGGGQQPGQS-YGGFKQSG----LGREASL 442
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
119-535 |
6.33e-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: 111.17 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 119 IDKSVEA-----QVKWDKVRLSDRIDIWERAAMLIaGRYRYNIIAATMLGQGKTLRQAEMDVAELVdfmrinpvflRELA 193
Cdd:cd07109 21 VDRAVQAarrafESGWLRLSPAERGRLLLRIARLI-REHADELARLESLDTGKPLTQARADVEAAA----------RYFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 194 NYEPIRD--------IQNNCRNSMrLRGLSGFVAAISPFNFT------GIAANLAytpalMGNSVIWKPSDSAILSNYFV 259
Cdd:cd07109 90 YYGGAADklhgetipLGPGYFVYT-VREPHGVTGHIIPWNYPlqitgrSVAPALA-----AGNAVVVKPAEDAPLTALRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 260 FKALREAGVPDGVVNFVP--AEETTFAsvVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFV 337
Cdd:cd07109 164 AELAEEAGLPAGALNVVTglGAEAGAA--LVAHPGVDHISFTGSVETGIAVMRAAAENVV------PVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 338 HSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEITASLV--VRQDATYCDSFCSAVINRRAYDRI 415
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRS-----IYDEVLERLVERFraLRVGPGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 416 YMWLRYIDQSpSCQILVGG---SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN--- 489
Cdd:cd07109 311 EGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEA-----EAIALANgtd 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 28571800 490 HGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKSTGLMVgQQPFG 535
Cdd:cd07109 385 YGLVAGVWTRD---GDRALRvARRLRAGQVFVNNYGAGGGI-ELPFG 427
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
119-547 |
8.77e-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: 8.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 119 IDKSVEAQVK------WDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRINPVFLREL 192
Cdd:cd07118 21 VDAAVAAARKafdkgpWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQARGEIEGAADLWRYAASLARTL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 193 ANyepirDIQNNCRNSMR---LRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGV 268
Cdd:cd07118 100 HG-----DSYNNLGDDMLglvLREPIGVVGIITPWNFPFLILSQKLPFALaAGCTVVVKPSEFTSGTTLMLAELLIEAGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 269 PDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVA 348
Cdd:cd07118 175 PAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK------KVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 349 CTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREpllEITASLVVR-QDATYCDSF-----CSAVINRRAYDRIymwLRYI 422
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHES-----IAD---AFVAAVVARsRKVRVGDPLdpetkVGAIINEAQLAKI---TDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 423 D--QSPSCQILVGG-SCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQI----NHGLTGS 495
Cdd:cd07118 318 DagRAEGATLLLGGeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF------DTVDEAIALandtVYGLSAG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571800 496 VFAQDqnfIEEAYDAFR-VNVGNLNVNDKSTGlmVGQQPFGAGHMTGTSDKLG 547
Cdd:cd07118 392 VWSKD---IDTALTVARrIRAGTVWVNTFLDG--SPELPFGGFKQSGIGRELG 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
124-535 |
2.03e-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: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 124 EAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMRinpvflrELANYePIR---- 199
Cdd:cd07151 43 AAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRESGSTRIKANIEWGAAMAITR-------EAATF-PLRmegr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 200 DIQNNC--RNSMRLRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKP-SDSAILSNYFVFKALREAGVPDGVVNF 275
Cdd:cd07151 114 ILPSDVpgKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 276 V--PAEETTFASVVTQHPKLagINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRA 353
Cdd:cd07151 194 VvgAGSEIGDAFVEHPVPRL--ISFTGSTPVGRHIGELAGRHLK------KVALELGGNNPFVVLEDADIDAAVNAAVFG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 354 AFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIymwLRYIDQSPS--CQIL 431
Cdd:cd07151 266 KFLHQGQICMAINRIIVHEDVYDEFV-EKFVERVKALPY-GDPSDPDTVVGPLINESQVDGL---LDKIEQAVEegATLL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 432 VGGscdKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-A 510
Cdd:cd07151 341 VGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALELANDTEYGLSGAVFTSD---LERGVQfA 412
|
410 420
....*....|....*....|....*...
gi 28571800 511 FRVNVGNLNVNDKStglmVGQQP---FG 535
Cdd:cd07151 413 RRIDAGMTHINDQP----VNDEPhvpFG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
115-535 |
8.64e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 108.12 E-value: 8.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 115 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAAtMLGQ--GKTLRQAEMDVAELvdfmrINPVFLREL 192
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALL--EENKEELAE-VIARetGKPLWEAATEVTAM-----INKIAISIQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 193 ANYE---PIRDIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGV 268
Cdd:PRK09457 111 AYHErtgEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVKLWQQAGL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 269 PDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNinfyqnyPR--LVGEGGGKNFHFVHSSAEPETA 346
Cdd:PRK09457 190 PAGVLNLVQGGRETGKALAA-HPDIDGLLFTGSANTGYLLHRQFAGQ-------PEkiLALEMGGNNPLVIDEVADIDAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 347 VACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVVRQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSP 426
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQL-LAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 427 SCQILVGGSCDKRRGYYVDPTVVlvkDLDNIICR--EELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfi 504
Cdd:PRK09457 341 GGKSLLEMTQLQAGTGLLTPGII---DVTGVAELpdEEYFGPLLQVVRYDD--FDEAIRLANNTRFGLSAGLLSDD---- 411
|
410 420 430
....*....|....*....|....*....|...
gi 28571800 505 EEAYDAFRVNV--GNLNVNDKSTGlMVGQQPFG 535
Cdd:PRK09457 412 REDYDQFLLEIraGIVNWNKPLTG-ASSAAPFG 443
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
164-502 |
2.19e-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: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 164 QGKTLRQAEMDVAELVDFMRinpvFLRELANYEPIRDIQNNCRN-SMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-G 241
Cdd:cd07120 70 NGKILGEARFEISGAISELR----YYAGLARTEAGRMIEPEPGSfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 242 NSVIWKPSDSAILSNYFVFKALREA-GVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyq 320
Cdd:cd07120 146 CTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 321 nypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVVrQDATYCD 400
Cdd:cd07120 223 ---RLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE-VRDRLAARLAAVKV-GPGLDPA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 401 SFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKR--RGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKl 478
Cdd:cd07120 298 SDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA- 376
|
330 340
....*....|....*....|....*..
gi 28571800 479 ketmEKVAQINH---GLTGSVFAQDQN 502
Cdd:cd07120 377 ----EAVALANDtdyGLAASVWTRDLA 399
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
142-513 |
2.48e-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: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 142 ERAAML--IA---GRYRYNIIAATMLGQGKTLRQAEMDV----------AELVDFMRINpvflRELANYEPIRDIQNNCR 206
Cdd:cd07110 42 ERAKYLraIAegvRERREELAELEARDNGKPLDEAAWDVddvagcfeyyADLAEQLDAK----AERAVPLPSEDFKARVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 207 nsmrlRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFAS 285
Cdd:cd07110 118 -----REPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 286 VVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSC 365
Cdd:cd07110 193 PLAAHPGIDKISFTGSTATGSQVMQAAAQDIK------PVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 366 SMLYVPESlwqnhIREPLLEitaSLVVRQDAT-YCDSF-----CSAVINRRAYDRIymwLRYIDQSPS--CQILVGGS-- 435
Cdd:cd07110 267 SRLLVHES-----IADAFLE---RLATAAEAIrVGDPLeegvrLGPLVSQAQYEKV---LSFIARGKEegARLLCGGRrp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 436 CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQDQNFIEEAYDAFR 512
Cdd:cd07110 336 AHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-----EAIALANdseYGLAAAVISRDAERCDRVAEALE 410
|
.
gi 28571800 513 V 513
Cdd:cd07110 411 A 411
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
116-561 |
7.13e-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: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 116 QMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRyRYNIIAATMLGQGKTLRQAEMDVAELVDFMrinpvFLRELANY 195
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAENICGDQVQLR-----ARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 EPIRDIQNNCRN---SMRLRGL---SGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNYFVFKALREAG- 267
Cdd:cd07084 76 YRIPHEPGNHLGqglKQQSHGYrwpYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 268 VPDGVVNFVPAEETTFASVVTqHPKLAGINFTGTSTVLKVLWQLVAQNinfyqnypRLVGEGGGKNFHFVHSSAEPETAV 347
Cdd:cd07084 156 LPPEDVTLINGDGKTMQALLL-HPNPKMVLFTGSSRVAEKLALDAKQA--------RIYLELAGFNWKVLGPDAQAVDYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 348 ACTI-RAAFEYAGQKCSSCSMLYVPESlWQnhiREPLLEITASLVVRQ-------DATYCDSFCSAVINRRAYDRIYmwL 419
Cdd:cd07084 227 AWQCvQDMTACSGQKCTAQSMLFVPEN-WS---KTPLVEKLKALLARRkledlllGPVQTFTTLAMIAHMENLLGSV--L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 420 RYidqspSCQILVGGSCDKRRGYYVDPTVVLVKDLDN---IICREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSV 496
Cdd:cd07084 301 LF-----SGKELKNHSIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571800 497 FAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGTSDKLGTPHSLLRWTSPQVI 561
Cdd:cd07084 376 YSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
216-547 |
2.81e-23 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 103.75 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:PLN02766 160 GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:PLN02766 240 KVSFTGSTEVGRKIMQAAATS-----NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WqNHIREPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIymwLRYID--QSPSCQILVGGSCDKRRGYYVDPT 447
Cdd:PLN02766 315 Y-DEFVKKLVEKAKDWVVG------DPFDPRArqgpqVDKQQFEKI---LSYIEhgKREGATLLTGGKPCGDKGYYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 VVLVKDLDNIICREELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNV-----ND 522
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCyfafdPD 462
|
330 340
....*....|....*....|....*
gi 28571800 523 kstglmvgqQPFGAGHMTGTSDKLG 547
Cdd:PLN02766 463 ---------CPFGGYKMSGFGRDQG 478
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
216-521 |
7.78e-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: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTgiAANLAYTPALM---GNSVIWKPSDS----AILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVt 288
Cdd:cd07130 134 GVVGVITAFNFP--VAVWGWNAAIAlvcGNVVVWKPSPTtpltAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALV- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 289 QHPKLAGINFTGTSTVLKvlwqLVAQNINfyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 368
Cdd:cd07130 211 KDPRVPLVSFTGSTAVGR----QVGQAVA--ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 369 YVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSPSCQILVGGSCDKRRGYYVDPTV 448
Cdd:cd07130 285 IVHESIYDE-VLERLKKAYKQVRI-GDPLDDGTLVGPLHTKAAVDNYLAAIEEA-KSQGGTVLFGGKVIDGPGNYVEPTI 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 449 VLVKDLDNIIcREELLAPILgvYVypdHKLKeTMEKVAQIN----HGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVN 521
Cdd:cd07130 362 VEGLSDAPIV-KEETFAPIL--YV---LKFD-TLEEAIAWNnevpQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVN 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
104-502 |
3.60e-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: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 104 IAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYNIIAATMlGQGKTLRQAE-MDVAELVDFM 182
Cdd:cd07117 29 LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL-DNGKPIRETRaVDIPLAADHF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 183 RINPVFLRelANYEPIRDIQNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFK 261
Cdd:cd07117 108 RYFAGVIR--AEEGSANMIDEDTL-SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 262 ALREAgVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNInfyqnYPRLVgEGGGKNFHFVHSSA 341
Cdd:cd07117 185 IIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANIIFDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 342 EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREPLLEITASLVvrQDATYCDSFCSAVINRRAYDRIymwLRY 421
Cdd:cd07117 258 NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKV--GNPLDPDTQMGAQVNKDQLDKI---LSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 422 ID--QSPSCQILVGG------SCDKrrGYYVDPTVVLVKDLDNIICREELLAPILGVYvypdhKLKETMEKVAQIN---H 490
Cdd:cd07117 333 VDiaKEEGAKILTGGhrltenGLDK--GFFIEPTLIVNVTNDMRVAQEEIFGPVATVI-----KFKTEDEVIDMANdseY 405
|
410
....*....|..
gi 28571800 491 GLTGSVFAQDQN 502
Cdd:cd07117 406 GLGGGVFTKDIN 417
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
81-561 |
5.06e-22 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 99.59 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQEFQAKED--FQQVLPYDiQQPIAHYGHAHRVLIQMAID--KSVEAQVKWDKVRLSDRIDIWERAAMLIAgRYRYNI 156
Cdd:PRK09847 24 INGEYTAAAENetFETVDPVT-QAPLAKIARGKSVDIDRAVSaaRGVFERGDWSLSSPAKRKAVLNKLADLME-AHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 157 IAATMLGQGKTLRQAEMD-----------VAELVD--FMRINPVFLRELAnyepirdiqnncrnsMRLRGLSGFVAAISP 223
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDdipgaarairwYAEAIDkvYGEVATTSSHELA---------------MIVREPVGVIAAIVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 224 FNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTS 302
Cdd:PRK09847 167 WNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGST 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 303 TVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSA-EPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIRe 381
Cdd:PRK09847 247 RTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 382 pLLEITASLVVRQDATYCDSFCSAVINRRAYDRIYmwlRYIDQSPS-CQILVGGscdKRRGY--YVDPTVVLVKDLDNII 458
Cdd:PRK09847 321 -LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH---SFIREGESkGQLLLDG---RNAGLaaAIGPTIFVDVDPNASL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 459 CREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVNDKSTGLMVgqQPFGAG 537
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSE--EQALQLANDSQYGLGAAVWTRD---LSRAHRmSRRLKAGSVFVNNYNDGDMT--VPFGGY 466
|
490 500
....*....|....*....|....*
gi 28571800 538 HMTGTS-DKlgTPHSLLRWTSPQVI 561
Cdd:PRK09847 467 KQSGNGrDK--SLHALEKFTELKTI 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
151-502 |
5.37e-22 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 98.65 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 151 RYRYNIIAATMLG-QGKTLRQAEMDVAELVDFMRinpvFLRELA-NYEPirDIQNNCR---NSMRLRGLSGFVAAISPFN 225
Cdd:PRK10090 9 RERASEISALIVEeGGKIQQLAEVEVAFTADYID----YMAEWArRYEG--EIIQSDRpgeNILLFKRALGVTTGILPWN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 226 FTG--IAANLAytPALM-GNSVIWKPSdSAILSNYFVF-KALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGT 301
Cdd:PRK10090 83 FPFflIARKMA--PALLtGNTIVIKPS-EFTPNNAIAFaKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 302 STVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrE 381
Cdd:PRK10090 160 VSAGEKIMAAAAKNIT------KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV-N 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 382 PLLEITASLVVRQDATYCDSFCSAVINRRAYDRIY-MWLRYIDQSPScqILVGGSCDKRRGYYVDPTVVLVKDLDNIICR 460
Cdd:PRK10090 233 RLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEqKVARAVEEGAR--VALGGKAVEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 28571800 461 EELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQN 502
Cdd:PRK10090 311 EETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLN 350
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
216-564 |
6.46e-22 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 99.57 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNF---TGIAANLaytPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHP 291
Cdd:PRK09407 156 GVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 292 KlaGINFTGTSTVLKVLWQLVAQninfyqnypRLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 368
Cdd:PRK09407 233 D--YLMFTGSTATGRVLAEQAGR---------RLIGfslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 369 YVPESLWQNHIREpLLEITASLVVRQDATYCDSFCSaVINRRAYDRIYmwlRYIDQSPS--CQILVGGscdKRR---G-Y 442
Cdd:PRK09407 302 YVHESIYDEFVRA-FVAAVRAMRLGAGYDYSADMGS-LISEAQLETVS---AHVDDAVAkgATVLAGG---KARpdlGpL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 443 YVDPTVVLVKDLDNIICREELLAPIlgVYVYPDHKLKETMEKVAQINHGLTGSVFAQDqnfIEEAYD-AFRVNVGNLNVN 521
Cdd:PRK09407 374 FYEPTVLTGVTPDMELAREETFGPV--VSVYPVADVDEAVERANDTPYGLNASVWTGD---TARGRAiAARIRAGTVNVN 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 28571800 522 D------KSTGL-MVGQQPFGAGHMTGtsdklgtPHSLLRWTSPQVIKES 564
Cdd:PRK09407 449 EgyaaawGSVDApMGGMKDSGLGRRHG-------AEGLLKYTESQTIATQ 491
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
142-500 |
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 28571800 142 ERAAML--IAGRYRYN---IIAATMLGQGKTLR-QAEMDVAELVDFMRINPVFLREL-----ANYEPirdiqnnCRNSMR 210
Cdd:cd07092 42 ERSKALlkLADAIEENaeeLAALESRNTGKPLHlVRDDELPGAVDNFRFFAGAARTLegpaaGEYLP-------GHTSMI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 211 LRGLSGFVAAISPFNFTGIAANLAYTPAL-MGNSVIWKPSDSAILSNyFVFKALREAGVPDGVVNFVPAEETTFASVVTQ 289
Cdd:cd07092 115 RREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTT-LLLAELAAEVLPPGVVNVVCGGGASAGDALVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 290 HPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVAcTIR-AAFEYAGQKCSSCSM 367
Cdd:cd07092 194 HPRVRMVSLTGsVRTGKKVA-RAAADTLK------RVHLELGGKAPVIVFDDADLDAAVA-GIAtAGYYNAGQDCTAACR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 368 LYVPESLWQnhirepllEITASLVVRQDAT-YCDSFCSAV-----INRRAYDRIymwLRYIDQSPS-CQILVGGSCDKRR 440
Cdd:cd07092 266 VYVHESVYD--------EFVAALVEAVSAIrVGDPDDEDTemgplNSAAQRERV---AGFVERAPAhARVLTGGRRAEGP 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571800 441 GYYVDPTVVL-VKDLDNIIcREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQD 500
Cdd:cd07092 335 GYFYEPTVVAgVAQDDEIV-QEEIFGPVVTVQPFDD--EDEAIELANDVEYGLASSVWTRD 392
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
137-552 |
1.43e-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: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 137 RIDIWERAAMLIAGRYRYNIIAATMLGqGKTLRQAEMDVAELVDFMRINPVFLRELANYEPIRDIQ--NNCRNSMRLRGL 214
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREG-GKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTpaSAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 215 SGFVAAISPFNFtgiAANLA---YTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQh 290
Cdd:cd07148 125 IGVVVAISAFNH---PLNLIvhqVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 291 PKLAGINFTGTStvlKVLWQLVAQNInfyqnyP--RLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 368
Cdd:cd07148 201 PRVAFFSFIGSA---RVGWMLRSKLA------PgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 369 YVPESLWQNhIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWlryIDQSPS--CQILVGGscdKRRGYYV-D 445
Cdd:cd07148 272 FVPAEIADD-FAQRLAAAAEKLVV-GDPTDPDTEVGPLIRPREVDRVEEW---VNEAVAagARLLCGG---KRLSDTTyA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 446 PTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDqnfIEEAYDAFR-VNVGNLNVNDKs 524
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDD--LDEAIAQANSLPVAFQAAVFTKD---LDVALKAVRrLDATAVMVNDH- 417
|
410 420 430
....*....|....*....|....*....|..
gi 28571800 525 TGLMVGQQPFG----AGHMTGtsdklGTPHSL 552
Cdd:cd07148 418 TAFRVDWMPFAgrrqSGYGTG-----GIPYTM 444
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
216-541 |
5.88e-21 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 96.80 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:PLN02466 277 KLAFTGSTDTGKIVLELAAKS-----NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WqnhirEPLLEITASLVVRQdaTYCDSFCSAV-----INRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKRRGYYVDPT 447
Cdd:PLN02466 352 Y-----DEFVEKAKARALKR--VVGDPFKKGVeqgpqIDSEQFEKI---LRYIKSgvESGATLECGGDRFGSKGYYIQPT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 448 VVL-VKDlDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVN---VGNLNVNDK 523
Cdd:PLN02466 422 VFSnVQD-DMLIAQDEIFGPVQSILKFKD--LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGtvwVNCFDVFDA 498
|
330
....*....|....*...
gi 28571800 524 STglmvgqqPFGAGHMTG 541
Cdd:PLN02466 499 AI-------PFGGYKMSG 509
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
216-515 |
6.30e-21 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 96.34 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNInfyqnypRLVG-EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPES 373
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMV-------KPVSlELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHER 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 374 lwqnhIREPLLEitaSLVVRQDA-TYCDSF---C--SAVINRRAYDRIymwLRYID--QSPSCQILVGGSCDK--RRGYY 443
Cdd:PLN02467 306 -----IASEFLE---KLVKWAKNiKISDPLeegCrlGPVVSEGQYEKV---LKFIStaKSEGATILCGGKRPEhlKKGFF 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571800 444 VDPTVVLVKDLDNIICREELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNV 515
Cdd:PLN02467 375 IEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGI 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
216-543 |
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 28571800 216 GFVAAISPFNFTGIaanLAYTPAL----MGNSVIWKPSD-----SAILSNyFVFKALREAGVpdGVVNFVPAEETTfasV 286
Cdd:cd07135 110 GVVLIIGPWNYPVL---LALSPLVgaiaAGCTVVLKPSEltphtAALLAE-LVPKYLDPDAF--QVVQGGVPETTA---L 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 287 VTQhpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCS 366
Cdd:cd07135 181 LEQ--KFDKIFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 367 MLYVPESLWQNHIREplLEITASLVVRQDATYCDSFcSAVINRRAYDRIymwLRYIDQSPScQILVGGSCDKRRgYYVDP 446
Cdd:cd07135 253 YVLVDPSVYDEFVEE--LKKVLDEFYPGGANASPDY-TRIVNPRHFNRL---KSLLDTTKG-KVVIGGEMDEAT-RFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 447 TVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNVGNLNVNDKSTG 526
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDD--LDEAIKVINSRDTPLALYIFTDDKSEIDHILT--RTRSGGVVINDTLIH 400
|
330
....*....|....*..
gi 28571800 527 LMVGQQPFGAghmTGTS 543
Cdd:cd07135 401 VGVDNAPFGG---VGDS 414
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
81-500 |
3.88e-19 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 90.71 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGQEFQAK--EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIA 158
Cdd:PRK13252 11 IDGAYVEATsgETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL--RERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 159 AT-MLGQGKTLRQAEM-------DVAE----LVDFMRINPVFLRELANY----EPIrdiqnncrnsmrlrglsGFVAAIS 222
Cdd:PRK13252 88 ALeTLDTGKPIQETSVvdivtgaDVLEyyagLAPALEGEQIPLRGGSFVytrrEPL-----------------GVCAGIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 223 PFNF-TGIAANLAyTPAL-MGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFAsVVTQHPKLAGINFTG 300
Cdd:PRK13252 151 AWNYpIQIACWKS-APALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGA-WLTEHPDIAKVSFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 301 TSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIr 380
Cdd:PRK13252 229 GVPTGKKVMAAAAASLK------EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 381 EPLLEITASLVV---RQDATycdSFcSAVINRRAYDRIymwLRYIDQ--SPSCQILVGGSCDKR----RGYYVDPTVVL- 450
Cdd:PRK13252 302 ARLLERVERIRIgdpMDPAT---NF-GPLVSFAHRDKV---LGYIEKgkAEGARLLCGGERLTEggfaNGAFVAPTVFTd 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571800 451 VKDlDNIICREELLAPILGVYVYPDHKlketmEKVAQINH---GLTGSVFAQD 500
Cdd:PRK13252 375 CTD-DMTIVREEIFGPVMSVLTFDDED-----EVIARANDteyGLAAGVFTAD 421
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
115-535 |
1.79e-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: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 115 IQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLiagrYRYN------IIAATMlgqGKTLRQAEMDV---AELVDFMRIN 185
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADL----LRERkdelarLITLEM---GKPIAEARAEVekcAWICRYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 186 -PVFL----RELA------NYEPIrdiqnncrnsmrlrglsGFVAAISPFNF-----TGIAAnlaytPALM-GNSVIWKP 248
Cdd:cd07100 74 aEAFLadepIETDagkayvRYEPL-----------------GVVLGIMPWNFpfwqvFRFAA-----PNLMaGNTVLLKH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 249 SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVtQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGE 328
Cdd:cd07100 132 ASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLK------KSVLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 329 GGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIREpLLEITASLVV---RQDATYCDSFCSA 405
Cdd:cd07100 205 LGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEK-FVEAMAALKVgdpMDEDTDLGPLARK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 406 vinrRAYDRIymwLRYIDQSPS--CQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETME 483
Cdd:cd07100 284 ----DLRDEL---HEQVEEAVAagATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKD--EEEAIA 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 28571800 484 KVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDkstglMVGQQ---PFG 535
Cdd:cd07100 355 LANDSPFGLGGSVFTTDLERAERV--ARRLEAGMVFING-----MVKSDprlPFG 402
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
216-548 |
8.15e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 86.81 E-value: 8.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDS----AILSNYFVFKALREAGVPDGVVNFVpAEETTFASVVTQH 290
Cdd:PLN02315 156 GIVGVITAFNFPCAVLGWNACIALVcGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLPGAIFTSF-CGGAEIGEAIAKD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 291 PKLAGINFTGTSTVlkvlWQLVAQNINfyQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYV 370
Cdd:PLN02315 235 TRIPLVSFTGSSKV----GLMVQQTVN--ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 371 PESLWQNHIrEPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYMWLRYIdQSPSCQILVGGSCDKRRGYYVDPTVVL 450
Cdd:PLN02315 309 HESIYDDVL-EQLLTVYKQVKI-GDPLEKGTLLGPLHTPESKKNFEKGIEII-KSQGGKILTGGSAIESEGNFVQPTIVE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 451 VKDlDNIICREELLAPILgvYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVG 530
Cdd:PLN02315 386 ISP-DADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG 462
|
330
....*....|....*...
gi 28571800 531 qQPFGAGHMTGTSDKLGT 548
Cdd:PLN02315 463 -GAFGGEKATGGGREAGS 479
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
118-500 |
1.13e-17 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 86.28 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWER-AAMLIAGRyryNIIAATM-LGQGKTLRQAEMDVAELVDFMrinpvflrELANY 195
Cdd:PLN02278 67 AIASAHDAFPSWSKLTASERSKILRRwYDLIIANK---EDLAQLMtLEQGKPLKEAIGEVAYGASFL--------EYFAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 196 EPIR---DI----QNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAG 267
Cdd:PLN02278 136 EAKRvygDIipspFPDRR-LLVLKQPVGVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 268 VPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAV 347
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 348 ACTIRAAFEYAGQKCSSCSMLYVPESLWQNHIrEPLLEITASLVVRqdatycDSFCSAV-----INRRAYDRIYmwlRYI 422
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFA-EAFSKAVQKLVVG------DGFEEGVtqgplINEAAVQKVE---SHV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 423 DQ--SPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdhklkETMEKVAQI----NHGLTGSV 496
Cdd:PLN02278 359 QDavSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF------KTEEEAIAIandtEAGLAAYI 432
|
....
gi 28571800 497 FAQD 500
Cdd:PLN02278 433 FTRD 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
115-563 |
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 28571800 115 IQMAIDKSVEAQVKWDKVRLSDRidiweRAAMLIAGRYRYN----IIAATMLGQGKTLRQAE----MDVAELVDFM---- 182
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAER-----RKVLRSLLKYILEnqeeICRVACRDTGKTMVDASlgeiLVTCEKIRWTlkhg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 183 --------RINPVFL---RELANYEPIrdiqnncrnsmrlrglsGFVAAISPFNFT-------GIAANLAytpalmGNSV 244
Cdd:cd07098 95 ekalrpesRPGGLLMfykRARVEYEPL-----------------GVVGAIVSWNYPfhnllgpIIAALFA------GNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 245 IWKPSDSAILSNYF----VFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyq 320
Cdd:cd07098 152 VVKVSEQVAWSSGFflsiIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 321 nyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESlwqnhIREPLLEITASLV--VRQDATY 398
Cdd:cd07098 228 --P-VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEK-----IYDKLLEILTDRVqaLRQGPPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 399 CDSF-CSAVINRRAYDRIYMWLRyiDQSPS-CQILVGGS----CDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYV 472
Cdd:cd07098 300 DGDVdVGAMISPARFDRLEELVA--DAVEKgARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 473 YPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVGQQPFGAGHMTGtSDKLGTPHSL 552
Cdd:cd07098 378 ASD--DEEAVEIANSTEYGLGASVFGKDIKRARRI--ASQLETGMVAINDFGVNYYVQQLPFGGVKGSG-FGRFAGEEGL 452
|
490
....*....|.
gi 28571800 553 LRWTSPQVIKE 563
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 ... |
216-535 |
3.19e-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: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSDSA---------ILSNYFVFKALReagvpdgVVNfVPAEETT 282
Cdd:cd07087 102 GVVLIIGPWNY---PLQLALAPligAIAaGNTVVLKPSELApatsallakLIPKYFDPEAVA-------VVE-GGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 283 fasVVTQHPkLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKC 362
Cdd:cd07087 171 ---ALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 363 SSCSMLYVPESlwqnhIREPLLE-ITASLV------VRQDATYcdsfcSAVINRRAYDRIymwLRYIDQSpscQILVGGS 435
Cdd:cd07087 241 IAPDYVLVHES-----IKDELIEeLKKAIKefygedPKESPDY-----GRIINERHFDRL---ASLLDDG---KVVIGGQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 436 CDKRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVNV 515
Cdd:cd07087 305 VDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDD--LDEAIEFINSRPKPLALYLFSEDKAVQERVLA--ETSS 379
|
330 340
....*....|....*....|
gi 28571800 516 GNLNVNDKSTGLMVGQQPFG 535
Cdd:cd07087 380 GGVCVNDVLLHAAIPNLPFG 399
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
208-500 |
4.14e-17 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 84.19 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 208 SMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAgVPDGVVNFVPAEETTFASV 286
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 287 VTQHPKLAGINFTG-TSTVLKVLwQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSC 365
Cdd:PRK13473 211 LVGHPKVRMVSLTGsIATGKHVL-SAAADSVK------RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 366 SMLYVPESLWQNHIrEPLLEITASLVV-RQDATycDSFCSAVINRRAYDRIYMWLRYIDQSPSCQILVGGSCDKRRGYYV 444
Cdd:PRK13473 284 CRIYAQRGIYDDLV-AKLAAAVATLKVgDPDDE--DTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYY 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28571800 445 DPTVVLVKDLDNIICREELLAPILGVYVYPDHKlketmEKVAQIN---HGLTGSVFAQD 500
Cdd:PRK13473 361 EPTLLAGARQDDEIVQREVFGPVVSVTPFDDED-----QAVRWANdsdYGLASSVWTRD 414
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
216-547 |
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 28571800 216 GFVAAISPFNFT------GIAANLAytpalMGNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQ 289
Cdd:cd07140 149 GVCGIVIPWNYPlmmlawKMAACLA-----AGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 290 HPKLAGINFTGTSTVLKVLWQLVAQNinfyqNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLY 369
Cdd:cd07140 224 HPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 370 VPESLWQNHIREPLLEItaslvvrQDATYCDSFCSAVI----NRRAY-DRIymwLRYIDQS--PSCQILVGGSCDKRRGY 442
Cdd:cd07140 299 VEESIHDEFVRRVVEEV-------KKMKIGDPLDRSTDhgpqNHKAHlDKL---VEYCERGvkEGATLVYGGKQVDRPGF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 443 YVDPTVVLVKDLDNIICREELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQN---FIEEAYDAFRVNVGNLN 519
Cdd:cd07140 369 FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINkalYVSDKLEAGTVFVNTYN 448
|
330 340
....*....|....*....|....*...
gi 28571800 520 VNDKSTglmvgqqPFGAGHMTGTSDKLG 547
Cdd:cd07140 449 KTDVAA-------PFGGFKQSGFGKDLG 469
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
216-535 |
2.39e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 82.00 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFtgiAANLAYTPAL----MGNSVIWKPSDSA---------ILSNYFVFKALR--EAGVPdgvvnfvpaeE 280
Cdd:PTZ00381 111 GVVLVIGAWNY---PLNLTLIPLAgaiaAGNTVVLKPSELSphtsklmakLLTKYLDPSYVRviEGGVE----------V 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 281 TTfasVVTQHPkLAGINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEY 357
Cdd:PTZ00381 178 TT---ELLKEP-FDHIFFTGSPRVGKLVMQAAAEN---------LTPctlELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 358 AGQKCSSCSMLYVPESlwqnhIREPLLEITASLVVRQ---DATYCDSFcSAVINRRAYDRIyMWLRYIDQSpscQILVGG 434
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRS-----IKDKFIEALKEAIKEFfgeDPKKSEDY-SRIVNEFHTKRL-AELIKDHGG---KVVYGG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 435 SCDKRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAYDafRVN 514
Cdd:PTZ00381 315 EVDIEN-KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYEN--IDEVLEFINSRPKPLALYYFGEDKRHKELVLE--NTS 389
|
330 340
....*....|....*....|.
gi 28571800 515 VGNLNVNDKSTGLMVGQQPFG 535
Cdd:PTZ00381 390 SGAVVINDCVFHLLNPNLPFG 410
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
216-535 |
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 28571800 216 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETtfASVVTQHP 291
Cdd:cd07134 102 GVCLIISPWNY---PFNLAFGPlvsAIAaGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEV--AQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 292 kLAGINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSML 368
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAAKH---------LASvtlELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 369 YVPESlwqnhIREPLLEITASLVVRQ-----DATYCDSFCSaVINRRAYDRIymwLRYIDQSPS--CQILVGGSCDKRRg 441
Cdd:cd07134 247 FVHES-----VKDAFVEHLKAEIEKFygkdaARKASPDLAR-IVNDRHFDRL---KGLLDDAVAkgAKVEFGGQFDAAQ- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 442 YYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKvaqINHG---LTGSVFAQDQNFIEEAYDafRVNVGNL 518
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYED--LDEVIEY---INAKpkpLALYVFSKDKANVNKVLA--RTSSGGV 389
|
330
....*....|....*..
gi 28571800 519 NVNDKSTGLMVGQQPFG 535
Cdd:cd07134 390 VVNDVVLHFLNPNLPFG 406
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
216-541 |
2.25e-14 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 75.71 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLA 294
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 295 GINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESL 374
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCAKDIK------KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 375 WqNHIREPLLEITASLVVrQDATYCDSFCSAVINRRAYDRIYmwlRYIDQ--SPSCQILVGGSCDKRRGYYVDPTVVLVK 452
Cdd:PRK11241 302 Y-DRFAEKLQQAVSKLHI-GDGLEKGVTIGPLIDEKAVAKVE---EHIADalEKGARVVCGGKAHELGGNFFQPTILVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 453 DLDNIICREELLAPILgvyvyPDHKLKETMEKVAQINH---GLTGSVFAQDQNFIEEAYDAFRVNVGNLNvndksTGLMV 529
Cdd:PRK11241 377 PANAKVAKEETFGPLA-----PLFRFKDEADVIAQANDtefGLAAYFYARDLSRVFRVGEALEYGIVGIN-----TGIIS 446
|
330
....*....|...
gi 28571800 530 GQ-QPFGAGHMTG 541
Cdd:PRK11241 447 NEvAPFGGIKASG 459
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
118-502 |
2.68e-14 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 75.56 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 118 AIDKSVEAQVKWDKVRLSDRIDIWERAAMLIagRYRYNIIAATMLGQ-GKTLRQAEMDV---AELVDFMRINPVflRELA 193
Cdd:PLN00412 58 AMESAKAAQKAWAKTPLWKRAELLHKAAAIL--KEHKAPIAECLVKEiAKPAKDAVTEVvrsGDLISYTAEEGV--RILG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 194 NYEPIRD--IQNNCRNSMRLRGLS--GFVAAISPFNFtgiAANLAYT---PALM-GNSVIWKPSDSAILSNYFVFKALRE 265
Cdd:PLN00412 134 EGKFLVSdsFPGNERNKYCLTSKIplGVVLAIPPFNY---PVNLAVSkiaPALIaGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 266 AGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKvlwqlVAQNINFYQnyprLVGEGGGKNFHFVHSSAEPET 345
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIA-----ISKKAGMVP----LQMELGGKDACIVLEDADLDL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 346 AVACTIRAAFEYAGQKCSSCSMLYVPESLwQNHIREPLLEITASLVVRQDATYCDsfCSAVINRRAYDRIymwlryidqs 425
Cdd:PLN00412 282 AAANIIKGGFSYSGQRCTAVKVVLVMESV-ADALVEKVNAKVAKLTVGPPEDDCD--ITPVVSESSANFI---------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 426 pscQILVGGSCDK---------RRGYYVDPTVvlvkdLDNI-----ICREELLAPILGVYVYPDhkLKETMEKVAQINHG 491
Cdd:PLN00412 349 ---EGLVMDAKEKgatfcqewkREGNLIWPLL-----LDNVrpdmrIAWEEPFGPVLPVIRINS--VEEGIHHCNASNFG 418
|
410
....*....|.
gi 28571800 492 LTGSVFAQDQN 502
Cdd:PLN00412 419 LQGCVFTRDIN 429
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
81-512 |
2.06e-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: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 81 INGqEFQAK---EDFQQVLPYDiQQPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWERAAMLIAGRYRYNII 157
Cdd:cd07116 5 IGG-EWVAPvkgEYFDNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 158 AATmLGQGKTLRQA-EMDVAELVDFMRINPVFLRelANYEPIRDIQNNCRnSMRLRGLSGFVAAISPFNFTGIAANLAYT 236
Cdd:cd07116 83 AET-WDNGKPVRETlAADIPLAIDHFRYFAGCIR--AQEGSISEIDENTV-AYHFHEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 237 PALM-GNSVIWKPSDSAILSnYFVFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQN 315
Cdd:cd07116 159 PALAaGNCVVLKPAEQTPAS-ILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 316 InfyqnYPRLVgEGGGK--NFHFVHSSAEPETAVACTIRAAFEYA---GQKCSSCSMLYVPESLWQNHIREPLLEITAsl 390
Cdd:cd07116 238 I-----IPVTL-ELGGKspNIFFADVMDADDAFFDKALEGFVMFAlnqGEVCTCPSRALIQESIYDRFMERALERVKA-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 391 vVRQ-----DATYCDSFCSAVinrrAYDRIymwLRYID--QSPSCQILVGG----SCDKRRGYYVDPTVVLvKDLDNIIC 459
Cdd:cd07116 310 -IKQgnpldTETMIGAQASLE----QLEKI---LSYIDigKEEGAEVLTGGerneLGGLLGGGYYVPTTFK-GGNKMRIF 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 28571800 460 REELLAPILGVYVYPDHklKETMEKVAQINHGLTGSVFAQDQNfieEAYDAFR 512
Cdd:cd07116 381 QEEIFGPVLAVTTFKDE--EEALEIANDTLYGLGAGVWTRDGN---TAYRMGR 428
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
164-468 |
4.88e-12 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 68.62 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 164 QGKTLRQAEMDVAELVDFMRiNPVFLRELANYEPIRDIQNNCrNSMRLRGLSGFVAAISPFNFTGIAANLAYTPALM-GN 242
Cdd:PLN02419 201 QGKTLKDSHGDIFRGLEVVE-HACGMATLQMGEYLPNVSNGV-DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTcGN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 243 SVIWKPSDSAILSNYFVFKALREAGVPDGVVNFVPAEETTfASVVTQHPKLAGINFTGTSTV-LKVLWQLVAQNinfyqn 321
Cdd:PLN02419 279 TFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDT-VNAICDDEDIRAVSFVGSNTAgMHIYARAAAKG------ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 322 yPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCS-MLYVPES-LWQNHI--REPLLEITAslvvrqdAT 397
Cdd:PLN02419 352 -KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALStVVFVGDAkSWEDKLveRAKALKVTC-------GS 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571800 398 YCDSFCSAVINRRAYDRIYMWLRY-IDQSPSC-----QILVGGScdkRRGYYVDPTVVLVKDLDNIICREELLAPIL 468
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSgVDDGAKLlldgrDIVVPGY---EKGNFIGPTILSGVTPDMECYKEEIFGPVL 497
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
216-505 |
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 28571800 216 GFVAAISPFNFtgiAANLAYTP---ALM-GNSVIWKPSD---------SAILSNYFvfkalreagvPDGVVNFVP--AEE 280
Cdd:cd07136 102 GVVLIIAPWNY---PFQLALAPligAIAaGNTAVLKPSEltpntskviAKIIEETF----------DEEYVAVVEggVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 281 TTFasvvTQHPKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 360
Cdd:cd07136 169 NQE----LLDQKFDYIFFTGSVRVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 361 KCSSCSMLYVPESlwqnhIREPLLEITASLVVRQ---DATYCDSFCSaVINRRAYDRIymwLRYIDQSpscQILVGGSCD 437
Cdd:cd07136 239 TCVAPDYVLVHES-----VKEKFIKELKEEIKKFygeDPLESPDYGR-IINEKHFDRL---AGLLDNG---KIVFGGNTD 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 438 KRRgYYVDPTVVLVKDLDNIICREELLAPILGVYVYpdHKLKETMEKVAQINHGLTGSVFAQDQNFIE 505
Cdd:cd07136 307 RET-LYIEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEK 371
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
216-575 |
2.35e-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: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFT-GIAANLAYTPALMGNSVIWKpSDS--AILSNYFVfKALREAGVPDGVVNFVPAEETTFASVVTQ-HP 291
Cdd:cd07126 144 GPVAIITPFNFPlEIPALQLMGALFMGNKPLLK-VDSkvSVVMEQFL-RLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 292 KLagINFTGTSTVLKVLWQLVAQNINFyqnyprlvgEGGGKNFHFVHSSAEPETAVA--CTiRAAFEYAGQKCSSCSMLY 369
Cdd:cd07126 222 RM--TLFTGSSKVAERLALELHGKVKL---------EDAGFDWKILGPDVSDVDYVAwqCD-QDAYACSGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 370 VPEslwqNHIREPLLEITASLVVR---QDATYCDSFcsAVINRRAYDRIYMWLryidQSPSCQILVGG------SCDKRR 440
Cdd:cd07126 290 AHE----NWVQAGILDKLKALAEQrklEDLTIGPVL--TWTTERILDHVDKLL----AIPGAKVLFGGkpltnhSIPSIY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 441 GYYvDPTVVLVKdLDNIICRE-------ELLAPILGVYVYPDHKLKETMEKVAQINHGLTGSVFAQDQNFIEEAYdAFRV 513
Cdd:cd07126 360 GAY-EPTAVFVP-LEEIAIEEnfelvttEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVL-ANTV 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571800 514 N-VGNLNVNDKSTGlmvgqQP----FG-AGHMTGTSdkLGTphsllrwtsPQVIKESYKTHRNIFYPY 575
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 ... |
216-535 |
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 28571800 216 GFVAAISPFNFT----------GIAAnlaytpalmGNSVIWKPSD-----SAILSN----YFVFKALR--EAGVPDGvvn 274
Cdd:cd07137 103 GVVLVISAWNFPfllslepvigAIAA---------GNAVVLKPSElapatSALLAKlipeYLDTKAIKviEGGVPET--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 275 fvpaeettfaSVVTQHpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPrLVGEGGGKNFHFVHSSAEPETAVACTIRAA 354
Cdd:cd07137 171 ----------TALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRIAGGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 355 FEY-AGQKCSSCSMLYVPESLWQNHIRepLLEITASLVVRQDATYCDSFcSAVINRRAYDRIYMWLRyiDQSPSCQILVG 433
Cdd:cd07137 234 WGCnNGQACIAPDYVLVEESFAPTLID--ALKNTLEKFFGENPKESKDL-SRIVNSHHFQRLSRLLD--DPSVADKIVHG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 434 GSCDKRRgYYVDPTVVLVKDLDNIICREELLAPILgvyvyPDHKLKETMEKVAQIN---HGLTGSVFAQDQNFIEEAYDA 510
Cdd:cd07137 309 GERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLL-----PIITVKKIEESIEIINsrpKPLAAYVFTKNKELKRRIVAE 382
|
330 340
....*....|....*....|....*
gi 28571800 511 frVNVGNLNVNDKSTGLMVGQQPFG 535
Cdd:cd07137 383 --TSSGGVTFNDTVVQYAIDTLPFG 405
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
216-536 |
5.58e-07 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 52.36 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIaanLAYTPAL----MGNSVIWKPSDSAILSNYFVFKALrEAGVPDGVVNFVPAEETTFASVVTQhp 291
Cdd:PLN02174 114 GVVLVISAWNYPFL---LSIDPVIgaisAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 292 KLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFE-YAGQKCSSCSMLYV 370
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLT------PVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 371 PESLWQNHIREPLLEItASLVVRQDATYCDsfCSAVINRRAYDRIYMWLRyiDQSPSCQILVGGSCDkRRGYYVDPTVVL 450
Cdd:PLN02174 262 TKEYAPKVIDAMKKEL-ETFYGKNPMESKD--MSRIVNSTHFDRLSKLLD--EKEVSDKIVYGGEKD-RENLKIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 451 VKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHGLTGSVFAQDQNFIEEAydAFRVNVGNLNVNDKSTGLMVG 530
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNN--LEESFDVIRSRPKPLAAYLFTHNKKLKERF--AATVSAGGIVVNDIAVHLALH 411
|
....*.
gi 28571800 531 QQPFGA 536
Cdd:PLN02174 412 TLPFGG 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
259-558 |
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 28571800 259 VFKALREAGVPDGVVNFVPAEETTFASVVTQHPKLAGINFTGTSTVLKVLWQLVAQN---INFYqnyprlvGEGGGKNFH 335
Cdd:cd07129 157 IRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepIPFY-------AELGSVNPV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 336 FVHSSAEPETAVActIRAAFEY-----AGQKCSSCSMLYVPESLWQnhirEPLLEITASLVVRQDAT------YCDSFCS 404
Cdd:cd07129 230 FILPGALAERGEA--IAQGFVGsltlgAGQFCTNPGLVLVPAGPAG----DAFIAALAEALAAAPAQtmltpgIAEAYRQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 405 AVINRRAydriymwlryidqSPSCQILVGGScDKRRGYYVDPTVVLVkDLDNIICREELLAPILG----VYVYPDHklkE 480
Cdd:cd07129 304 GVEALAA-------------APGVRVLAGGA-AAEGGNQAAPTLFKV-DAAAFLADPALQEEVFGpaslVVRYDDA---A 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 481 TMEKVAQINHG-LTGSVFA--QDQNFIEEAYDAFRVNVGNLNVNDKSTGLMVG--QQ---PFGAghmtgTSDKLGT---P 549
Cdd:cd07129 366 ELLAVAEALEGqLTATIHGeeDDLALARELLPVLERKAGRLLFNGWPTGVEVCpaMVhggPYPA-----TTDPRFTsvgT 440
|
....*....
gi 28571800 550 HSLLRWTSP 558
Cdd:cd07129 441 AAIERFLRP 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
102-521 |
4.56e-06 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 49.47 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 102 QPIAHYGHAHRVLIQMAIDKSVEAQVKWDKVRLSDRIDIWER--AAMLIAGRYRYNIIAATMlgqGKTLRQAEMDVAE-- 177
Cdd:PRK13968 18 EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDigKALRARSEEMAQMITREM---GKPINQARAEVAKsa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 178 -LVD-FMRINPVFLrelaNYEPIrdIQNNCRNSMRLRGLsGFVAAISPFNFTGIAANLAYTPALM-GNSVIWKPSDSAIL 254
Cdd:PRK13968 95 nLCDwYAEHGPAML----KAEPT--LVENQQAVIEYRPL-GTILAIMPWNFPLWQVMRGAVPILLaGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 255 SNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQhPKLAGINFTGTSTVLKVLWQLVAQNINfyqnypRLVGEGGGKNF 334
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 335 HFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYVPESLWQNhIREPLLEITASLVV---RQDATYCDSFCSAVINRRA 411
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASA-FTERFVAAAAALKMgdpRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 412 YDRIYMWLryidqSPSCQILVGGSCDKRRGYYVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETMEKVAQINHG 491
Cdd:PRK13968 320 HHQVEATL-----AEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKD--AEHALELANDSEFG 392
|
410 420 430
....*....|....*....|....*....|
gi 28571800 492 LTGSVFAQDQNFIEEAydAFRVNVGNLNVN 521
Cdd:PRK13968 393 LSATIFTTDETQARQM--AARLECGGVFIN 420
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
216-374 |
2.54e-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: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFTGIAANLAYTPALMGNSVIWKPSDSAILSNY---FVFKALREAGVPDGVVNFVPAEETTFASVVTQHPK 292
Cdd:cd07077 102 GVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPFTNRalaLLFQAADAAHGPKILVLYVPHPSDELAEELLSHPK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 293 LAGINFTGTSTVLKVLWQlvaqninfYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYaGQKCSSCSMLYVPE 372
Cdd:cd07077 182 IDLIVATGGRDAVDAAVK--------HSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVD 252
|
..
gi 28571800 373 SL 374
Cdd:cd07077 253 DV 254
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
216-535 |
4.71e-04 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 43.18 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNFtgiAANLAYTPAL----MGNSVIWKPSD-----SAILSN----YFVFKALReagvpdgVVNFVPAeett 282
Cdd:PLN02203 110 GVVLIFSSWNF---PIGLSLEPLIgaiaAGNAVVLKPSElapatSAFLAAnipkYLDSKAVK-------VIEGGPA---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 283 FASVVTQHpKLAGINFTGTSTVLKVLWQLVAQNINfyqnyPRLVgEGGGKN---FHFVHSSAEPETAVACTIRAAFEY-A 358
Cdd:PLN02203 176 VGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLT-----PVAL-ELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 359 GQKCSSCSMLYVPESLWQNHIRepLLEITASLVVRQDATYCDSFCSaVINRRAYDRIYMWLRyiDQSPSCQILVGGSCDK 438
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIE--LLKSTIKKFFGENPRESKSMAR-ILNKKHFQRLSNLLK--DPRVAASIVHGGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 439 RRgYYVDPTVVLVKDLDNIICREELLAPILgvyvyPDHKLKETMEKVAQIN---HGLTGSVFAQDQNF----IEEAydaf 511
Cdd:PLN02203 324 KK-LFIEPTILLNPPLDSDIMTEEIFGPLL-----PIITVKKIEDSIAFINskpKPLAIYAFTNNEKLkrriLSET---- 393
|
330 340
....*....|....*....|....
gi 28571800 512 rvNVGNLNVNDKSTGLMVGQQPFG 535
Cdd:PLN02203 394 --SSGSVTFNDAIIQYACDSLPFG 415
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
216-535 |
5.94e-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: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPFNF----------TGIAAnlaytpalmGNSVIWKPSDSAILSNYFVFKALREAGVPD--GVVNFVPAEETTF 283
Cdd:cd07133 103 GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAELLAEYFDEDevAVVTGGADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 284 ASVVTQHpklagINFTGTSTVLKVLWQLVAQNinfyqnyprLVG---EGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQ 360
Cdd:cd07133 174 SSLPFDH-----LLFTGSTAVGRHVMRAAAEN---------LTPvtlELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 361 KCSSCSMLYVPESLwqnhiREPLLEITASLVVRQDATYCDSF-CSAVINRRAYDRIYMWL--------RYIDQSPSCQIL 431
Cdd:cd07133 240 TCVAPDYVLVPEDK-----LEEFVAAAKAAVAKMYPTLADNPdYTSIINERHYARLQGLLedarakgaRVIELNPAGEDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 432 VGGscdkRRgyyVDPTVVLVKDLDNIICREELLAPILGVYVYPDhkLKETmekVAQIN---HGLTGSVFAQD---QNFIE 505
Cdd:cd07133 315 AAT----RK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDS--LDEA---IDYINarpRPLALYYFGEDkaeQDRVL 382
|
330 340 350
....*....|....*....|....*....|..
gi 28571800 506 EaydafRVNVGNLNVNDksTGLMVGQ--QPFG 535
Cdd:cd07133 383 R-----RTHSGGVTIND--TLLHVAQddLPFG 407
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
216-381 |
3.66e-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: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 216 GFVAAISPF-NFTGIAANLAYTPALMGNSVIWKP----SDSAILSNYFVFKALREAGVPDGVVNFVPAEETTFASVVTQH 290
Cdd:cd07081 97 GVVASITPStNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571800 291 PKLAGINFTGTSTVLKVLwqlvaqninfYQNYPRLVGEGGGKNFHFVHSSAEPETAVACTIRAAFEYAGQKCSSCSMLYV 370
Cdd:cd07081 177 PGIGLLLATGGPAVVKAA----------YSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170
....*....|.
gi 28571800 371 PESLWQNHIRE 381
Cdd:cd07081 247 VDSVYDEVMRL 257
|
|
| |
