|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
13-532 |
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: 853.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 13 NEPCPSYEKGSSDRAAIMKAYGELvSSLPVNVPLEHISKGVDTKSIQ-QVNPANHKQVVAEYIPSTRFDVQNAIESALQA 91
Cdd:cd07123 3 NEPVLSYAPGSPERAKLQEALAEL-KSLTVEIPLVIGGKEVRTGNTGkQVMPHDHAHVLATYHYADAALVEKAIEAALEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 92 KSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMVGQGKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPSGM 171
Cdd:cd07123 82 RKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 172 WNRLEYRPLEGFVYAISPFNFTALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITS 251
Cdd:cd07123 162 WNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 252 TVLENRAFAGLNFTGSSAVFKQLIARIGQATgeDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCS 331
Cdd:cd07123 242 TVLASPHLAGLHFTGSTPTFKSLWKQIGENL--DRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 332 AASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKETGYFVH 411
Cdd:cd07123 320 AASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 412 PTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAEITQVIDSTAPYALTGSIFARDAAAIRYAEDKLRNSAGNFYINTKS 491
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 630034702 492 TGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAIKEDF 532
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
13-543 |
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: 723.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 13 NEPCPSYEKGSSDRAAIMKAYGELVSSlPVNVPL----EHISKgvDTKSIQQVNPANHKQVVAEYIPSTRFDVQNAIESA 88
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSS-SLEIPLviggEEVYD--SNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 89 LQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMVGQGKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNP 168
Cdd:TIGR01236 79 LDAKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 169 sGMWNRLEYRPLEGFVYAISPFNFTALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEA 248
Cdd:TIGR01236 159 -GEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 249 ITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatGEDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQ 328
Cdd:TIGR01236 238 VSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQ--NLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 329 KCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTD-SQLTLLCGGKTSKETG 407
Cdd:TIGR01236 316 KCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDpEALTILYGGKYDDSQG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 408 YFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAEITQVIDSTAPYALTGSIFARDAAAIRYAEDKLRNSAGNFYI 487
Cdd:TIGR01236 396 YFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYI 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 488 NTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAIKEDFEGTPDFRYPSN 543
Cdd:TIGR01236 476 NDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYM 531
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
26-532 |
8.07e-153 |
|
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: 447.03 E-value: 8.07e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 26 RAAIMKAYGELVSSLPVNVPLEHISKGVDTKSIQ-QVNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRA 104
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMvSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 105 AIFLRAAGLVAGKYRHALMAATMVGqGKNiWQAEIDAAAETCDLLRFNVQCAMDLFKQQP-AVNPSGMWNRLEYRPLeGF 183
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKN-WVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 184 VYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGL 262
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 263 NFTGSSAVFKQLIARIGQAtgEDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESI 342
Cdd:cd07083 238 NFTGSLETGKKIYEAAARL--APGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 343 WPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKtdSQLTLLCGGKTSKETGYFVHPTIYQTSDAHH 422
Cdd:cd07083 316 YEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGK--NEGQLVLGGKRLEGEGYFVAPTVVEEVPPKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 423 EILQKEFFGPLLAVYVYPDSEWAEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLrnSAGNFYINTKSTGSVVGQQPFG 502
Cdd:cd07083 394 RIAQEEIFGPVLSVIRYKDDDFAEALEVANST-PYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFG 470
|
490 500 510
....*....|....*....|....*....|
gi 630034702 503 GMRGSGTNDKVGSVNVLSRFTSVRAIKEDF 532
Cdd:cd07083 471 GFKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
61-532 |
2.12e-138 |
|
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: 409.13 E-value: 2.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQA--E 138
Cdd:COG1012 26 INPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE-ERREELAALLTLETGKPLAEArgE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 IDAAAETcdlLRFNVQCAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPSPS 217
Cdd:COG1012 104 VDRAADF---LRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAWKLAPaLAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 218 AFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPRIVGET 297
Cdd:COG1012 180 TPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE--------NLKRVTLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 298 GGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQS 377
Cdd:COG1012 252 GGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 378 FDKLAAVIERAKTDSqLTLLCGGKT-SKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaP 456
Cdd:COG1012 332 LERVLAYIEDAVAEG-AELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA-IALANDT--E 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 457 YALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGsVVGQQPFGGMRGSGTNDKvGSVNVLSRFTSVRAIKEDF 532
Cdd:COG1012 408 YGLAASVFTRDLARARRVARRLE--AGMVWINDGTTG-AVPQAPFGGVKQSGIGRE-GGREGLEEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-532 |
5.68e-130 |
|
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: 388.89 E-value: 5.68e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 11 FQNEPCPSYEKgSSDRAAIMKAYGELVSSLPVNVPLEHISKGVDTKS-IQQVNPANHKQVVAEYIPSTRFDVQNAIESAL 89
Cdd:cd07124 1 FRNEPFTDFAD-EENRAAFRAALARVREELGREYPLVIGGKEVRTEEkIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 90 QAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALmAATMVGQ-GKNiWqAEIDA-AAETCDLLRFNVQCAMDLfKQQPAVN 167
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLRRR-RFEL-AAWMVLEvGKN-W-AEADAdVAEAIDFLEYYAREMLRL-RGFPVEM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 168 PSGMWNRLEYRPLeGFVYAISPFNF-TALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDA 246
Cdd:cd07124 155 VPGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 247 EAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQATGEDKFLNfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQ 326
Cdd:cd07124 234 EEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLK--RVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 327 GQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKET 406
Cdd:cd07124 312 GQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 407 GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDseWAEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGNFY 486
Cdd:cd07124 392 GYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDT-EYGLTGGVFSRSPEHLERARREFE--VGNLY 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 630034702 487 INTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAIKEDF 532
Cdd:cd07124 467 ANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
54-528 |
3.41e-120 |
|
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: 361.85 E-value: 3.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKN 133
Cdd:pfam00171 5 ESETIEVINPATGE-VIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE-ERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQAEIDAAaETCDLLRFNVQCAMDLfKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVW 212
Cdd:pfam00171 83 LAEARGEVD-RAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPL-GVVGAITPWNFPLLLPAWKIAPaLAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPR 292
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ--------NLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKTDSqLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVID 452
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEG-AKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEA-IEIAND 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 453 StaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGqQPFGGMRGSGTNDKVGSvNVLSRFTSVRAI 528
Cdd:pfam00171 390 T--EYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGREGGP-YGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-528 |
1.38e-112 |
|
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: 341.50 E-value: 1.38e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 82 QNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIWQAEIDAAaETCDLLRFNVQCAMDLFK 161
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEVA-RAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 162 QQPAVNPSGMWNRLEYRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQ 240
Cdd:cd07078 79 EVIPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 241 FVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIR 320
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE--------NLKRVTLELGGKSPLIVFDDADLDAAVKGAVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 321 SAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGG 400
Cdd:cd07078 230 GAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGA-KLLCGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 401 KTSK-ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLR 479
Cdd:cd07078 309 KRLEgGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEE--EAIELANDT-EYGLAAGVFTRDLERALRVAERLE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 630034702 480 nsAGNFYINTKSTGsVVGQQPFGGMRGSGTNdKVGSVNVLSRFTSVRAI 528
Cdd:cd07078 386 --AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-532 |
4.37e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 335.37 E-value: 4.37e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 11 FQNEPCPSY---EKGSSDRAAIMKAYGELVSSLPVNVPLEHISKgvdTKSIQQVNPANHKQVVAEYIPSTRFDVQNAIES 87
Cdd:PRK03137 5 YKHEPFTDFsveENVEAFEEALKKVEKELGQDYPLIIGGERITT---EDKIVSINPANKSEVVGRVSKATKELAEKAMQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 88 ALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKNiWqAEIDA-AAETCDLLRFNVQCAMDLFKQQPA 165
Cdd:PRK03137 82 ALEAFETWKKWSPEDRARILLRAAAII--RRRKHEFSAWLVKEaGKP-W-AEADAdTAEAIDFLEYYARQMLKLADGKPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 166 VNPSGMWNRLEYRPLeGFVYAISPFNF-TALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAG 244
Cdd:PRK03137 158 ESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 245 DAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQATGEDKFLNfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFE 324
Cdd:PRK03137 237 SGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLK--RVIAEMGGKDAIVVDEDADLDLAAESIVASAFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 325 YQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTnFVNPVIHEQSFDKLAAVIERAKTDSQltLLCGGKTSK 404
Cdd:PRK03137 315 FSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGR--LVLGGEGDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 405 ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDseWAEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGN 484
Cdd:PRK03137 392 SKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANNT-EYGLTGAVISNNREHLEKARREFH--VGN 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 630034702 485 FYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAIKEDF 532
Cdd:PRK03137 467 LYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
61-528 |
5.86e-100 |
|
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: 311.82 E-value: 5.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQAeID 140
Cdd:cd07125 51 IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLE-ANRGELIALAAAEAGKTLADA-DA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNF---TALGATLAcgPLLMGNVVVWKPSPS 217
Cdd:cd07125 129 EVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGR-GVFVCISPWNFplaIFTGQIAA--ALAAGNTVIAKPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 218 AFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQ----LIARIGQatgedkflnFPRI 293
Cdd:cd07125 206 TPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLinraLAERDGP---------ILPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 294 VGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI 373
Cdd:cd07125 277 IAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 374 HEQSFDKLAAVIERAKTDSqlTLLCGGKTSKETGYFVHPTIYqtsdahhEI-----LQKEFFGPLLAVYVYPDSEWAEIT 448
Cdd:cd07125 357 DKPAGKLLRAHTELMRGEA--WLIAPAPLDDGNGYFVAPGII-------EIvgifdLTTEVFGPILHVIRFKAEDLDEAI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 449 QVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAI 528
Cdd:cd07125 428 EDINAT-GYGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTV 504
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
11-532 |
9.42e-97 |
|
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: 303.33 E-value: 9.42e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 11 FQNEPCPSYEKgSSDRAAIMKAYGELVSSLPVNVPLEHISKGVDTKS-IQQVNPANHKQVVAEYIPSTRFDVQNAIESAL 89
Cdd:TIGR01237 1 YKHEPFTDFAD-EENRQAFFKALATVKEQLGKTYPLVINGERVETENkIVSINPCDKSEVVGTVSKASQEHAEHALQAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 90 QAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIWQAEIDAAaETCDLLRFNVQCAMDLFKQQPAVNPS 169
Cdd:TIGR01237 80 KAFEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVNSRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 170 GMWNRLEYRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEA 248
Cdd:TIGR01237 158 GETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 249 ITSTVLENRAFAGLNFTGSSAVFKQLIARIGQATGEDKFLNfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQ 328
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLK--RVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 329 KCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLlcGGKTSKETGY 408
Cdd:TIGR01237 315 KCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVS--GGCGDDSKGY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 409 FVHPTIYQTSDAHHEILQKEFFGPLLAvyVYPDSEWAEITQVIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYIN 488
Cdd:TIGR01237 393 FIGPTIFADVDRKARLAQEEIFGPVVA--FIRASDFDEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYFN 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 630034702 489 TKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAIKEDF 532
Cdd:TIGR01237 468 RNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
86-528 |
1.86e-80 |
|
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: 256.39 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 86 ESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMVGqGKNIWQAEIDAAaETCDLLRFNVQCAMDLFKQQPA 165
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLET-GKPIEEALGEVA-RAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 166 VNPSGMWNRLEYRPLeGFVYAISPFNF-TALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAG 244
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 245 DAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFE 324
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGK----AIMKAAAE----NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 325 YQGQKCSAASRLYVPESIWPAFKEnllaKMATIKVGSPEDvtnfvnpviheqsfdklaavieraktdsqltllcggktsk 404
Cdd:cd06534 230 NAGQICTAASRLLVHESIYDEFVE----KLVTVLVDVDPD---------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 405 etgyfvhptiyqtsdahHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGN 484
Cdd:cd06534 266 -----------------MPIAQEEIFGPVLPVIRFKDEE--EAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGT 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 630034702 485 FYINTKSTGsVVGQQPFGGMRGSGTNDKVGSVnVLSRFTSVRAI 528
Cdd:cd06534 324 VYINDSSIG-VGPEAPFGGVKNSGIGREGGPY-GLEEYTRTKTV 365
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
61-508 |
2.24e-74 |
|
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: 243.70 E-value: 2.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAA-GLVAGKYRHALMAATMVGQGKNIWQAEI 139
Cdd:cd07097 19 RNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGdELEARKEELARLLTREEGKTLPEARGEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 140 DAAAetcDLLRFNVQCAMDLF-KQQPAVNP-SGMWNRLEyrPLeGFVYAISPFNF-TALGATLACGPLLMGNVVVWKPSP 216
Cdd:cd07097 99 TRAG---QIFRYYAGEALRLSgETLPSTRPgVEVETTRE--PL-GVVGLITPWNFpIAIPAWKIAPALAYGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 217 SAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRIVGE 296
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGR----RIAAAAAA----RGARVQLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 297 TGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQ 376
Cdd:cd07097 245 MGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 377 SFDKLAAVIERAKTDSQlTLLCGGK--TSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDST 454
Cdd:cd07097 325 QLEKDLRYIEIARSEGA-KLVYGGErlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYD--EALAIANDT 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 455 aPYALTGSIFARDaaaIRYAEDKLRNS-AGNFYINTKSTGsVVGQQPFGGMRGSG 508
Cdd:cd07097 402 -EFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSS 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
55-532 |
6.90e-73 |
|
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: 239.94 E-value: 6.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 55 TKSIQQVNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKN 133
Cdd:cd07131 13 GETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELL--KKRKEELARLVTREmGKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQAEIDAAaETCDLLRFNVQCAMDLFKQqpaVNPSGMWNRLEY---RPLeGFVYAISPFNF-TALGATLACGPLLMGNV 209
Cdd:cd07131 91 LAEGRGDVQ-EAIDMAQYAAGEGRRLFGE---TVPSELPNKDAMtrrQPI-GVVALITPWNFpVAIPSWKIFPALVCGNT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 210 VVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflN 289
Cdd:cd07131 166 VVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGE----RIGETCAR----P 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 FPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFV 369
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 370 NPVIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSK----ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwa 445
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGK-EEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 446 EITQVIDSTaPYALTGSIFARDAAAIRYAEDKLrnSAGNFYINTKSTGSVVgQQPFGGMRGSGTNDKVGSVNVLSRFTSV 525
Cdd:cd07131 395 EAIEIANDT-EYGLSSAIYTEDVNKAFRARRDL--EAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTEW 470
|
....*..
gi 630034702 526 RAIKEDF 532
Cdd:cd07131 471 KAVYVDY 477
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
61-528 |
1.11e-72 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 250.50 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIwqaeID 140
Cdd:PRK11904 567 VSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE-ANRAELIALCVREAGKTL----QD 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAA---ETCDLLRFNVQCAMDLFKQ-QPAVNPSGMWNRLEYRPLEGFVyAISPFNFTalgatLA--CGP----LLMGNVV 210
Cdd:PRK11904 642 AIAevrEAVDFCRYYAAQARRLFGApEKLPGPTGESNELRLHGRGVFV-CISPWNFP-----LAifLGQvaaaLAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIAR-IGQATGEdkfln 289
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTET-ARIINRtLAARDGP----- 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 fprIV---GETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVT 366
Cdd:PRK11904 790 ---IVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLS 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 367 NFVNPVIHEQSFDKLAAVIERAKTDSqlTLLCGGKTSKET--GYFVHPTIYQTSDAhhEILQKEFFGPLLAVYVYPDSEW 444
Cdd:PRK11904 867 TDVGPVIDAEAKANLDAHIERMKREA--RLLAQLPLPAGTenGHFVAPTAFEIDSI--SQLEREVFGPILHVIRYKASDL 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 445 AEITQVIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTS 524
Cdd:PRK11904 943 DKVIDAINATG-YGLTLGIHSRIEETADRIADRVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFAT 1019
|
....
gi 630034702 525 VRAI 528
Cdd:PRK11904 1020 EKTV 1023
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
80-528 |
1.22e-69 |
|
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: 230.11 E-value: 1.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 80 DVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLV---AGKYRHALMAATMVGQGKNIWqaEIDAAAETCDllrfnvQCA 156
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILeerRDEIADWLIRESGSTRPKAAF--EVGAAIAILR------EAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 157 MDLFKQQPAVNPS---GMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPSP-SAFHSSWLLYKIMIE 231
Cdd:cd07104 73 GLPRRPEGEILPSdvpGKESMVRRVPL-GVVGVISPFNFPLILAMRSVAPaLALGNAVVLKPDSrTPVTGGLLIAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 232 AGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRIVGETGGKNFHLVHKSADI 311
Cdd:cd07104 152 AGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGR----HIGELAGR----HLKKVALELGGNNPLIVLDDADL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 312 ENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTD 391
Cdd:cd07104 224 DLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 392 SqLTLLCGGktsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaPYALTGSIFARDAA-A 470
Cdd:cd07104 304 G-ARLLTGG---TYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEA-VELANDT--EYGLSAAVFTRDLErA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 471 IRYAEdKLRnsAGNFYIN--TKSTGSVVgqqPFGGMRGSGtndkVGSVN---VLSRFTSVRAI 528
Cdd:cd07104 377 MAFAE-RLE--TGMVHINdqTVNDEPHV---PFGGVKASG----GGRFGgpaSLEEFTEWQWI 429
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
61-528 |
4.55e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 238.30 E-value: 4.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWqaeiD 140
Cdd:COG4230 575 RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLE-AHRAELMALLVREAGKTLP----D 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETC---DLLRFNVQCAMDLFKqqpavnpsgmwNRLEYRPLeGFVYAISPFNFtalgaTLA--CGP----LLMGNVVV 211
Cdd:COG4230 650 AIAEVReavDFCRYYAAQARRLFA-----------APTVLRGR-GVFVCISPWNF-----PLAifTGQvaaaLAAGNTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 212 WKPSPS----AFHSSwllyKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIAR-IGQATGEDk 286
Cdd:COG4230 713 AKPAEQtpliAARAV----RLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTET-ARLINRtLAARDGPI- 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 287 flnfPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVT 366
Cdd:COG4230 787 ----VPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 367 NFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHeiLQKEFFGPLLAVYVYPDSewaE 446
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISD--LEREVFGPVLHVVRYKAD---E 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 447 ITQVID---STApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFT 523
Cdd:COG4230 938 LDKVIDainATG-YGLTLGVHSRIDETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFA 1014
|
....*
gi 630034702 524 SVRAI 528
Cdd:COG4230 1015 TERTV 1019
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
54-508 |
2.40e-67 |
|
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: 225.52 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANHKQVVAEYiPSTRFDVQNAIESALQAKSAWENTPFEDRAAIfLRAAGLVAGKYRHALmaATMVGQ--G 131
Cdd:cd07086 11 GGETFTSRNPANGEPIARVF-PASPEDVEAAVAAAREAFKEWRKVPAPRRGEI-VRQIGEALRKKKEAL--GRLVSLemG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 132 KNIWQA--EIDAAAETCDllrFNVQCAMDLFKQqpaVNPSGMWNR--LE-YRPLeGFVYAISPFNF-TALGATLACGPLL 205
Cdd:cd07086 87 KILPEGlgEVQEMIDICD---YAVGLSRMLYGL---TIPSERPGHrlMEqWNPL-GVVGVITAFNFpVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 206 MGNVVVWKPSPSAFHSSWLLYKIMIEA----GLPENVLQFVAGDAEaITSTVLENRAFAGLNFTGSSAVFKQliarIGQA 281
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRR----VGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 282 TGEdkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGS 361
Cdd:cd07086 235 VAR----RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 362 PEDVTNFVNPVIHEQSFDKLAAVIERAKTDSqLTLLCGGK--TSKETGYFVHPTIYqtSDAHH--EILQKEFFGPLLAVY 437
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQG-GTVLTGGKriDGGEPGNYVEPTIV--TGVTDdaRIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630034702 438 VYPDSEWAeITqvIDSTAPYALTGSIFARDAAAIRYAEDKLRNSAGNFYINTKSTGSVVGqQPFGGMRGSG 508
Cdd:cd07086 388 KFDSLEEA-IA--INNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
61-508 |
1.37e-65 |
|
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: 220.11 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPAnHKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAgkyRHA-LMAATMVGQGKNIW-- 135
Cdd:cd07114 2 INPA-TGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIE---ANAeELAELETRDNGKLIre 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 136 -QAEIDAAAETcdlLRFNVQCAMdlfKQQPAVNPSG---MWNRLEYRPLeGFVYAISPFNFTALGATLACGPLL-MGNVV 210
Cdd:cd07114 78 tRAQVRYLAEW---YRYYAGLAD---KIEGAVIPVDkgdYLNFTRREPL-GVVAAITPWNSPLLLLAKKLAPALaAGNTV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNF 290
Cdd:cd07114 151 VLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGR----HIARAAAE----NL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 291 PRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVN 370
Cdd:cd07114 223 APVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 371 PVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKET----GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAe 446
Cdd:cd07114 303 PLATERQLEKVERYVARAREEGA-RVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEA- 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 447 ITQVIDStaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKSTGSVVgqQPFGGMRGSG 508
Cdd:cd07114 381 IALANDS--EYGLAAGIWTRDLArAHRVAR-AIE--AGTVWVNTYRALSPS--SPFGGFKDSG 436
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
62-508 |
1.45e-64 |
|
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: 217.20 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 62 NPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLV---AGKYRHALMAATMVGQGKNIWQAE 138
Cdd:cd07150 5 NPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMerrADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 -----IDAAAETCDLLRFNVQcamdlfkQQPAVNPSGMWNRleyRPLeGFVYAISPFNFTALGAT-LACGPLLMGNVVVW 212
Cdd:cd07150 84 ftpelLRAAAGECRRVRGETL-------PSDSPGTVSMSVR---RPL-GVVAGITPFNYPLILATkKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPR 292
Cdd:cd07150 153 KPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR--------HLKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:cd07150 225 ITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKTDSQlTLLCGGktsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVID 452
Cdd:cd07150 305 ISPRQVERIKRQVEDAVAKGA-KLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAE--EALELAN 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 630034702 453 STApYALTGSIFARDAA-AIRYAEdklRNSAGNFYIN--TKSTGSVVgqqPFGGMRGSG 508
Cdd:cd07150 379 DTE-YGLSAAILTNDLQrAFKLAE---RLESGMVHINdpTILDEAHV---PFGGVKASG 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
27-524 |
1.87e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 227.83 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 27 AAIMKAYGELVSSLPVNVPLehISKGVDTKSIQQV-NPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAA 105
Cdd:PRK11905 539 AALDEALNAFAAKTWHAAPL--LAGGDVDGGTRPVlNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAA 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 106 IFLRAAGLVAgkyRHA--LMAATMVGQGKNIWQAeIDAAAETCDLLRFNVQCAMDLFKQQPAvnpsgmwnrleyRPLeGF 183
Cdd:PRK11905 617 ILERAADLME---AHMpeLFALAVREAGKTLANA-IAEVREAVDFLRYYAAQARRLLNGPGH------------KPL-GP 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 184 VYAISPFNFTalgatLA------CGPLLMGNVVVWKPSPS----AFHSswllYKIMIEAGLPENVLQFVAGDAEAITSTV 253
Cdd:PRK11905 680 VVCISPWNFP-----LAiftgqiAAALVAGNTVLAKPAEQtpliAARA----VRLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 254 LENRAFAGLNFTGSSAVF----KQLIARIGQATgedkflnfPRIvGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQK 329
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVArliqRTLAKRSGPPV--------PLI-AETGGQNAMIVDSSALPEQVVADVIASAFDSAGQR 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 330 CSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKETGYF 409
Cdd:PRK11905 822 CSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTF 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 410 VHPTIYQTSdaHHEILQKEFFGPLLAVYVYpdsEWAEITQVID---STApYALTGSIFARDAAAIRYAEDKLRnsAGNFY 486
Cdd:PRK11905 902 VAPTLIEID--SISDLEREVFGPVLHVVRF---KADELDRVIDdinATG-YGLTFGLHSRIDETIAHVTSRIR--AGNIY 973
|
490 500 510
....*....|....*....|....*....|....*...
gi 630034702 487 INTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTS 524
Cdd:PRK11905 974 VNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVR 1011
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
51-528 |
6.33e-63 |
|
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: 213.32 E-value: 6.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 51 KGVDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQ 130
Cdd:cd07151 5 DGTSERTIDVLNPYTGE-TLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQAEIDAAAETCDLLRfnvqcAMDL-FKQQPAVNPS---GMWNRLeYRPLEGFVYAISPFNFTALGATLACGPLL- 205
Cdd:cd07151 83 GSTRIKANIEWGAAMAITRE-----AATFpLRMEGRILPSdvpGKENRV-YREPLGVVGVISPWNFPLHLSMRSVAPALa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 206 MGNVVVWKP-SPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGE 284
Cdd:cd07151 157 LGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRH----IGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 285 dkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPED 364
Cdd:cd07151 233 ----HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 365 VTNFVNPVIHEQSFDKLAAVIERAKTDSqLTLLCGGKTskeTGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEw 444
Cdd:cd07151 309 PDTVVGPLINESQVDGLLDKIEQAVEEG-ATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 445 aEITQVIDSTaPYALTGSIFARDAA-AIRYAedkLRNSAGNFYINTKStgsvVGQQP---FGGMRGSGtndkVGSVN--- 517
Cdd:cd07151 384 -EALELANDT-EYGLSGAVFTSDLErGVQFA---RRIDAGMTHINDQP----VNDEPhvpFGGEKNSG----LGRFNgew 450
|
490
....*....|.
gi 630034702 518 VLSRFTSVRAI 528
Cdd:cd07151 451 ALEEFTTDKWI 461
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
61-509 |
3.71e-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: 210.88 E-value: 3.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQA--- 137
Cdd:cd07093 2 FNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE-ARADELALLESLDTGKPITLArtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 EIDAAAETcdlLRFNVqcamDLFKQQPAV---NPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWK 213
Cdd:cd07093 80 DIPRAAAN---FRFFA----DYILQLDGEsypQDGGALNYVLRQPV-GVAGLITPWNLPLMLLTWKIAPaLAFGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 214 PSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRI 293
Cdd:cd07093 152 PSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGR----TIMRAAAP----NLKPV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 294 VGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI 373
Cdd:cd07093 224 SLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 374 HEQSFDKLAAVIERAKTDSQlTLLCGGKTSK----ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYpDSEwAEITQ 449
Cdd:cd07093 304 SKEHLEKVLGYVELARAEGA-TILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPF-DDE-EEAIE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630034702 450 VIDSTaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSGT 509
Cdd:cd07093 381 LANDT-PYGLAAYVWTRDLGrAHRVAR-RLE--AGTVWVNCWLVRDL--RTPFGGVKASGI 435
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-508 |
9.35e-62 |
|
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: 209.60 E-value: 9.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALmAATMV-GQGKNIWQA-- 137
Cdd:cd07103 2 INPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR-ERAEDL-ARLLTlEQGKPLAEArg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 EIDAAAetcDLLRFNVQCAMDLFKQQ-PAVNPsGMWNRLEYRPLeGFVYAISPFNFTA------LGATLACGpllmgNVV 210
Cdd:cd07103 79 EVDYAA---SFLEWFAEEARRIYGRTiPSPAP-GKRILVIKQPV-GVVAAITPWNFPAamitrkIAPALAAG-----CTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIArigQATGEDKflnf 290
Cdd:cd07103 149 VLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMA---QAADTVK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 291 pRIVGETGGknfH---LVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSP--EDV 365
Cdd:cd07103 222 -RVSLELGG---NapfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGldEGT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 366 TnfVNPVIHEQSFDKLAAVIERAKTDsQLTLLCGGKTSKETGYFVHPTIyqTSDAHHE--ILQKEFFGPLLAVYVYpDSE 443
Cdd:cd07103 298 D--MGPLINERAVEKVEALVEDAVAK-GAKVLTGGKRLGLGGYFYEPTV--LTDVTDDmlIMNEETFGPVAPIIPF-DTE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 444 wAEITQVIDSTaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTksTGSVVGQQPFGGMRGSG 508
Cdd:cd07103 372 -DEVIARANDT-PYGLAAYVFTRDLArAWRVAE-ALE--AGMVGINT--GLISDAEAPFGGVKESG 430
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
61-526 |
4.24e-61 |
|
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: 209.38 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQAeID 140
Cdd:TIGR01238 56 TNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLFKQQPAvnpsgmwnrleyRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAF 219
Cdd:TIGR01238 134 EVREAVDFCRYYAKQVRDVLGEFSV------------ESR-GVFVCISPWNFPlAIFTGQISAALAAGNTVIAKPAEQTS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 220 HSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfkqliARIGQATGEDKFLNFPRIVGETGG 299
Cdd:TIGR01238 201 LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEV-----AQLINQTLAQREDAPVPLIAETGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 300 KNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFD 379
Cdd:TIGR01238 276 QNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 380 KLAAVIER----AKTDSQLTLlcGGKTSKETGYFVHPTIYQTSDAHHeiLQKEFFGPLLAVYVYPDSEWAEITQVIDSTA 455
Cdd:TIGR01238 356 NLLAHIEHmsqtQKKIAQLTL--DDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKARELDQIVDQINQTG 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630034702 456 pYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVR 526
Cdd:TIGR01238 432 -YGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
58-509 |
1.33e-60 |
|
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: 206.82 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 58 IQQVNPANHKqvVAEYIPS-TRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKNIW 135
Cdd:cd07145 1 IEVRNPANGE--VIDTVPSlSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELI--ERRKEELAKLLTIEvGKPIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 136 QA--EIDAAAETcdlLRFNVQCAMDLFKQQPAV-NPSGMWNRLEY---RPLeGFVYAISPFNFTA-LGATLACGPLLMGN 208
Cdd:cd07145 77 QSrvEVERTIRL---FKLAAEEAKVLRGETIPVdAYEYNERRIAFtvrEPI-GVVGAITPFNFPAnLFAHKIAPAIAVGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 209 VVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGqatgedkfL 288
Cdd:cd07145 153 SVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG--------G 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 289 NFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNF 368
Cdd:cd07145 225 TGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 369 VNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKtsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEIT 448
Cdd:cd07145 305 LGPLISPEAVERMENLVNDAVEKGG-KILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE--EAV 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 630034702 449 QVIDSTaPYALTGSIFARD-AAAIRYAeDKLRnsAGNFYINtKSTGSVVGQQPFGGMRGSGT 509
Cdd:cd07145 380 EIANST-EYGLQASVFTNDiNRALKVA-RELE--AGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
68-509 |
4.85e-60 |
|
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: 205.14 E-value: 4.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 68 QVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKNIWQA--EIDAAAE 144
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIALEaGKPIKDArkEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 145 TcdlLRFNVQCAMDLFKQQPAVNPS-GMWNRLEY---RPLeGFVYAISPFNFTAlgaTLAC---GPLLM-GNVVVWKPSP 216
Cdd:cd07149 88 T---LRLSAEEAKRLAGETIPFDASpGGEGRIGFtirEPI-GVVAAITPFNFPL---NLVAhkvGPAIAaGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 217 SAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGEDKflnfprIVGE 296
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEA----IARKAGLKK------VTLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 297 TGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQ 376
Cdd:cd07149 231 LGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 377 SFDKLAAVIERAKtDSQLTLLCGGktsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYpdsewAEITQVIDST-- 454
Cdd:cd07149 311 EAERIEEWVEEAV-EGGARLLTGG---KRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPF-----DTLDEAIAMAnd 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 455 APYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSvVGQQPFGGMRGSGT 509
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
62-508 |
5.27e-60 |
|
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: 205.23 E-value: 5.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 62 NPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIWQAEIDA 141
Cdd:cd07090 3 EPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 142 AAeTCDLLRFNVQCAMDLFKQQ-PAVNPSGMWNRLEyrPLeGFVYAISPFNFTALGATLACGPLLM-GNVVVWKPSPSAF 219
Cdd:cd07090 81 DS-SADCLEYYAGLAPTLSGEHvPLPGGSFAYTRRE--PL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 220 HSSWLLYKIMIEAGLPENVLQFVAGDAEAiTSTVLENRAFAGLNFTGSSAVFKQLIArigQATGEDKflnfpRIVGETGG 299
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMS---AAAKGIK-----HVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 300 KNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFD 379
Cdd:cd07090 228 KSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 380 KLAAVIERAKTDSQlTLLCGGKTSK-----ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYpDSEWAEITQVIDST 454
Cdd:cd07090 308 KVLGYIESAKQEGA-KVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF-DTEEEVIRRANDTT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 455 apYALTGSIFARD-AAAIRYAeDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSG 508
Cdd:cd07090 386 --YGLAAGVFTRDlQRAHRVI-AQLQ--AGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
63-508 |
1.33e-59 |
|
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: 204.11 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 63 PAnHKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIWQA--E 138
Cdd:cd07118 4 PA-HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 IDAAAetcDLLRFNVQCAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFT----------ALGAtlacgpllmGN 208
Cdd:cd07118 82 IEGAA---DLWRYAASLARTLHGDSYNNLGDDMLGLVLREPI-GVVGIITPWNFPflilsqklpfALAA---------GC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 209 VVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkfl 288
Cdd:cd07118 149 TVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 289 NFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNF 368
Cdd:cd07118 221 NLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 369 VNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGK-TSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEI 447
Cdd:cd07118 301 VGAIINEAQLAKITDYVDAGRAEGA-TLLLGGErLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD--EA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630034702 448 TQVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSG 508
Cdd:cd07118 378 IALANDT-VYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
54-488 |
2.02e-59 |
|
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: 204.04 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKN 133
Cdd:cd07088 11 SGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR-ENADELAKLIVEEQGKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQAEIDAAAeTCDLLRFNVQCAMdlfKQQPAVNPSGMWNR---LEYRPLeGFVYAISPFNFTALGATLACGPLLM-GNV 209
Cdd:cd07088 89 LSLARVEVEF-TADYIDYMAEWAR---RIEGEIIPSDRPNEnifIFKVPI-GVVAGILPWNFPFFLIARKLAPALVtGNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 210 VVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflN 289
Cdd:cd07088 164 IVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE--------N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 FPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFV 369
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 370 NPVIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSK-ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeIT 448
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAV-EAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA-IE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 630034702 449 QVIDSTapYALTGSIFARDAAAIRYAEDKLRnsAGNFYIN 488
Cdd:cd07088 394 LANDSE--YGLTSYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
61-508 |
4.04e-59 |
|
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: 202.76 E-value: 4.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPAnHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgkyRHALMAATMVG--QGKNIWQA- 137
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIE---ANAEELARLLTleQGKPLAEAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 -EIDAAAEtcdllRFNVQCAMDLfKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPS 215
Cdd:cd07106 78 fEVGGAVA-----WLRYTASLDL-PDEVIEDDDTRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPaLLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 216 PSAFHSSWLLYKIMIEAgLPENVLQFVAGDAE---AITStvleNRAFAGLNFTGSSAVFKQLIArigQATGEDKflnfpR 292
Cdd:cd07106 151 PFTPLCTLKLGELAQEV-LPPGVLNVVSGGDElgpALTS----HPDIRKISFTGSTATGKKVMA---SAAKTLK-----R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:cd07106 218 VTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVID 452
Cdd:cd07106 298 QNKMQYDKVKELVEDAK-AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEV-IARAND 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 453 StaPYALTGSIFARD-AAAIRYAEdklRNSAGNFYINTKstGSVVGQQPFGGMRGSG 508
Cdd:cd07106 376 S--EYGLGASVWSSDlERAEAVAR---RLEAGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
52-515 |
7.15e-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: 202.67 E-value: 7.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 52 GVDTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA-KSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQ 130
Cdd:cd07113 11 GQSEKRLDITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEELAQLETLCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPSGM-------WNRLEyrPLeGFVYAISPFNFTALGATLACGP 203
Cdd:cd07113 89 GKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMqgerytaFTRRE--PV-GVVAGIVPWNFSVMIAVWKIGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 204 -LLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaITSTVLENRAFAGLNFTGSSAVfkqliariGQAT 282
Cdd:cd07113 166 aLATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVAT--------GKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 283 GEDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSP 362
Cdd:cd07113 237 GRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 363 EDVTNFVNPVIHEQSFDKLAAVIERAKTDsQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDS 442
Cdd:cd07113 317 MDESVMFGPLANQPHFDKVCSYLDDARAE-GDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 443 EwaEITQVIDSTaPYALTGSIFARD-AAAIRYAEdklRNSAGNFYINTKS--TGSVvgqqPFGGMRGSGTNDKVGS 515
Cdd:cd07113 396 E--ELIQLINDT-PFGLTASVWTNNlSKALRYIP---RIEAGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS 461
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
68-508 |
1.14e-58 |
|
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: 201.51 E-value: 1.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 68 QVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKNIWQA--EIDAAAE 144
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLL--KKRAEEFAKIIACEgGKPIKDArvEVDRAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 145 TCDLL------RFNVQCAMDLfkQQPAVNPSGmWNRLEyrPLeGFVYAISPFNFTALGATLACGPLL-MGNVVVWKPSPS 217
Cdd:cd07094 88 TLRLAaeeaerIRGEEIPLDA--TQGSDNRLA-WTIRE--PV-GVVLAITPFNFPLNLVAHKLAPAIaTGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 218 AFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGqatgedkflnFPRIVGET 297
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG----------GKRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 298 GGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQS 377
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 378 FDKLAAVIERAKTDSQlTLLCGGKTSKETgyfVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPY 457
Cdd:cd07094 312 AERVERWVEEAVEAGA-RLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFE--EAIRIANST-DY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 630034702 458 ALTGSIFARDAAAIRYAEDKLRnsAGNFYINtKSTGSVVGQQPFGGMRGSG 508
Cdd:cd07094 385 GLQAGIFTRDLNVAFKAAEKLE--VGGVMVN-DSSAFRTDWMPFGGVKESG 432
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
76-530 |
1.71e-58 |
|
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: 201.38 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 76 STRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQA--EIDAAAETCdllRFNV 153
Cdd:cd07101 15 STPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEVLDVAIVA---RYYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 154 QCAMDLFKQQPA--VNPSGMWNRLEYRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKP-SPSAFHSSWLLyKIM 229
Cdd:cd07101 91 RRAERLLKPRRRrgAIPVLTRTTVNRRPK-GVVGVISPWNYPlTLAVSDAIPALLAGNAVVLKPdSQTALTALWAV-ELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 230 IEAGLPENVLQFVAGDAEAITSTVLENRAFagLNFTGSSAVFKqliaRIGQATGEdkflnfpRIVG---ETGGKNFHLVH 306
Cdd:cd07101 169 IEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGR----VVAERAGR-------RLIGcslELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 307 KSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIE 386
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 387 RAKTdSQLTLLCGGKTSKETG-YFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaPYALTGSIFA 465
Cdd:cd07101 316 DAVA-KGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEA-IELANDT--DYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 630034702 466 RDAAAIRYAEDKLRnsAGNFYIN---TKSTGSVvgQQPFGGMRGSGTNDKVGSVNVLsRFTSVRAIKE 530
Cdd:cd07101 392 RDGARGRRIAARLR--AGTVNVNegyAAAWASI--DAPMGGMKDSGLGRRHGAEGLL-KYTETQTVAV 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-528 |
3.55e-58 |
|
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: 200.36 E-value: 3.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQAEID 140
Cdd:cd07115 2 LNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLFKQQPAVNPSGMwNRLEYRPLeGFVYAISPFNFTALGATLACGPLL-MGNVVVWKPSPSAF 219
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFL-NYTVREPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 220 HSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRIVGETGG 299
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGR----KIMQGAAG----NLKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 300 KNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFD 379
Cdd:cd07115 230 KSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 380 KLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTApYAL 459
Cdd:cd07115 310 RVLDYVDVGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE--EALRIANGTE-YGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 460 TGSIFARDAA-AIRYAEdklRNSAGNFYINTksTGSVVGQQPFGGMRGSGTNDKVGSVnVLSRFTSVRAI 528
Cdd:cd07115 386 AAGVWTRDLGrAHRVAA---ALKAGTVWINT--YNRFDPGSPFGGYKQSGFGREMGRE-ALDEYTEVKSV 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
61-536 |
1.35e-55 |
|
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: 194.07 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAgkyRHALMAATM--VGQGKNIWQ 136
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR---EDAEELARLetLNTGKTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 137 AEIDAA-AETCdlLRFNVQCAMDLFKQQPAVNPSgMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKP 214
Cdd:cd07119 94 SEIDIDdVANC--FRYYAGLATKETGEVYDVPPH-VISRTVREPV-GVCGLITPWNYPLLQAAWKLAPaLAAGNTVVIKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 215 SPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIARigQATGedkflNFPRIV 294
Cdd:cd07119 170 SEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT-GRSIMR--AAAG-----NVKKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 295 GETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIH 374
Cdd:cd07119 242 LELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 375 EQSFDKLAAVIERAKTDSQlTLLCGGKTSKE----TGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQV 450
Cdd:cd07119 322 AEHREKVLSYIQLGKEEGA-RLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE--EAIRL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 451 IDSTaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINtkSTGSVVGQQPFGGMRGSGTNDKVGSVNvLSRFTSVRAIK 529
Cdd:cd07119 399 ANDT-PYGLAGAVWTKDIArANRVAR-RLR--AGTVWIN--DYHPYFAEAPWGGYKQSGIGRELGPTG-LEEYQETKHIN 471
|
....*..
gi 630034702 530 EDFEGTP 536
Cdd:cd07119 472 INLSPQP 478
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
81-508 |
1.67e-54 |
|
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: 189.98 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 81 VQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRH--ALMAATMvgqGKNIWQA--EIDAAAETCdllRFNVQCA 156
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDElaRLITLEM---GKPIAEAraEVEKCAWIC---RYYAENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 157 MDLFKQQPaVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGPLLM-GNVVVWKPSPSAFHSSWLLYKIMIEAGLP 235
Cdd:cd07100 75 EAFLADEP-IETDAGKAYVRYEPL-GVVLGIMPWNFPFWQVFRFAAPNLMaGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 236 ENVLQFVAGDAEAItSTVLENRAFAGLNFTGSSavfkqliaRIGQATGEDKFLNFPRIVGETGGKNFHLVHKSADIENAV 315
Cdd:cd07100 153 EGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSE--------RAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 316 NCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKtDSQLT 395
Cdd:cd07100 224 KTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAV-AAGAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 396 LLCGGKTSKETGYFVHPTIY----QTSDAHHEilqkEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAAAI 471
Cdd:cd07100 303 LLLGGKRPDGPGAFYPPTVLtdvtPGMPAYDE----ELFGPVAAVIKVKDEE--EAIALANDS-PFGLGGSVFTTDLERA 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 630034702 472 RYAEDKLRnsAGNFYIN--TKSTGSVvgqqPFGGMRGSG 508
Cdd:cd07100 376 ERVARRLE--AGMVFINgmVKSDPRL----PFGGVKRSG 408
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
61-528 |
2.25e-54 |
|
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: 190.12 E-value: 2.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKniwqAEID 140
Cdd:cd07099 1 RNPAT-GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAETGK----PRAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAE---TCDLLRFNVQCAMDLFKQQPAVNPSGMWN---RLEYRPLeGFVYAISPFNF---TALGATLACgpLLMGNVVV 211
Cdd:cd07099 75 AGLEvllALEAIDWAARNAPRVLAPRKVPTGLLMPNkkaTVEYRPY-GVVGVISPWNYpllTPMGDIIPA--LAAGNAVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 212 WKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaiTSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFP 291
Cdd:cd07099 152 LKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA--TGAALIDAGVDKVAFTGSVATGRKVMAAAAE--------RLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 292 RIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNP 371
Cdd:cd07099 222 PVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 372 VIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKETGYFVHPTIYqtSDAHHE--ILQKEFFGPLLAVYVYPDSEWAeITQ 449
Cdd:cd07099 302 MTTARQLDIVRRHVDDAV-AKGAKALTGGARSNGGGPFYEPTVL--TDVPHDmdVMREETFGPVLPVMPVADEDEA-IAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 450 VIDStaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNdKVGSVNVLSRFTSVRAI 528
Cdd:cd07099 378 ANDS--RYGLSASVFSRDLArAEAIAR-RLE--AGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAI 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-528 |
2.60e-54 |
|
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: 189.33 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 80 DVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMvgqgkniwqAEIDAAAETCDllrFNVQCAMDL 159
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLE-SRRDEFIEAMM---------EETGATAAWAG---FNVDLAAGM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 160 FKQQ------------PAVNP--SGMWNRleyRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWL 224
Cdd:cd07105 68 LREAaslitqiiggsiPSDKPgtLAMVVK---EPV-GVVLGIAPWNAPvILGTRAIAYPLAAGNTVVLKASELSPRTHWL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 225 LYKIMIEAGLPENVLQFV---AGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGEdkflNFPRIVGETGGKN 301
Cdd:cd07105 144 IGRVFHEAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRI----IAETAAK----HLKPVLLELGGKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 302 FHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEdvtnfVNPVIHEQSFDKL 381
Cdd:cd07105 216 PAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 382 AAVIERAkTDSQLTLLCGGKTSKE-TGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTApYALT 460
Cdd:cd07105 291 KELVDDA-LSKGAKLVVGGLADESpSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEE--EAVRIANDSE-YGLS 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 630034702 461 GSIFARDAA-AIRYAEdklRNSAGNFYINtkstGSVVG---QQPFGGMRGSGTNdKVGSVNVLSRFTSVRAI 528
Cdd:cd07105 367 AAVFTRDLArALAVAK---RIESGAVHIN----GMTVHdepTLPHGGVKSSGYG-RFNGKWGIDEFTETKWI 430
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
61-488 |
3.34e-54 |
|
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: 189.76 E-value: 3.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRA-AGLVAGKYRHALMAATMVGqgKNIWQA-- 137
Cdd:cd07102 1 ISPIDGS-VIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAANTDEIAEELTWQMG--RPIAQAgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 EIDAAAETCdllRFNVQCAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPSP 216
Cdd:cd07102 78 EIRGMLERA---RYMISIAEEALADIRVPEKDGFERYIRREPL-GVVLIIAPWNYPYLTAVNAVIPaLLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 217 SAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGedkflnfPRIVG- 295
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGR----AIQRAAA-------GRFIKv 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 296 --ETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI 373
Cdd:cd07102 222 glELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 374 HEQSFDKLAAVIERAKTDSQlTLLCGGKT---SKETGYFVHPTIYqtSDAHH--EILQKEFFGPLLAVY-VYPDSEwaEI 447
Cdd:cd07102 302 SARAADFVRAQIADAIAKGA-RALIDGALfpeDKAGGAYLAPTVL--TNVDHsmRVMREETFGPVVGIMkVKSDAE--AI 376
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 630034702 448 TQVIDStaPYALTGSIFARD-AAAIRYAEdklRNSAGNFYIN 488
Cdd:cd07102 377 ALMNDS--EYGLTASVWTKDiARAEALGE---QLETGTVFMN 413
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
56-528 |
3.64e-54 |
|
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: 189.74 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKN 133
Cdd:cd07112 2 ETFATINPAT-GRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE-AHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPS--GMWNRleyRPLeGFVYAISPFNFTALGATLACGPLL-MGNVV 210
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDalALITR---EPL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFV------AGDAEAITSTVlenrafAGLNFTGSSAVFKQLIARIGQAtge 284
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLNVVpgfghtAGEALGLHMDV------DALAFTGSTEVGRRFLEYSGQS--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 285 dkflNFPRIVGETGGKNFHLV-HKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPE 363
Cdd:cd07112 227 ----NLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 364 DVTNFVNPVIHEQSFDKLAAVIERAKTDsQLTLLCGGKTSKET--GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPD 441
Cdd:cd07112 303 DPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 442 SEWAeITQVIDStaPYALTGSIFARD-AAAIRYAeDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSGT-NDKvgSVNVL 519
Cdd:cd07112 382 EEEA-VALANDS--VYGLAASVWTSDlSRAHRVA-RRLR--AGTVWVNCFDEGDI--TTPFGGFKQSGNgRDK--SLHAL 451
|
....*....
gi 630034702 520 SRFTSVRAI 528
Cdd:cd07112 452 DKYTELKTT 460
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
80-508 |
3.87e-54 |
|
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: 189.02 E-value: 3.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 80 DVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVGQ-GKNIW--QAEIDAAAETCDllrFNVQCA 156
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELL--KANKEELARLISREtGKPLWeaQTEVAAMAGKID---ISIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 157 MDLFKQQPAVNPSGMwNRLEYRPLeGFVYAISPFNFTAlgaTLACG---P-LLMGNVVVWKPSPSAFHSSWLLYKIMIEA 232
Cdd:cd07095 76 HERTGERATPMAQGR-AVLRHRPH-GVMAVFGPFNFPG---HLPNGhivPaLLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 233 GLPENVLQFVAGDAEAiTSTVLENRAFAGLNFTGSSAVFKQLiarigqatgEDKFLNFP-RIVG-ETGGKNFHLVHKSAD 310
Cdd:cd07095 151 GLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLL---------HRQFAGRPgKILAlEMGGNNPLVVWDVAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 311 IENAVNCTIRSAFEYQGQKCSAASRLYVPESIW-PAFKENLLAKMATIKVGSPEDVTNFVNPVIHeqsfdklAAVIERAK 389
Cdd:cd07095 221 IDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLII-------AAAAARYL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 390 TDSQLTLLCGGKTS------KETGYFVHPTIYQTSDAhHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaPYALTGSI 463
Cdd:cd07095 294 LAQQDLLALGGEPLlamerlVAGTAFLSPGIIDVTDA-ADVPDEEIFGPLLQVYRYDDFDEA-IALANAT--RFGLSAGL 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 630034702 464 FARDAAAIRYAEDKLRnsAGNFYINTKSTGSvVGQQPFGGMRGSG 508
Cdd:cd07095 370 LSDDEALFERFLARIR--AGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
54-525 |
1.06e-53 |
|
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: 188.93 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANHkQVVAEYIPSTRFDVQNAIESALQA-KSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATM--VGQ 130
Cdd:cd07082 14 SGKTIEVYSPIDG-EVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEEVANLLMweIGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQAEIDAaaeTCDLLRFNVQCAMDLFKQQ-PAVNPSGMWNRL-EYR--PLeGFVYAISPFN---FTALgATLAcgP 203
Cdd:cd07082 92 TLKDALKEVDR---TIDYIRDTIEELKRLDGDSlPGDWFPGTKGKIaQVRrePL-GVVLAIGPFNyplNLTV-SKLI--P 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 204 -LLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQlIARIGqat 282
Cdd:cd07082 165 aLIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR-LKKQH--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 283 gedkflnfPRI--VGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVG 360
Cdd:cd07082 241 --------PMKrlVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 361 SPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKtsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYP 440
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGA-TVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 441 DSEWAeITQVIDStaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKStgsvvgQQ-----PFGGMRGSGtndkVG- 514
Cdd:cd07082 390 DIEEA-IELANKS--NYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG----IGt 454
|
490
....*....|....*.
gi 630034702 515 -----SVNVLSRFTSV 525
Cdd:cd07082 455 qgigdALRSMTRRKGI 470
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
61-528 |
1.88e-53 |
|
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: 187.94 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPAnHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAiFLR--AAGLVAGkyRHALMAATMVGQGKNIWQAE 138
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAK-YLRaiAEGVRER--REELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 ID---AAAetCdlLRFNVQCAMDLFKQQPAVNP---SGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVV 211
Cdd:cd07110 78 WDvddVAG--C--FEYYADLAEQLDAKAERAVPlpsEDFKARVRREPV-GVVGLITPWNFPLLMAAWKVAPaLAAGCTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 212 WKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGEDkflnFP 291
Cdd:cd07110 153 LKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQ----VMQAAAQD----IK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 292 RIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNP 371
Cdd:cd07110 225 PVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 372 VIHEQSFDKLAAVIERAKTDSqLTLLCGGKTSK--ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYpDSEWAEITQ 449
Cdd:cd07110 305 LVSQAQYEKVLSFIARGKEEG-ARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSF-ATEDEAIAL 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 630034702 450 VIDSTapYALTGSIFARDAAAIRYAEDKLRnsAGNFYINtkSTGSVVGQQPFGGMRGSGTNDKVGsVNVLSRFTSVRAI 528
Cdd:cd07110 383 ANDSE--YGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSGIGRELG-EWGLDNYLEVKQI 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
80-523 |
3.18e-53 |
|
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: 186.73 E-value: 3.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 80 DVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLV---AGKYRHALMAATMVGQGKNIWqaEIDAAAETCdllrfnVQCA 156
Cdd:cd07152 14 DVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLeehADEIADWIVRESGSIRPKAGF--EVGAAIGEL------HEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 157 MDLFKQQPAVNPS--GMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPSP-SAFHSSWLLYKIMIEA 232
Cdd:cd07152 86 GLPTQPQGEILPSapGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPaLALGNAVVLKPDPrTPVSGGVVIARLFEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 233 GLPENVLQFVAGDAEAiTSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflNFPRIVGETGGKNFHLVHKSADIE 312
Cdd:cd07152 165 GLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGR----KVGEAAGR----HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 313 NAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIErAKTDS 392
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD-DSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 393 QLTLLCGGkTSKetGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaPYALTGSIFARDAA-AI 471
Cdd:cd07152 315 GARLEAGG-TYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEA-VALANDT--EYGLSAGIISRDVGrAM 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 630034702 472 RYAeDKLRnsAGNFYIN--TKSTGSVVgqqPFGGMRGSGTNDKVGSVNVLSRFT 523
Cdd:cd07152 389 ALA-DRLR--TGMLHINdqTVNDEPHN---PFGGMGASGNGSRFGGPANWEEFT 436
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
76-528 |
1.16e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 187.39 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 76 STRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWqaeiDAAAETCDLL---RFN 152
Cdd:PRK09407 51 STAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVL-ENREELLDLVQLETGKARR----HAFEEVLDVAltaRYY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 153 VQCAMDLFKQQ--PAVNPSGMWNRLEYRPLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKP-SPSAFHSSWLLyKI 228
Cdd:PRK09407 126 ARRAPKLLAPRrrAGALPVLTKTTELRQPK-GVVGVISPWNYPlTLAVSDAIPALLAGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 229 MIEAGLPENVLQFVAGDAEAITSTVLENRAFagLNFTGSSAVFKQLIARIGQatgedkflnfpRIVG---ETGGKNFHLV 305
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAGR-----------RLIGfslELGGKNPMIV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 306 HKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVI 385
Cdd:PRK09407 271 LDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 386 E--RAKTdsqLTLLCGGKTSKETG-YFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDStaPYALTGS 462
Cdd:PRK09407 351 DdaVAKG---ATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA-VERANDT--PYGLNAS 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 630034702 463 IFARDAAAIRYAEDKLRnsAGNFYIN---TKSTGSVvgQQPFGGMRGSGTNDKVGSVNVLsRFTSVRAI 528
Cdd:PRK09407 425 VWTGDTARGRAIAARIR--AGTVNVNegyAAAWGSV--DAPMGGMKDSGLGRRHGAEGLL-KYTESQTI 488
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
61-528 |
2.12e-52 |
|
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: 185.14 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWeNTPFEDRAAIFLR-AAGLVAGKYRHALMAATMVGQGKNIWQA 137
Cdd:cd07089 2 INPAT-EEVIGTAPDAGAADVDAAIAAARRAfdTGDW-STDAEERARCLRQlHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 -EIDAAAEtcDLLRFNVQCAMDLFKQQ---PAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVW 212
Cdd:cd07089 80 mQVDGPIG--HLRYFADLADSFPWEFDlpvPALRGGPGRRVVRREPV-GVVAAITPWNFPFFLNLAKLAPaLAAGNTVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPR 292
Cdd:cd07089 157 KPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA--------TLKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:cd07089 229 VLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKtDSQLTLLCGGKTSK--ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWA-EITQ 449
Cdd:cd07089 309 ISAAQRDRVEGYIARGR-DEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAvRIAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 450 viDStaPYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKSTGSVVGqqPFGGMRGSGTNDKVGSVNvLSRFTSVRAI 528
Cdd:cd07089 388 --DS--DYGLSGGVWSADVDrAYRVAR-RIR--TGSVGINGGGGYGPDA--PFGGYKQSGLGRENGIEG-LEEFLETKSI 457
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
61-526 |
8.76e-52 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 190.96 E-value: 8.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYrHALMAATMVGQGKNIWQAeID 140
Cdd:PRK11809 664 INPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQM-QTLMGLLVREAGKTFSNA-IA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLFKQQpavnpsgmwnrlEYRPLeGFVYAISPFNFT------ALGATLACgpllmGNVVVWKP 214
Cdd:PRK11809 742 EVREAVDFLRYYAGQVRDDFDND------------THRPL-GPVVCISPWNFPlaiftgQVAAALAA-----GNSVLAKP 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 215 SPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfkqliARIGQATGEDKFLNFPR-- 292
Cdd:PRK11809 804 AEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV-----ARLLQRNLAGRLDPQGRpi 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 -IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNP 371
Cdd:PRK11809 879 pLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGP 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 372 VIHEQSFDKLAAVIE--RAKTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAhhEILQKEFFGPLLAVYVYPDSEWAEITQ 449
Cdd:PRK11809 959 VIDAEAKANIERHIQamRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSF--DELKREVFGPVLHVVRYNRNQLDELIE 1036
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 450 VIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGQQPFGGMRGSGTNDKVGSVNVLSRFTSVR 526
Cdd:PRK11809 1037 QINASG-YGLTLGVHTRIDETIAQVTGSAH--VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
54-508 |
1.79e-51 |
|
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: 182.77 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAGkyRHALMAATMVGQ- 130
Cdd:cd07139 12 GSETIDVVSPAT-EEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEA--RADELARLWTAEn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNV 209
Cdd:cd07139 89 GMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPV-GVVAAIVPWNAPLFLAALKIAPaLAAGCT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 210 VVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVlENRAFAGLNFTGSSAVFKqliaRIGQATGEdkflN 289
Cdd:cd07139 168 VVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLV-RHPGVDKVSFTGSTAAGR----RIAAVCGE----R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 FPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFV 369
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 370 NPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSK--ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeI 447
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGA-RLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA-V 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 630034702 448 TQVIDStaPYALTGSIFARD-AAAIRYAEdklRNSAGNFYINTKSTGSVVgqqPFGGMRGSG 508
Cdd:cd07139 397 RIANDS--DYGLSGSVWTADvERGLAVAR---RIRTGTVGVNGFRLDFGA---PFGGFKQSG 450
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
61-508 |
2.67e-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: 182.32 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLR-AAGLVAgkyRHALMAATMVGQ-GKNIWQAE 138
Cdd:cd07138 19 INPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERiAEAYEA---RADELAQAITLEmGAPITLAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 -------IDAAAETCDLLRfnvqcAMDLFKQQPAvnpsgmwNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVV 210
Cdd:cd07138 95 aaqvglgIGHLRAAADALK-----DFEFEERRGN-------SLVVREPI-GVCGLITPWNWPLNQIVLKVAPaLAAGCTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKqliaRIGQATGEDkflnF 290
Cdd:cd07138 162 VLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGK----RVAEAAADT----V 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 291 PRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVN 370
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 371 PVIHEQSFDKLAAVIERAkTDSQLTLLCGGK---TSKETGYFVHPTIYqtSDAHHE--ILQKEFFGPLLAVYVYPDSEWA 445
Cdd:cd07138 314 PLASAAQFDRVQGYIQKG-IEEGARLVAGGPgrpEGLERGYFVKPTVF--ADVTPDmtIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 446 eITQVIDStaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINtksTGSVVGQQPFGGMRGSG 508
Cdd:cd07138 391 -IAIANDT--PYGLAGYVWSADPERARAVARRLR--AGQVHIN---GAAFNPGAPFGGYKQSG 445
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
47-528 |
3.78e-51 |
|
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: 182.34 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 47 EHIsKGVDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQA-KSAW-ENTPFEDRAAIFLRAAGLVAgKYRHALMA 124
Cdd:cd07143 14 EFV-DSVHGGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfETDWgLKVSGSKRGRCLSKLADLME-RNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 125 ATMVGQGKNI-WQAEIDAAaETCDLLRFNVQCAMDLFKQQPAVNPSgmwnRLEYRPLE--GFVYAISPFNFTALGATLAC 201
Cdd:cd07143 91 IEALDNGKTFgTAKRVDVQ-ASADTFRYYGGWADKIHGQVIETDIK----KLTYTRHEpiGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 202 GPLLM-GNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQ 280
Cdd:cd07143 166 APALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 281 AtgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVG 360
Cdd:cd07143 246 S-------NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 361 SPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYP 440
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 441 DSEWAeITQVIDSTapYALTGSIFARD-AAAIRYAeDKLRnsAGNFYINTKSTgsVVGQQPFGGMRGSGTNDKVGSVnVL 519
Cdd:cd07143 398 TEEEA-IKRANDST--YGLAAAVFTNNiNNAIRVA-NALK--AGTVWVNCYNL--LHHQVPFGGYKQSGIGRELGEY-AL 468
|
....*....
gi 630034702 520 SRFTSVRAI 528
Cdd:cd07143 469 ENYTQIKAV 477
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
51-529 |
4.22e-51 |
|
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: 182.02 E-value: 4.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 51 KGVDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAgkyRHALMAATM- 127
Cdd:cd07091 14 DSVSGKTFPTINPATEE-VICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIE---RDRDELAALe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 128 -VGQGKNIWQA---EIDAAAETcdlLRFnvqCAMDLFKQQPAVNPSGMwNRLEYRPLE--GFVYAISPFNFTALGATLAC 201
Cdd:cd07091 90 sLDNGKPLEESakgDVALSIKC---LRY---YAGWADKIQGKTIPIDG-NFLAYTRREpiGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 202 GP-LLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAG----DAEAITSTVLENRafagLNFTGSSAVFKQlia 276
Cdd:cd07091 163 APaLAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfgptAGAAISSHMDVDK----IAFTGSTAVGRT--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 277 rIGQATGEDkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMAT 356
Cdd:cd07091 236 -IMEAAAKS---NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 357 IKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAV 436
Cdd:cd07091 312 RVVGDPFDPDTFQGPQVSKAQFDKILSYIESGK-KEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 437 YVYPDSEwaEITQVIDSTApYALTGSIFARDAA-AIRYAeDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSGTNDKVGs 515
Cdd:cd07091 391 LKFKTED--EVIERANDTE-YGLAAGVFTKDINkALRVS-RALK--AGTVWVNTYNVFDA--AVPFGGFKQSGFGRELG- 461
|
490
....*....|....
gi 630034702 516 VNVLSRFTSVRAIK 529
Cdd:cd07091 462 EEGLEEYTQVKAVT 475
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
68-528 |
4.60e-50 |
|
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: 178.32 E-value: 4.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 68 QVVAEYIPSTRFDVQNAIESALQAKSAWenTPFeDRAAIFLRAAGLVAgkyRHALMAATMVGQ--GKNIWQA--EIDAAa 143
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAASYRSTL--TRY-QRSAILNKAAALLE---ARREEFARLITLesGLCLKDTryEVGRA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 144 etCDLLRFnvqCAMDLFKQQ----PAVNPSGMWNRLEY---RPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPS 215
Cdd:cd07146 83 --ADVLRF---AAAEALRDDgesfSCDLTANGKARKIFtlrEPL-GVVLAITPFNHPLNQVAHKIAPaIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 216 PSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGqatgedkflnFPRIVG 295
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG----------YKRQLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 296 ETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHE 375
Cdd:cd07146 227 ELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 376 QSFDKLAAVIERAKTDSQlTLLCGGktsKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTA 455
Cdd:cd07146 307 EAAIQIENRVEEAIAQGA-RVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLD--EAIAISNSTA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 456 pYALTGSIFARDAAAIRYAEDKLRnsagnfyINTKSTGSVVGQQ----PFGGMRGSGTNDKVGSVNVLSRFTSVRAI 528
Cdd:cd07146 381 -YGLSSGVCTNDLDTIKRLVERLD-------VGTVNVNEVPGFRselsPFGGVKDSGLGGKEGVREAMKEMTNVKTY 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
62-528 |
1.62e-49 |
|
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: 177.17 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 62 NPAnHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIWQAEIDA 141
Cdd:cd07108 3 NPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEAR-SEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 142 AAETCDLLRFNVQCAMDLFKQQPAVNPsgmwNRLEY---RPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWKPSPS 217
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGP----DVLTYtvrEPL-GVVGAILPWNAPLMLAALKIAPaLVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 218 AFHSSWLLYKIMIEAgLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGEdkflnfpRIVG-- 295
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKI----IYRAAAD-------RLIPvs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 296 -ETGGKNFHLVHKSADIENAVNCTIRSA-FEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI 373
Cdd:cd07108 224 lELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 374 HEQSFDKLAAVIERAKTDSQLTLLCGGKTSKET----GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYvypdsEWAEITQ 449
Cdd:cd07108 304 SEKQFAKVCGYIDLGLSTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAI-----PWKDEDE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 450 VIDST--APYALTGSIFARD-AAAIRYAedkLRNSAGNFYINTKstgsvVGQQP---FGGMRGSGTNDKVGSVNVLSRFT 523
Cdd:cd07108 379 VIAMAndSHYGLAAYVWTRDlGRALRAA---HALEAGWVQVNQG-----GGQQPgqsYGGFKQSGLGREASLEGMLEHFT 450
|
....*
gi 630034702 524 SVRAI 528
Cdd:cd07108 451 QKKTV 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
61-509 |
2.61e-48 |
|
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: 173.67 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHaLMAATMVGQGKNIWQAEID 140
Cdd:cd07092 2 VDPAT-GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEE-LAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLfkQQPAVNP--SGMWNRLEYRPLeGFVYAISPFNFTALGATLACGPLL-MGNVVVWKPSPS 217
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTL--EGPAAGEylPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 218 AFHSSWLLYKIMIEaGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQlIARIGQATGEDKFLnfprivgET 297
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKK-VARAAADTLKRVHL-------EL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 298 GGKNFHLVHKSADIENAVNcTIRSAFEYQ-GQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQ 376
Cdd:cd07092 228 GGKAPVIVFDDADLDAAVA-GIATAGYYNaGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 377 SFDKLAAVIERAKTDSqlTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDS----EWAEITqvid 452
Cdd:cd07092 307 QRERVAGFVERAPAHA--RVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEdeaiELANDV---- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 453 staPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKstGSVVGQQPFGGMRGSGT 509
Cdd:cd07092 381 ---EYGLASSVWTRDVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
62-528 |
3.46e-48 |
|
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: 173.72 E-value: 3.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 62 NPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgkyRHALMAATM-VGQGKNIWQAEID 140
Cdd:cd07107 3 NPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLR---EHAEELALIdALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 141 AAAETCDLLRFNVQCAMDLfKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTAL-GATLACGPLLMGNVVVWKPSPSAF 219
Cdd:cd07107 79 DVMVAAALLDYFAGLVTEL-KGETIPVGGRNLHYTLREPY-GVVARIVAFNHPLMfAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 220 HSSWLLYKIMIEAgLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIARigQATGEDKFLNFprivgETGG 299
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPT-GRAIMR--AAAEGIKHVTL-----ELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 300 KNFHLVHKSADIENAVNCTIRSA-FEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSF 378
Cdd:cd07107 228 KNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 379 DKLAAVIERAKTDSQlTLLCGGKTSK----ETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSewAEITQVIDST 454
Cdd:cd07107 308 DRVMHYIDSAKREGA-RLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANGV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 630034702 455 aPYALTGSIFARD-AAAIRYAedkLRNSAGNFYINTKST---GSvvgqqPFGGMRGSGTNDKVGSVNVLSrFTSVRAI 528
Cdd:cd07107 385 -EYGLTAAIWTNDiSQAHRTA---RRVEAGYVWINGSSRhflGA-----PFGGVKNSGIGREECLEELLS-YTQEKNV 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
61-508 |
2.67e-47 |
|
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: 170.88 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQA-KSAWENTPFEDRAAIFLRAAGLVaGKYRHALMAATMVGQGKNIWQA-- 137
Cdd:cd07109 2 FDPST-GEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLI-REHADELARLESLDTGKPLTQAra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 EIDAAAETcdlLRFNVQCAMDLFKQQPAVNPsGMWNRLEYRPLeGFVYAISPFNFTA--LGATLACGpLLMGNVVVWKPS 215
Cdd:cd07109 80 DVEAAARY---FEYYGGAADKLHGETIPLGP-GYFVYTVREPH-GVTGHIIPWNYPLqiTGRSVAPA-LAAGNAVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 216 PSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIARigqATGEdkflNFPRIVG 295
Cdd:cd07109 154 EDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET-GIAVMR---AAAE----NVVPVTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 296 ETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNfVNPVIHE 375
Cdd:cd07109 226 ELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 376 QSFDKLAAVIERAKtDSQLTLLCGG---KTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYpDSEwAEITQVID 452
Cdd:cd07109 305 KQLDRVEGFVARAR-ARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF-DDE-AEAIALAN 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 453 STApYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKSTGSVVgQQPFGGMRGSG 508
Cdd:cd07109 382 GTD-YGLVAGVWTRDGDrALRVAR-RLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
50-528 |
3.73e-47 |
|
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: 171.44 E-value: 3.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 50 SKGVDTKSIQQVNPANHKQVVAEYIPSTRfDVQNAIESALQA-KSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMV 128
Cdd:cd07144 17 VKSSDGETIKTVNPSTGEVIASVYAAGEE-DVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVE-KNRDLLAAIEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 129 GQGKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPsgmwNRLEY---RPLeGFVYAISPFNFT-ALGATLACGPL 204
Cdd:cd07144 95 DSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSP----NKLAYtlhEPY-GVCGQIIPWNYPlAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 205 LMGNVVVWKPSPSAFHSswLLY--KIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfkqliariGQAT 282
Cdd:cd07144 170 AAGNTVVIKPAENTPLS--LLYfaNLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT--------GRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 283 GEDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMA-TIKVGS 361
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 362 PEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKET---GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYV 438
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 439 YPDSEWAeITQVIDSTapYALTGSIFARD-AAAIRYAeDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSGTNDKVGSvN 517
Cdd:cd07144 399 FKTYEEA-IKKANDTT--YGLAAAVFTKDiRRAHRVA-RELE--AGMVWINSSNDSDV--GVPFGGFKMSGIGRELGE-Y 469
|
490
....*....|.
gi 630034702 518 VLSRFTSVRAI 528
Cdd:cd07144 470 GLETYTQTKAV 480
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
55-467 |
2.81e-46 |
|
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: 168.54 E-value: 2.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 55 TKSIQQVNPANHkQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIfLRAAGLVAGKYRHALMAATMVGQGKnI 134
Cdd:cd07130 11 GGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEI-VRQIGDALRKKKEALGKLVSLEMGK-I 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 135 WQ---AEIDAAAETCDLlrfnvqcAMDLFKQQP-AVNPS--------GMWNrleyrPLeGFVYAISPFNF-TALGATLAC 201
Cdd:cd07130 88 LPeglGEVQEMIDICDF-------AVGLSRQLYgLTIPSerpghrmmEQWN-----PL-GVVGVITAFNFpVAVWGWNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 202 GPLLMGNVVVWKPSPSAFHSSWLLYKIMIEA----GLPENVLQFVAGDAEAITSTVLENRaFAGLNFTGSSAVFKQliar 277
Cdd:cd07130 155 IALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPR-VPLVSFTGSTAVGRQ---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 278 IGQATGEdkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATI 357
Cdd:cd07130 230 VGQAVAA----RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 358 KVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYqTSDAHHEILQKEFFGPLLAVY 437
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVL 383
|
410 420 430
....*....|....*....|....*....|
gi 630034702 438 VYPDSEWAeITqvIDSTAPYALTGSIFARD 467
Cdd:cd07130 384 KFDTLEEA-IA--WNNEVPQGLSSSIFTTD 410
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
61-508 |
6.14e-45 |
|
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: 164.73 E-value: 6.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQA--E 138
Cdd:cd07147 4 TNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE-ERFEELAETIVLEAGKPIKDArgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 IDAAAETCDL-----LRFNVQcAMDLFKQQPAVNPSGMWNRLeyrPLeGFVYAISPFNFTAlgaTLAC---GPLL-MGNV 209
Cdd:cd07147 82 VARAIDTFRIaaeeaTRIYGE-VLPLDISARGEGRQGLVRRF---PI-GPVSAITPFNFPL---NLVAhkvAPAIaAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 210 VVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaITSTVLENRAFAGLNFTGSSAVFKQLIARIGQAtgedkfln 289
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRD-DADLLVTDERIKLLSFTGSPAVGWDLKARAGKK-------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 fpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFV 369
Cdd:cd07147 225 --KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 370 NPVIHEQSFDKLAAVIERAkTDSQLTLLCGGKTSketGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQ 449
Cdd:cd07147 303 GPMISESEAERVEGWVNEA-VDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEA-LAA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 630034702 450 VIDStaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSvVGQQPFGGMRGSG 508
Cdd:cd07147 378 VNDS--KFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
61-531 |
9.92e-45 |
|
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: 164.40 E-value: 9.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHkQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAiFLRAagLVAGKYRHA--LMAATMVGQGKNIWQAE 138
Cdd:cd07098 1 YDPATG-QHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRK-VLRS--LLKYILENQeeICRVACRDTGKTMVDAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 IDAAAETCDLLRFNVQCAMDLFKQQPAVNPSGMW---NRLEYRPLeGFVYAISPFNF---TALGATLACgpLLMGNVVVW 212
Cdd:cd07098 77 LGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFykrARVEYEPL-GVVGAIVSWNYpfhNLLGPIIAA--LFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSS-W---LLYKIMIEAGLPENVLQFV---AGDAEAITSTVlenrAFAGLNFTGSSAVFKqliaRIGQATGEd 285
Cdd:cd07098 154 KVSEQVAWSSgFflsIIRECLAACGHDPDLVQLVtclPETAEALTSHP----VIDHITFIGSPPVGK----KVMAAAAE- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 286 kflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDV 365
Cdd:cd07098 225 ---SLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 366 TNFVNPVIHEQSFDKLAAVIERAkTDSQLTLLCGGK----TSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPD 441
Cdd:cd07098 302 DVDVGAMISPARFDRLEELVADA-VEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 442 SEwaEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLrnSAGNFYINTKSTGSVVGQQPFGGMRGSGTnDKVGSVNVLSR 521
Cdd:cd07098 381 DE--EAVEIANST-EYGLGASVFGKDIKRARRIASQL--ETGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGEEGLRG 454
|
490
....*....|
gi 630034702 522 FTSVRAIKED 531
Cdd:cd07098 455 LCNPKSVTED 464
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
61-508 |
1.54e-44 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 163.93 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgkyRHA-LMAATMVGQ-GKNIWQAE 138
Cdd:PRK13473 22 YNPATGE-VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE---ENAdEFARLESLNcGKPLHLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 139 IDAAAETCDLLRFNVQCAMDLfkQQPAvnpSGmwnrlEY---------RPLEGFVYAISPFNFtalgatlacgPLLM--- 206
Cdd:PRK13473 98 NDEIPAIVDVFRFFAGAARCL--EGKA---AG-----EYleghtsmirRDPVGVVASIAPWNY----------PLMMaaw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 207 --------GNVVVWKPSPSAFHSSWLLYKIMIEAgLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARi 278
Cdd:PRK13473 158 klapalaaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 279 gqATGEDKflnfpRIVGETGGKNFHLVHKSADIENAVNcTIRSAFEYQ-GQKCSAASRLYVPESIWPAFKENLLAKMATI 357
Cdd:PRK13473 236 --AADSVK-----RTHLELGGKAPVIVFDDADLDAVVE-GIRTFGYYNaGQDCTAACRIYAQRGIYDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 358 KVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVY 437
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVT 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 630034702 438 VYPDSEWAeITQVIDStaPYALTGSIFARD-------AAAIRYaedklrnsaGNFYINTKstGSVVGQQPFGGMRGSG 508
Cdd:PRK13473 388 PFDDEDQA-VRWANDS--DYGLASSVWTRDvgrahrvSARLQY---------GCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
54-507 |
1.63e-44 |
|
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: 163.84 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPAnHKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKN 133
Cdd:cd07085 14 TTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE-ENLDELARLITLEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQA--EIDAAAETCDllrfnVQCAM-DLFKQQPAVNPS-GMWNRLEYRPLeGFVYAISPFNFTALGatlacgPLLM--- 206
Cdd:cd07085 92 LADArgDVLRGLEVVE-----FACSIpHLLKGEYLENVArGIDTYSYRQPL-GVVAGITPFNFPAMI------PLWMfpm 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 207 ----GNVVVWKPS---PSAfhsSWLLYKIMIEAGLPENVLQFVAGDAEAITStVLENRAFAGLNFTGSSAVFKQLIARiG 279
Cdd:cd07085 160 aiacGNTFVLKPServPGA---AMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYER-A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 280 QATGEdkflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKV 359
Cdd:cd07085 235 AANGK-------RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 360 GSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSK----ETGYFVHPTIYQTSDAHHEILQKEFFGPLLA 435
Cdd:cd07085 308 GAGDDPGADMGPVISPAAKERIEGLIESGVEEGA-KLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLS 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 436 VyVYPDSeWAEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLrnSAGNFYINtkstgsV-----VGQQPFGGMRGS 507
Cdd:cd07085 387 I-VRVDT-LDEAIAIINAN-PYGNGAAIFTRSGAAARKFQREV--DAGMVGIN------VpipvpLAFFSFGGWKGS 452
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
58-508 |
8.83e-43 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 159.35 E-value: 8.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 58 IQQVNPANHkQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVaGKYRHALmaATMVGQ--GKNIW 135
Cdd:PRK09457 17 FESRNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL-EENKEEL--AEVIARetGKPLW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 136 QA--EIDAAAETCDLlrfNVQCAMDLF--KQQPAVNPSGMwnrLEYRPLeGFVYAISPFNFTAlgaTLACG---P-LLMG 207
Cdd:PRK09457 93 EAatEVTAMINKIAI---SIQAYHERTgeKRSEMADGAAV---LRHRPH-GVVAVFGPYNFPG---HLPNGhivPaLLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 208 NVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaiTSTVL-ENRAFAGLNFTGSS----AVFKQLIARIGqat 282
Cdd:PRK09457 163 NTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRE--TGKALaAHPDIDGLLFTGSAntgyLLHRQFAGQPE--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 283 gedKFLNFprivgETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWP-AFKENLLAKMATIKVGS 361
Cdd:PRK09457 238 ---KILAL-----EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 362 P-EDVTNFVNPVIHEQSFDKLaavierakTDSQLTLLC-GGKTSKE-------TGyFVHPTIYQTSDAhHEILQKEFFGP 432
Cdd:PRK09457 310 WdAEPQPFMGAVISEQAAQGL--------VAAQAQLLAlGGKSLLEmtqlqagTG-LLTPGIIDVTGV-AELPDEEYFGP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 433 LLAVYVYPDSEWAeiTQVIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSvVGQQPFGGMRGSG 508
Cdd:PRK09457 380 LLQVVRYDDFDEA--IRLANNTR-FGLSAGLLSDDREDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
56-528 |
3.32e-42 |
|
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: 157.66 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKN 133
Cdd:cd07142 19 KTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 134 IWQAEIDAAAETCDLLRFNVQCAMDLFKQQPAVNPSGMWNRLeYRPLeGFVYAISPFNFTALGATLACGPLLM-GNVVVW 212
Cdd:cd07142 97 YEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTL-HEPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQAtgedkflNFPR 292
Cdd:cd07142 175 KPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS-------NLKP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:cd07142 248 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVID 452
Cdd:cd07142 328 VDKEQFEKILSYIEHGK-EEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD--EVIKRAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 453 STApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTksTGSVVGQQPFGGMRGSGTNDKVGsVNVLSRFTSVRAI 528
Cdd:cd07142 405 NSK-YGLAAGVFSKNIDTANTLSRALK--AGTVWVNC--YDVFDASIPFGGYKMSGIGREKG-IYALNNYLQVKAV 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-544 |
4.23e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 157.97 E-value: 4.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANHKQVvaEYIPS-TRFDVQNAIESALQAKSA-----WENTPFEDRAAiFLRAAGLVAGKYRHALMAATMVG 129
Cdd:PLN02467 23 KRIPVVNPATEETI--GDIPAaTAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAK-YLRAIAAKITERKSELAKLETLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 130 QGKNIWQAEID----AA-----AETCDLL----RFNVQCAMDLFKqqpavnpsgmwNRLEYRPLeGFVYAISPFNFTALG 196
Cdd:PLN02467 100 CGKPLDEAAWDmddvAGcfeyyADLAEALdakqKAPVSLPMETFK-----------GYVLKEPL-GVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 197 ATLACGP-LLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAG---DAEAITSTvleNRAFAGLNFTGSSAVFK 272
Cdd:PLN02467 168 ATWKVAPaLAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlgtEAGAPLAS---HPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 273 qliaRIGQATGEDkflnfPRIVG-ETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLL 351
Cdd:PLN02467 245 ----KIMTAAAQM-----VKPVSlELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 352 AKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSK--ETGYFVHPTIYQTSDAHHEILQKEF 429
Cdd:PLN02467 316 KWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGA-TILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 430 FGPLLAVYVYPDSEWAeITQVIDSTapYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKStgSVVGQQPFGGMRGSGT 509
Cdd:PLN02467 395 FGPVLCVKTFSTEDEA-IELANDSH--YGLAGAVISNDLERCERVSEAFQ--AGIVWINCSQ--PCFCQAPWGGIKRSGF 467
|
490 500 510
....*....|....*....|....*....|....*
gi 630034702 510 NDKVGSvNVLSRFTSVRAIKedfegtpdfRYPSNE 544
Cdd:PLN02467 468 GRELGE-WGLENYLSVKQVT---------KYISDE 492
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
57-508 |
4.83e-42 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 156.82 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 57 SIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRH--ALMAATMvgqGKNI 134
Cdd:PRK09406 2 PIATINPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQvaALMTLEM---GKTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 135 WQAEIDAAaeTC-DLLRFNVQCAMDLFKQQPA----VNPSGMWNRleYRPLeGFVYAISPFNFTALGATLACGPLLM-GN 208
Cdd:PRK09406 78 ASAKAEAL--KCaKGFRYYAEHAEALLADEPAdaaaVGASRAYVR--YQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 209 VVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFV---AGDAEAItstvLENRAFAGLNFTGSSAVfKQLIARIgqATGED 285
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLlvgSGAVEAI----LRDPRVAAATLTGSEPA-GRAVAAI--AGDEI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 286 KflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDV 365
Cdd:PRK09406 226 K-----KTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 366 TNFVNPVIHEQSFDKLAAVIERAkTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwa 445
Cdd:PRK09406 301 DTDVGPLATEQGRDEVEKQVDDA-VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADID-- 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 446 EITQVIDSTaPYALTGSIFARDAAAIRYAEDKLrnSAGNFYIN--TKSTGSVvgqqPFGGMRGSG 508
Cdd:PRK09406 378 EAIEIANAT-TFGLGSNAWTRDEAEQERFIDDL--EAGQVFINgmTVSYPEL----PFGGVKRSG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
53-528 |
7.21e-42 |
|
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: 156.74 E-value: 7.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 53 VDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQA---KSAWENTPFEDRAAIFLRAAGLVAgkyRHALMAATM-- 127
Cdd:cd07141 19 VSGKTFPTINPATGE-KICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIE---RDRAYLASLet 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 128 VGQGKNIWQAEIDAAAETCDLLRFNVQCAMDLF-KQQPAVNPSGMWNRLEyrPLeGFVYAISPFNFTALGATLACGPLL- 205
Cdd:cd07141 95 LDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHgKTIPMDGDFFTYTRHE--PV-GVCGQIIPWNFPLLMAAWKLAPALa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 206 MGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfKQLIArigQATGED 285
Cdd:cd07141 172 CGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQ---QAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 286 kflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDV 365
Cdd:cd07141 248 ---NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 366 TNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDsewa 445
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT---- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 446 eITQVID--STAPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVvgQQPFGGMRGSGTNDKVGSVNvLSRFT 523
Cdd:cd07141 400 -IDEVIEraNNTTYGLAAAVFTKDIDKAITFSNALR--AGTVWVNCYNVVSP--QAPFGGYKMSGNGRELGEYG-LQEYT 473
|
....*
gi 630034702 524 SVRAI 528
Cdd:cd07141 474 EVKTV 478
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
51-528 |
1.53e-41 |
|
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: 155.69 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 51 KGVDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMvGQ 130
Cdd:cd07117 11 KGSSGETIDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL-DN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQ---AEIDAAAetcDLLRFNVQCAMDLFKQQPAVNPSGMwNRLEYRPLeGFVYAISPFNFTALGATLACGPLLM- 206
Cdd:cd07117 89 GKPIREtraVDIPLAA---DHFRYFAGVIRAEEGSANMIDEDTL-SIVLREPI-GVVGQIIPWNFPFLMAAWKLAPALAa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 207 GNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIGQATGEdk 286
Cdd:cd07117 164 GNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRD----VAIAAAK-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 287 flnfpRIVGET---GGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPE 363
Cdd:cd07117 237 -----KLIPATlelGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 364 DVTNFVNPVIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKET----GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVY 439
Cdd:cd07117 312 DPDTQMGAQVNKDQLDKILSYVDIAK-EEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 440 PDSEWAeITQVIDSTapYALTGSIFARD-AAAIRYAEDKlrnSAGNFYINTKStgSVVGQQPFGGMRGSGTNDKVGSVnV 518
Cdd:cd07117 391 KTEDEV-IDMANDSE--YGLGGGVFTKDiNRALRVARAV---ETGRVWVNTYN--QIPAGAPFGGYKKSGIGRETHKS-M 461
|
490
....*....|
gi 630034702 519 LSRFTSVRAI 528
Cdd:cd07117 462 LDAYTQMKNI 471
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-532 |
2.03e-41 |
|
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: 154.81 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANHkQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPfEDRAAIFLR-AAGLVAGKYRHALMAATmvGQGKNIWQA 137
Cdd:cd07120 2 IDPATG-EVIGTYADGGVAEAEAAIAAARRAfdETDWAHDP-RLRARVLLElADAFEANAERLARLLAL--ENGKILGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 --EIDAAAETcdlLRFNVQCAMDLFKQQPAVNPsGMWNRLEYRPLeGFVYAISPFNFTALGATLACGPLLM-GNVVVWKP 214
Cdd:cd07120 78 rfEISGAISE---LRYYAGLARTEAGRMIEPEP-GSFSLVLREPM-GVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 215 SPSAFHSSWLLYKIMIEA-GLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVfkqliariGQATGEDKFLNFPRI 293
Cdd:cd07120 153 AGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT--------GRAIMAAAAPTLKRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 294 VGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI 373
Cdd:cd07120 225 GLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 374 HEQSFDKLAAVIERAKTDSQLTLLCGGKTSKET--GYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVI 451
Cdd:cd07120 305 DRANVDRVDRMVERAIAAGAEVVLRGGPVTEGLakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEA-VALAN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 452 DSTapYALTGSIFARDAA-AIRYAEdKLRnsAGNFYINTKstGSVVGQQPFGGMRGSGtndkvgsvnvLSRFTSVRAIkE 530
Cdd:cd07120 384 DTD--YGLAASVWTRDLArAMRVAR-AIR--AGTVWINDW--NKLFAEAEEGGYRQSG----------LGRLHGVAAL-E 445
|
..
gi 630034702 531 DF 532
Cdd:cd07120 446 DF 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
51-508 |
2.77e-40 |
|
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: 152.11 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 51 KGVDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMvGQ 130
Cdd:cd07559 11 APSKGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL-DN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQ---AEIDAAAetcDLLRFNVQC-------AMDLFKQQPAVnpsgmwnrLEYRPLeGFVYAISPFNFTALGATLA 200
Cdd:cd07559 89 GKPIREtlaADIPLAI---DHFRYFAGViraqegsLSEIDEDTLSY--------HFHEPL-GVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 201 CGPLLM-GNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQliarIG 279
Cdd:cd07559 157 LAPALAaGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRL----IM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 280 QATGEdkflNFPRIVGETGGKNFHLVHKSA-----DIENAVNcTIRSAFEY-QGQKCSAASRLYVPESIWPAFKENLLAK 353
Cdd:cd07559 232 QYAAE----NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAE-EGQLGFAFnQGEVCTCPSRALVQESIYDEFIERAVER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 354 MATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKET----GYFVHPTIYQTSDAHHEILQKEF 429
Cdd:cd07559 307 FEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGK-EEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 430 FGPLLAVYVYPDSEWAeITQVIDStaPYALTGSIFARDAA-AIRYAEDKlrnSAGNFYINTKStgSVVGQQPFGGMRGSG 508
Cdd:cd07559 386 FGPVLAVITFKDEEEA-IAIANDT--EYGLGGGVWTRDINrALRVARGI---QTGRVWVNCYH--QYPAHAPFGGYKKSG 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
56-508 |
4.81e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 151.57 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKyRHALMAATMVGQGKNIW 135
Cdd:PRK13252 22 ETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRER-NDELAALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 136 QAEIDAAAETCDLLRFNVQCAMDLF-KQQPAVNPSGMWNRLEyrPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVWK 213
Cdd:PRK13252 100 ETSVVDIVTGADVLEYYAGLAPALEgEQIPLRGGSFVYTRRE--PL-GVCAGIGAWNYPIQIACWKSAPaLAAGNAMIFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 214 PSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEaiTSTVL-ENRAFAGLNFTGSSAVFKQLIArigQATGEDKflnfpR 292
Cdd:PRK13252 177 PSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR--VGAWLtEHPDIAKVSFTGGVPTGKKVMA---AAAASLK-----E 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPED-VTNFvNP 371
Cdd:PRK13252 247 VTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDpATNF-GP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 372 VIHEQSFDKLAAVIERAKtDSQLTLLCGGKTSKE----TGYFVHPTIYqtSDAHHE--ILQKEFFGPLLAVYVYPDSEwa 445
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGK-AEGARLLCGGERLTEggfaNGAFVAPTVF--TDCTDDmtIVREEIFGPVMSVLTFDDED-- 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 446 eitQVID--STAPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTksTGSVVGQQPFGGMRGSG 508
Cdd:PRK13252 401 ---EVIAraNDTEYGLAAGVFTADLSRAHRVIHQLE--AGICWINT--WGESPAEMPVGGYKQSG 458
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
54-509 |
8.26e-40 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 151.38 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANhKQVVAEyIPST-RFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagkYRHAL-MAATMVG-Q 130
Cdd:PLN02278 38 DGKTFPVYNPAT-GEVIAN-VPCMgRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI---IANKEdLAQLMTLeQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWQA--EIDAAAETCDL-LRFNVQCAMDLFkqqpavnPSGMWNR--LEYRPLEGFVYAISPFNFTALGATLACGPLL 205
Cdd:PLN02278 113 GKPLKEAigEVAYGASFLEYfAEEAKRVYGDII-------PSPFPDRrlLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 206 M-GNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIArigQATGE 284
Cdd:PLN02278 186 AaGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA---GAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 285 DKflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGS--P 362
Cdd:PLN02278 263 VK-----RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDgfE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 363 EDVTnfVNPVIHEQSFDKLA-----AVIERAKtdsqltLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVY 437
Cdd:PLN02278 338 EGVT--QGPLINEAAVQKVEshvqdAVSKGAK------VLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 438 VYPDSEWAeITQVIDSTApyALTGSIFARDAA-AIRYAEdKLRNsaGNFYINTKSTGSVVGqqPFGGMRGSGT 509
Cdd:PLN02278 410 RFKTEEEA-IAIANDTEA--GLAAYIFTRDLQrAWRVSE-ALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-508 |
1.75e-39 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 149.63 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 61 VNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIfLRAAGlVAGKYRHALMAATMVGQ-GKNIWQA-- 137
Cdd:PRK13968 12 VNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQK-LRDIG-KALRARSEEMAQMITREmGKPINQAra 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 138 EIDAAAETCDLLRFNVQCAMD----LFKQQPAVnpsgmwnrLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVVVW 212
Cdd:PRK13968 89 EVAKSANLCDWYAEHGPAMLKaeptLVENQQAV--------IEYRPL-GTILAIMPWNFPLWQVMRGAVPiLLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 213 KPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRaFAGLNFTGSsavfkqliARIGQATGEDKFLNFPR 292
Cdd:PRK13968 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGS--------VRAGAAIGAQAGAALKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 293 IVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPV 372
Cdd:PRK13968 231 CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 373 IHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKETGYFVhPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVID 452
Cdd:PRK13968 311 ARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYA-PTVLANVTPEMTAFREELFGPVAAITVAKDAEHA-LELAND 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 630034702 453 STapYALTGSIF-ARDAAAIRYAEdklRNSAGNFYINTKSTGSvvGQQPFGGMRGSG 508
Cdd:PRK13968 389 SE--FGLSATIFtTDETQARQMAA---RLECGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
54-528 |
2.42e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 144.27 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMvGQG 131
Cdd:PRK09847 33 ENETFETVDPVT-QAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 132 KNIWQAEIDAAAETCDLLRFNVQcAMDLFKQQPAVNPSGMWNRLEYRPLeGFVYAISPFNFTALGATLACGP-LLMGNVV 210
Cdd:PRK09847 111 KPIRHSLRDDIPGAARAIRWYAE-AIDKVYGEVATTSSHELAMIVREPV-GVIAAIVPWNFPLLLTCWKLGPaLAAGNSV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 211 VWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAG-DAEAITSTVLENRAFAgLNFTGSSAVFKQLIARIGQAtgedkflN 289
Cdd:PRK09847 189 ILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDA-IAFTGSTRTGKQLLKDAGDS-------N 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 290 FPRIVGETGGKNFHLVHKSA-DIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNF 368
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 369 VNPVIHEQSFDKLAAVIERAktDSQLTLLCGGKTSKETGYfVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeIT 448
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREG--ESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA-LQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 449 QVIDSTapYALTGSIFARD-AAAIRYAEdklRNSAGNFYINTKSTGSVVgqQPFGGMRGSGtNDKVGSVNVLSRFTSVRA 527
Cdd:PRK09847 417 LANDSQ--YGLGAAVWTRDlSRAHRMSR---RLKAGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKT 488
|
.
gi 630034702 528 I 528
Cdd:PRK09847 489 I 489
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
54-514 |
4.90e-37 |
|
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: 143.40 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 54 DTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESAlqaKSAWENTPF-----EDRAAIFLRAAGLVAgkyRHALMAATMv 128
Cdd:cd07140 19 GGKTYNTINPTDGS-VICKVSLATVEDVDRAVAAA---KEAFENGEWgkmnaRDRGRLMYRLADLME---EHQEELATI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 129 gqgkniwqAEIDAAAETCDLLRFNVQCAMDLF--------KQQPA---VNPSGMWNRLEYRPLE--GFVYAISPFNFTAL 195
Cdd:cd07140 91 --------ESLDSGAVYTLALKTHVGMSIQTFryfagwcdKIQGKtipINQARPNRNLTLTKREpiGVCGIVIPWNYPLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 196 ---GATLACgpLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFK 272
Cdd:cd07140 163 mlaWKMAAC--LAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 273 QLIARIGQAtgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLA 352
Cdd:cd07140 241 HIMKSCAVS-------NLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 353 KMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAkTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGP 432
Cdd:cd07140 314 EVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERG-VKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 433 LLAVYVYPDSEWAEITQVIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVGqqPFGGMRGSGTNDK 512
Cdd:cd07140 393 IMIISKFDDGDVDGVLQRANDTE-YGLASGVFTKDINKALYVSDKLE--AGTVFVNTYNKTDVAA--PFGGFKQSGFGKD 467
|
..
gi 630034702 513 VG 514
Cdd:cd07140 468 LG 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-508 |
3.39e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.81 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANHKQVVAeyIPST-RFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNI 134
Cdd:PRK11241 26 EVIDVTNPANGDKLGS--VPKMgADETRAAIDAANRALPAWRALTAKERANILRRWFNLMM-EHQDDLARLMTLEQGKPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 135 WQA--EIDAAAEtcdLLRFNVQCAMDLFKQQ-PAVNPSgmwNRLEY--RPLeGFVYAISPFNFTALGATLACGP-LLMGN 208
Cdd:PRK11241 103 AEAkgEISYAAS---FIEWFAEEGKRIYGDTiPGHQAD---KRLIVikQPI-GVTAAITPWNFPAAMITRKAGPaLAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 209 VVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkfl 288
Cdd:PRK11241 176 TMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 289 NFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGS--PEDVT 366
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDglEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 367 nfVNPVIHEQSFDKLAAVIERAkTDSQLTLLCGGKTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSewAE 446
Cdd:PRK11241 328 --IGPLIDEKAVAKVEEHIADA-LEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE--AD 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 447 ITQVIDSTApYALTGSIFARDAAAI-RYAEDKLRNSAGnfyINTKSTGSVVGqqPFGGMRGSG 508
Cdd:PRK11241 403 VIAQANDTE-FGLAAYFYARDLSRVfRVGEALEYGIVG---INTGIISNEVA--PFGGIKASG 459
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
51-508 |
2.64e-35 |
|
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: 138.30 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 51 KGVDTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGKYRHALMAATMVGq 130
Cdd:cd07111 32 KPENRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIwqaeidaaAETCDLlrfNVQCAMDLFKQQpavnpSGMWNRLEY-----RPLeGFVYAISPFNFTALGATLACGPLL 205
Cdd:cd07111 110 GKPI--------RESRDC---DIPLVARHFYHH-----AGWAQLLDTelagwKPV-GVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 206 -MGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAfAGLNFTGSSAVFKqLIARigQATGE 284
Cdd:cd07111 173 aMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV-DKVAFTGSTEVGR-ALRR--ATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 285 DKFLNFprivgETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPED 364
Cdd:cd07111 249 GKKLSL-----ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 365 VTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKTSKEtGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEw 444
Cdd:cd07111 324 KAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAK- 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 630034702 445 aEITQVIDSTaPYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTksTGSVVGQQPFGGMRGSG 508
Cdd:cd07111 402 -EAVALANNT-PYGLAASVWSENLSLALEVALSLK--AGVVWING--HNLFDAAAGFGGYRESG 459
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
178-488 |
9.93e-35 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 135.25 E-value: 9.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 178 RPLeGFVYAISPFNFTA-LGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLEN 256
Cdd:PRK10090 70 RAL-GVTTGILPWNFPFfLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 257 RAFAGLNFTGSSAVfkqliariGQATGEDKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRL 336
Cdd:PRK10090 149 PKVAMVSMTGSVSA--------GEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 337 YVPESIWPAFKENLLAKMATIKVGSPEDVTNF-VNPVIHEQSFDKLAAVIERAkTDSQLTLLCGGKTSKETGYFVHPTIY 415
Cdd:PRK10090 221 YVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARA-VEEGARVALGGKAVEGKGYYYPPTLL 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 416 QTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDSTapYALTGSIFARDAAAIRYAEDKLRnsAGNFYIN 488
Cdd:PRK10090 300 LDVRQEMSIMHEETFGPVLPVVAFDTLEEA-IAMANDSD--YGLTSSIYTQNLNVAMKAIKGLK--FGETYIN 367
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
30-528 |
4.48e-32 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 129.17 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 30 MKAYGELVSSLPVNVPLEHISK---------GVDTKSIQQVNPANhKQVVAEYIPSTRFDVQNAIESALQA--KSAWENT 98
Cdd:PLN02766 1 MGSNGNCGGASGVKVPEIKFTKlfingefvdAASGKTFETRDPRT-GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 99 PFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQAEIDAAAETCDLLRFNVQCAMDLFKQqpAVNPSGMWNRLEYR 178
Cdd:PLN02766 80 SGFERGRIMMKFADLIE-EHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGE--TLKMSRQLQGYTLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLEGFVYAISPFNFTALGATLACGPLLM-GNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENR 257
Cdd:PLN02766 157 EPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 258 AFAGLNFTGSSAVFKqliaRIGQATGEDkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLY 337
Cdd:PLN02766 237 DVDKVSFTGSTEVGR----KIMQAAATS---NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 338 VPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYQT 417
Cdd:PLN02766 310 VQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFTD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 418 SDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTApYALTGSIFARDAAAIRYAEDKLRnsAGNFYINTKstgSVVG 497
Cdd:PLN02766 389 VTEDMKIAQDEIFGPVMSLMKFKTVE--EAIKKANNTK-YGLAAGIVTKDLDVANTVSRSIR--AGTIWVNCY---FAFD 460
|
490 500 510
....*....|....*....|....*....|..
gi 630034702 498 QQ-PFGGMRGSGTNDKVGsVNVLSRFTSVRAI 528
Cdd:PLN02766 461 PDcPFGGYKMSGFGRDQG-MDALDKYLQVKSV 491
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
174-508 |
1.20e-31 |
|
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: 126.96 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 174 RLEYRPlEGFVYAISPFNFTAlgaTLACGPLL----MGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVaGDAEai 249
Cdd:cd07134 95 KIRYEP-KGVCLIISPWNYPF---NLAFGPLVsaiaAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE-GDAE-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 250 TSTVLENRAFAGLNFTGSSAVFKQLIARIGQatgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQK 329
Cdd:cd07134 168 VAQALLELPFDHIFFTGSPAVGKIVMAAAAK--------HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 330 CSAASRLYVPESIWPAFKENLLAKMA-----TIKVGSPEDVTNFVNpvihEQSFDKLAAVIERAKTDSQlTLLCGGKTSK 404
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEkfygkDAARKASPDLARIVN----DRHFDRLKGLLDDAVAKGA-KVEFGGQFDA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 405 ETGYfVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDsewaeITQVIDST--APYALTGSIFARDAAAIRYAEDklRNSA 482
Cdd:cd07134 315 AQRY-IAPTVLTNVTPDMKIMQEEIFGPVLPIITYED-----LDEVIEYInaKPKPLALYVFSKDKANVNKVLA--RTSS 386
|
330 340 350
....*....|....*....|....*....|
gi 630034702 483 GNFYINtkstGSVV----GQQPFGGMRGSG 508
Cdd:cd07134 387 GGVVVN----DVVLhflnPNLPFGGVNNSG 412
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
2-528 |
1.71e-31 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 128.00 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 2 ALSSYTKPFFQNEPCPSYEKGSSDRAAIMKAYGELVSSLPVNVPL-EHISKG--VDT---KSIQQVNPANhKQVVAEYIP 75
Cdd:PLN02466 13 SLSASSSALLRSRGRNGGRGRGIRRFSTAAAAVEEPITPPVQVSYtQLLINGqfVDAasgKTFPTLDPRT-GEVIAHVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 76 STRFDVQNAIESALQA--KSAWEN-TPFEdRAAIFLRAAGLVAgKYRHALMAATMVGQGKNIWQAEIDAAAETCDLLRFN 152
Cdd:PLN02466 92 GDAEDVNRAVAAARKAfdEGPWPKmTAYE-RSRILLRFADLLE-KHNDELAALETWDNGKPYEQSAKAELPMFARLFRYY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 153 VQCAMDLFKQQ-PAVNPSGMwnRLEYRPLeGFVYAISPFNFTAL------GATLACGpllmgNVVVWKPSPSAFHSSWLL 225
Cdd:PLN02466 170 AGWADKIHGLTvPADGPHHV--QTLHEPI-GVAGQIIPWNFPLLmfawkvGPALACG-----NTIVLKTAEQTPLSALYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 226 YKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQAtgedkflNFPRIVGETGGKNFHLV 305
Cdd:PLN02466 242 AKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS-------NLKPVTLELGGKSPFIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 306 HKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVI 385
Cdd:PLN02466 315 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 386 eRAKTDSQLTLLCGGKTSKETGYFVHPTIYqtSDAHHEIL--QKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSI 463
Cdd:PLN02466 395 -KSGVESGATLECGGDRFGSKGYYIQPTVF--SNVQDDMLiaQDEIFGPVQSILKFKDLD--EVIRRANNT-RYGLAAGV 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 464 FARDAAAIRYAEDKLRnsAGNFYINTKSTGSVVgqQPFGGMRGSGTNDKVGsVNVLSRFTSVRAI 528
Cdd:PLN02466 469 FTQNLDTANTLSRALR--VGTVWVNCFDVFDAA--IPFGGYKMSGIGREKG-IYSLNNYLQVKAV 528
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
56-515 |
1.11e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 125.33 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANHkQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIfLRAAGLVAGKYRHALMAATMVGQGKnIW 135
Cdd:PLN02315 34 PLVSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEI-VRQIGDALRAKLDYLGRLVSLEMGK-IL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 136 QAEIDAAAETCDLLRFNVQCAMDLFKQQ-PAVNPSGM----WNRLeyrpleGFVYAISPFNF--TALGATlACGPLLMGN 208
Cdd:PLN02315 111 AEGIGEVQEIIDMCDFAVGLSRQLNGSIiPSERPNHMmmevWNPL------GIVGVITAFNFpcAVLGWN-ACIALVCGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 209 VVVWKPSPSAFHSSWLLYKIMIEA----GLPENVLQFVAGDAEaITSTVLENRAFAGLNFTGSSavfkqliaRIGQATGE 284
Cdd:PLN02315 184 CVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAE-IGEAIAKDTRIPLVSFTGSS--------KVGLMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 285 DKFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPED 364
Cdd:PLN02315 255 TVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 365 VTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYFVHPTIYQTSdAHHEILQKEFFGPLLavYVYPDSEW 444
Cdd:PLN02315 335 KGTLLGPLHTPESKKNFEKGIEIIKSQGG-KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTL 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630034702 445 AEITQvIDSTAPYALTGSIFARDAAAIRYAEDKLRNSAGNFYINTKSTGSVVGQQpFGGMRGSGTNDKVGS 515
Cdd:PLN02315 411 EEAIE-INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAGS 479
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
58-510 |
1.13e-30 |
|
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: 124.45 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 58 IQQVNPANHKqvvaeYIPSTRFDVQNAIESALQA-------KSAWenTPFEDRAAIFLRAAGLVAGKYRHalMAATMVGQ 130
Cdd:cd07148 1 LEVVNPFDLK-----PIGEVPTVDWAAIDKALDTahalfldRNNW--LPAHERIAILERLADLMEERADE--LALLIARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 131 GKNIWqaeIDAAAETCDLLRfNVQCAMDLFKQQPAVN-PSGMW----NRLEYRPLE--GFVYAISPFNFTALGATLACGP 203
Cdd:cd07148 72 GGKPL---VDAKVEVTRAID-GVELAADELGQLGGREiPMGLTpasaGRIAFTTREpiGVVVAISAFNHPLNLIVHQVAP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 204 LL-MGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAfAGLNFTGSSAVFKQLIARIGQAT 282
Cdd:cd07148 148 AIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRV-AFFSFIGSARVGWMLRSKLAPGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 283 gedkflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSP 362
Cdd:cd07148 227 ---------RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 363 EDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSKETGYfvHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDs 442
Cdd:cd07148 298 TDPDTEVGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDD- 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 443 ewaeITQVID--STAPYALTGSIFARDAAAIRYAEDKLRNSAgnFYINtKSTGSVVGQQPFGGMRGSGTN 510
Cdd:cd07148 374 ----LDEAIAqaNSLPVAFQAAVFTKDLDVALKAVRRLDATA--VMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
175-541 |
7.78e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 122.44 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 175 LEYRPLeGFVYAISPFNFTALGATLAC-GPLLMGNVVVWKPSPSAFHSSWLLYKiMIEAGLPENVLQFVAGDAEAITStV 253
Cdd:PTZ00381 105 IIPEPL-GVVLVIGAWNYPLNLTLIPLaGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVIEGGVEVTTE-L 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 254 LENRaFAGLNFTGSSAVFKqLIArigQATGEdkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAA 333
Cdd:PTZ00381 182 LKEP-FDHIFFTGSPRVGK-LVM---QAAAE----NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 334 SRLYVPESIWPAFKENLlaKMATIKVGSPEDVT-NFVNPVIHEQSFDKLAAVIEraktDSQLTLLCGGKTSKETGYfVHP 412
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEAL--KEAIKEFFGEDPKKsEDYSRIVNEFHTKRLAELIK----DHGGKVVYGGEVDIENKY-VAP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 413 TIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAAAIRYAEDKlrNSAGNFYINTkst 492
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENID--EVLEFINSR-PKPLALYYFGEDKRHKELVLEN--TSSGAVVIND--- 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 493 gSVV----GQQPFGGM--RGSGTNDKVGSVNVLSRFTSVRAIKEDFEGTPDFRYP 541
Cdd:PTZ00381 398 -CVFhllnPNLPFGGVgnSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYP 451
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
174-508 |
1.01e-26 |
|
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: 112.62 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 174 RLEYRPLeGFVYAISPFNFTALgatLACGPLL----MGNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEaI 249
Cdd:cd07087 95 YVIPEPL-GVVLIIGPWNYPLQ---LALAPLIgaiaAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVE-V 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 250 TSTVLENRaFAGLNFTGSSAVFKqLIARigQATgedKFLNfPrIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQK 329
Cdd:cd07087 169 ATALLAEP-FDHIFFTGSPAVGK-IVME--AAA---KHLT-P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 330 CSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFvNPVIHEQSFDKLAAVIERAKtdsqltLLCGGKTSKETGYF 409
Cdd:cd07087 240 CIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLDDGK------VVIGGQVDKEERYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 410 VhPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDSTAPYALTgsIFARDAAAIRYAEDKLrnSAGNFYINt 489
Cdd:cd07087 313 A-PTILDDVSPDSPLMQEEIFGPILPILTYDDLDEA-IEFINSRPKPLALY--LFSEDKAVQERVLAET--SSGGVCVN- 385
|
330 340
....*....|....*....|....
gi 630034702 490 kstgSVVGQQ-----PFGGMRGSG 508
Cdd:cd07087 386 ----DVLLHAaipnlPFGGVGNSG 405
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
164-509 |
1.59e-26 |
|
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: 111.93 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 164 PAVNPSGMWN---RLEYRPLeGFVYAISPFNFTALgatLACGPLL----MGNVVVWKPSPSAFHSSWLLYKImIEAGLPE 236
Cdd:cd07135 90 VKDGPLAFMFgkpRIRKEPL-GVVLIIGPWNYPVL---LALSPLVgaiaAGCTVVLKPSELTPHTAALLAEL-VPKYLDP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 237 NVLQFVAGDAEAiTSTVLENRaFAGLNFTGSSAVfkqliARIgQATGEDKFLNfPrIVGETGGKNFHLVHKSADIENAVN 316
Cdd:cd07135 165 DAFQVVQGGVPE-TTALLEQK-FDKIFYTGSGRV-----GRI-IAEAAAKHLT-P-VTLELGGKSPVIVTKNADLELAAK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 317 CTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNpVIHEQSFDKLAAVIERAKTDSQLtl 396
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTR-IVNPRHFNRLKSLLDTTKGKVVI-- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 397 lcGGKTSKETgYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWA-EITQVIDSTapyaLTGSIFARDAAAIRYAE 475
Cdd:cd07135 312 --GGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAiKVINSRDTP----LALYIFTDDKSEIDHIL 384
|
330 340 350
....*....|....*....|....*....|....*
gi 630034702 476 DKLRnsAGNFYIN-TKSTGSVVgQQPFGGMRGSGT 509
Cdd:cd07135 385 TRTR--SGGVVINdTLIHVGVD-NAPFGGVGDSGY 416
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
81-528 |
3.02e-26 |
|
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: 111.56 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 81 VQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAGK---YRHALMAATmvGQGkniWQAEIDAAAETCDLLRFNVQCAM 157
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKsydIAAGAVLVT--GKG---WMFAENICGDQVQLRARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 158 DLFKQQPAVNPS---GMWNRLEYRPLeGFVYAISPFNFTALGATL-ACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAG 233
Cdd:cd07084 76 YRIPHEPGNHLGqglKQQSHGYRWPY-GPVLVIGAFNFPLWIPLLqLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 234 -LPENVLQFVAGDAEAiTSTVLENRAFAGLNFTGSSAVFKQLIARIGQAtgedkflnfpRIVGETGGKNFHLVHKSADIE 312
Cdd:cd07084 155 lLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA----------RIYLELAGFNWKVLGPDAQAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 313 NAV--NCtIRSAFEYQGQKCSAASRLYVPESiWP--AFKENLLAKMATIKVGspedvTNFVNPViheQSFDKLAAVIERa 388
Cdd:cd07084 224 DYVawQC-VQDMTACSGQKCTAQSMLFVPEN-WSktPLVEKLKALLARRKLE-----DLLLGPV---QTFTTLAMIAHM- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 389 KTDSQLTLLCGGKTSKET------GYFVHPTIYQTSD---AHHEILQKEFFGPLLAVYVYPDSEWAEITQVIDSTAPyAL 459
Cdd:cd07084 293 ENLLGSVLLFSGKELKNHsipsiyGACVASALFVPIDeilKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG-SL 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 460 TGSIFARDAAAIRYAEDKLRnSAGNFYINTKSTGSV-VGQQPFGGMRGSGTNDKVGSVNVLSRFTSVRAI 528
Cdd:cd07084 372 TAAIYSNDPIFLQELIGNLW-VAGRTYAILRGRTGVaPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
40-536 |
3.82e-26 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 112.53 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 40 LPVNVPLEHISKGVDTKS---IQQVNPANhKQVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAG 116
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSssfIDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 117 KYRHALMAATmVGQGKNIWQAEIDAAAetcDLLRFNVQCAMDLFKQQPAV-NPSGMWNRLEYRPLEGFVYAISPFNFTAL 195
Cdd:PLN02419 189 NMDKLAMNIT-TEQGKTLKDSHGDIFR---GLEVVEHACGMATLQMGEYLpNVSNGVDTYSIREPLGVCAGICPFNFPAM 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 196 GatlacgPLLM-------GNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITStVLENRAFAGLNFTGSS 268
Cdd:PLN02419 265 I------PLWMfpvavtcGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 269 AVFKQLIARiGQATGEdkflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASR-LYVPESiwPAFK 347
Cdd:PLN02419 338 TAGMHIYAR-AAAKGK-------RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 348 ENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQLTLLCGGKT---SKETGYFVHPTIYQTSDAHHEI 424
Cdd:PLN02419 408 DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpGYEKGNFIGPTILSGVTPDMEC 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 425 LQKEFFGPLLAvyVYPDSEWAEITQVIDSTApYALTGSIFARDAAAIRyaEDKLRNSAGNFYINTkstgSVVGQQPFGGM 504
Cdd:PLN02419 488 YKEEIFGPVLV--CMQANSFDEAISIINKNK-YGNGAAIFTSSGAAAR--KFQMDIEAGQIGINV----PIPVPLPFFSF 558
|
490 500 510
....*....|....*....|....*....|....*..
gi 630034702 505 RGSGTNdKVGSVNVLSR-----FTSVRAIKEDFEGTP 536
Cdd:PLN02419 559 TGNKAS-FAGDLNFYGKagvdfFTQIKLVTQKQKDIH 594
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
56-524 |
3.61e-25 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 108.69 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 56 KSIQQVNPANHK---QVVAeyipSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVagKYRHALMAATMVgqgK 132
Cdd:PLN00412 31 KSVAITNPSTRKtqyKVQA----CTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAIL--KEHKAPIAECLV---K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 133 NIWQAEIDAAAE---TCDLLRFnvqCAMD----LFKQQPAVNPSGMWN-RLEY-----RPLeGFVYAISPFNFTALGATL 199
Cdd:PLN00412 102 EIAKPAKDAVTEvvrSGDLISY---TAEEgvriLGEGKFLVSDSFPGNeRNKYcltskIPL-GVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 200 ACGPLLM-GNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSavfkqliari 278
Cdd:PLN00412 178 KIAPALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD---------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 279 gqaTGedkfLNFPRIVG------ETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLA 352
Cdd:PLN00412 248 ---TG----IAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 353 KMATIKVGSPEDVTNfVNPVIHEQSFDKLAAVIERAKtdSQLTLLCggKTSKETGYFVHPTIYQTSDAHHEILQKEFFGP 432
Cdd:PLN00412 321 KVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDAK--EKGATFC--QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 433 LLAVyVYPDSEWAEITQVIDSTapYALTGSIFARDA-AAIRYAEdklRNSAGNFYINTkSTGSVVGQQPFGGMRGSGTND 511
Cdd:PLN00412 396 VLPV-IRINSVEEGIHHCNASN--FGLQGCVFTRDInKAILISD---AMETGTVQINS-APARGPDHFPFQGLKDSGIGS 468
|
490
....*....|....*
gi 630034702 512 K--VGSVNVLSRFTS 524
Cdd:PLN00412 469 QgiTNSINMMTKVKS 483
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
177-508 |
7.64e-25 |
|
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: 107.20 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 177 YRPLeGFVYAISPFNFTALgatLACGPLL----MGNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEaITST 252
Cdd:cd07136 98 YEPY-GVVLIIAPWNYPFQ---LALAPLIgaiaAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVE-ENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 253 VLENRaFAGLNFTGSSAVFK---QLIARigqatgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQK 329
Cdd:cd07136 172 LLDQK-FDYIFFTGSVRVGKivmEAAAK-----------HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 330 CSAASRLYVPESIwpafKENLLAKM-ATIK---VGSPEDVTNFVNpVIHEQSFDKLAAVIERAKtdsqltLLCGGKTSKE 405
Cdd:cd07136 240 CVAPDYVLVHESV----KEKFIKELkEEIKkfyGEDPLESPDYGR-IINEKHFDRLAGLLDNGK------IVFGGNTDRE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 406 TGYfVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTA-PYALTgsIFARDAAAIRYAEDKLrnSAGN 484
Cdd:cd07136 309 TLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLD--EAIEIIKSRPkPLALY--LFSEDKKVEKKVLENL--SFGG 381
|
330 340
....*....|....*....|....
gi 630034702 485 FYINTKSTGSVVGQQPFGGMRGSG 508
Cdd:cd07136 382 GCINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
53-508 |
5.06e-23 |
|
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: 102.15 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 53 VDTKSIQQVNPANHKqVVAEYIPSTRFDVQNAIESALQAKSAWENTPFEDRAAIFLRAAGLVAgKYRHALMAATMVGQGK 132
Cdd:cd07116 13 VKGEYFDNITPVTGK-VFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRME-ANLEMLAVAETWDNGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 133 NIwqaeidaaAETcdlLRFNVQCAMDLFKQQPAV--NPSGMWNRLE--------YRPLeGFVYAISPFNFTALGATLACG 202
Cdd:cd07116 91 PV--------RET---LAADIPLAIDHFRYFAGCirAQEGSISEIDentvayhfHEPL-GVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 203 PLLM-GNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIARIGQa 281
Cdd:cd07116 159 PALAaGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 282 tgedkflNFPRIVGETGGKN----FHLVHKSAD--IENAVNCTIRSAFEyQGQKCSAASRLYVPESIWPAFKENLLAKMA 355
Cdd:cd07116 237 -------NIIPVTLELGGKSpnifFADVMDADDafFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 356 TIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQlTLLCGGKTSK-----ETGYFVHPTIYQTSDAhhEILQKEFF 430
Cdd:cd07116 309 AIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGA-EVLTGGERNElggllGGGYYVPTTFKGGNKM--RIFQEEIF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 630034702 431 GPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAA-AIRYAEDKlrnSAGNFYINTKStgSVVGQQPFGGMRGSG 508
Cdd:cd07116 386 GPVLAVTTFKDEE--EALEIANDT-LYGLGAGVWTRDGNtAYRMGRGI---QAGRVWTNCYH--LYPAHAAFGGYKQSG 456
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
179-445 |
8.27e-19 |
|
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: 89.64 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLEGFVYAISPFNFTALGATLACGPLLMGNV-VVWKPSPSAFHSSWLLYKIMIEAG-LPENVLQFVAGDAEAITSTVLEN 256
Cdd:cd07128 143 PRRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 257 RAFAglnFTGSSAVFKQL------IARIGQATGEDKFLNFPrIVGET---GGKNFHLVHKsadiENAVNCTIRSafeyqG 327
Cdd:cd07128 223 DVVA---FTGSAATAAKLrahpniVARSIRFNAEADSLNAA-ILGPDatpGTPEFDLFVK----EVAREMTVKA-----G 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 328 QKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVI-HEQSFDKLAAVierAKTDSQLTLLCGGKTS--- 403
Cdd:cd07128 290 QKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVsREQREDVRAAV---ATLLAEAEVVFGGPDRfev 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 630034702 404 ----KETGYFVHPTIYQTSDAH-----HEIlqkEFFGPLLAVYVYPDSEWA 445
Cdd:cd07128 367 vgadAEKGAFFPPTLLLCDDPDaatavHDV---EAFGPVATLMPYDSLAEA 414
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
179-502 |
3.92e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 81.29 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLEGFVYAISPFNFTALG-ATLACGPLLMGNVVVWKPspsAFHSSWLLYKIM---IEAG-LPENVLQFVAGDAEAITSTV 253
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGlWEKAAPALLAGVPVIVKP---ATATAWLTQRMVkdvVAAGiLPAGALSVVCGSSAGLLDHL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 254 lenRAFAGLNFTGSSAVFKQL------IARIGQATGEDKFLNfPRIVG---ETGGKNFHLVHKsadiENAVNCTIRSafe 324
Cdd:PRK11903 224 ---QPFDVVSFTGSAETAAVLrshpavVQRSVRVNVEADSLN-SALLGpdaAPGSEAFDLFVK----EVVREMTVKS--- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 325 yqGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFVNPVIHEQSFDKLAAVIERAKTDSQltLLCGGKTSK 404
Cdd:PRK11903 293 --GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAE--VLFDGGGFA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 405 ------ETGYFVHPTIYQTSD--AHHEILQKEFFGPLLAVYVYPDSEWAeITQVIDSTApyALTGSIFARDAAAIRYAED 476
Cdd:PRK11903 369 lvdadpAVAACVGPTLLGASDpdAATAVHDVEVFGPVATLLPYRDAAHA-LALARRGQG--SLVASVYSDDAAFLAAAAL 445
|
330 340
....*....|....*....|....*.
gi 630034702 477 KLRNSAGNFYINTKStgsvVGQQPFG 502
Cdd:PRK11903 446 ELADSHGRVHVISPD----VAALHTG 467
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
179-508 |
7.12e-14 |
|
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: 73.79 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLeGFVYAISPFNFtALGATLA--CGPLLMGNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEAiTSTVLEN 256
Cdd:cd07132 100 PL-GVVLIIGAWNY-PLQLTLVplVGAIAAGNCVVIKPSEVSPATAKLLAEL-IPKYLDKECYPVVLGGVEE-TTELLKQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 257 RaFAGLNFTGSSAVFKQliarIGQATGedKFLNfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAasrl 336
Cdd:cd07132 176 R-FDYIFYTGSTSVGKI----VMQAAA--KHLT--PVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 337 yvPESIW--PAFKENLLAKM-ATIKVGSPEDVTNFVN--PVIHEQSFDKLAAVIERAKtdsqltLLCGGKTSKETGYfVH 411
Cdd:cd07132 243 --PDYVLctPEVQEKFVEALkKTLKEFYGEDPKESPDygRIINDRHFQRLKKLLSGGK------VAIGGQTDEKERY-IA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 412 PTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDS-TAPYALTgsIFARDAAAIRYAEDklRNSAGNFYINTK 490
Cdd:cd07132 314 PTVLTDVKPSDPVMQEEIFGPILPIVTVNNLD--EAIEFINSrEKPLALY--VFSNNKKVINKILS--NTSSGGVCVNDT 387
|
330
....*....|....*...
gi 630034702 491 STGSVVGQQPFGGMRGSG 508
Cdd:cd07132 388 IMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
177-532 |
8.03e-12 |
|
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: 67.52 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 177 YRPLEGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMIEAGLPENVLQFVAGDAEAITSTVLE 255
Cdd:cd07126 139 YRWPYGPVAIITPFNFPlEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 256 NRaFAGLNFTGSSAVFKQLIARI-GQATGEDKFLNFpRIVGETGGkNFHLVHKSADienavnctiRSAFEYQGQKCSAAS 334
Cdd:cd07126 219 AN-PRMTLFTGSSKVAERLALELhGKVKLEDAGFDW-KILGPDVS-DVDYVAWQCD---------QDAYACSGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 335 RLYVPESiWpaFKENLLAKMATIKVG-SPEDVTnfVNPVIH------EQSFDKLAAvIERAKtdsqltLLCGGKTSKE-- 405
Cdd:cd07126 287 ILFAHEN-W--VQAGILDKLKALAEQrKLEDLT--IGPVLTwtteriLDHVDKLLA-IPGAK------VLFGGKPLTNhs 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 406 ----------TGYFVhPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEWAEITQVIDSTaPYALTGSIFARDaaaIRYAE 475
Cdd:cd07126 355 ipsiygayepTAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERM-HAHLTAAVVSND---IRFLQ 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 630034702 476 DKLRNSA-GNFY--INTKSTGSVVGQ--QPFGGMRGSGtndkVGSVN-VLSRFTSVRAIKEDF 532
Cdd:cd07126 430 EVLANTVnGTTYagIRARTTGAPQNHwfGPAGDPRGAG----IGTPEaIRLVWSCHREIITDI 488
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
165-509 |
6.25e-10 |
|
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: 61.27 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 165 AVNPSgmWNRLEYRPLeGFVYAISPFNFTALgatLACGPLL----MGNVVVWKPSPSAFHSSWLLYKiMIEAGLPENVLQ 240
Cdd:cd07137 89 TTFPA--KAEIVSEPL-GVVLVISAWNFPFL---LSLEPVIgaiaAGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 241 FVAGDAeAITSTVLENRaFAGLNFTGSSAvfkqlIARIGQATGEDkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIR 320
Cdd:cd07137 162 VIEGGV-PETTALLEQK-WDKIFFTGSPR-----VGRIIMAAAAK---HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 321 SAF-EYQGQKCSAASRLYVPESIWPAFKENL---LAKMATIKVGSPEDVTNFVNpvihEQSFDKLAAVIERAKTDSQltL 396
Cdd:cd07137 232 GKWgCNNGQACIAPDYVLVEESFAPTLIDALkntLEKFFGENPKESKDLSRIVN----SHHFQRLSRLLDDPSVADK--I 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 397 LCGGkTSKETGYFVHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIdSTAPYALTGSIFARDAAAIRYAED 476
Cdd:cd07137 306 VHGG-ERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIE--ESIEII-NSRPKPLAAYVFTKNKELKRRIVA 381
|
330 340 350
....*....|....*....|....*....|...
gi 630034702 477 KLrnSAGNFYINTKSTGSVVGQQPFGGMRGSGT 509
Cdd:cd07137 382 ET--SSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
179-541 |
1.24e-09 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 60.44 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLeGFVYAISPFNFT-ALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIMiEAGLPENVLQFVAGdAEAITSTVLENR 257
Cdd:PLN02174 112 PL-GVVLVISAWNYPfLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEG-AVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 258 aFAGLNFTGSSAVFKQLIARIGQatgedkflNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFE-YQGQKCSAASRL 336
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMAAAAK--------HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 337 YVPESIWPAFKENLLAKMATIKVGSPEDVTNfVNPVIHEQSFDKLAAVIERAKTDSQLTLlcGGKTSKETgYFVHPTIYQ 416
Cdd:PLN02174 260 LTTKEYAPKVIDAMKKELETFYGKNPMESKD-MSRIVNSTHFDRLSKLLDEKEVSDKIVY--GGEKDREN-LKIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 417 TSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAA-AIRYAEDKlrnSAGNFYINTKSTGSV 495
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLE--ESFDVIRSR-PKPLAAYLFTHNKKlKERFAATV---SAGGIVVNDIAVHLA 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 630034702 496 VGQQPFGGMRGSGTNDKVGSVNvLSRFTSVRAI-KEDFEGTPDFRYP 541
Cdd:PLN02174 410 LHTLPFGGVGESGMGAYHGKFS-FDAFSHKKAVlYRSLFGDSAVRYP 455
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
179-541 |
8.42e-09 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 57.81 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 179 PLeGFVYAISPFNFtALGATL--ACGPLLMGNVVVWKPSPSAFHSSWLLYKImIEAGLPENVLQFVAGDAEaITSTVLEN 256
Cdd:PLN02203 108 PL-GVVLIFSSWNF-PIGLSLepLIGAIAAGNAVVLKPSELAPATSAFLAAN-IPKYLDSKAVKVIEGGPA-VGEQLLQH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 257 RaFAGLNFTGSSAVFKQLIARIGQatgedkflNFPRIVGETGGKN---FHLVHKSADIENAVNCTIRSAFEY-QGQKCSA 332
Cdd:PLN02203 184 K-WDKIFFTGSPRVGRIIMTAAAK--------HLTPVALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 333 ASRLYVPESIWPAFKENL---LAKMATIKVGSPEDVTNFVNpvihEQSFDKLAAVIERAKTdsQLTLLCGGKTSKETgYF 409
Cdd:PLN02203 255 IDYVLVEERFAPILIELLkstIKKFFGENPRESKSMARILN----KKHFQRLSNLLKDPRV--AASIVHGGSIDEKK-LF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 410 VHPTIYQTSDAHHEILQKEFFGPLLAVYVYPDSEwaEITQVIDSTaPYALTGSIFARDAAAIRYAEDKlrNSAGNFYINT 489
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIE--DSIAFINSK-PKPLAIYAFTNNEKLKRRILSE--TSSGSVTFND 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 630034702 490 KSTGSVVGQQPFGGMRGSGTNDKVG--SVNVLSRFTSV--RAIKEDFEgtpdFRYP 541
Cdd:PLN02203 403 AIIQYACDSLPFGGVGESGFGRYHGkySFDTFSHEKAVlrRSLLTEFE----FRYP 454
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
204-510 |
3.22e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 52.87 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 204 LLMGNVVVWKPSPSAFHSSWLLYKI----MIEAGLPENVLQFVAGDAEA-ITSTVLENRAFAGLNFTGSSAVFKQLIARI 278
Cdd:cd07127 218 LATGNPVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWLEANA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 279 GQAtgedkflnfpRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQGQKCSAASRLYVP------ESIWPAFKENLLA 352
Cdd:cd07127 298 RQA----------QVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgiqtDDGRKSFDEVAAD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 353 KMATIK--VGSPEDVTNFVNPVIHEQSfdklAAVIERAktdSQLTLLCGGKTSKETGYF----VH-PTIYQTSDAHHEIL 425
Cdd:cd07127 368 LAAAIDglLADPARAAALLGAIQSPDT----LARIAEA---RQLGEVLLASEAVAHPEFpdarVRtPLLLKLDASDEAAY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 426 QKEFFGPLLAVyVYPDSEWAEITQVIDSTAPY-ALTGSIFARDAAAIRYAEDKLRNSAGNFYINTksTGSVVGQQP--FG 502
Cdd:cd07127 441 AEERFGPIAFV-VATDSTDHSIELARESVREHgAMTVGVYSTDPEVVERVQEAALDAGVALSINL--TGGVFVNQSaaFS 517
|
....*...
gi 630034702 503 GMRGSGTN 510
Cdd:cd07127 518 DFHGTGAN 525
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
182-365 |
3.97e-06 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 49.14 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 182 GFVYAISPFNFTALGATLACGPLLMGNVVVWKPSPSAFHSSW---LLYKIMIEAGLPENVLQFVAgDAEAITSTVLenra 258
Cdd:cd07077 102 GVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPFTNRalaLLFQAADAAHGPKILVLYVP-HPSDELAEEL---- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 259 fagLNFTGSSAVfkqlIARIGQATGED--KFLNFPRIVGETGGKNFHLVHKSADIENAVNCTIRSAFEYQgQKCSAASRL 336
Cdd:cd07077 177 ---LSHPKIDLI----VATGGRDAVDAavKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NACASEQNL 248
|
170 180
....*....|....*....|....*....
gi 630034702 337 YVPESIWPAFKENLLAKMATIKVGSPEDV 365
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVVEGLKVPQET 277
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
84-437 |
7.88e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.42 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 84 AIESALQAKSAWENTPFEDRAAIFlRAAGLVAGKYRHAL--MAATMVGQG-------KNIWQAEIDAAAEtCDLLRFNVQ 154
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIF-RAAAEAAEDARIDLakLAVSETGMGrvedkviKNHFAAEYIYNVY-KDEKTCGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 155 CAMDLFKQQPAVNPSGMwnrleyrplegfVYAISPF-NFTALGATLACGPLLMGNVVVWKPSPSAFHSSWLLYKIM---- 229
Cdd:cd07081 82 TGDENGGTLIIAEPIGV------------VASITPStNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLlqaa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 230 IEAGLPENVLQFVAGDAEAITSTVLEnraFAGLNFtgssavfkqLIARIGQATGEDKFLNFPRIVGETGGKNFHLVHKSA 309
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMK---FPGIGL---------LLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 310 DIENAVNCTIRSAFEYQGQKCSAASRLYVPESIWPAFKENLLAKMATIKVGSPEDVTNFV-------NPVIHEQSFDKLA 382
Cdd:cd07081 218 DIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVilkngdvNRDIVGQDAYKIA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 630034702 383 AVIeraktdsqltllcGGKTSKETGYFVHPTiyqTSDAHHEILQKEFFGPLLAVY 437
Cdd:cd07081 298 AAA-------------GLKVPQETRILIGEV---TSLAEHEPFAHEKLSPVLAMY 336
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
80-352 |
4.46e-03 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 39.53 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 80 DVQNAIESALQAKSAWENTPFEDRAAIF--LRAAgLVAGKYRHALMAATMVGQG-------KNIWQAEIDAAAEtcdllr 150
Cdd:cd07121 5 TVDDAVAAAKAAQKQYRKCTLADREKIIeaIREA-LLSNAEELAEMAVEETGMGrvedkiaKNHLAAEKTPGTE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 151 fnvqcamDLfkQQPAVNPSGMWNRLEYRPLeGFVYAISPFnfTALGATLACGPLLM---GNVVVWKPSPSAFH-SSW--- 223
Cdd:cd07121 78 -------DL--TTTAWSGDNGLTLVEYAPF-GVIGAITPS--TNPTETIINNSISMlaaGNAVVFNPHPGAKKvSAYave 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630034702 224 LLYKIMIEAGLPENVLQFVAGDAEAITSTVLENRAFAGLNFTGSSAVFKQLIAR----IGQATGedkflNFPRIVGETgg 299
Cdd:cd07121 146 LINKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSgkkaIGAGAG-----NPPVVVDET-- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 630034702 300 knfhlvhksADIENAVNCTIRSA-FEYQgQKCSAASRLYVPESIWPAFKENLLA 352
Cdd:cd07121 219 ---------ADIEKAARDIVQGAsFDNN-LPCIAEKEVIAVDSVADYLIAAMQR 262
|
|
| |
