|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-531 |
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: 969.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 11 AVNEPVKSYAPNSPEKAAVQAAYTTMWNSQIDVPLYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALE 90
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 91 ARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATMIGQSKNIHQAEIDSSCELIDFLRYNVEFMTQIYNDQPKS-DST 169
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSsPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 170 VWNRVEYRPLEGFVYAITPFNFTAIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMIT 249
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 250 DTVLASRDFAGIHFTGSTHVFKDIWAKIGANINNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSA 329
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 330 ASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDADAEIIVGGNYDKSVGYFIEP 409
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 410 TVIVTTNPKYTTMETELFGPVITLYVYEDAKWEETLELVDTTSEYALTGAVFSQDRYAIEVATTKLQNAAGNFYINDKPT 489
Cdd:cd07123 401 TVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2006071571 490 GAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTIKETFVT 531
Cdd:cd07123 481 GAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
13-541 |
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: 770.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 13 NEPVKSYAPNSPEKAAVQAAYTTMWNSQIDVPLYIGSEEIRTGN-TKNITAPHDHQHVVGKYHLAEKKHIESAIANALEA 91
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNeRIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 92 RKAWANMAWEQRAAIFLKAAELIAGPYRARINAATMIGQSKNIHQAEIDSSCELIDFLRYNVEFMTQIYNDQPKSDSTVW 171
Cdd:TIGR01236 82 KKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGEW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 172 NRVEYRPLEGFVYAITPFNFTAIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDT 251
Cdd:TIGR01236 162 NRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 252 VLASRDFAGIHFTGSTHVFKDIWAKIGANINNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAAS 331
Cdd:TIGR01236 242 VLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAAS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 332 RAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDADA-EIIVGGNYDKSVGYFIEPT 410
Cdd:TIGR01236 322 RLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGYFVEPT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 411 VIVTTNPKYTTMETELFGPVITLYVYEDAKWEETLELVDTTSEYALTGAVFSQDRYAIEVATTKLQNAAGNFYINDKPTG 490
Cdd:TIGR01236 402 VVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCTG 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2006071571 491 AVVGMQPFGGARASGTNDKAGSALNLLRWASPRTIKETFVTPEDYRYPFLG 541
Cdd:TIGR01236 482 AVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
39-529 |
2.53e-149 |
|
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: 436.86 E-value: 2.53e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 39 SQIDVPLYIGSEEIR--TGNTKNITAPHDhQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAG 116
Cdd:COG1012 2 TTPEYPLFIGGEWVAaaSGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 117 pYRARINAATMIGQSKNIHQA--EIDsscELIDFLRYNVEFMTQIYNDQ-PKSDSTVWNRVEYRPLeGFVYAITPFNFTA 193
Cdd:COG1012 81 -RREELAALLTLETGKPLAEArgEVD---RAADFLRYYAGEARRLYGETiPSDAPGTRAYVRREPL-GVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 194 IAANLPASAAM-MGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKD 272
Cdd:COG1012 156 ALAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 273 IWAKIGANInnyktyPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVK 352
Cdd:COG1012 236 IAAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 353 SMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkKDADAEIIVGGNY-DKSVGYFIEPTVIVTTNPKYTTMETELFGPVI 431
Cdd:COG1012 310 ALKVGDPLDPGTDMGPLISEAQLERVLAYIEDA-VAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 432 TLYVYEDakWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMqPFGGARASGTNDKAG 511
Cdd:COG1012 389 SVIPFDD--EEEAIALANDT-EYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGAVPQA-PFGGVKQSGIGREGG 462
|
490
....*....|....*...
gi 2006071571 512 SAlNLLRWASPRTIKETF 529
Cdd:COG1012 463 RE-GLEEYTETKTVTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
44-529 |
2.17e-148 |
|
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: 435.47 E-value: 2.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 44 PLYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRARIN 123
Cdd:cd07083 20 PLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 124 AATMIGqSKNIHQaEIDSSCELIDFLRYN----VEFMTQIYNDQPKSDSTvwNRVEYRPLeGFVYAITPFNFT-AIAANL 198
Cdd:cd07083 100 TLTYEV-GKNWVE-AIDDVAEAIDFIRYYaraaLRLRYPAVEVVPYPGED--NESFYVGL-GAGVVISPWNFPvAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 199 PASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIG 278
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 279 ANINNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGS 358
Cdd:cd07083 255 RLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 359 PEDFGNFITAVIHEGSFDKLASYIDQAKKdaDAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYED 438
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 439 AKWEETLELVDTTSEYALTGAVFSQDRYAIEvATTKLqnAAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLR 518
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHLEE-ARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRR 489
|
490
....*....|.
gi 2006071571 519 WASPRTIKETF 529
Cdd:cd07083 490 FLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-529 |
1.33e-122 |
|
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: 369.63 E-value: 1.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 12 VNEPVKSYAPnsPE-KAAVQAAYTTMWNS-QIDVPLYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANAL 89
Cdd:cd07124 2 RNEPFTDFAD--EEnRAAFRAALARVREElGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 90 EARKAWANMAWEQRAAIFLKAAELIagpyRAR---INAATMIGQSKNIHQAEIDSsCELIDFLRYNVEFMTQiYNDQPKS 166
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALL----RRRrfeLAAWMVLEVGKNWAEADADV-AEAIDFLEYYAREMLR-LRGFPVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 167 DST-VWNRVEYRPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGD 244
Cdd:cd07124 154 MVPgEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 245 ALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQG 324
Cdd:cd07124 233 GEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 325 QKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKdaDAEIIVGGNYDKSV- 403
Cdd:cd07124 313 QKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS--EGRLLLGGEVLELAa 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 404 -GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDakWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNF 482
Cdd:cd07124 391 eGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDT-EYGLTGGVFSRSPEHLERARREFE--VGNL 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2006071571 483 YINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTIKETF 529
Cdd:cd07124 466 YANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
54-513 |
2.88e-113 |
|
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: 343.74 E-value: 2.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 54 TGNTKNITAPHDhQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARINAATMIGQSKN 133
Cdd:pfam00171 5 ESETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEE-RKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 134 IHQA--EIDSScelIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVV 210
Cdd:pfam00171 83 LAEArgEVDRA---IDVLRYYAGLARRLDGETLPSDPGRLAYTRREPL-GVVGAITPWNFpLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 211 WKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyktyPRI 290
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 291 VGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVI 370
Cdd:pfam00171 233 TLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 371 HEGSFDKLASYIDQAKKDaDAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDT 450
Cdd:pfam00171 313 SKAQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEIAND 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006071571 451 TsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMqPFGGARASGTNDKAGSA 513
Cdd:pfam00171 390 T-EYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADGL-PFGGFKQSGFGREGGPY 448
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
13-529 |
2.76e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 330.36 E-value: 2.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 13 NEPVKSYApNSPEKAAVQAAYTTMwNSQI--DVPLYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALE 90
Cdd:PRK03137 7 HEPFTDFS-VEENVEAFEEALKKV-EKELgqDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 91 ARKAWANMAWEQRAAIFLKAAELIagpyRAR---INAATMIGQSKNIHQAEIDSsCELIDFLRYNVEFMTQIYNDQP-KS 166
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAII----RRRkheFSAWLVKEAGKPWAEADADT-AEAIDFLEYYARQMLKLADGKPvES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 167 DSTVWNRVEYRPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDA 245
Cdd:PRK03137 160 RPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 246 LMITDTVLASRDFAGIHFTGSTHVFKDIW---AKIGANINNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEF 322
Cdd:PRK03137 239 SEVGDYLVDHPKTRFITFTGSREVGLRIYeraAKVQPGQIWLK---RVIAEMGGKDAIVVDEDADLDLAAESIVASAFGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 323 QGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFgNFITAVIHEGSFDKLASYIDQAKKdaDAEIIVGGNYDKS 402
Cdd:PRK03137 316 SGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKE--EGRLVLGGEGDDS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 403 VGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDakWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNF 482
Cdd:PRK03137 393 KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANNT-EYGLTGAVISNNREHLEKARREFH--VGNL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2006071571 483 YINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTIKETF 529
Cdd:PRK03137 468 YFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-529 |
4.80e-102 |
|
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: 316.81 E-value: 4.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 13 NEPVKSYAPNSPEKAAVQAAYTTMWNSQIDVPLYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEAR 92
Cdd:TIGR01237 3 HEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 93 KAWANMAWEQRAAIFLKAAElIAGPYRARINAATMIGQSKNIHQAEIDSScELIDFLRYNVEFMTQIYNDQPKSD-STVW 171
Cdd:TIGR01237 83 EAWKKTDPEERAAILFKAAA-IVRRRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVNSrEGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 172 NRVEYRPLeGFVYAITPFNFT-AIAANLPASAAMMGNVVVWKP-SDSQVFSAKIiVDVFKEAGVPDGVINVVFGDALMIT 249
Cdd:TIGR01237 161 NQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPaEAAPVIAAKF-VEILEEAGLPKGVVQFVPGSGSEVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 250 DTVLASRDFAGIHFTGSTHVFKDIWAKIGANINNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSA 329
Cdd:TIGR01237 239 DYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 330 ASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKkdADAEIIVGGNYDKSVGYFIEP 409
Cdd:TIGR01237 319 GSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGK--AEGRLVSGGCGDDSKGYFIGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 410 TVIVTTNPKYTTMETELFGPVITlyVYEDAKWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPT 489
Cdd:TIGR01237 397 TIFADVDRKARLAQEEIFGPVVA--FIRASDFDEALEIANNT-EYGLTGGVISNNRDHINRAKAEFE--VGNLYFNRNIT 471
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2006071571 490 GAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTIKETF 529
Cdd:TIGR01237 472 GAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-525 |
4.29e-101 |
|
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: 311.83 E-value: 4.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 82 ESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATMIGQsKNIHQA--EIDsscELIDFLRYNVEFMTQI 159
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETG-KPIEEAlgEVA---RAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 160 YNDQPKSDSTVW-NRVEYRPLeGFVYAITPFNFT-AIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGV 237
Cdd:cd07078 77 HGEVIPSPDPGElAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 238 INVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyktyPRIVGETGGKDFIIAHPSANVKQVVTGITR 317
Cdd:cd07078 156 LNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 318 GAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGG 397
Cdd:cd07078 230 GAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-AKLLCGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 398 NYDKS-VGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQ 476
Cdd:cd07078 309 KRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDT-EYGLAAGVFTRDLERALRVAERLE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2006071571 477 naAGNFYINDKPTGAVVGMqPFGGARASGTNdKAGSALNLLRWASPRTI 525
Cdd:cd07078 386 --AGTVWINDYSVGAEPSA-PFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
44-525 |
1.54e-77 |
|
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: 253.27 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 44 PLYIGsEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARIN 123
Cdd:cd07125 35 PIING-EETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEA-NRGELI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 124 AATMIGQSKNIHQAEIDSScELIDFLRYNVEFMTQIYNDQPKSDSTVW-NRVEYRPLeGFVYAITPFNF-TAIAANLPAS 201
Cdd:cd07125 113 ALAAAEAGKTLADADAEVR-EAIDFCRYYAAQARELFSDPELPGPTGElNGLELHGR-GVFVCISPWNFpLAIFTGQIAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 202 AAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwakIGANI 281
Cdd:cd07125 191 ALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI---NRALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 282 NNYKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPED 361
Cdd:cd07125 268 ERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 362 FGNFITAVIHEGSFDKLASYIDqaKKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPkyTTMETELFGPVITLYVYEDAKW 441
Cdd:cd07125 348 LSTDVGPLIDKPAGKLLRAHTE--LMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGI--FDLTTEVFGPILHVIRFKAEDL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 442 EETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWAS 521
Cdd:cd07125 424 DEAIEDINAT-GYGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGN 500
|
....
gi 2006071571 522 PRTI 525
Cdd:cd07125 501 EKTV 504
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
88-525 |
1.79e-68 |
|
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: 224.80 E-value: 1.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 88 ALEARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATMIGQsKNIHQAEIDSsCELIDFLRYNVEFMTQI-YNDQPKS 166
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-KPIEEALGEV-ARAIDTFRYAAGLADKLgGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 167 DSTVWNRVEYRPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDA 245
Cdd:cd06534 81 DPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 246 LMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyktyPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQ 325
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 326 KCSAASRAYIPQSLWPAVKEQLIadvksmkmgspedfgnfitavihegsfdklasyidqakkdadaeiivggnydksvgy 405
Cdd:cd06534 234 ICTAASRLLVHESIYDEFVEKLV--------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 406 fiepTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYIN 485
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGTVYIN 327
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2006071571 486 DKPTGAVVGMqPFGGARASGTNDKAGSALnLLRWASPRTI 525
Cdd:cd06534 328 DSSIGVGPEA-PFGGVKNSGIGREGGPYG-LEEYTRTKTV 365
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
81-505 |
2.71e-65 |
|
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: 218.55 E-value: 2.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRARInAATMIGQSKNIH---QAEIDSScelIDFLRYNVEFMT 157
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE-ERRDEI-ADWLIRESGSTRpkaAFEVGAA---IAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 158 QIYND-QPKSDSTVWNRVEYRPLeGFVYAITPFNFT---AIAANLPASAamMGNVVVWKPS-DSQVFSAKIIVDVFKEAG 232
Cdd:cd07104 77 RPEGEiLPSDVPGKESMVRRVPL-GVVGVISPFNFPlilAMRSVAPALA--LGNAVVLKPDsRTPVTGGLLIAEIFEEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 233 VPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDFIIAHPSANVKQVV 312
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLK------KVALELGGNNPLIVLDDADLDLAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 313 TGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkKDADAE 392
Cdd:cd07104 228 SAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDA-VAAGAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 393 IIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDRY-AIEVA 471
Cdd:cd07104 307 LLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVELANDT-EYGLSAAVFTRDLErAMAFA 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 2006071571 472 ttkLQNAAGNFYINDKPT--GAVVgmqPFGGARASG 505
Cdd:cd07104 381 ---ERLETGMVHINDQTVndEPHV---PFGGVKASG 410
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-505 |
6.07e-65 |
|
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: 217.97 E-value: 6.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARIN--AATMIGQSKNIHQAEIDSSCELI 146
Cdd:cd07150 11 VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM----ERRADdlIDLLIDEGGSTYGKAWFETTFTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 147 DFLRYNVEFMTQIYNDQPKSDST-VWNRVEYRPLeGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDSQVFSAKII 224
Cdd:cd07150 87 ELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPL-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 225 VDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDFIIAHP 304
Cdd:cd07150 166 AEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLK------KITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 305 SANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQ 384
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 385 AKKDAdAEIIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQD 464
Cdd:cd07150 320 AVAKG-AKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDA--EEALELANDT-EYGLSAAILTND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2006071571 465 ryaIEVATTKLQNA-AGNFYINDKP--TGAVVgmqPFGGARASG 505
Cdd:cd07150 393 ---LQRAFKLAERLeSGMVHINDPTilDEAHV---PFGGVKASG 430
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
46-505 |
7.53e-64 |
|
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: 215.96 E-value: 7.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 46 YIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAA 125
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEA--RKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 126 TMI---GQSKNIHQAEIDSSCELIDFlrYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNF-TAIAANLPAS 201
Cdd:cd07097 82 LLTreeGKTLPEARGEVTRAGQIFRY--YAGEALRLSGETLPSTRPGVEVETTREPL-GVVGLITPWNFpIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 202 AAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANI 281
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 282 NnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPED 361
Cdd:cd07097 239 A------RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 362 FGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSV--GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDa 439
Cdd:cd07097 313 EGVDIGPVVSERQLEKDLRYIEIARSEG-AKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD- 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 440 kWEETLELVDTTsEYALTGAvfsqdryaieVATTKLQNA--------AGNFYINdKPTGAVVGMQPFGGARASG 505
Cdd:cd07097 391 -YDEALAIANDT-EFGLSAG----------IVTTSLKHAthfkrrveAGVVMVN-LPTAGVDYHVPFGGRKGSS 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
69-506 |
1.89e-62 |
|
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: 211.65 E-value: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARINAATMIGQSKNIHQA---EIDSSCEL 145
Cdd:cd07093 9 VLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEA-RADELALLESLDTGKPITLArtrDIPRAAAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 146 IDFLrynVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFT------AIAanlPASAAmmGNVVVWKPSDSQVF 219
Cdd:cd07093 88 FRFF---ADYILQLDGESYPQDGGALNYVLRQPV-GVAGLITPWNLPlmlltwKIA---PALAF--GNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 220 SAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDF 299
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLK------PVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 300 IIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLA 379
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 380 SYIDQAKKDaDAEIIVGGNYDKSV----GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYA 455
Cdd:cd07093 313 GYVELARAE-GATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDT-PYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006071571 456 LTGAVFSQD-RYAIEVAtTKLQnaAGNFYIN-----DKPTgavvgmqPFGGARASGT 506
Cdd:cd07093 389 LAAYVWTRDlGRAHRVA-RRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
60-506 |
1.83e-61 |
|
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: 208.99 E-value: 1.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 60 ITAPHDhQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAATMIGQS-KNIHQA- 137
Cdd:cd07149 3 VISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEE--RREEFARTIALEAgKPIKDAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 138 -EIDSScelIDFLRYNVEFMTQIYNDQPKSDSTVW--NRVEY---RPLeGFVYAITPFNFtaiAANL------PASAAmm 205
Cdd:cd07149 80 kEVDRA---IETLRLSAEEAKRLAGETIPFDASPGgeGRIGFtirEPI-GVVAAITPFNF---PLNLvahkvgPAIAA-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 206 GNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANinnyk 285
Cdd:cd07149 151 GNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 286 typRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNF 365
Cdd:cd07149 226 ---KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 366 ITAVIHEGSFDKLASYIDQAkKDADAEIIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDakWEETL 445
Cdd:cd07149 303 VGPMISEAEAERIEEWVEEA-VEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDT--LDEAI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 446 ELVDtTSEYALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKPTGAVVGMqPFGGARASGT 506
Cdd:cd07149 377 AMAN-DSPYGLQAGVFTNDlQKALKAA-RELE--VGGVMINDSSTFRVDHM-PYGGVKESGT 433
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
46-505 |
4.44e-59 |
|
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: 203.19 E-value: 4.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 46 YIGSEEIRT-GNTKNITAPHDHQhVVGKYHLAEKKHIESAIANALEARKAWAN-MAWEQRAAIFLKAAELIAgPYRARIN 123
Cdd:cd07082 5 LINGEWKESsGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLK-ENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 124 AATM--IGQSKNIHQAEIDSScelIDFLRYNVEFMTQIYNDQPKSDSTVWNR-----VEYRPLeGFVYAITPFNFTA-IA 195
Cdd:cd07082 83 NLLMweIGKTLKDALKEVDRT---IDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaqVRREPL-GVVLAIGPFNYPLnLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 196 ANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwA 275
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 276 KIGANInnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMK 355
Cdd:cd07082 238 KQHPMK-------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 356 MGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDksVGYFIEPTVIVTTNPKYTTMETELFGPVITLYV 435
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKG-ATVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006071571 436 YEDAkwEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPT-GavVGMQPFGGARASG 505
Cdd:cd07082 388 VNDI--EEAIELAN-KSNYGLQASIFTKDINKARKLADALE--VGTVNINSKCQrG--PDHFPFLGRKDSG 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
45-513 |
5.06e-59 |
|
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: 203.06 E-value: 5.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 45 LYIGSEEIRTGNTK--NITAPHDHQhVVGKYHLAEKKHIESAIANALEA-RKAWANMAWEQRAAIFLKAAELIAGpYRAR 121
Cdd:cd07113 2 HFIDGRPVAGQSEKrlDITNPATEQ-VIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 122 INAATMIGQSKNIHQA---EIDSScelIDFLRYNVEFMTQIYND--QPKSDS------TVWNRVEyrPLeGFVYAITPFN 190
Cdd:cd07113 80 LAQLETLCSGKSIHLSrafEVGQS---ANFLRYFAGWATKINGEtlAPSIPSmqgeryTAFTRRE--PV-GVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 191 FTA-IAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHV 269
Cdd:cd07113 154 FSVmIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 270 FKdiwaKIGANINNYKTypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIA 349
Cdd:cd07113 233 GK----KIGRQAASDLT--RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 350 DVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDADaEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGP 429
Cdd:cd07113 307 ALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 430 VITLYVYEDAkwEETLELVDTTsEYALTGAVFSQD-----RYAievatTKLQnaAGNFYINDKP--TGAVvgmqPFGGAR 502
Cdd:cd07113 386 VVSFVPYEDE--EELIQLINDT-PFGLTASVWTNNlskalRYI-----PRIE--AGTVWVNMHTflDPAV----PFGGMK 451
|
490
....*....|.
gi 2006071571 503 ASGTNDKAGSA 513
Cdd:cd07113 452 QSGIGREFGSA 462
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
46-506 |
5.30e-59 |
|
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: 202.96 E-value: 5.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 46 YIGSE--EIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAgpyRARIN 123
Cdd:cd07131 2 YIGGEwvDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK---KRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 124 AATMIGQS--KNIHQAEIDSScELIDFLRYNVEFMTQIYNDQpkSDSTVWNRVEY---RPLeGFVYAITPFNF-TAIAAN 197
Cdd:cd07131 79 LARLVTREmgKPLAEGRGDVQ-EAIDMAQYAAGEGRRLFGET--VPSELPNKDAMtrrQPI-GVVALITPWNFpVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 198 LPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwAKI 277
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERI-GET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 278 GAninnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMG 357
Cdd:cd07131 234 CA-----RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 358 SPEDFGNFITAVIHEGSFDKLASYIDQAKKDA-----DAEIIVGGNYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVIT 432
Cdd:cd07131 309 DGLDEETDMGPLINEAQLEKVLNYNEIGKEEGatlllGGERLTGGGYEK--GYFVEPTVFTDVTPDMRIAQEEIFGPVVA 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 433 LYVYEDakWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMqPFGGARASGT 506
Cdd:cd07131 387 LIEVSS--LEEAIEIANDT-EYGLSSAIYTEDVNKAFRARRDLE--AGITYVNAPTIGAEVHL-PFGGVKKSGN 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
69-505 |
8.23e-59 |
|
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: 201.89 E-value: 8.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINA-ATMIG--QSKNIHQA--EIDSSC 143
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI----RERAEDlARLLTleQGKPLAEArgEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 144 eliDFLRYNVEFMTQIYNDQ-PKSDSTVWNRVEYRPLeGFVYAITPFNFTAiaANL-----PASAAmmGNVVVWKPSDSQ 217
Cdd:cd07103 85 ---SFLEWFAEEARRIYGRTiPSPAPGKRILVIKQPV-GVVAAITPWNFPA--AMItrkiaPALAA--GCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 218 VFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKdIWAKIGAninnyKTYPRIVGETGGK 297
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGK-LLMAQAA-----DTVKRVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 298 DFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDK 377
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 378 LASYIDQAkKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALT 457
Cdd:cd07103 311 VEALVEDA-VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE--DEVIARANDT-PYGLA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2006071571 458 GAVFSQD-RYAIEVAtTKLQnaAGNFYIND-KPTGAVVgmqPFGGARASG 505
Cdd:cd07103 387 AYVFTRDlARAWRVA-EALE--AGMVGINTgLISDAEA---PFGGVKESG 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
69-506 |
5.08e-58 |
|
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: 199.88 E-value: 5.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAATMIGQS-KNIHQA--EIDSSCEL 145
Cdd:cd07145 11 VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIER--RKEELAKLLTIEVgKPIKQSrvEVERTIRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 146 idfLRYNVEFMTQIYNDQPKSDSTVWNR----VEYRPLEGFVYAITPFNFTA-IAANLPASAAMMGNVVVWKPSDS---- 216
Cdd:cd07145 89 ---FKLAAEEAKVLRGETIPVDAYEYNErriaFTVREPIGVVGAITPFNFPAnLFAHKIAPAIAVGNSVVVKPSSNtplt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 217 QVFSAKIIVdvfkEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGAninnykTYPRIVGETGG 296
Cdd:cd07145 166 AIELAKILE----EAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 297 KDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFD 376
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 377 KLASYIDQAkKDADAEIIVGGNYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDakWEETLELVDTTsEYAL 456
Cdd:cd07145 316 RMENLVNDA-VEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD--DEEAVEIANST-EYGL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2006071571 457 TGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKPTGAVVGMqPFGGARASGT 506
Cdd:cd07145 390 QASVFTNDiNRALKVA-RELE--AGGVVINDSTRFRWDNL-PFGGFKKSGI 436
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-505 |
7.32e-57 |
|
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: 196.76 E-value: 7.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 68 HVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINA-ATM--IGQSKNIHQA--EIDSS 142
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLL----RERNDEiARLetIDNGKPIEEArvDIDSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 143 celIDFLRYNVEFMTQIYND--QPKSDSTVWNRVEyrPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVF 219
Cdd:cd07090 84 ---ADCLEYYAGLAPTLSGEhvPLPGGSFAYTRRE--PL-GVCAGIGAWNYpIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 220 SAKIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDF 299
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 300 IIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLA 379
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 380 SYIDQAKKDAdAEIIVGGNYDKSV-----GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEY 454
Cdd:cd07090 311 GYIESAKQEG-AKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTE--EEVIRRANDT-TY 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2006071571 455 ALTGAVFSQD-RYAIEVAtTKLQnaAGNFYIN---DKPTgavvgMQPFGGARASG 505
Cdd:cd07090 387 GLAAGVFTRDlQRAHRVI-AQLQ--AGTCWINtynISPV-----EVPFGGYKQSG 433
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
82-512 |
8.88e-57 |
|
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: 197.02 E-value: 8.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 82 ESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINAatmIGQSKNIHQAEIDSSC-----ELIDFLRYNVEFM 156
Cdd:cd07086 38 EAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL----RKKKEA---LGRLVSLEMGKILPEGlgevqEMIDICDYAVGLS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 157 TQIYND-----QPKSDS-TVWNrveyrPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSA----KIIV 225
Cdd:cd07086 111 RMLYGLtipseRPGHRLmEQWN-----PL-GVVGVITAFNFpVAVPGWNAAIALVCGNTVVWKPSETTPLTAiavtKILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 226 DVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIwAKIGAninnyKTYPRIVGETGGKDFIIAHPS 305
Cdd:cd07086 185 EVLEKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRV-GETVA-----RRFGRVLLELGGNNAIIVMDD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 306 ANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQA 385
Cdd:cd07086 258 ADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 386 KKDaDAEIIVGGNY--DKSVGYFIEPTVIVTTNPKYTTMETELFGPVitLYVYEDAKWEETLELVDTTsEYALTGAVFSQ 463
Cdd:cd07086 338 KSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPI--LYVIKFDSLEEAIAINNDV-PQGLSSSIFTE 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2006071571 464 DRYAIEVATTKLQNAAGNFYINDKPTGAVVGMqPFGGARASGTNDKAGS 512
Cdd:cd07086 414 DLREAFRWLGPKGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGS 461
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
69-505 |
9.29e-54 |
|
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: 188.12 E-value: 9.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIA--GPYRARINAATMiGQSKNIHQAEIDSScelI 146
Cdd:cd07106 9 VFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEanAEELARLLTLEQ-GKPLAEAQFEVGGA---V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 147 DFLRY--NVEFMTQIYNDqpksDSTVWNRVEYRPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSAKI 223
Cdd:cd07106 85 AWLRYtaSLDLPDEVIED----DDTRRVELRRKPL-GVVAAIVPWNFpLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 224 IVDVFKEAgVPDGVINVVFGDA---LMITdtvlASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDFI 300
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDelgPALT----SHPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 301 IAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLAS 380
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 381 YIDQAKKDaDAEIIVGGNYDKSVGYFIEPTVIvtTNPKYTTM--ETELFGPVITLYVYEDAkwEETLELVDTTsEYALTG 458
Cdd:cd07106 309 LVEDAKAK-GAKVLAGGEPLDGPGYFIPPTIV--DDPPEGSRivDEEQFGPVLPVLKYSDE--DEVIARANDS-EYGLGA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2006071571 459 AVFSQDR-YAIEVAtTKLQnaAGNFYINDKptGAVVGMQPFGGARASG 505
Cdd:cd07106 383 SVWSSDLeRAEAVA-RRLE--AGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
60-505 |
2.55e-53 |
|
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: 187.07 E-value: 2.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 60 ITAPHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAATMIGQS-KNIHQAE 138
Cdd:cd07147 3 VTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEE--RFEELAETIVLEAgKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 139 IDSScELIDFLRYNVEFMTQIYNDQPKSDST--------VWNRVeyrPLeGFVYAITPFNFtaiAANL------PASAAm 204
Cdd:cd07147 80 GEVA-RAIDTFRIAAEEATRIYGEVLPLDISargegrqgLVRRF---PI-GPVSAITPFNF---PLNLvahkvaPAIAA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 205 mGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVV----FGDALMITDtvlasRDFAGIHFTGSTHVFKDIWAKIGAN 280
Cdd:cd07147 151 -GCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLpcsrDDADLLVTD-----ERIKLLSFTGSPAVGWDLKARAGKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 281 innyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPE 360
Cdd:cd07147 225 --------KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 361 DFGNFITAVIHEGSFDKLASYIDQAkKDADAEIIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDak 440
Cdd:cd07147 297 DDATDVGPMISESEAERVEGWVNEA-VDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDD-- 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006071571 441 WEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMqPFGGARASG 505
Cdd:cd07147 371 FDEALAAVN-DSKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFRVDHM-PYGGVKDSG 431
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
45-505 |
6.81e-53 |
|
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: 186.65 E-value: 6.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 45 LYIGSE--EIRTGNTKNITAPHDHQhVVGKYHLAEKKHIESAIANALEARKA--WANMAWEQRAAIFLKAAELIAgpyRA 120
Cdd:cd07091 6 LFINNEfvDSVSGKTFPTINPATEE-VICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIE---RD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 121 R--------INAATMIGQSKNIHQAEidssceLIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFT 192
Cdd:cd07091 82 RdelaalesLDNGKPLEESAKGDVAL------SIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPI-GVCGQIIPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 193 -AIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFK 271
Cdd:cd07091 155 lLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 272 DIwaKIGANINNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADV 351
Cdd:cd07091 235 TI--MEAAAKSNLK---KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 352 KSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKdADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVI 431
Cdd:cd07091 310 EKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKK-EGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 432 TLYVYEDAkwEETLELVDTTsEYALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINdkpTGAVVGMQ-PFGGARASG 505
Cdd:cd07091 389 TILKFKTE--DEVIERANDT-EYGLAAGVFTKDiNKALRVS-RALK--AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
60-505 |
1.29e-52 |
|
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: 185.33 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 60 ITAPHDHQHVvGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAATMIGQS-KNIHQA- 137
Cdd:cd07094 3 VHNPYDGEVI-GKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKK--RAEEFAKIIACEGgKPIKDAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 138 -EIDSScelIDFLRYNVEFMTQIYNDQPKSDST-------VWNRVEyrPLeGFVYAITPFNFtaiAANLP----ASAAMM 205
Cdd:cd07094 80 vEVDRA---IDTLRLAAEEAERIRGEEIPLDATqgsdnrlAWTIRE--PV-GVVLAITPFNF---PLNLVahklAPAIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 206 GNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGaninnyk 285
Cdd:cd07094 151 GCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 286 tYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNF 365
Cdd:cd07094 224 -GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 366 ITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSVgyfIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETL 445
Cdd:cd07094 303 VGPLISEEAAERVERWVEEAVEAG-ARLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDF--EEAI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 446 ELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMqPFGGARASG 505
Cdd:cd07094 377 RIANST-DYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVNDSSAFRTDWM-PFGGVKESG 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
69-505 |
1.31e-52 |
|
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: 185.45 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIA--GPYRARINA-------ATMIGQSKNihqa 137
Cdd:cd07114 9 PWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEanAEELAELETrdngkliRETRAQVRY---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 138 eidssceLIDFLRYNVEFMTQIYNDQPKSDS-TVWNRVEYRPLeGFVYAITPFN----FTA--IAanlPASAAmmGNVVV 210
Cdd:cd07114 85 -------LAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPL-GVVAAITPWNspllLLAkkLA---PALAA--GNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 211 WKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRI 290
Cdd:cd07114 152 LKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLA------PV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 291 VGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVI 370
Cdd:cd07114 226 TLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 371 HEGSFDKLASYIDQAKKDAdAEIIVGGN----YDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLE 446
Cdd:cd07114 306 TERQLEKVERYVARAREEG-ARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 447 LVDTTsEYALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKPtgAVVGMQPFGGARASG 505
Cdd:cd07114 383 LANDS-EYGLAAGIWTRDlARAHRVA-RAIE--AGTVWVNTYR--ALSPSSPFGGFKDSG 436
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
63-513 |
1.49e-52 |
|
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: 185.34 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 63 PHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARINAATMIGQSKNIHQAEIDSS 142
Cdd:cd07115 4 PATGE-LIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 143 CELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFT-AIAANLPASAAMMGNVVVWKPSDSQVFSA 221
Cdd:cd07115 82 PRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPV-GVVGAIVPWNFPlMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 222 KIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwakIGANINNYKtypRIVGETGGKDFII 301
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKI---MQGAAGNLK---RVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 302 AHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASY 381
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 382 IDQAKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVF 461
Cdd:cd07115 315 VDVGREEG-ARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGT-EYGLAAGVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2006071571 462 SQD-RYAIEVATtklQNAAGNFYINdkPTGAVVGMQPFGGARASGTNDKAGSA 513
Cdd:cd07115 391 TRDlGRAHRVAA---ALKAGTVWIN--TYNRFDPGSPFGGYKQSGFGREMGRE 438
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
54-505 |
5.60e-52 |
|
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: 184.04 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 54 TGNTKNITAPHDhQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRA------------R 121
Cdd:cd07151 8 SERTIDVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEivewliresgstR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 122 INAATMIGQSKNIhqaeIDSSCELIdfLRYNVEFMTqiYNDQPKSdstvwNRVeYRPLEGFVYAITPFNFT---AIAANL 198
Cdd:cd07151 87 IKANIEWGAAMAI----TREAATFP--LRMEGRILP--SDVPGKE-----NRV-YREPLGVVGVISPWNFPlhlSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 199 PASAAmmGNVVVWKP-SDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKI 277
Cdd:cd07151 153 PALAL--GNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 278 GANINnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMG 357
Cdd:cd07151 231 GRHLK------KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 358 SPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGnydKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYE 437
Cdd:cd07151 305 DPSDPDTVVGPLINESQVDGLLDKIEQAVEEG-ATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKAD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006071571 438 DAkwEETLELVDTTsEYALTGAVFSQDRY-AIEVAttkLQNAAGNFYINDKPTGAVVGMqPFGGARASG 505
Cdd:cd07151 381 DE--EEALELANDT-EYGLSGAVFTSDLErGVQFA---RRIDAGMTHINDQPVNDEPHV-PFGGEKNSG 442
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
69-511 |
1.13e-51 |
|
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: 182.94 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKawaNMAWEQRAAIFLKAAELIAgpyRARINAATMI----GQSKNIHQAEIDSSCE 144
Cdd:cd07146 11 VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLE---ARREEFARLItlesGLCLKDTRYEVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 145 LIDFLRYNVE------FMTQIY-NDQPKSDSTVWnrveyRPLeGFVYAITPFNF------TAIAanlPASAAmmGNVVVW 211
Cdd:cd07146 85 VLRFAAAEALrddgesFSCDLTaNGKARKIFTLR-----EPL-GVVLAITPFNHplnqvaHKIA---PAIAA--NNRIVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 212 KPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGaninnyktYPRIV 291
Cdd:cd07146 154 KPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 292 GETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIH 371
Cdd:cd07146 226 LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 372 EGSFDKLASYIDQAKKDAdAEIIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTT 451
Cdd:cd07146 306 EEAAIQIENRVEEAIAQG-ARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNST 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 452 sEYALTGAVFSQDRYAIEVATTKLQNAAGNfyINDKPtGAVVGMQPFGGARASGTNDKAG 511
Cdd:cd07146 380 -AYGLSSGVCTNDLDTIKRLVERLDVGTVN--VNEVP-GFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
69-505 |
3.06e-51 |
|
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: 181.93 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELiagpYRARIN--AATM-------IGQSKNIH-QAE 138
Cdd:cd07138 26 VIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEA----YEARADelAQAItlemgapITLARAAQvGLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 139 IDSSCELIDFLRyNVEFMTQIYNDqpksdstvwnRVEYRPLeGFVYAITPFNFTA--IAANL-PASAAmmGNVVVWKPSD 215
Cdd:cd07138 102 IGHLRAAADALK-DFEFEERRGNS----------LVVREPI-GVCGLITPWNWPLnqIVLKVaPALAA--GCTVVLKPSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 216 SQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwAKIGAninnyKTYPRIVGETG 295
Cdd:cd07138 168 VAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV-AEAAA-----DTVKRVALELG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 296 GKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSF 375
Cdd:cd07138 242 GKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 376 DKLASYIDQAKKDAdAEIIVGG-----NYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDT 450
Cdd:cd07138 322 DRVQGYIQKGIEEG-ARLVAGGpgrpeGLER--GYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE--DEAIAIAND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006071571 451 TsEYALTGAVFSQDR-YAIEVAtTKLQnaAGNFYINdkptGAVVGMQ-PFGGARASG 505
Cdd:cd07138 397 T-PYGLAGYVWSADPeRARAVA-RRLR--AGQVHIN----GAAFNPGaPFGGYKQSG 445
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
27-525 |
7.71e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 187.84 E-value: 7.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 27 AAVQAAYTTMWNSQidvPlyIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAI 106
Cdd:COG4230 546 AALAAAAEKQWQAA---P--LIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAI 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 107 FLKAAELI--------------AGpyrarinaatmigqsKNIH--QAEIdssCELIDFLRYnvefmtqiYNDQPKSDSTv 170
Cdd:COG4230 621 LERAADLLeahraelmallvreAG---------------KTLPdaIAEV---REAVDFCRY--------YAAQARRLFA- 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 171 wNRVEYRPLeGFVYAITPFNFT-AI-----AANLpasAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGD 244
Cdd:COG4230 674 -APTVLRGR-GVFVCISPWNFPlAIftgqvAAAL---AA--GNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 245 ALMITDTVLASRDFAGIHFTGSTHVfkdiwAKIganINnyKT-------YPRIVGETGGKDFIIAHPSANVKQVVTGITR 317
Cdd:COG4230 747 GETVGAALVADPRIAGVAFTGSTET-----ARL---IN--RTlaardgpIVPLIAETGGQNAMIVDSSALPEQVVDDVLA 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 318 GAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAD--AEIIV 395
Cdd:COG4230 817 SAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRlvHQLPL 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 396 GGNYDKsvGYFIEPTVIVTTNPKYttMETELFGPVITLYVYEDAKWEETLELVDTTSeYALTGAVFSQDRYAIEVATTKL 475
Cdd:COG4230 897 PEECAN--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRYKADELDKVIDAINATG-YGLTLGVHSRIDETIDRVAARA 971
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2006071571 476 QnaAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTI 525
Cdd:COG4230 972 R--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
81-505 |
7.77e-51 |
|
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: 179.96 E-value: 7.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELI---AGPYrARINAATM---IGQSKnihqAEIDSSCELIDFLRYNVE 154
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLrerKDEL-ARLITLEMgkpIAEAR----AEVEKCAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 155 -FMTQIYNDQPKSDStvwnRVEYRPLeGFVYAITPFNF------TAIAANLpasaaMMGNVVVWKPSdSQVF-SAKIIVD 226
Cdd:cd07100 76 aFLADEPIETDAGKA----YVRYEPL-GVVLGIMPWNFpfwqvfRFAAPNL-----MAGNTVLLKHA-SNVPgCALAIEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 227 VFKEAGVPDGVINVVFGDALMItDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyKtypRIVGETGGKD-FIIAhPS 305
Cdd:cd07100 145 LFREAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNL---K---KSVLELGGSDpFIVL-DD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 306 ANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQA 385
Cdd:cd07100 217 ADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 386 KkDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDR 465
Cdd:cd07100 297 V-AAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALAN-DSPFGLGGSVFTTDL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2006071571 466 YAIEVATTKLQnaAGNFYINDkPTGAVVGMqPFGGARASG 505
Cdd:cd07100 373 ERAERVARRLE--AGMVFING-MVKSDPRL-PFGGVKRSG 408
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
27-525 |
1.12e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 187.33 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 27 AAVQAAYTTMWNSqidVPLYIGseeirTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAI 106
Cdd:PRK11904 541 AAIAAFLEKQWQA---GPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAI 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 107 FLKAAELIAGpYRARINAATMIGQSKNIHQAeIDSSCELIDFLRYnvefmtqiYNDQPKSDSTVWNRV--------EYRp 178
Cdd:PRK11904 613 LERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRY--------YAAQARRLFGAPEKLpgptgesnELR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 179 LEG---FVyAITPFNFT-AIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLA 254
Cdd:PRK11904 682 LHGrgvFV-CISPWNFPlAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 255 SRDFAGIHFTGSTHVFKDI----WAKIGANInnyktyPRIvGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAA 330
Cdd:PRK11904 761 DPRIAGVAFTGSTETARIInrtlAARDGPIV------PLI-AETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 331 SRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAD--AEIIVGGNYDKsvGYFIE 408
Cdd:PRK11904 834 RVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARllAQLPLPAGTEN--GHFVA 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 409 PTVIVTTNPKYttMETELFGPVitLYV--YEDAKWEETLELVDTTSeYALTGAVFSQDRYAIEVATTKLQnaAGNFYIND 486
Cdd:PRK11904 912 PTAFEIDSISQ--LEREVFGPI--LHVirYKASDLDKVIDAINATG-YGLTLGIHSRIEETADRIADRVR--VGNVYVNR 984
|
490 500 510
....*....|....*....|....*....|....*....
gi 2006071571 487 KPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTI 525
Cdd:PRK11904 985 NQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-505 |
5.81e-50 |
|
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: 178.21 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIAnalEARKAWANMAW----EQRAAIFLKAAELI---AGPYRARINAATmiGQSKNIHQAEIDS 141
Cdd:cd07089 9 VIGTAPDAGAADVDAAIA---AARRAFDTGDWstdaEERARCLRQLHEALearKEELRALLVAEV--GAPVMTARAMQVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 142 SceLIDFLRYNVEFMTQIYNDQPKSDSTVWN-----RVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKP 213
Cdd:cd07089 84 G--PIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPV-GVVAAITPWNFpffLNLAKLAPALAA--GNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 214 SDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGE 293
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK------RVLLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYIDQAkKDADAEIIVGG----NYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVD 449
Cdd:cd07089 313 QRDRVEGYIARG-RDEGARLVTGGgrpaGLDK--GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVRIAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006071571 450 tTSEYALTGAVFSQD--RyAIEVATtklQNAAGNFYINdkpTGAVVGMQ-PFGGARASG 505
Cdd:cd07089 388 -DSDYGLSGGVWSADvdR-AYRVAR---RIRTGSVGIN---GGGGYGPDaPFGGYKQSG 438
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
66-505 |
6.20e-49 |
|
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: 175.60 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 66 HQHVVGKYHLAEKKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIagpyRARINAATMIG---QSKNIHQA--E 138
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLI----RARRERLALIEtleSGKPISQArgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 139 IDSScelIDFLRYNVEFMTQIYNDQPKS--DSTVwNRVEYRPLeGFVYAITPFNFTAIAAN--LP-ASAAmmGNVVVWKP 213
Cdd:cd07118 82 IEGA---ADLWRYAASLARTLHGDSYNNlgDDML-GLVLREPI-GVVGIITPWNFPFLILSqkLPfALAA--GCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 214 SDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGE 293
Cdd:cd07118 155 SEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK------KVSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:cd07118 229 LGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYIDQAKkDADAEIIVGGN-YDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTs 452
Cdd:cd07118 309 QLAKITDYVDAGR-AEGATLLLGGErLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTV--DEAIALANDT- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 453 EYALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKPTGAVvgMQPFGGARASG 505
Cdd:cd07118 385 VYGLSAGVWSKDiDTALTVA-RRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-525 |
1.20e-48 |
|
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: 174.72 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARInAATMI---GQSKNIHQAEIDSSCEL 145
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALAD-HADEL-AELLHaetGKPRADAGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 146 IDFLRYNVEFmtqIYNDQPKSDSTVW----NRVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPSDSQV 218
Cdd:cd07099 86 IDWAARNAPR---VLAPRKVPTGLLMpnkkATVEYRPY-GVVGVISPWNYpllTPMGDIIPALAA--GNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 219 FSAKIIVDVFKEAGVPDGVINVVFGD----ALMItDTVLASrdfagIHFTGSTHVFKdiwaKIGANINNYKTyPrIVGET 294
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDgatgAALI-DAGVDK-----VAFTGSVATGR----KVMAAAAERLI-P-VVLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 295 GGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGS 374
Cdd:cd07099 228 GGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 375 FDKLASYIDQAkKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEY 454
Cdd:cd07099 308 LDIVRRHVDDA-VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIALAN-DSRY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 455 ALTGAVFSQDR-YAIEVAtTKLQnaAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGsALNLLRWASPRTI 525
Cdd:cd07099 384 GLSASVFSRDLaRAEAIA-RRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHG-AEGLREFCRPKAI 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
69-516 |
1.34e-48 |
|
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: 174.40 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELI------AGPYRARINAATMigqskniHQAEIDSS 142
Cdd:cd07152 3 VLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLeehadeIADWIVRESGSIR-------PKAGFEVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 143 cELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFT---AIAANLPASAamMGNVVVWKPsDSQ-- 217
Cdd:cd07152 76 -AAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPL-GVVGVISPFNFPlilAMRSVAPALA--LGNAVVLKP-DPRtp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 218 VFSAKIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGK 297
Cdd:cd07152 151 VSGGVVIARLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLK------KVSLELGGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 298 DFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDK 377
Cdd:cd07152 224 NALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 378 LASyIDQAKKDADAEIIVGGNYDksvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALT 457
Cdd:cd07152 304 VHA-IVDDSVAAGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALANDT-EYGLS 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006071571 458 GAVFSQD--RyAIEVATtklQNAAGNFYINDKPTGAVVGMqPFGGARASGTNDKAGSALNL 516
Cdd:cd07152 377 AGIISRDvgR-AMALAD---RLRTGMLHINDQTVNDEPHN-PFGGMGASGNGSRFGGPANW 432
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
47-523 |
2.41e-48 |
|
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: 175.10 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 47 IGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyraRINAAT 126
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLL------ELHMPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 127 MIG-----QSKNIHQAeIDSSCELIDFLRYnveFMTQIYNDQPKSdstvwnrvEYRPLeGFVYAITPFNFT-AIAANLPA 200
Cdd:TIGR01238 116 LMAlcvreAGKTIHNA-IAEVREAVDFCRY---YAKQVRDVLGEF--------SVESR-GVFVCISPWNFPlAIFTGQIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 201 SAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGAN 280
Cdd:TIGR01238 183 AALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 281 INNYKTyprIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPE 360
Cdd:TIGR01238 263 EDAPVP---LIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPH 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 361 DFGNFITAVIHEGSFDKLASYIDQAKKDAD--AEIIVGGNYDKSVGYFIEPTVIVTTNpkYTTMETELFGPVITLYVYED 438
Cdd:TIGR01238 340 LLTTDVGPVIDAEAKQNLLAHIEHMSQTQKkiAQLTLDDSRACQHGTFVAPTLFELDD--IAELSEEVFGPVLHVVRYKA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 439 AKWEETLELVDTTSeYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLR 518
Cdd:TIGR01238 418 RELDQIVDQINQTG-YGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYR 494
|
....*
gi 2006071571 519 WASPR 523
Cdd:TIGR01238 495 LTQVQ 499
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
45-505 |
7.47e-48 |
|
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: 172.76 E-value: 7.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 45 LYIGSEEIR--TGNTKNITAPHDHQhVVGKYHLAEKKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIA--GPY 118
Cdd:cd07139 1 LFIGGRWVApsGSETIDVVSPATEE-VVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEarADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 119 RARINAATM---IGQSKNIHQAEIdsscelIDFLRYNVEFMTQIYNDQPKSDSTVWN-RVEYRPLeGFVYAITPFN---F 191
Cdd:cd07139 80 LARLWTAENgmpISWSRRAQGPGP------AALLRYYAALARDFPFEERRPGSGGGHvLVRREPV-GVVAAIVPWNaplF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 192 TAIAANLPASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFK 271
Cdd:cd07139 153 LAALKIAPALAA--GCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 272 DIWAKIGANINnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADV 351
Cdd:cd07139 230 RIAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 352 KSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSV--GYFIEPTVIVTTNPKYTTMETELFGP 429
Cdd:cd07139 304 AALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEG-ARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGP 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006071571 430 VITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDR-YAIEVATtklQNAAGNFYINdkptGAVVGMQ-PFGGARASG 505
Cdd:cd07139 383 VLSVIPYDDE--DDAVRIAN-DSDYGLSGSVWTADVeRGLAVAR---RIRTGTVGVN----GFRLDFGaPFGGFKQSG 450
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
60-506 |
4.78e-47 |
|
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: 170.25 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 60 ITAPHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINAATMIG--QSKNIHQA 137
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRL----REHAEELALIDalDCGNPVSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 138 EIDSSCELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAI-AANLPASAAMMGNVVVWKPSDS 216
Cdd:cd07107 76 MLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPY-GVVARIVAFNHPLMfAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 217 QVFSAKIIVDVFKEAgVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGG 296
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 297 KDFIIAHPSANVKQVVTGITRGA-FEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSF 375
Cdd:cd07107 228 KNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 376 DKLASYIDQAKKDAdAEIIVGGNYDKSV----GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTT 451
Cdd:cd07107 308 DRVMHYIDSAKREG-ARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANGV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006071571 452 sEYALTGAVFSQD-----RYAIEVattklqnAAGNFYINDKPT---GAvvgmqPFGGARASGT 506
Cdd:cd07107 385 -EYGLTAAIWTNDisqahRTARRV-------EAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-505 |
1.14e-46 |
|
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: 168.52 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 80 HIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARIN--AATM---IGQSKNIHQAEIDSSCELIDflrynvE 154
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLL----ESRRDefIEAMmeeTGATAAWAGFNVDLAAGMLR------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 155 FMTQIYNDQ----PKSDSTVWNRVEYRPLeGFVYAITPFNFTAIaanLPASAAMM----GNVVVWKPSDsqvFSAK---I 223
Cdd:cd07105 71 AASLITQIIggsiPSDKPGTLAMVVKEPV-GVVLGIAPWNAPVI---LGTRAIAYplaaGNTVVLKASE---LSPRthwL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 224 IVDVFKEAGVPDGVINVVF---GDALMITDTVLASRDFAGIHFTGSTHVFKDIwAKIGANinNYKtypRIVGETGGKDFI 300
Cdd:cd07105 144 IGRVFHEAGLPKGVLNVVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRII-AETAAK--HLK---PVLLELGGKAPA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 301 IAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEdfgnfITAVIHEGSFDKLAS 380
Cdd:cd07105 218 IVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 381 YIDQAkKDADAEIIVGGNYDKSV-GYFIEPTVI--VTTNPK-YTtmeTELFGPVITLYVYEDAkwEETLELVDtTSEYAL 456
Cdd:cd07105 293 LVDDA-LSKGAKLVVGGLADESPsGTSMPPTILdnVTPDMDiYS---EESFGPVVSIIRVKDE--EEAVRIAN-DSEYGL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2006071571 457 TGAVFSQD-RYAIEVAtTKLQnaAGNFYIN-----DKPTGavvgmqPFGGARASG 505
Cdd:cd07105 366 SAAVFTRDlARALAVA-KRIE--SGAVHINgmtvhDEPTL------PHGGVKSSG 411
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
76-505 |
4.64e-46 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 168.29 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 76 AEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATM-----IGQSKNihqAEIDSScelIDFLR 150
Cdd:cd07559 35 STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLdngkpIRETLA---ADIPLA---IDHFR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 151 YnveFMTQIYNDQPKS---DSTVWNRVEYRPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQVFS---- 220
Cdd:cd07559 109 Y---FAGVIRAQEGSLseiDEDTLSYHFHEPL-GVVGQIIPWNFPLLMAAwklAPALAA--GNTVVLKPASQTPLSilvl 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 221 AKIIVDVfkeagVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyktYPRIVgETGGK--- 297
Cdd:cd07559 183 MELIGDL-----LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IPVTL-ELGGKspn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 298 ---DFIIAHPSANVKQVVTGITRGAFEfQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGS 374
Cdd:cd07559 252 iffDDAMDADDDFDDKAEEGQLGFAFN-QGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 375 FDKLASYIDQAKKDaDAEIIVGG------NYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELV 448
Cdd:cd07559 331 LEKILSYVDIGKEE-GAEVLTGGerltlgGLDK--GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE--EEAIAIA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 449 DTTsEYALTGAVFSQDryaievATTKLQNA----AGNFYIN---DKPTGAvvgmqPFGGARASG 505
Cdd:cd07559 406 NDT-EYGLGGGVWTRD------INRALRVArgiqTGRVWVNcyhQYPAHA-----PFGGYKKSG 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
53-505 |
5.25e-46 |
|
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: 167.83 E-value: 5.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 53 RTGNTKNITAPHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpYRARINAATMIGQSK 132
Cdd:cd07088 10 SSGETIDVLNPATGE-VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRE-NADELAKLIVEEQGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 133 NIHQA--EIDSSCeliDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLEGFVYAITPFNFT-AIAANLPASAAMMGNVV 209
Cdd:cd07088 88 TLSLArvEVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAPALVTGNTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 210 VWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypR 289
Cdd:cd07088 165 VIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT------K 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 290 IVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAV 369
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 370 IHEGSFDKLASYIDQAKKdADAEIIVGGNYDKS-VGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELV 448
Cdd:cd07088 319 VNEAALDKVEEMVERAVE-AGATLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSL--DEAIELA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006071571 449 DtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAvvgMQPF-GGARASG 505
Cdd:cd07088 396 N-DSEYGLTSYIYTENLNTAMRATNELE--FGETYINRENFEA---MQGFhAGWKKSG 447
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-518 |
1.35e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 172.36 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 26 KAAVQAAYTTMWNSQidvplYIGSEEIRTGNTKNITAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAA 105
Cdd:PRK11905 542 DEALNAFAAKTWHAA-----PLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAA 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 106 IFLKAAELiagpYRARINAATMI-----GQSKNIHQAEIDsscELIDFLRYnvefmtqiYNDQPKSDstvWNRVEYRPLe 180
Cdd:PRK11905 617 ILERAADL----MEAHMPELFALavreaGKTLANAIAEVR---EAVDFLRY--------YAAQARRL---LNGPGHKPL- 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 181 GFVYAITPFNFT-AIAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFA 259
Cdd:PRK11905 678 GPVVCISPWNFPlAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 260 GIHFTGSTHVFKDIWAKIGANINnyKTYPRIvGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSL 339
Cdd:PRK11905 758 GVMFTGSTEVARLIQRTLAKRSG--PPVPLI-AETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 340 WPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAD--AEIIVGGNYDKsvGYFIEPTVIVTTNP 417
Cdd:PRK11905 835 ADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRlvHQLPLPAETEK--GTFVAPTLIEIDSI 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 418 kyTTMETELFGPVitLYV--YEDAKWEETLELVDTTSeYALTGAVFS--QDRyaIEVATTKLQnaAGNFYINDKPTGAVV 493
Cdd:PRK11905 913 --SDLEREVFGPV--LHVvrFKADELDRVIDDINATG-YGLTFGLHSriDET--IAHVTSRIR--AGNIYVNRNIIGAVV 983
|
490 500
....*....|....*....|....*
gi 2006071571 494 GMQPFGGARASGTNDKAGSALNLLR 518
Cdd:PRK11905 984 GVQPFGGEGLSGTGPKAGGPLYLGR 1008
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
69-485 |
3.13e-45 |
|
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: 165.11 E-value: 3.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINA-----ATMIGqsKNIHQAEidssc 143
Cdd:cd07102 8 VIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELL----AANTDEiaeelTWQMG--RPIAQAG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 144 ELIDFLRYNVEFMTQIYND------QPKSDStVWNRVEYRPLeGFVYAITPFN---FTAIAANLPASAAmmGNVVVWKPS 214
Cdd:cd07102 77 GEIRGMLERARYMISIAEEaladirVPEKDG-FERYIRREPL-GVVLIIAPWNypyLTAVNAVIPALLA--GNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 215 DSQVFSAKIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIwAKIGAninnyktyPRIVG-- 292
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAI-QRAAA--------GRFIKvg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 293 -ETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIH 371
Cdd:cd07102 223 lELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 372 EGSFDKLASYIDQAkKDADAEIIVGGN---YDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLY-VYEDakwEETLEL 447
Cdd:cd07102 303 ARAADFVRAQIADA-IAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMkVKSD---AEAIAL 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 2006071571 448 VDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYIN 485
Cdd:cd07102 379 MN-DSEYGLTASVWTKDIARAEALGEQLE--TGTVFMN 413
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
43-504 |
3.32e-45 |
|
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: 165.77 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 43 VPLYIGSEEIR--TGNTKNITAPHdHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRA 120
Cdd:cd07085 1 LKLFINGEWVEskTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE-ENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 121 RINAATMIGQSKNIHQAEIDsscelidFLR--YNVEFMTQIYNDQ-----PKSDSTVWNRVEYRPLeGFVYAITPFNFTA 193
Cdd:cd07085 79 ELARLITLEHGKTLADARGD-------VLRglEVVEFACSIPHLLkgeylENVARGIDTYSYRQPL-GVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 194 -IAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDAlmitDTV---LASRDFAGIHFTGSTHV 269
Cdd:cd07085 151 mIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAVnalLDHPDIKAVSFVGSTPV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 270 FKDIWAKIGAninNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIA 349
Cdd:cd07085 227 GEYIYERAAA---NGK---RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 350 DVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKdADAEIIVGG------NYDKsvGYFIEPTVIVTTNPKYTTME 423
Cdd:cd07085 301 RAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVE-EGAKLVLDGrgvkvpGYEN--GNFVGPTILDNVTPDMKIYK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 424 TELFGPVitLYVYEDAKWEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINdKPTGAVVGMQPFGGARA 503
Cdd:cd07085 378 EEIFGPV--LSIVRVDTLDEAIAIIN-ANPYGNGAAIFTRSGAAARKFQREVD--AGMVGIN-VPIPVPLAFFSFGGWKG 451
|
.
gi 2006071571 504 S 504
Cdd:cd07085 452 S 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
81-505 |
3.82e-45 |
|
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: 165.08 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEA--RKAWANMAWEQRAAIFLKAAELIagpyRAR---------INAATMIGQSKNIhqaEIDSScelIDFL 149
Cdd:cd07112 26 VDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLI----EAHrdelalletLDMGKPISDALAV---DVPSA---ANTF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 150 RYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANL---PASAAmmGNVVVWKPSDSQVFSAKIIVD 226
Cdd:cd07112 96 RWYAEAIDKVYGEVAPTGPDALALITREPL-GVVGAVVPWNFPLLMAAWkiaPALAA--GNSVVLKPAEQSPLTALRLAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 227 VFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANinNYKtypRIVGETGGKD-FIIAHPS 305
Cdd:cd07112 173 LALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQS--NLK---RVWLECGGKSpNIVFADA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 306 ANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQA 385
Cdd:cd07112 248 PDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 386 KKDAdAEIIVGGNYDKSV--GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQ 463
Cdd:cd07112 328 KAEG-ARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALANDS-VYGLAASVWTS 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2006071571 464 D-RYAIEVAtTKLQnaAGNFYINdkpTGAVVGMQ-PFGGARASG 505
Cdd:cd07112 404 DlSRAHRVA-RRLR--AGTVWVN---CFDEGDITtPFGGFKQSG 441
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
81-527 |
4.39e-45 |
|
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: 164.79 E-value: 4.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRARINAATMIGQ---SKNIHQAeIDSSCELIDFLRY------ 151
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLV----LERRDELLDLIQletGKARRHA-FEEVLDVAIVARYyarrae 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 152 ----------NVEFMTQiyndqpksdstvwNRVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPsDSQV 218
Cdd:cd07101 95 rllkprrrrgAIPVLTR-------------TTVNRRPK-GVVGVISPWNYpltLAVSDAIPALLA--GNAVVLKP-DSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 219 -FSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFagIHFTGSTHVFKDIWAKIGAninnyktypRIVG---ET 294
Cdd:cd07101 158 aLTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGR---------RLIGcslEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 295 GGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGS 374
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 375 FDKLASYIDQAKKdADAEIIVGGNYDKSVG-YFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsE 453
Cdd:cd07101 307 LDRVTAHVDDAVA-KGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELANDT-D 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006071571 454 YALTGAVFSQD-RYAIEVATtklQNAAGNFYIND--KPTGAVVGmQPFGGARASGTNDKAGsALNLLRWASPRTIKE 527
Cdd:cd07101 383 YGLNASVWTRDgARGRRIAA---RLRAGTVNVNEgyAAAWASID-APMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-505 |
6.39e-45 |
|
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: 164.46 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 61 TAPHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAgpyrARINA-ATMIG--QSKNIHQA 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALE----ARSEElARLLAleTGNALRTQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 138 EIDSSCELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDS 216
Cdd:cd07108 77 ARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 217 QVFSAKIIVDVFKEAgVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGaninnyktyPRIVG---E 293
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvslE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGA-FEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHE 372
Cdd:cd07108 226 LGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 373 GSFDKLASYIDQAKKDADAEIIVGGNYDKSV----GYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDakWEETLELV 448
Cdd:cd07108 306 KQFAKVCGYIDLGLSTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDEVIAMA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006071571 449 DtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDkpTGAVVGMQPFGGARASG 505
Cdd:cd07108 384 N-DSHYGLAAYVWTRDLGRALRAAHALE--AGWVQVNQ--GGGQQPGQSYGGFKQSG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
46-505 |
1.49e-44 |
|
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: 164.02 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 46 YIGSEEIR--TGNTKNITAPHDhQHVVGKYHLAEKKHIESAIAnalEARKA-----WANMAWEQRAAIFLKAAELIA--G 116
Cdd:cd07119 1 YIDGEWVEaaSGKTRDIINPAN-GEVIATVPEGTAEDAKRAIA---AARRAfdsgeWPHLPAQERAALLFRIADKIRedA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 117 PYRARINAatmIGQSKNIHQAEIDSSCeLIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAA 196
Cdd:cd07119 77 EELARLET---LNTGKTLRESEIDIDD-VANCFRYYAGLATKETGEVYDVPPHVISRTVREPV-GVCGLITPWNYPLLQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 197 N---LPASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDI 273
Cdd:cd07119 152 AwklAPALAA--GNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 274 wakIGANINNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKS 353
Cdd:cd07119 230 ---MRAAAGNVK---KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 354 MKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGN------YDKsvGYFIEPTVIVTTNPKYTTMETELF 427
Cdd:cd07119 304 IKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEG-ARLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIF 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006071571 428 GPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYIND-KPTGAvvgMQPFGGARASG 505
Cdd:cd07119 381 GPVLTVERFDTE--EEAIRLANDT-PYGLAGAVWTKDIARANRVARRLR--AGTVWINDyHPYFA---EAPWGGYKQSG 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
45-513 |
6.13e-44 |
|
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: 162.58 E-value: 6.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 45 LYIGSEEIRTGNTKNI--TAPHDHQhVVGKYHLAEKKHIESAIANALEARKA-WANMAWEQRAAIFLKAAELIAgPYRAR 121
Cdd:cd07144 10 LFINNEFVKSSDGETIktVNPSTGE-VIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVE-KNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 122 INAATMIGQSKNIHQAEIDSSCELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFT-AIAANLPA 200
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPY-GVCGQIIPWNYPlAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 201 SAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGAN 280
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 281 INNyktyprIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKS-MKMGSP 359
Cdd:cd07144 247 LKA------VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 360 EDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSV---GYFIEPTVIVTTNPKYTTMETELFGPVITLYVY 436
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEG-AKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 437 EDakWEETLELVDTTsEYALTGAVFSQDryaIEVA---TTKLQnaAGNFYINDKPTGAvVGMqPFGGARASGTNDKAGSA 513
Cdd:cd07144 400 KT--YEEAIKKANDT-TYGLAAAVFTKD---IRRAhrvARELE--AGMVWINSSNDSD-VGV-PFGGFKMSGIGRELGEY 469
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
63-505 |
7.11e-44 |
|
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: 161.75 E-value: 7.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 63 PHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAiFLK--AAELIAGpyRARINAATMIGQSKNIHQAEID 140
Cdd:cd07110 4 PATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAK-YLRaiAEGVRER--REELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 141 SScELIDFLRYNVEFMTQIYNDQPKS----DSTVWNRVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKP 213
Cdd:cd07110 80 VD-DVAGCFEYYADLAEQLDAKAERAvplpSEDFKARVRREPV-GVVGLITPWNFpllMAAWKVAPALAA--GCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 214 SDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINNyktyprIVGE 293
Cdd:cd07110 156 SELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:cd07110 230 LGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYIDQAkKDADAEIIVGGNY--DKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtT 451
Cdd:cd07110 310 QYEKVLSFIARG-KEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIALAN-D 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 452 SEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINdkPTGAVVGMQPFGGARASG 505
Cdd:cd07110 386 SEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-512 |
4.31e-43 |
|
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: 160.00 E-value: 4.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 40 QIDVPLYIGSEEIRT--GNTKNITAPHDHQhVVGKYHLAEKKHIESAIANALEA-RKAWA-NMAWEQRAAIFLKAAELIA 115
Cdd:cd07143 4 EQPTGLFINGEFVDSvhGGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLME 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 116 G--PYRARINAatmIGQSKNIHQAEIDSSCELIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTA 193
Cdd:cd07143 83 RnlDYLASIEA---LDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPI-GVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 194 IAANL---PASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVF 270
Cdd:cd07143 159 LMCAWkiaPALAA--GNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 271 KDIWAkiGANINNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIAD 350
Cdd:cd07143 237 RKVME--AAAKSNLK---KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 351 VKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKdADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPV 430
Cdd:cd07143 312 AKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKA-EGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 431 ITLYVYEDAkwEETLELVDtTSEYALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKPTgaVVGMQPFGGARASGTNDK 509
Cdd:cd07143 391 VAVIKFKTE--EEAIKRAN-DSTYGLAAAVFTNNiNNAIRVA-NALK--AGTVWVNCYNL--LHHQVPFGGYKQSGIGRE 462
|
...
gi 2006071571 510 AGS 512
Cdd:cd07143 463 LGE 465
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
63-523 |
1.20e-42 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 163.61 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 63 PHDHQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyrariNAATMI-------GQSKNIH 135
Cdd:PRK11809 666 PADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEA------QMQTLMgllvreaGKTFSNA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 136 QAEIDsscELIDFLRYnvefmtqiYNDQPKSDstvWNRVEYRPLeGFVYAITPFNFT-AIAANLPASAAMMGNVVVWKPS 214
Cdd:PRK11809 740 IAEVR---EAVDFLRY--------YAGQVRDD---FDNDTHRPL-GPVVCISPWNFPlAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 215 DSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINNY-KTYPRIvGE 293
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQgRPIPLI-AE 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:PRK11809 884 TGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAE 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYID--QAKKDADAEIIVGGNYDKSVGYFIEPTVIVTTNpkYTTMETELFGPVITLYVYEDAKWEETLELVDTT 451
Cdd:PRK11809 964 AKANIERHIQamRAKGRPVFQAARENSEDWQSGTFVPPTLIELDS--FDELKREVFGPVLHVVRYNRNQLDELIEQINAS 1041
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 452 SeYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPR 523
Cdd:PRK11809 1042 G-YGLTLGVHTRIDETIAQVTGSAH--VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
80-505 |
1.84e-42 |
|
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: 157.78 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 80 HIESAIANALEA-RKAWANMAWEQRAAIFLKAAELIagpyRARINAATMI---GQSKNIHQAEIDSScELIDFLRYNVEF 155
Cdd:cd07109 20 DVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLI----REHADELARLeslDTGKPLTQARADVE-AAARYFEYYGGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 156 MTQIYNDQ--PKSDSTVWnrVEYRPLeGFVYAITPFNFTA-IAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAG 232
Cdd:cd07109 95 ADKLHGETipLGPGYFVY--TVREPH-GVTGHIIPWNYPLqITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 233 VPDGVINVV------FGDALMitdtvlASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDFIIAHPSA 306
Cdd:cd07109 172 LPAGALNVVtglgaeAGAALV------AHPGVDHISFTGSVETGIAVMRAAAENVV------PVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 307 NVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNfITAVIHEGSFDKLASYIDQAk 386
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARA- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 387 KDADAEIIVGG---NYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQ 463
Cdd:cd07109 318 RARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANGT-DYGLVAGVWTR 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2006071571 464 D-----RYAIEVattklqnAAGNFYINDkpTGAVVGMQ-PFGGARASG 505
Cdd:cd07109 395 DgdralRVARRL-------RAGQVFVNN--YGAGGGIElPFGGVKKSG 433
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
76-505 |
2.31e-42 |
|
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: 158.00 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 76 AEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATM-----IGQSKNIhqaEIDSScelIDFLR 150
Cdd:cd07117 35 ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLdngkpIRETRAV---DIPLA---ADHFR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 151 YnveFMTQIYNDQPKS---DSTVWNRVEYRPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQVFS---- 220
Cdd:cd07117 109 Y---FAGVIRAEEGSAnmiDEDTLSIVLREPI-GVVGQIIPWNFPFLMAAwklAPALAA--GNTVVIKPSSTTSLSllel 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 221 AKIIVDVfkeagVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIwakigANINNYKTYPRIVgETGGKDFI 300
Cdd:cd07117 183 AKIIQDV-----LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV-----AIAAAKKLIPATL-ELGGKSAN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 301 IAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLAS 380
Cdd:cd07117 252 IIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 381 YIDQAKKDaDAEIIVGG------NYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEY 454
Cdd:cd07117 332 YVDIAKEE-GAKILTGGhrltenGLDK--GFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE--DEVIDMAN-DSEY 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 455 ALTGAVFSQD-----RYAIEVATTKLQNaagNFYiNDKPTGAvvgmqPFGGARASG 505
Cdd:cd07117 406 GLGGGVFTKDinralRVARAVETGRVWV---NTY-NQIPAGA-----PFGGYKKSG 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
69-506 |
4.13e-42 |
|
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: 156.72 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQAEIDSSCELIDF 148
Cdd:cd07092 9 EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE-ENAEELAALESRNTGKPLHLVRDDELPGAVDN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 149 LRynveFMTQIYNDQPKSDSTvwnrvEY----------RPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPSD 215
Cdd:cd07092 88 FR----FFAGAARTLEGPAAG-----EYlpghtsmirrEPI-GVVAQIAPWNYplmMAAWKIAPALAA--GNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 216 ----SQVFSAKIIVDVFkeagvPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIV 291
Cdd:cd07092 156 ttplTTLLLAELAAEVL-----PPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 292 GETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIH 371
Cdd:cd07092 225 LELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 372 EGSFDKLASYIDQAKKdaDAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTT 451
Cdd:cd07092 305 AAQRERVAGFVERAPA--HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELANDV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2006071571 452 sEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKptGAVVGMQPFGGARASGT 506
Cdd:cd07092 381 -EYGLASSVWTRDVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
63-505 |
1.03e-41 |
|
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: 155.92 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 63 PHDHQHVvGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAI-------FLKAAELIAgpyrarinAATMIGQSKNIH 135
Cdd:cd07098 3 PATGQHL-GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVlrsllkyILENQEEIC--------RVACRDTGKTMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 136 QA---EIDSSCELIDFLRYNVEFMTQiyndqPKSDST---VW---NRVEYRPLeGFVYAITPFNFTAIAANLPASAAMM- 205
Cdd:cd07098 74 DAslgEILVTCEKIRWTLKHGEKALR-----PESRPGgllMFykrARVEYEPL-GVVGAIVSWNYPFHNLLGPIIAALFa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 206 GNVVVWKPSDSQVFSA----KIIVDVFKEAGVPDGVINVV--FGDAlmiTDTVLASRDFAGIHFTGSTHVFKDIwAKIGA 279
Cdd:cd07098 148 GNAIVVKVSEQVAWSSgfflSIIRECLAACGHDPDLVQLVtcLPET---AEALTSHPVIDHITFIGSPPVGKKV-MAAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 280 ninnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSP 359
Cdd:cd07098 224 -----ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 360 EDfGNF-ITAVIHEGSFDKLASYIDQAKKdADAEIIVGGNYDKS----VGYFIEPTVIVTTNPKYTTMETELFGPVITLY 434
Cdd:cd07098 299 LD-GDVdVGAMISPARFDRLEELVADAVE-KGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVM 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006071571 435 VYEDAkwEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGMQPFGGARASG 505
Cdd:cd07098 377 KASDD--EEAVEIANST-EYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSG 442
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
69-505 |
1.30e-41 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 155.84 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIA--GPYRARINAATMigqSKNIHQAEIDSSCELI 146
Cdd:PRK13473 29 VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEenADEFARLESLNC---GKPLHLALNDEIPAIV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 147 DFLRYnveFMTQIYNDQPKS------DSTVWNRVEyrPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSD-- 215
Cdd:PRK13473 106 DVFRF---FAGAARCLEGKAageyleGHTSMIRRD--PV-GVVASIAPWNYPLMMAAwklAPALAA--GNTVVLKPSEit 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 216 --SQVFSAKIIVDVFkeagvPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGE 293
Cdd:PRK13473 178 plTALKLAELAADIL-----PPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK------RTHLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYIDQAKKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSE 453
Cdd:PRK13473 327 HRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE--DQAVRWAN-DSD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 454 YALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKptGAVVGMQPFGGARASG 505
Cdd:PRK13473 404 YGLASSVWTRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
81-525 |
4.19e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 155.42 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyrariNAATMIgqskNIHQAE--------IDSSCELIDFLRY- 151
Cdd:PRK09407 56 VEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLE------NREELL----DLVQLEtgkarrhaFEEVLDVALTARYy 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 152 ---------------NVEFMTQiyndqpksdstvwNRVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKP 213
Cdd:PRK09407 126 arrapkllaprrragALPVLTK-------------TTELRQPK-GVVGVISPWNYpltLAVSDAIPALLA--GNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 214 sDSQ-VFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFagIHFTGSTHVFKDIWAKIGAninnyktypRIVG 292
Cdd:PRK09407 190 -DSQtPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAGR---------RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 293 ---ETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAV 369
Cdd:PRK09407 258 fslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 370 IHEGSFDKLASYIDQAKKdADAEIIVGGNYDKSVG-YFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELV 448
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVA-KGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006071571 449 DTTsEYALTGAVFSQD-RYAIEVATtklQNAAGNFYINDKPTGAVVGMQ-PFGGARASGTNDKAGSAlNLLRWASPRTI 525
Cdd:PRK09407 415 NDT-PYGLNASVWTGDtARGRAIAA---RIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGRRHGAE-GLLKYTESQTI 488
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
78-506 |
8.57e-41 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 154.08 E-value: 8.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 78 KKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyrarINAATMIGQSKNIHQAE--IDSSCELI---DFLRYN 152
Cdd:PLN02278 61 RAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI-------IANKEDLAQLMTLEQGKplKEAIGEVAygaSFLEYF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 153 VEFMTQIYND---QPKSDSTVWnrVEYRPLeGFVYAITPFNF-----TAIAAnlPASAAmmGNVVVWKPSDSQVFSAKII 224
Cdd:PLN02278 134 AEEAKRVYGDiipSPFPDRRLL--VLKQPV-GVVGAITPWNFplamiTRKVG--PALAA--GCTVVVKPSELTPLTALAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 225 VDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGaninnyKTYPRIVGETGGKDFIIAHP 304
Cdd:PLN02278 207 AELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATVKRVSLELGGNAPFIVFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 305 SANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQ 384
Cdd:PLN02278 281 DADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 385 AKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQD 464
Cdd:PLN02278 361 AVSKG-AKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDT-EAGLAAYIFTRD 436
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2006071571 465 -RYAIEVAtTKLQNaaGNFYINDKPTGAVVGmqPFGGARASGT 506
Cdd:PLN02278 437 lQRAWRVS-EALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
91-511 |
1.81e-38 |
|
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: 147.26 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 91 ARKA-----WANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQAEIDSSCELIDFLRYNVEFMTQIYNDQPK 165
Cdd:cd07142 50 ARKAfdegpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 166 SDSTVWNRVEYRPLeGFVYAITPFNFTAIAANL---PASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVV- 241
Cdd:cd07142 129 ADGPHHVYTLHEPI-GVVGQIIPWNFPLLMFAWkvgPALAC--GNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVt 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 242 -FGDAlmiTDTVLASR-DFAGIHFTGSTHVFKDIwAKIGANINnyktYPRIVGETGGKDFIIAHPSANVKQVVTGITRGA 319
Cdd:cd07142 206 gFGPT---AGAAIASHmDVDKVAFTGSTEVGKII-MQLAAKSN----LKPVTLELGGKSPFIVCEDADVDKAVELAHFAL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 320 FEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkKDADAEIIVGGNY 399
Cdd:cd07142 278 FFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHG-KEEGATLITGGDR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 400 DKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaA 479
Cdd:cd07142 357 IGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV--DEVIKRAN-NSKYGLAAGVFSKNIDTANTLSRALK--A 431
|
410 420 430
....*....|....*....|....*....|....
gi 2006071571 480 GNFYIN--DKPTGAVvgmqPFGGARASGTNDKAG 511
Cdd:cd07142 432 GTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
76-506 |
4.44e-38 |
|
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: 145.95 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 76 AEKKHIESAIANALEARK---AWANMAWEQRAAIFLKAAELIAgpyRARINAATM--IGQSKNIHQAEIDSSCELIDFLR 150
Cdd:cd07141 41 GDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIE---RDRAYLASLetLDNGKPFSKSYLVDLPGAIKVLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 151 YNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANL---PASAAmmGNVVVWKPSDSQVFSAKIIVDV 227
Cdd:cd07141 118 YYAGWADKIHGKTIPMDGDFFTYTRHEPV-GVCGQIIPWNFPLLMAAWklaPALAC--GNTVVLKPAEQTPLTALYLASL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 228 FKEAGVPDGVINVV--FGDalmITDTVLASR-DFAGIHFTGSTHVFKDIwaKIGANINNYKtypRIVGETGGKDFIIAHP 304
Cdd:cd07141 195 IKEAGFPPGVVNVVpgYGP---TAGAAISSHpDIDKVAFTGSTEVGKLI--QQAAGKSNLK---RVTLELGGKSPNIVFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 305 SANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQ 384
Cdd:cd07141 267 DADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIES 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 385 AKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQD 464
Cdd:cd07141 347 GKKEG-AKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI--DEVIERANNT-TYGLAAAVFTKD 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2006071571 465 -RYAIEVaTTKLQnaAGNFYINdkpTGAVVGMQ-PFGGARASGT 506
Cdd:cd07141 423 iDKAITF-SNALR--AGTVWVN---CYNVVSPQaPFGGYKMSGN 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
54-512 |
4.91e-37 |
|
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: 143.12 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 54 TGNTKNITA--PHDHQhVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIflkaAELIAGPYRARINA-ATMI-- 128
Cdd:cd07130 8 GGGGGVVTSisPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEI----VRQIGDALRKKKEAlGKLVsl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 129 --GQSKNIHQAEIDsscELIDFLRYNVEFMTQIYNDQPKSDST------VWNrveyrPLeGFVYAITPFNF-TAIAANLP 199
Cdd:cd07130 83 emGKILPEGLGEVQ---EMIDICDFAVGLSRQLYGLTIPSERPghrmmeQWN-----PL-GVVGVITAFNFpVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 200 ASAAMMGNVVVWKPSDSQVFSA----KIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIWA 275
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 276 KIGANinnyktYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMK 355
Cdd:cd07130 233 AVAAR------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 356 MGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDaDAEIIVGGNYDKSVGYFIEPTvIVTTNPKYTTMETELFGPVitLYV 435
Cdd:cd07130 307 IGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQ-GGTVLFGGKVIDGPGNYVEPT-IVEGLSDAPIVKEETFAPI--LYV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 436 YEDAKWEETLELVDTTSEyALTGAVFSQDRYAIEvattKLQNAAG------NfyINDKPTGAVVGmQPFGGARASGTNDK 509
Cdd:cd07130 383 LKFDTLEEAIAWNNEVPQ-GLSSSIFTTDLRNAF----RWLGPKGsdcgivN--VNIGTSGAEIG-GAFGGEKETGGGRE 454
|
...
gi 2006071571 510 AGS 512
Cdd:cd07130 455 SGS 457
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
41-505 |
2.77e-36 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 141.41 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 41 IDVP---LYIGSEEIR--TGNTKNITAPHDHQHVvGKYHLAEKKHIESAIANALEA-----RKAWANMAWEQRAAiFLKA 110
Cdd:PLN02467 3 IPVPrrqLFIGGEWREpvLGKRIPVVNPATEETI-GDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAK-YLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 111 aelIAGPYRARINA---ATMIGQSKNIHQAEID------------SSCELIDflrynvefmtqIYNDQPKS--DSTVWNR 173
Cdd:PLN02467 81 ---IAAKITERKSElakLETLDCGKPLDEAAWDmddvagcfeyyaDLAEALD-----------AKQKAPVSlpMETFKGY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 174 VEYRPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITD 250
Cdd:PLN02467 147 VLKEPL-GVVGLITPWNYPLLMATwkvAPALAA--GCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 251 TVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktyPrIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAA 330
Cdd:PLN02467 224 PLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 331 SRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDK--SVGYFIE 408
Cdd:PLN02467 298 SRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEG-ATILCGGKRPEhlKKGFFIE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 409 PTVIVTTNPKYTTMETELFGPVitLYVYEDAKWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYIN-DK 487
Cdd:PLN02467 377 PTIITDVTTSMQIWREEVFGPV--LCVKTFSTEDEAIELANDS-HYGLAGAVISNDLERCERVSEAFQ--AGIVWINcSQ 451
|
490
....*....|....*...
gi 2006071571 488 PTGAvvgMQPFGGARASG 505
Cdd:PLN02467 452 PCFC---QAPWGGIKRSG 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
69-505 |
5.34e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 140.40 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIagpyRAR---INAATMIGQSKNIHQAEIDSSCEL 145
Cdd:PRK13252 34 VLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL----RERndeLAALETLDTGKPIQETSVVDIVTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 146 IDFLRYNVEFMTQIYNDQ-P-KSDSTVWNRVEyrPLeGFVYAITPFNF-TAIAANLPASAAMMGNVVVWKPSDSQVFSAK 222
Cdd:PRK13252 110 ADVLEYYAGLAPALEGEQiPlRGGSFVYTRRE--PL-GVCAGIGAWNYpIQIACWKSAPALAAGNAMIFKPSEVTPLTAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 223 IIVDVFKEAGVPDGVINVVFGDA---LMITdtvlASRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDF 299
Cdd:PRK13252 187 KLAEIYTEAGLPDGVFNVVQGDGrvgAWLT----EHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVTMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 300 IIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLA 379
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 380 SYIDQAKKDAdAEIIVGG------NYDKsvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsE 453
Cdd:PRK13252 337 GYIEKGKAEG-ARLLCGGerltegGFAN--GAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE--DEVIARANDT-E 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 454 YALTGAVFSQD-RYAIEVAtTKLQnaAGNFYIN---DKPtgavVGMqPFGGARASG 505
Cdd:PRK13252 411 YGLAAGVFTADlSRAHRVI-HQLE--AGICWINtwgESP----AEM-PVGGYKQSG 458
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
80-511 |
6.94e-36 |
|
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: 138.94 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 80 HIESAIANALEARKAWANMAWEQRAAIFLKAAEL-----------IA----GP-YRARINAATMIGQsknihqaeIDSSc 143
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELlkankeelarlISretgKPlWEAQTEVAAMAGK--------IDIS- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 144 eLIDFLRYNVEfmTQIYNDQPKSdstvwnRVEYRPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQVFS 220
Cdd:cd07095 72 -IKAYHERTGE--RATPMAQGRA------VLRHRPH-GVMAVFGPFNFPGHLPNghiVPALLA--GNTVVFKPSELTPAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 221 AKIIVDVFKEAGVPDGVINVVFGDAlmitDT---VLASRDFAGIHFTGSTHVFKDIWAKIGANinnyktYPRIVG-ETGG 296
Cdd:cd07095 140 AELMVELWEEAGLPPGVLNLVQGGR----ETgeaLAAHEGIDGLLFTGSAATGLLLHRQFAGR------PGKILAlEMGG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 297 KDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLW-PAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSF 375
Cdd:cd07095 210 NNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 376 DKLASYIDQAKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMEtELFGPVITLYVYEDakWEETLELVDTTsEYA 455
Cdd:cd07095 290 ARYLLAQQDLLALG-GEPLLAMERLVAGTAFLSPGIIDVTDAADVPDE-EIFGPLLQVYRYDD--FDEAIALANAT-RFG 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 456 LTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAvVGMQPFGGARASGtNDKAG 511
Cdd:cd07095 365 LSAGLLSDDEALFERFLARIR--AGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPS 416
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
69-505 |
2.80e-35 |
|
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: 137.48 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEA--RKAWANMAwEQRAAIFLKAA---ELIAGPYrARINAA---TMIGQSKNihqaEID 140
Cdd:cd07120 9 VIGTYADGGVAEAEAAIAAARRAfdETDWAHDP-RLRARVLLELAdafEANAERL-ARLLALengKILGEARF----EIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 141 SScelIDFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTA---IAANLPASAAmmGNVVVWKPSDSQ 217
Cdd:cd07120 83 GA---ISELRYYAGLARTEAGRMIEPEPGSFSLVLREPM-GVAGIIVPWNSPVvllVRSLAPALAA--GCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 218 VFSAKIIVDVFKEA-GVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAkIGAninnyKTYPRIVGETGG 296
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMA-AAA-----PTLKRLGLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 297 KDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFD 376
Cdd:cd07120 231 KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 377 KLASYIDQAKKDADAEIIVGG--NYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAKweETLELVDTTsEY 454
Cdd:cd07120 311 RVDRMVERAIAAGAEVVLRGGpvTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALANDT-DY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 455 ALTGAVFSQD-RYAIEVAtTKLQnaAGNFYINDKptGAVVGMQPFGGARASG 505
Cdd:cd07120 388 GLAASVWTRDlARAMRVA-RAIR--AGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
69-505 |
2.08e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 135.37 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAaiflKAAELIAGPYRARINA-ATMIGQS--KNIHQA--EIDSSC 143
Cdd:PRK13968 19 QLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRA----QKLRDIGKALRARSEEmAQMITREmgKPINQAraEVAKSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 144 ELIDflrYNVEFMTQIYNDQPksdSTVWNR---VEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPSDSQ 217
Cdd:PRK13968 95 NLCD---WYAEHGPAMLKAEP---TLVENQqavIEYRPL-GTILAIMPWNFplwQVMRGAVPILLA--GNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 218 VFSAKIIVDVFKEAGVPDGVINVVFGD----ALMITDtvlasRDFAGIHFTGSTHVFKDIWAKIGANINnyktypRIVGE 293
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADndgvSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAALK------KCVLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 294 TGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEG 373
Cdd:PRK13968 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 374 SFDKLASYIdQAKKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSE 453
Cdd:PRK13968 315 LRDELHHQV-EATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDA--EHALELAN-DSE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2006071571 454 YALTGAVFSQDRYAIEVATTKLQnaAGNFYIND-KPTGAVVGmqpFGGARASG 505
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLE--CGGVFINGyCASDARVA---FGGVKKSG 438
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
78-505 |
7.64e-34 |
|
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: 134.12 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 78 KKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPYRARINAATmIGQSKNIHQAEIDSSCELIDFLRYnveFMT 157
Cdd:cd07116 37 AEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-WDNGKPVRETLAADIPLAIDHFRY---FAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 158 QIyNDQPKSDSTV-WNRVEY---RPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQVFSAKIIVDVFKE 230
Cdd:cd07116 113 CI-RAQEGSISEIdENTVAYhfhEPL-GVVGQIIPWNFPLLMATwklAPALAA--GNCVVLKPAEQTPASILVLMELIGD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 231 AgVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANInnyktYPrIVGETGGK------DFIIAHP 304
Cdd:cd07116 189 L-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKspniffADVMDAD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 305 SANVKQVVTGITRGAFEfQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQ 384
Cdd:cd07116 262 DAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 385 AKKDAdAEIIVGGNY----DKSVGYFIEPTVIVTTNpKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAV 460
Cdd:cd07116 341 GKEEG-AEVLTGGERnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDE--EEALEIANDT-LYGLGAGV 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2006071571 461 FSQDRYAIEVATTKLQnaAGNFYIN---DKPTGAvvgmqPFGGARASG 505
Cdd:cd07116 416 WTRDGNTAYRMGRGIQ--AGRVWTNcyhLYPAHA-----AFGGYKQSG 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
78-514 |
3.70e-33 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 132.33 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 78 KKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIAGpYRARINAATMIGQSKNIHQAEIDSSCELIDFLRYNVEF 155
Cdd:PRK09847 56 SVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEA-HAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 156 MTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANL---PASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAG 232
Cdd:PRK09847 135 IDKVYGEVATTSSHELAMIVREPV-GVIAAIVPWNFPLLLTCWklgPALAA--GNSVILKPSEKSPLSAIRLAGLAKEAG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 233 VPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGAniNNYKtypRIVGETGGKDF-IIAHPSANVKQV 311
Cdd:PRK09847 212 LPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD--SNMK---RVWLEAGGKSAnIVFADCPDLQQA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 312 VTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkkDADA 391
Cdd:PRK09847 287 ASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREG--ESKG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 392 EIIVGGNYDKSVGYfIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDRYAIEVA 471
Cdd:PRK09847 365 QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAN-DSQYGLGAAVWTRDLSRAHRM 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2006071571 472 TTKLQnaAGNFYINDKPTGAVVgmQPFGGARASGT-NDKAGSAL 514
Cdd:PRK09847 441 SRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSGNgRDKSLHAL 480
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
69-505 |
2.07e-32 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 130.33 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 69 VVGKYHLAEKKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQAEIDSSCELI 146
Cdd:PLN02766 48 VIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE-EHIEELAALDTIDAGKLFALGKAVDIPAAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 147 DFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANLPASAAMM-GNVVVWKPSDSQVFSAKIIV 225
Cdd:PLN02766 127 GLLRYYAGAADKIHGETLKMSRQLQGYTLKEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 226 DVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAkiGANINNYKtypRIVGETGGKDFIIAHPS 305
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ--AAATSNLK---QVSLELGGKSPLLIFDD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 306 ANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQA 385
Cdd:PLN02766 281 ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 386 KKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDr 465
Cdd:PLN02766 361 KREG-ATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV--EEAIKKANNT-KYGLAAGIVTKD- 435
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2006071571 466 yaIEVATTKLQNA-AGNFYINdkptgAVVGMQ---PFGGARASG 505
Cdd:PLN02766 436 --LDVANTVSRSIrAGTIWVN-----CYFAFDpdcPFGGYKMSG 472
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
81-505 |
3.40e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 129.09 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELIAGpyRARINAATM---IGQSKNIHQAEIdSSCelIDFLRYNVEFMT 157
Cdd:PRK09406 25 VDAAIARAHARFRDYRTTTFAQRARWANAAADLLEA--EADQVAALMtleMGKTLASAKAEA-LKC--AKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 158 QIYNDQPKSDSTVWNR---VEYRPLeGFVYAITPFNFTAI-AANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGV 233
Cdd:PRK09406 100 ALLADEPADAAAVGASrayVRYQPL-GVVLAVMPWNFPLWqVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 234 PDGVinvvFGDALMITDTVLAS-RD--FAGIHFTGSTHVFKDIWAKIGANINnyKTypriVGETGGKDFIIAHPSANVKQ 310
Cdd:PRK09406 179 PDGC----FQTLLVGSGAVEAIlRDprVAAATLTGSEPAGRAVAAIAGDEIK--KT----VLELGGSDPFIVMPSADLDR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 311 VVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkKDAD 390
Cdd:PRK09406 249 AAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA-VAAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 391 AEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTSeYALTGAVFS-----QDR 465
Cdd:PRK09406 328 ATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADI--DEAIEIANATT-FGLGSNAWTrdeaeQER 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2006071571 466 YAIEVattklqnAAGNFYINdkptgavvGMQ------PFGGARASG 505
Cdd:PRK09406 405 FIDDL-------EAGQVFIN--------GMTvsypelPFGGVKRSG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
181-505 |
2.58e-31 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 126.74 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 181 GFVYAITPFNFTAIAAN---LPASAamMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALmiTDTVLASR- 256
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAwkiCPALA--MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS--FGSALANHp 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 257 DFAGIHFTGSTHVFKDIwAKIGANinnykTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIP 336
Cdd:cd07111 225 GVDKVAFTGSTEVGRAL-RRATAG-----TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 337 QSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTN 416
Cdd:cd07111 299 ESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEG-ADVFQPGADLPSKGPFYPPTLFTNVP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 417 PKYTTMETELFGPVITLYVYEDAKweETLELVDTTsEYALTGAVFSQD-RYAIEVAttkLQNAAGNFYINDkpTGAVVGM 495
Cdd:cd07111 378 PASRIAQEEIFGPVLVVLTFRTAK--EAVALANNT-PYGLAASVWSENlSLALEVA---LSLKAGVVWING--HNLFDAA 449
|
330
....*....|
gi 2006071571 496 QPFGGARASG 505
Cdd:cd07111 450 AGFGGYRESG 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
46-515 |
9.17e-31 |
|
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: 125.30 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 46 YIGSEEIRTGNTKNitaPHDhQHVVGKYHLAEKKHIESAIANALEA--RKAWANMAWEQRAAIFLKAAELIAGPYR--AR 121
Cdd:cd07140 14 FVDAEGGKTYNTIN---PTD-GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEelAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 122 INA-----------ATMIGQSknihqaeidsscelIDFLRYNVEFMTQIY-------NDQPKSDSTVWNRveyRPLeGFV 183
Cdd:cd07140 90 IESldsgavytlalKTHVGMS--------------IQTFRYFAGWCDKIQgktipinQARPNRNLTLTKR---EPI-GVC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 184 YAITPFNFTAIAANLPASAAMM-GNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIH 262
Cdd:cd07140 152 GIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 263 FTGSTHVFKDIWAKigANINNYKtypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPA 342
Cdd:cd07140 232 FTGSTPIGKHIMKS--CAVSNLK---KVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 343 VKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTM 422
Cdd:cd07140 307 FVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEG-ATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 423 ETELFGPVITLYVYEDAKWEETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAVVGmqPFGGAR 502
Cdd:cd07140 386 KEESFGPIMIISKFDDGDVDGVLQRANDT-EYGLASGVFTKDINKALYVSDKLE--AGTVFVNTYNKTDVAA--PFGGFK 460
|
490
....*....|....
gi 2006071571 503 ASGTNDKAG-SALN 515
Cdd:cd07140 461 QSGFGKDLGeEALN 474
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
114-505 |
2.23e-30 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 122.92 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 114 IAGPYRARIN--AATMI---GQSKNIHQAEIDSSCELIDFL-----RYNVEFmtqIYNDQPKSDSTVWNRveyrPLeGFV 183
Cdd:PRK10090 4 IAAGIRERASeiSALIVeegGKIQQLAEVEVAFTADYIDYMaewarRYEGEI---IQSDRPGENILLFKR----AL-GVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 184 YAITPFNFT--AIAANLpASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGI 261
Cdd:PRK10090 76 TGILPWNFPffLIARKM-APALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 262 HFTGSTHVFKDIWAKIGANINnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWP 341
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNIT------KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 342 AVKEQLIADVKSMKMGSPEDFGNF-ITAVIHEGSFDKLASYIDQAKKdADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYT 420
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVE-EGARVALGGKAVEGKGYYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 421 TMETELFGPVITLYVYEdaKWEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINDKPTGAvvgMQPF-G 499
Cdd:PRK10090 308 IMHEETFGPVLPVVAFD--TLEEAIAMAN-DSDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRENFEA---MQGFhA 379
|
....*.
gi 2006071571 500 GARASG 505
Cdd:PRK10090 380 GWRKSG 385
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
173-505 |
4.73e-29 |
|
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: 119.25 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 173 RVEYRPlEGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPSD-----SQVfSAKIIVDVFKEAGVPdgvinVVFGD 244
Cdd:cd07134 95 KIRYEP-KGVCLIISPWNYpfnLAFGPLVSAIAA--GNTAILKPSEltphtSAV-IAKIIREAFDEDEVA-----VFEGD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 245 ALmiTDTVLASRDFAGIHFTGSTHVFKDIWAKIGaninnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQG 324
Cdd:cd07134 166 AE--VAQALLELPFDHIFFTGSPAVGKIVMAAAA------KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 325 QKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPE-----DFGNfitaVIHEGSFDKLASYIDQAKKDAdAEIIVGGNY 399
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAArkaspDLAR----IVNDRHFDRLKGLLDDAVAKG-AKVEFGGQF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 400 DKSvGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDRYAIEvatTKLQN-A 478
Cdd:cd07134 313 DAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDL--DEVIEYIN-AKPKPLALYVFSKDKANVN---KVLARtS 385
|
330 340
....*....|....*....|....*..
gi 2006071571 479 AGNFYINDKPTGAVVGMQPFGGARASG 505
Cdd:cd07134 386 SGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
173-505 |
9.85e-29 |
|
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: 118.40 E-value: 9.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 173 RVEYRPLeGFVYAITPFNF---TAIAANLPASAAmmGNVVVWKPSDSQVFSAKIIVDVFKEAgVPDGVINVVFGDALMIT 249
Cdd:cd07087 95 YVIPEPL-GVVLIIGPWNYplqLALAPLIGAIAA--GNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 250 DtVLASRdFAGIHFTGSTHVFKDIWAKIGANINnyktyPrIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSA 329
Cdd:cd07087 171 A-LLAEP-FDHIFFTGSPAVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 330 ASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFiTAVIHEGSFDKLASYIDQAKkdadaeIIVGGNYDKSvGYFIEP 409
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLDDGK------VVIGGQVDKE-ERYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 410 TVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTSEyALTGAVFSQDRYAIE--VATTklqnAAGNFYINDk 487
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDL--DEAIEFINSRPK-PLALYLFSEDKAVQErvLAET----SSGGVCVND- 386
|
330 340
....*....|....*....|....
gi 2006071571 488 ptgavVGMQ------PFGGARASG 505
Cdd:cd07087 387 -----VLLHaaipnlPFGGVGNSG 405
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
81-505 |
2.02e-28 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 118.52 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIF------LKA-----AELIA----GP-YRARINAATMIGQsknihqaeIDSSce 144
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVerfaalLEEnkeelAEVIAretgKPlWEAATEVTAMINK--------IAIS-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 145 lidflrynvefmTQIYNDQ--PKSDSTVWNR--VEYRPLeGFVYAITPFNFTAIAAN---LPASAAmmGNVVVWKPSDSQ 217
Cdd:PRK09457 109 ------------IQAYHERtgEKRSEMADGAavLRHRPH-GVVAVFGPYNFPGHLPNghiVPALLA--GNTVVFKPSELT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 218 VFSAKIIVDVFKEAGVPDGVINVVFGDAlmitDT---VLASRDFAGIHFTGSthvfkdiwAKIGANIN-NYKTYPRIVG- 292
Cdd:PRK09457 174 PWVAELTVKLWQQAGLPAGVLNLVQGGR----ETgkaLAAHPDIDGLLFTGS--------ANTGYLLHrQFAGQPEKILa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 293 -ETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWP-AVKEQLIADVKSMKMGSP-EDFGNFITAV 369
Cdd:PRK09457 242 lEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRWdAEPQPFMGAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 370 IHEGSFDKLASyiDQAKKDAD-AEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMEtELFGPVITLYVYEDakWEETLELV 448
Cdd:PRK09457 322 ISEQAAQGLVA--AQAQLLALgGKSLLEMTQLQAGTGLLTPGIIDVTGVAELPDE-EYFGPLLQVVRYDD--FDEAIRLA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006071571 449 DTTsEYALTGAVFSQDRyaiEVATTKLQNA-AGnfYIN-DKPTGAVVGMQPFGGARASG 505
Cdd:PRK09457 397 NNT-RFGLSAGLLSDDR---EDYDQFLLEIrAG--IVNwNKPLTGASSAAPFGGVGASG 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
53-505 |
3.23e-28 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 117.70 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 53 RTGNTKNITAPHDHQHV--VGKYHLAEKKhieSAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQ 130
Cdd:PRK11241 23 NNGEVIDVTNPANGDKLgsVPKMGADETR---AAIDAANRALPAWRALTAKERANILRRWFNLMM-EHQDDLARLMTLEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 131 SKNIHQA--EIDSSCElidFLRYNVEFMTQIYND-----QPKSDSTVWNRveyrPLeGFVYAITPFNFTAIAANLPASAA 203
Cdd:PRK11241 99 GKPLAEAkgEISYAAS---FIEWFAEEGKRIYGDtipghQADKRLIVIKQ----PI-GVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 204 MM-GNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANIN 282
Cdd:PRK11241 171 LAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 283 nyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDF 362
Cdd:PRK11241 251 ------KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 363 GNFITAVIHEGSFDKLASYIDQAKKDAdAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwE 442
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKG-ARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE--A 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006071571 443 ETLELVDTTsEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINdkpTGAVVG-MQPFGGARASG 505
Cdd:PRK11241 402 DVIAQANDT-EFGLAAYFYARDLSRVFRVGEALE--YGIVGIN---TGIISNeVAPFGGIKASG 459
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
162-506 |
4.09e-28 |
|
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: 116.55 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 162 DQPKSDSTVWN-----RVEYRPLeGFVYAITPFNFTAIAANLPASAAMM-GNVVVWKPSDSQVFSAKIIVDVFKEAgVPD 235
Cdd:cd07135 87 DEKVKDGPLAFmfgkpRIRKEPL-GVVLIIGPWNYPVLLALSPLVGAIAaGCTVVLKPSELTPHTAALLAELVPKY-LDP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 236 GVINVVFGdALMITDTVLASRdFAGIHFTGSTHVFKDIWAKigANinnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGI 315
Cdd:cd07135 165 DAFQVVQG-GVPETTALLEQK-FDKIFYTGSGRVGRIIAEA--AA----KHLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 316 TRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFiTAVIHEGSFDKLASYIDQAKkdadAEIIV 395
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLDTTK----GKVVI 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 396 GGNYDKSVgYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELV---DTTseyaLTGAVFSQDRYAIEVAT 472
Cdd:cd07135 312 GGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL--DEAIKVInsrDTP----LALYIFTDDKSEIDHIL 384
|
330 340 350
....*....|....*....|....*....|....*.
gi 2006071571 473 TKLQnaAGNFYINDkpTGAVVGMQ--PFGGARASGT 506
Cdd:cd07135 385 TRTR--SGGVVIND--TLIHVGVDnaPFGGVGDSGY 416
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
74-511 |
6.88e-28 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 117.22 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 74 HLAE--KKHIESAIAnalEARKA-----WANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQAEIDSSCELI 146
Cdd:PLN02466 88 HVAEgdAEDVNRAVA---AARKAfdegpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQSAKAELPMFA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 147 DFLRYNVEFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTAIAANL---PASAAmmGNVVVWKPSDSQVFSAKI 223
Cdd:PLN02466 164 RLFRYYAGWADKIHGLTVPADGPHHVQTLHEPI-GVAGQIIPWNFPLLMFAWkvgPALAC--GNTIVLKTAEQTPLSALY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 224 IVDVFKEAGVPDGVINVVFGDALMITDTVLASRDFAGIHFTGSTHVFKDIWAKigANINNYKTyprIVGETGGKDFIIAH 303
Cdd:PLN02466 241 AAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL--AAKSNLKP---VTLELGGKSPFIVC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 304 PSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYId 383
Cdd:PLN02466 316 EDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 384 QAKKDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTSeYALTGAVFSQ 463
Cdd:PLN02466 395 KSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL--DEVIRRANNTR-YGLAAGVFTQ 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 464 DryaIEVATTkLQNA--AGNFYIN--DKPTGAVvgmqPFGGARASGTNDKAG 511
Cdd:PLN02466 472 N---LDTANT-LSRAlrVGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
81-464 |
6.61e-27 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 114.08 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 81 IESAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQA--EIDSSCELIDF-----LRYNV 153
Cdd:PLN00412 55 VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILK-EHKAPIAECLVKEIAKPAKDAvtEVVRSGDLISYtaeegVRILG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 154 EFMTQIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTA-IAANLPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAG 232
Cdd:PLN00412 134 EGKFLVSDSFPGNERNKYCLTSKIPL-GVVLAIPPFNYPVnLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 233 VPDGVINVVFGDALMITDTVLASRDFAGIHFTGsthvfkdiwAKIGANINNYKTYPRIVGETGGKDFIIAHPSANVKQVV 312
Cdd:PLN00412 213 FPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG---------GDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 313 TGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNfITAVIHEGSfdklASYIDQAKKDADAE 392
Cdd:PLN00412 284 ANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESS----ANFIEGLVMDAKEK 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006071571 393 IIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQD 464
Cdd:PLN00412 359 GATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV--EEGIHHCN-ASNFGLQGCVFTRD 427
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
173-505 |
6.78e-27 |
|
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: 113.37 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 173 RVEYRPLeGFVYAITPFNFT----------AIAAnlpasaammGNVVVWKPSDSQVFSAKIIVDVFKEAgVPDGVINVVF 242
Cdd:cd07136 95 YIYYEPY-GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 243 GDAlMITDTVLASRdFAGIHFTGSTHVFKDIWAKIGANINNyktyprIVGETGGKDFIIAHPSANVKQVVTGITRGAFEF 322
Cdd:cd07136 164 GGV-EENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTP------VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 323 QGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFiTAVIHEGSFDKLASYIDQAKkdadaeIIVGGNYDKS 402
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGK------IVFGGNTDRE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 403 VGYfIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVdTTSEYALTGAVFSQDRYAIEVATTKLQNAAGnf 482
Cdd:cd07136 309 TLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTL--DEAIEII-KSRPKPLALYLFSEDKKVEKKVLENLSFGGG-- 382
|
330 340
....*....|....*....|....*....
gi 2006071571 483 YINDkptgavVGMQ------PFGGARASG 505
Cdd:cd07136 383 CIND------TIMHlanpylPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
174-505 |
1.01e-24 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 107.42 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 174 VEYRPLeGFVYAITPFNFTAIAANLPASAAMM-GNVVVWKPSDSQVFSAKIIVDVFKEAgVPDGVINVVFGDALMITDtv 252
Cdd:PTZ00381 105 IIPEPL-GVVLVIGAWNYPLNLTLIPLAGAIAaGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTE-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 253 LASRDFAGIHFTGSTHVfkdiwAKIGANINNYKTYPRIVgETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASR 332
Cdd:PTZ00381 181 LLKEPFDHIFFTGSPRV-----GKLVMQAAAENLTPCTL-ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 333 AYIPQS----LWPAVKEQLIadvksmKMGSP-----EDFGNFITavihEGSFDKLASYIDQAKKDadaeIIVGGNYDKSV 403
Cdd:PTZ00381 255 VLVHRSikdkFIEALKEAIK------EFFGEdpkksEDYSRIVN----EFHTKRLAELIKDHGGK----VVYGGEVDIEN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 404 GYfIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTSEyALTGAVFSQDRYAIEVATTKLQnaAGNFY 483
Cdd:PTZ00381 321 KY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENI--DEVLEFINSRPK-PLALYYFGEDKRHKELVLENTS--SGAVV 394
|
330 340
....*....|....*....|....*.
gi 2006071571 484 INDkptgAVVGMQ----PFGGARASG 505
Cdd:PTZ00381 395 IND----CVFHLLnpnlPFGGVGNSG 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-508 |
2.13e-24 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 107.14 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 43 VPLYIGSEEIRTGNTK--NITAPHDhQHVVGKYHLAEKKHIESAIANALEARKAWANMAWEQRAAIFLKAAELIAGPY-R 119
Cdd:PLN02419 114 VPNLIGGSFVESQSSSfiDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMdK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 120 ARINAATMIGQSKNIHQAEIDSSCELIDflrYNVEFMT-QIYNDQPKSDSTVWNRVEYRPLeGFVYAITPFNFTA-IAAN 197
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVE---HACGMATlQMGEYLPNVSNGVDTYSIREPL-GVCAGICPFNFPAmIPLW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 198 LPASAAMMGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDGVINVVFGdalmITDTVLA---SRDFAGIHFTGSTHVFKDIW 274
Cdd:PLN02419 269 MFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHG----TNDTVNAicdDEDIRAVSFVGSNTAGMHIY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 275 AKIGANINnyktypRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYI--PQSLWpavKEQLIADVK 352
Cdd:PLN02419 345 ARAAAKGK------RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSW---EDKLVERAK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 353 SMKM---GSPE-DFGNFITAVIHEGSFDKLASYIDQ-AKKDADAEIIVGGNYDKsvGYFIEPTVIVTTNPKYTTMETELF 427
Cdd:PLN02419 416 ALKVtcgSEPDaDLGPVISKQAKERICRLIQSGVDDgAKLLLDGRDIVVPGYEK--GNFIGPTILSGVTPDMECYKEEIF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 428 GPVitLYVYEDAKWEETLELVDtTSEYALTGAVFSQDRYAIEVATTKLQnaAGNFYINdKPTGAVVGMQPFGGARASGTN 507
Cdd:PLN02419 494 GPV--LVCMQANSFDEAISIIN-KNKYGNGAAIFTSSGAAARKFQMDIE--AGQIGIN-VPIPVPLPFFSFTGNKASFAG 567
|
.
gi 2006071571 508 D 508
Cdd:PLN02419 568 D 568
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
172-507 |
1.60e-23 |
|
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: 103.27 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 172 NRVEYRPLE--GFVYAITPFNF----------TAIAANLPasaammgnvVVWKPSDSQVFSAKIIVDVFKEAGVPDGVIN 239
Cdd:cd07148 115 GRIAFTTREpiGVVVAISAFNHplnlivhqvaPAIAAGCP---------VIVKPALATPLSCLAFVDLLHEAGLPEGWCQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 240 VVFGDA----LMITDTVLAsrdFagIHFTGSthvfkdiwAKIGANINNyKTYP--RIVGETGGKDFIIAHPSANVKQVVT 313
Cdd:cd07148 186 AVPCENavaeKLVTDPRVA---F--FSFIGS--------ARVGWMLRS-KLAPgtRCALEHGGAAPVIVDRSADLDAMIP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 314 GITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAkKDADAEI 393
Cdd:cd07148 252 PLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEA-VAAGARL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 394 IVGGNYDKSVGYfiEPTVIVttNP----KYTTMetELFGPVITLYVYEDAkwEETLELVDTTsEYALTGAVFSQDryaIE 469
Cdd:cd07148 331 LCGGKRLSDTTY--APTVLL--DPprdaKVSTQ--EIFGPVVCVYSYDDL--DEAIAQANSL-PVAFQAAVFTKD---LD 398
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2006071571 470 VA--TTKLQNAAGnFYINDkPTGAVVGMQPFGGARASGTN 507
Cdd:cd07148 399 VAlkAVRRLDATA-VMVND-HTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
137-505 |
4.17e-22 |
|
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: 98.71 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 137 AEIDSSCELIDFLRYNV-EFMtqiyndQPKSDSTVW------NRVEYRPLeGFVYAITPFNF----------TAIAAnlp 199
Cdd:cd07133 59 AEILPSIAGIKHARKHLkKWM------KPSRRHVGLlflpakAEVEYQPL-GVVGIIVPWNYplylalgpliAALAA--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 200 asaammGNVVVWKPSD-----SQVFsAKIIVDVFKEAgvpdgVINVVFGDALMitdtvlaSRDFAGI---H--FTGSTHV 269
Cdd:cd07133 129 ------GNRVMIKPSEftprtSALL-AELLAEYFDED-----EVAVVTGGADV-------AAAFSSLpfdHllFTGSTAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 270 FKDIWAKIGANINnyktyPrIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIA 349
Cdd:cd07133 190 GRHVMRAAAENLT-----P-VTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 350 DVKSM---KMGSPEdfgnfITAVIHEGSFDKLASYIDQAK-KDADAEIIVGGNYDKSVGYFIEPTVIVTTNPKYTTMETE 425
Cdd:cd07133 264 AVAKMyptLADNPD-----YTSIINERHYARLQGLLEDARaKGARVIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 426 LFGPVITLYVYEDAkwEETLELVdTTSEYALTGAVFSQDRYAIEVATTklQNAAGNFYINDKPTGAVVGMQPFGGARASG 505
Cdd:cd07133 339 IFGPILPILTYDSL--DEAIDYI-NARPRPLALYYFGEDKAEQDRVLR--RTHSGGVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
144-512 |
4.94e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 99.52 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 144 ELIDFLRYNVEFMTQIYNDQPKSDS------TVWNrveyrPLeGFVYAITPFNFTAIAANLPASAAMM-GNVVVWK--PS 214
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERpnhmmmEVWN-----PL-GIVGVITAFNFPCAVLGWNACIALVcGNCVVWKgaPT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 215 DSQVFSA--KIIVDVFKEAGVPDGVINVVFGDAlMITDTVLASRDFAGIHFTGSTHVFKDIWAKIGANinnyktYPRIVG 292
Cdd:PLN02315 193 TPLITIAmtKLVAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 293 ETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHE 372
Cdd:PLN02315 266 ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTP 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 373 GSFDKLASYIdQAKKDADAEIIVGGNYDKSVGYFIEPTvIVTTNPKYTTMETELFGPVitLYVYEDAKWEETLELVDTTS 452
Cdd:PLN02315 346 ESKKNFEKGI-EIIKSQGGKILTGGSAIESEGNFVQPT-IVEISPDADVVKEELFGPV--LYVMKFKTLEEAIEINNSVP 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 453 EyALTGAVFSQDRYAIEVATTKLQNAAGNFYINDKPTGAVVGmQPFGGARASGTNDKAGS 512
Cdd:PLN02315 422 Q-GLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
82-525 |
1.76e-20 |
|
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: 94.23 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 82 ESAIANALEARKAWANMAWEQRAAIFLKAAELIAgPYRARINAATMIGQSKNIHQA-EIDSSC---ELIDFLRYNVEFMT 157
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAeNICGDQvqlRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 158 QIYNDQPKSDSTVWNRveYRPLEGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDSQVFSAKIIVDVFKEAG-VPD 235
Cdd:cd07084 81 EPGNHLGQGLKQQSHG--YRWPYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 236 GVINVVFGDAlMITDTVLASRDFAGIHFTGSthvfkdiwAKIGANINNYKTYPRIVGETGGKDFIIAHPSAN-VKQVVTG 314
Cdd:cd07084 159 EDVTLINGDG-KTMQALLLHPNPKMVLFTGS--------SRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 315 ITRGAFEFQGQKCSAASRAYIPQSlwpAVKEQLIADVKSmKMGSPEDFGNFITAVIHEGSFDKLASY--IDQAKKDADAE 392
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVPEN---WSKTPLVEKLKA-LLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 393 IIVGGNYDKSVGYFIEPTVIVTTNP---KYTTMETELFGPVITLYVYEDAKWEETLELVDTTSEyALTGAVFSQDRYAIE 469
Cdd:cd07084 306 ELKNHSIPSIYGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG-SLTAAIYSNDPIFLQ 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 470 VATTKLQNAAGNFYINDKPTGAVVGMQPFGGARASGTNDKAGSALNLLRWASPRTI 525
Cdd:cd07084 385 ELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
178-473 |
2.93e-18 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 87.71 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 178 PLEGFVYAITPFNFTA------IAANLPAsaammGNVVVWKPSDSQVFSAKIIVDVFKEAGV-PDGVINVVFGDALMITD 250
Cdd:cd07128 143 PRRGVAVHINAFNFPVwgmlekFAPALLA-----GVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 251 TvLASRDFagIHFTGSthvfkdiwAKIGANInnyKTYPRIVGEtgGKDFIIAHPSAN------------------VKQVV 312
Cdd:cd07128 218 H-LGEQDV--VAFTGS--------AATAAKL---RAHPNIVAR--SIRFNAEADSLNaailgpdatpgtpefdlfVKEVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 313 TGITRGAfefqGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDA--- 389
Cdd:cd07128 282 REMTVKA----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAevv 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 390 ----DAEIIVGGNYDKsvGYFIEPTVIVTTNPKYTTM--ETELFGPVITLYVYEDAkwEETLELVdTTSEYALTGAVFSQ 463
Cdd:cd07128 358 fggpDRFEVVGADAEK--GAFFPPTLLLCDDPDAATAvhDVEAFGPVATLMPYDSL--AEAIELA-ARGRGSLVASVVTN 432
|
330
....*....|....*
gi 2006071571 464 DR-----YAIEVATT 473
Cdd:cd07128 433 DPafareLVLGAAPY 447
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
188-505 |
1.34e-17 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 85.35 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 188 PFNFT------AIAAnlpasaammGNVVVWKPSDSQVFSAKIIVDV---------FK--EAGVPDgvinvvfgdalmiTD 250
Cdd:cd07132 113 PLQLTlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAELipkyldkecYPvvLGGVEE-------------TT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 251 TVLASRdFAGIHFTGSTHVFKDIWAkiGANinnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQGQKCSAA 330
Cdd:cd07132 171 ELLKQR-FDYIFYTGSTSVGKIVMQ--AAA----KHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 331 SraYIPQSlwPAVKEQLIADVK-SMK-------MGSPeDFGNfitaVIHEGSFDKLASYIDQAKkdadaeIIVGGNYDKS 402
Cdd:cd07132 244 D--YVLCT--PEVQEKFVEALKkTLKefygedpKESP-DYGR----IINDRHFQRLKKLLSGGK------VAIGGQTDEK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 403 VGYfIEPTVIVTTNPKYTTMETELFGPVITLYVYEDAkwEETLELVDtTSEYALTGAVFSQDRyaiEVATTKLQN-AAGN 481
Cdd:cd07132 309 ERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNL--DEAIEFIN-SREKPLALYVFSNNK---KVINKILSNtSSGG 381
|
330 340
....*....|....*....|....
gi 2006071571 482 FYINDKPTGAVVGMQPFGGARASG 505
Cdd:cd07132 382 VCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
178-473 |
5.48e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 83.99 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 178 PLEGFVYAITPFNFTAIAANLPASAAMMGNV-VVWKPSDSQVFSAKIIVDVFKEAGV-PDGVINVVFGDALMITDTVlas 255
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 256 RDFAGIHFTGSthvfkdiwAKIGANInnyKTYPRIVG-------ETGGKDFIIAHPSAN---------VKQVVTGITRGA 319
Cdd:PRK11903 224 QPFDVVSFTGS--------AETAAVL---RSHPAVVQrsvrvnvEADSLNSALLGPDAApgseafdlfVKEVVREMTVKS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 320 fefqGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPED----FGNFITAVIHEGSFDKLASYIDQAKKDADAEIIV 395
Cdd:PRK11903 293 ----GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNdgvrMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 396 GGNYDKSVGYFIEPTVIVTTNPKYTTM--ETELFGPVITLYVYEDAkwEETLELVdTTSEYALTGAVFSQD-----RYAI 468
Cdd:PRK11903 369 LVDADPAVAACVGPTLLGASDPDAATAvhDVEVFGPVATLLPYRDA--AHALALA-RRGQGSLVASVYSDDaaflaAAAL 445
|
....*
gi 2006071571 469 EVATT 473
Cdd:PRK11903 446 ELADS 450
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
171-506 |
1.27e-12 |
|
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: 69.75 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 171 WNRVEYRPLeGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDSQVFSAKIIVDVFKEAgVPDGVINVVFGDALMIT 249
Cdd:cd07137 94 KAEIVSEPL-GVVLVISAWNFPFLLSLEPVIGAIaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 250 dtVLASRDFAGIHFTGSTHVFKDIWAKIGANINnyktyPrIVGETGGKDFIIAHPSANVKQVVTGITRGAFEF-QGQKCS 328
Cdd:cd07137 172 --ALLEQKWDKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 329 AASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDFGNfITAVIHEGSFDKLASYIDQAKkdADAEIIVGGNYDKSvGYFIE 408
Cdd:cd07137 244 APDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQRLSRLLDDPS--VADKIVHGGERDEK-NLYIE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 409 PTVIVTTNPKYTTMETELFGP---VITLyvyedAKWEETLELVDTTSEyALTGAVFSQDRyAIE---VATTklqnAAGNF 482
Cdd:cd07137 320 PTILLDPPLDSSIMTEEIFGPllpIITV-----KKIEESIEIINSRPK-PLAAYVFTKNK-ELKrriVAET----SSGGV 388
|
330 340
....*....|....*....|....
gi 2006071571 483 YINDKPTGAVVGMQPFGGARASGT 506
Cdd:cd07137 389 TFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
178-505 |
7.34e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 64.30 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 178 PLeGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDSQVFSAKIIVDVFKEAGVPDgVINVVFGdalMITDT-VLAS 255
Cdd:PLN02174 112 PL-GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEG---AVTETtALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 256 RDFAGIHFTGSTHVFKDIWAKIGaninnyKTYPRIVGETGGKDFIIAHPSANVKQVVTGITRGAFEFQ-GQKCSAASRAY 334
Cdd:PLN02174 187 QKWDKIFYTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNnGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 335 IPQSLWPAVKEQLIADVKSMKMGSPEDFGNfITAVIHEGSFDKLASYIDQakKDADAEIIVGGNYDKSvGYFIEPTVIVT 414
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPMESKD-MSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGEKDRE-NLKIAPTILLD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 415 TNPKYTTMETELFGPVITLYVYEDAkwEETLELVDTTSEyALTGAVFSQDRYAIEVATTKLqnAAGNFYINDKPTGAVVG 494
Cdd:PLN02174 337 VPLDSLIMSEEIFGPLLPILTLNNL--EESFDVIRSRPK-PLAAYLFTHNKKLKERFAATV--SAGGIVVNDIAVHLALH 411
|
330
....*....|.
gi 2006071571 495 MQPFGGARASG 505
Cdd:PLN02174 412 TLPFGGVGESG 422
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
176-464 |
1.03e-07 |
|
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: 54.42 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 176 YRPLEGFVYAITPFNFtaiAANLPASAAM----MGNVVVWKpSDSQV-FSAKIIVDVFKEAGVPDGVINVVFGDALMITD 250
Cdd:cd07126 139 YRWPYGPVAIITPFNF---PLEIPALQLMgalfMGNKPLLK-VDSKVsVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 251 TVLASrDFAGIHFTGSTHVfkdiwAKIGANInnykTYPRIVGETGGKDFIIAHPS-ANVKQVVTGITRGAFEFQGQKCSA 329
Cdd:cd07126 215 ILLEA-NPRMTLFTGSSKV-----AERLALE----LHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 330 ASRAYIPQSlWpaVKEQLIADVKSmkMGSPEDFGNFITAVIHEGSFDKLASYIDQAKKDADAEIIVGG----NYDKSVGY 405
Cdd:cd07126 285 QSILFAHEN-W--VQAGILDKLKA--LAEQRKLEDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGkpltNHSIPSIY 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006071571 406 -FIEPTVI------VTTNPKYTTMETELFGPVITLYVYEDAKWEETLELVDTTsEYALTGAVFSQD 464
Cdd:cd07126 360 gAYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERM-HAHLTAAVVSND 424
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
173-505 |
1.88e-06 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 50.50 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 173 RVEYRPLeGFVYAITPFNFTAIAANLPASAAM-MGNVVVWKPSDSQVFSAKIIVDVF------KEAGVPDGVINVvfGDA 245
Cdd:PLN02203 103 EVVPEPL-GVVLIFSSWNFPIGLSLEPLIGAIaAGNAVVLKPSELAPATSAFLAANIpkyldsKAVKVIEGGPAV--GEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 246 LMitdtvlaSRDFAGIHFTGSTHVFKDIWAKIGaninnyKTYPRIVGETGGK-DFIIAHPSA--NVKQVVTGITRGAF-E 321
Cdd:PLN02203 180 LL-------QHKWDKIFFTGSPRVGRIIMTAAA------KHLTPVALELGGKcPCIVDSLSSsrDTKVAVNRIVGGKWgS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 322 FQGQKCSAASRAYIPQSLWPAVKEQLIADVKSMKMGSPEDfGNFITAVIHEGSFDKLASYIDQakKDADAEIIVGGNYDK 401
Cdd:PLN02203 247 CAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRE-SKSMARILNKKHFQRLSNLLKD--PRVAASIVHGGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006071571 402 SvGYFIEPTVIVTTNPKYTTMETELFG---PVITLyvyedAKWEETLELVDTTSE----YALTGAVFSQDRYAIEVATtk 474
Cdd:PLN02203 324 K-KLFIEPTILLNPPLDSDIMTEEIFGpllPIITV-----KKIEDSIAFINSKPKplaiYAFTNNEKLKRRILSETSS-- 395
|
330 340 350
....*....|....*....|....*....|.
gi 2006071571 475 lqnaaGNFYINDKPTGAVVGMQPFGGARASG 505
Cdd:PLN02203 396 -----GSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| |
