|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-518 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 1010.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 11 YKHEPFTDFTLEENKKEFKKALETVHSQLGKDYPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALS 90
Cdd:PRK03137 5 YKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 91 TFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEE 170
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDY 250
Cdd:PRK03137 165 NRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 251 LVQHPKTRFVSFTGSREVGCRIYEKASKVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGS 330
Cdd:PRK03137 245 LVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 331 RAVVHQDVYDIVLEKAVALTKTLKVGNPEDVsTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDSKGYFIQPTIFA 410
Cdd:PRK03137 325 RAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPTIFA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 411 DVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPF 490
Cdd:PRK03137 404 DVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPF 483
|
490 500
....*....|....*....|....*...
gi 1267504047 491 GGFNMSGTDSKAGGPDYLILHMQAKTTS 518
Cdd:PRK03137 484 GGFNMSGTDSKAGGPDYLLLFLQAKTVS 511
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-518 |
0e+00 |
|
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: 858.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 11 YKHEPFTDFTLEENKKEFKKALETVHSQLGKDYPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALS 90
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 91 TFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKdGVPVQSREGEE 170
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLR-GFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDY 250
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 251 LVQHPKTRFVSFTGSREVGCRIYEKASKVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGS 330
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 331 RAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADD--SKGYFIQPTI 408
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLElaAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 409 FADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYH 488
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|
gi 1267504047 489 PFGGFNMSGTDSKAGGPDYLILHMQAKTTS 518
Cdd:cd07124 480 PFGGFKMSGTGSKAGGPDYLLQFMQPKTVT 509
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
11-518 |
0e+00 |
|
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: 818.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 11 YKHEPFTDFTLEENKKEFKKALETVHSQLGKDYPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALS 90
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 91 TFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEE 170
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDY 250
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 251 LVQHPKTRFVSFTGSREVGCRIYEKASKVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGS 330
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 331 RAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDSKGYFIQPTIFA 410
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 411 DVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPF 490
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500
....*....|....*....|....*...
gi 1267504047 491 GGFNMSGTDSKAGGPDYLILHMQAKTTS 518
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVT 508
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
54-516 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 532.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 54 TDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW 133
Cdd:pfam00171 5 ESETIEVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 134 NEADADTAEAIDFLEFYARQMLKLkDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPA 213
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 214 DATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEM 293
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTG 452
Cdd:pfam00171 317 LERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267504047 453 ALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGyHPFGGFNMSGTdSKAGGPDYLILHMQAKT 516
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADG-LPFGGFKQSGF-GREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-521 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 522.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 41 KDYPLVIGEELIT--TDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRK 118
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPATG-EVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 119 HEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTA 198
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 199 AAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASk 278
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 279 vqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNP 358
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 359 EDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEA-DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDF 436
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 437 DHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAiVGYHPFGGFNMSGTDSKaGGPDYLILHMQAKT 516
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
....*
gi 1267504047 517 TSTAL 521
Cdd:COG1012 475 VTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
28-516 |
4.07e-168 |
|
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: 484.78 E-value: 4.07e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 28 FKKALETVHSQLGKDYPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANIL 107
Cdd:cd07083 4 MREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 108 FRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVP-VQSREGEENKFNYIPLGVGIIISP 186
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGLGAGVVISP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 187 FNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSR 266
Cdd:cd07083 164 WNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 267 EVGCRIYEKASKVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKA 346
Cdd:cd07083 244 ETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 347 VALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGP 426
Cdd:cd07083 324 LKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 427 V--VAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGG 504
Cdd:cd07083 404 VlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGG 483
|
490
....*....|..
gi 1267504047 505 PDYLILHMQAKT 516
Cdd:cd07083 484 PHYLRRFLEMKA 495
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-516 |
2.53e-151 |
|
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: 439.72 E-value: 2.53e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 82 EKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGV 161
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 162 PVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIP 241
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 242 GVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASkvqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGF 321
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA------ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 322 SGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDS- 399
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 400 KGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRG 479
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1267504047 480 CTGAIVGYhPFGGFNMSGTdSKAGGPDYLILHMQAKT 516
Cdd:cd07078 395 SVGAEPSA-PFGGVKQSGI-GREGGPYGLEEYTEPKT 429
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
19-519 |
3.37e-143 |
|
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: 421.99 E-value: 3.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 19 FTLEENKKEFKKALETVHSQLGKDYPLVIGEELITTDEKIVsINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKE 98
Cdd:cd07125 10 FDLEVPLEALADALKAFDEKEWEAIPIINGEETETGEGAPV-IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 99 NPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPL 178
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 179 GVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTR 258
Cdd:cd07125 169 GVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 259 FVSFTGSREVGCRIyekaskvqpgQKWLK-------RVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSR 331
Cdd:cd07125 249 GVIFTGSTETAKLI----------NRALAerdgpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 332 AVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDSKGYFIQPTIFAD 411
Cdd:cd07125 319 LYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 412 VdeKARLMQEEIFGPV--VAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHP 489
Cdd:cd07125 399 V--GIFDLTTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQP 476
|
490 500 510
....*....|....*....|....*....|
gi 1267504047 490 FGGFNMSGTDSKAGGPDYLILHMQAKTTST 519
Cdd:cd07125 477 FGGWGLSGTGPKAGGPNYLLRFGNEKTVSL 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-516 |
1.85e-138 |
|
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: 408.18 E-value: 1.85e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 43 YPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFS 122
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 123 SYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKdGVPVQS-REGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAA 201
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLS-GETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 202 IVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQp 281
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 282 gqkwlKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDV 361
Cdd:cd07097 239 -----ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 362 STYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDS--KGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDH 438
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267504047 439 MMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGaiVGYH-PFGGFNMSGTDSKAGGPDYLILHMQAKT 516
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALEFYTTIKT 470
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
54-505 |
1.66e-128 |
|
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: 382.85 E-value: 1.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 54 TDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW 133
Cdd:cd07131 12 SGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 134 NEADADTAEAIDFLEFYARQMLKLKdGVPVQSREgeENKFNY---IPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILL 210
Cdd:cd07131 92 AEGRGDVQEAIDMAQYAAGEGRRLF-GETVPSEL--PNKDAMtrrQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 211 KPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwlKRVI 290
Cdd:cd07131 169 KPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN------KRVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 291 AEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSH 370
Cdd:cd07131 243 LEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 371 EASYNKVLSYIEIGKEEG-RLMTGGEA----DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANN 445
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGaTLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAND 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 446 TDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVgyH-PFGGFNMSGTDSKAGGP 505
Cdd:cd07131 403 TEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV--HlPFGGVKKSGNGHREAGT 461
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-509 |
1.07e-122 |
|
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: 369.61 E-value: 1.07e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 12 KHEPFTDFTL-EENKKEFKKALETVHSqLGKDYPLVIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALS 90
Cdd:cd07123 2 VNEPVLSYAPgSPERAKLQEALAELKS-LTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 91 TFNTWKKENPEVRANILFRAADIIR-RRKHEFSSYLVKEAGKPWNEADADTA-EAIDFLEFYARQMLKLKDGVPVQSREG 168
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 169 EENKFNYIPL-GVGIIISPFNFPLAIMAGTAAAAIVtGNTILLKPADaTPVVAAKFV-EVMEEAGLPKGVLNFIPGVTPE 246
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 247 IGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKC 326
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 327 SAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKE--EGRLMTGGEADDSKGYFI 404
Cdd:cd07123 319 SAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 405 QPTIFADVDEKARLMQEEIFGPVVAF--CKARDFDHMMEIANNT-DYALTGALLSSTPAHIERAKEEFH--VGNLYFNRG 479
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDK 478
|
490 500 510
....*....|....*....|....*....|
gi 1267504047 480 CTGAIVGYHPFGGFNMSGTDSKAGGPDYLI 509
Cdd:cd07123 479 PTGAVVGQQPFGGARASGTNDKAGSPLNLL 508
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
45-497 |
8.55e-117 |
|
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: 353.05 E-value: 8.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 45 LVIGEELI--TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHE 120
Cdd:cd07091 6 LFINNEFVdsVSGKTFPTINPATE-EVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 121 FSSYLVKEAGKPWNE-ADADTAEAIDFLEFYArqmlKLKDGVPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAG 196
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYA----GWADKIQGKTIPIDGNFLAYTrrePIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 197 TAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKA 276
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 277 SKVQpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVG 356
Cdd:cd07091 241 AKSN-----LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 357 NPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARD 435
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267504047 436 FDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgcTGAIVGYH-PFGGFNMSG 497
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
60-517 |
1.86e-116 |
|
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: 351.47 E-value: 1.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD 137
Cdd:cd07114 1 SINPATG-EPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 138 ADTAEAIDFLEFYARQMLKLKDGV-PVQSRegeeNKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPA 213
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAViPVDKG----DYLNFTrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 214 DATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEM 293
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGE----ADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDY 448
Cdd:cd07114 310 LEKVERYVARAREEGaRVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEY 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 449 ALTGALLSSTPAHIERAKEEFHVGNLYFNrgctgaivGYH------PFGGFNMSGTDsKAGGPDYLILHMQAKTT 517
Cdd:cd07114 390 GLAAGIWTRDLARAHRVARAIEAGTVWVN--------TYRalspssPFGGFKDSGIG-RENGIEAIREYTQTKSV 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
53-512 |
7.80e-114 |
|
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: 345.02 E-value: 7.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 53 TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKP 132
Cdd:cd07088 10 SSGETIDVLNPATG-EVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 133 WNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKP 212
Cdd:cd07088 89 LSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 213 ADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAE 292
Cdd:cd07088 169 SEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEN------ITKVSLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 293 MGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEA 372
Cdd:cd07088 243 LGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 373 SYNKVLSYIEIGKEEG-RLMTGGEADDS-KGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYAL 450
Cdd:cd07088 323 ALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 451 TGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHpfGGFNMSGT---DSKAGGPDYLILHM 512
Cdd:cd07088 403 TSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHGLEEYLQTKV 465
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-497 |
1.56e-113 |
|
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: 343.65 E-value: 1.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07103 2 INPATG-EVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYARQMLKLkDGVPVQSREGeeNKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATP 217
Cdd:cd07103 81 DYAASFLEWFAEEARRI-YGRTIPSPAP--GKRILVikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 218 VVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKD 297
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT------VKRVSLELGGNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 298 TVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKV 377
Cdd:cd07103 232 PFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 378 LSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLS 456
Cdd:cd07103 312 EALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1267504047 457 STPAHIERAKEEFHVGNLYFNRGCTGAIVGyhPFGGFNMSG 497
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGINTGLISDAEA--PFGGVKESG 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
68-512 |
5.89e-113 |
|
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: 342.27 E-value: 5.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFL 147
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 EFYARQMLKLK-DGVPVQSREGEENKFNY---IPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKF 223
Cdd:cd07149 90 RLSAEEAKRLAgETIPFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 224 VEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASkvqpgqkwLKRVIAEMGGKDTVVVDK 303
Cdd:cd07149 170 AELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 304 DADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEI 383
Cdd:cd07149 242 DADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 384 GKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHI 462
Cdd:cd07149 322 AVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1267504047 463 ERAKEEFHVGNLYFNRGCTgAIVGYHPFGGFNMSGTDSKagGPDYLILHM 512
Cdd:cd07149 399 LKAARELEVGGVMINDSST-FRVDHMPYGGVKESGTGRE--GPRYAIEEM 445
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
60-517 |
1.99e-110 |
|
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: 335.69 E-value: 1.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA- 138
Cdd:cd07093 1 NFNPATG-EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYArQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPV 218
Cdd:cd07093 80 DIPRAAANFRFFA-DYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 219 VAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDT 298
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 299 VVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVL 378
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 379 SYIEIGKEEG-RLMTGG----EADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGA 453
Cdd:cd07093 313 GYVELARAEGaTILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 454 LLSSTPAHIERAKEEFHVG----NLYFNRGCTGaivgyhPFGGFNMSGTdSKAGGPDYLILHMQAKTT 517
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGtvwvNCWLVRDLRT------PFGGVKASGI-GREGGDYSLEFYTELKNV 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
81-505 |
3.38e-110 |
|
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: 334.50 E-value: 3.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 81 AEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLeFYARQMLKLKDG 160
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL-REAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 161 VPVQSreGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAA-KFVEVMEEAGLPKGV 236
Cdd:cd07104 81 EILPS--DVPGKESMVrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 237 LNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVY 316
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 317 SAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGE 395
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 396 ADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTpahIERAK---EEFHVG 472
Cdd:cd07104 313 YE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRD---LERAMafaERLETG 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 1267504047 473 NLYFNrGCT---GAIVgyhPFGGFNMSGTdSKAGGP 505
Cdd:cd07104 387 MVHIN-DQTvndEPHV---PFGGVKASGG-GRFGGP 417
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
86-516 |
1.53e-109 |
|
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: 330.35 E-value: 1.53e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 86 QTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQS 165
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 166 REGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTP 245
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 246 EIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQK 325
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN------LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 326 CSAGSRAVVHQDVYDIVLEKAValtktlkvgnpedvstymgpvsheasynkvlsyieigkeegrlmtggeaddskgyfiq 405
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 406 pTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIV 485
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP 335
|
410 420 430
....*....|....*....|....*....|.
gi 1267504047 486 GYhPFGGFNMSGTdSKAGGPDYLILHMQAKT 516
Cdd:cd06534 336 EA-PFGGVKNSGI-GREGGPYGLEEYTRTKT 364
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
56-497 |
4.07e-108 |
|
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: 330.68 E-value: 4.07e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 56 EKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNE 135
Cdd:cd07086 13 ETFTSRNPANG-EPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 136 ADADTAEAIDFLEFYA---RQMlklkDGVPVQS-REGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLK 211
Cdd:cd07086 92 GLGEVQEMIDICDYAVglsRML----YGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 212 PADATPVVAAKFVEVMEEA----GLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGCRIYEKAskvqpgQKWLK 287
Cdd:cd07086 168 PSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETV------ARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 288 RVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGP 367
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 368 VSHEASYNKVLSYIEIGKEEG-RLMTGGEA--DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIAN 444
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGgTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 445 NTDYALTGALLSSTPAHIERA--KEEFHVGNLYFNRGCTGAIVGYhPFGGFNMSG 497
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGG-AFGGEKETG 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
62-497 |
1.36e-107 |
|
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: 328.52 E-value: 1.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 62 NPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTA 141
Cdd:cd07150 5 NPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 142 EAIDFLEFYARQMLKLKDGVPVQSREGeenKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPV 218
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPG---TVSMSvrrPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 219 VAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDT 298
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRH------LKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 299 VVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVL 378
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 379 SYIEIGKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSS 457
Cdd:cd07150 315 RQVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1267504047 458 tpaHIERA---KEEFHVGNLYFNrgCTGAIVGYH-PFGGFNMSG 497
Cdd:cd07150 392 ---DLQRAfklAERLESGMVHIN--DPTILDEAHvPFGGVKASG 430
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
12-508 |
5.80e-107 |
|
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: 329.44 E-value: 5.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 12 KHEPFTDFTLEENKKE-FKKALETVHSQLgKDYPLVIG-EELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTAL 89
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDlLRKSLKELKSSS-LEIPLVIGgEEVYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 90 STFNTWKKENPEVRANILFRAADIIR-RRKHEFSSYLVKEAGK-PWnEADADT-AEAIDFLEFYARQMLKLKDGVPVqSR 166
Cdd:TIGR01236 80 DAKKDWSNLPFYDRAAIFLKAADLLSgPYRYEILAATMLGQSKtVY-QAEIDAvAELIDFFRFNVKYARELYAQQPI-SA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 167 EGEENKFNYIPL-GVGIIISPFNFPLAIMAGTAAAAIVtGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTP 245
Cdd:TIGR01236 158 PGEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 246 EIGDYLVQHPKTRFVSFTGSREVGCRIYEK-ASKVQPGQKWlKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQ 324
Cdd:TIGR01236 237 QVSDQVLADPDLAGIHFTGSTNTFKHLWKKvAQNLDRYHNF-PRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 325 KCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGK---EEGRLMTGGEADDSKG 401
Cdd:TIGR01236 316 KCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKkdpEALTILYGGKYDDSQG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 402 YFIQPTIFADVDEKARLMQEEIFGPVVAFCKARD--FDHMMEIANNT-DYALTGALLSSTPAHIERAKE--EFHVGNLYF 476
Cdd:TIGR01236 396 YFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVDSTsQYGLTGAVFAKDRKAILEADKklRFAAGNFYI 475
|
490 500 510
....*....|....*....|....*....|..
gi 1267504047 477 NRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 508
Cdd:TIGR01236 476 NDKCTGAVVGQQPFGGARMSGTNDKAGGPNNL 507
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
60-497 |
2.76e-106 |
|
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: 325.16 E-value: 2.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA-DA 138
Cdd:cd07115 1 TLNPATG-ELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLKLK-DGVPVQSRegeenKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPAD 214
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEgEVIPVRGP-----FLNYTvrePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 215 ATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIyekaskVQPGQKWLKRVIAEMG 294
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKI------MQGAAGNLKRVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 295 GKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASY 374
Cdd:cd07115 229 GKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 375 NKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGA 453
Cdd:cd07115 309 DRVLDYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1267504047 454 LLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
61-497 |
1.01e-105 |
|
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: 324.07 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07138 19 INPATE-EVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AE-AIDFLEFYARQMlklkDGVPVQSREGEeNKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVV 219
Cdd:cd07138 98 VGlGIGHLRAAADAL----KDFEFEERRGN-SLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 220 AAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTV 299
Cdd:cd07138 173 AIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT------VKRVALELGGKSAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 300 VVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLS 379
Cdd:cd07138 247 IILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 380 YIEIGKEEG-RLMTGG-EADD--SKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALL 455
Cdd:cd07138 327 YIQKGIEEGaRLVAGGpGRPEglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVW 406
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1267504047 456 SSTPAHIERAKEEFHVGNLYFNrgctGAIVGYH-PFGGFNMSG 497
Cdd:cd07138 407 SADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSG 445
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
61-497 |
1.26e-105 |
|
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: 324.26 E-value: 1.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA 138
Cdd:cd07119 18 INPANG-EVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLKLKDGV-----PVQSREGEEnkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPA 213
Cdd:cd07119 97 DIDDVANCFRYYAGLATKETGEVydvppHVISRTVRE------PVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 214 DATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEM 293
Cdd:cd07119 171 EVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07119 245 GGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADD----SKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDY 448
Cdd:cd07119 325 REKVLSYIQLGKEEGaRLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPY 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 449 ALTGALLSSTPAHIERAKEEFHVGNLYFNRgctgaivgYH------PFGGFNMSG 497
Cdd:cd07119 405 GLAGAVWTKDIARANRVARRLRAGTVWIND--------YHpyfaeaPWGGYKQSG 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
56-517 |
3.08e-103 |
|
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: 317.62 E-value: 3.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 56 EKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFN--TWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW 133
Cdd:cd07112 2 ETFATINPATG-RVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 134 NEA-DADTAEAIDFLEFYARQMLKLKDGV-PVqsregEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTI 208
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYAEAIDKVYGEVaPT-----GPDALALItrePLGVVGAVVPWNFPLLMAAWKIAPALAAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 209 LLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKAskvqpGQKWLKR 288
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS-----GQSNLKR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 289 VIAEMGGKDTVVVDKDA-DLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGP 367
Cdd:cd07112 231 VWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 368 VSHEASYNKVLSYIEIGKEEG-RLMTGGEAD--DSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIAN 444
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 445 NTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtdskaGGPDyLILH-----MQAKTT 517
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG-----NGRD-KSLHaldkyTELKTT 460
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
61-516 |
4.20e-102 |
|
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: 314.57 E-value: 4.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWK-KENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKP-WNEADA 138
Cdd:cd07089 2 INPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLK--LKDGVPVQSREGEEN--KFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPAD 214
Cdd:cd07089 81 QVDGPIGHLRYFADLADSfpWEFDLPVPALRGGPGrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 215 ATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMG 294
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 295 GKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASY 374
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 375 NKVLSYIEIGKEEG-RLMTGGEADDS--KGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALT 451
Cdd:cd07089 315 DRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 452 GALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIvgYHPFGGFNMSGTdSKAGGPDYLILHMQAKT 516
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGL-GRENGIEGLEEFLETKS 456
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
28-519 |
2.66e-100 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 324.84 E-value: 2.66e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 28 FKKALETVHSQLGKDYPLVIGeelitTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANIL 107
Cdd:PRK11904 539 LAAAIAAFLEKQWQAGPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAIL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 108 FRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKL-KDGVPVQSREGEENKFNYIPLGVGIIISP 186
Cdd:PRK11904 614 ERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLfGAPEKLPGPTGESNELRLHGRGVFVCISP 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 187 FNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSR 266
Cdd:PRK11904 694 WNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGST 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 267 EVGCRI----YEKASKVQPgqkwlkrVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIV 342
Cdd:PRK11904 774 ETARIInrtlAARDGPIVP-------LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 343 LEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDS--KGYFIQPTIF--ADVDEkarl 418
Cdd:PRK11904 847 IEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGteNGHFVAPTAFeiDSISQ---- 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 419 MQEEIFGPV--VAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMS 496
Cdd:PRK11904 923 LEREVFGPIlhVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS 1002
|
490 500
....*....|....*....|...
gi 1267504047 497 GTDSKAGGPDYLILHMQAKTTST 519
Cdd:PRK11904 1003 GTGPKAGGPHYLLRFATEKTVTV 1025
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
60-497 |
1.73e-99 |
|
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: 307.62 E-value: 1.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNT-WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA 138
Cdd:cd07109 1 VFDPSTG-EVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLKLK-DGVPVQsregeENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPAD 214
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHgETIPLG-----PGYFVYTvrePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 215 ATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASK-VQPgqkwlkrVIAEM 293
Cdd:cd07109 155 DAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEnVVP-------VTLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDvSTYMGPVSHEAS 373
Cdd:cd07109 228 GGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEA---DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYA 449
Cdd:cd07109 307 LDRVEGFVARARARGaRIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1267504047 450 LTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYhPFGGFNMSG 497
Cdd:cd07109 387 LVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
61-497 |
1.92e-99 |
|
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: 307.74 E-value: 1.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07110 2 INPATE-ATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATP 217
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 218 VVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKD 297
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 298 TVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKV 377
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 378 LSYIEIGKEEG-RLMTGGEADD--SKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGAL 454
Cdd:cd07110 315 LSFIARGKEEGaRLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1267504047 455 LSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
18-508 |
7.73e-99 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 323.74 E-value: 7.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 18 DFTLEENKKEFKKALETVHSQLGKDYPLVIGEEliTTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKK 97
Cdd:PRK11905 531 DLSDEATLAALDEALNAFAAKTWHAAPLLAGGD--VDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 98 ENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQsregeenkfnyiP 177
Cdd:PRK11905 609 TPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHK------------P 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 178 LGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKT 257
Cdd:PRK11905 677 LGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRI 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 258 RFVSFTGSREVGCRIyekaskvqpgQKWL-KRV------IAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGS 330
Cdd:PRK11905 757 AGVMFTGSTEVARLI----------QRTLaKRSgppvplIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALR 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 331 RAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADD--SKGYFIQPTI 408
Cdd:PRK11905 827 VLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAetEKGTFVAPTL 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 409 F--ADVDEkarlMQEEIFGPV--VAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAI 484
Cdd:PRK11905 907 IeiDSISD----LEREVFGPVlhVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAV 982
|
490 500
....*....|....*....|....
gi 1267504047 485 VGYHPFGGFNMSGTDSKAGGPDYL 508
Cdd:PRK11905 983 VGVQPFGGEGLSGTGPKAGGPLYL 1006
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
61-497 |
8.16e-99 |
|
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: 305.61 E-value: 8.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07106 2 INPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYARqmLKLKDGVpVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVA 220
Cdd:cd07106 81 GGAVAWLRYTAS--LDLPDEV-IEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 221 AKFVEVMEEAgLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVV 300
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 301 VDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSY 380
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 381 IEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTP 459
Cdd:cd07106 310 VEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 1267504047 460 AHIERAKEEFHVGNLYFNrgcTGAIVGYH-PFGGFNMSG 497
Cdd:cd07106 390 ERAEAVARRLEAGTVWIN---THGALDPDaPFGGHKQSG 425
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
60-503 |
1.82e-98 |
|
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: 305.07 E-value: 1.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADAD 139
Cdd:cd07107 1 VINPATG-QVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 140 TAEAIDFLEFYARQMLKLK-DGVPVQSRegeenKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADA 215
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKgETIPVGGR-----NLHYTlrePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 216 TPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGG 295
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 296 KDTVVVDKDADLDLAASSIVYSA-FGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASY 374
Cdd:cd07107 228 KNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 375 NKVLSYIEIGKEEG-RLMTGG----EADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYA 449
Cdd:cd07107 308 DRVMHYIDSAKREGaRLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 450 LTGALLSSTPAHIERAKEEFHVGNLYFNRgctgaiVGYH----PFGGFNMSGTDSKAG 503
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWING------SSRHflgaPFGGVKNSGIGREEC 439
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
44-508 |
1.27e-97 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 319.58 E-value: 1.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 44 PLVIGEEliTTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSS 123
Cdd:COG4230 560 PLIAGEA--ASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMA 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 124 YLVKEAGKPWNEADADTAEAIDFLEFYARQmlklkdgvpvqSREGEENKFNYIPLGVGIIISPFNFPLaimagtaaaAI- 202
Cdd:COG4230 638 LLVREAGKTLPDAIAEVREAVDFCRYYAAQ-----------ARRLFAAPTVLRGRGVFVCISPWNFPL---------AIf 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 203 --------VTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIye 274
Cdd:COG4230 698 tgqvaaalAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI-- 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 275 kaskvqpgQKWL-KR------VIAEMGGKDTVVVDkdadldlaaSS---------IVYSAFGFSGQKCSAgSRAV-VHQD 337
Cdd:COG4230 776 --------NRTLaARdgpivpLIAETGGQNAMIVD---------SSalpeqvvddVLASAFDSAGQRCSA-LRVLcVQED 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 338 VYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDS--KGYFIQPTIF--ADVD 413
Cdd:COG4230 838 IADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcaNGTFVAPTLIeiDSIS 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 414 EkarlMQEEIFGP---VVAFcKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPF 490
Cdd:COG4230 918 D----LEREVFGPvlhVVRY-KADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPF 992
|
490
....*....|....*...
gi 1267504047 491 GGFNMSGTDSKAGGPDYL 508
Cdd:COG4230 993 GGEGLSGTGPKAGGPHYL 1010
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
43-497 |
1.20e-96 |
|
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: 301.03 E-value: 1.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 43 YPLVIGEELITTDEKIVSI-NPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENP-EVRANILFRAADIIRRRKHE 120
Cdd:cd07082 2 FKYLINGEWKESSGKTIEVySPIDG-EVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 121 FSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLkDGVPVQSREGEENK-----FNYIPLGVGIIISPFNFPLAIMA 195
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGDSLPGDWFPGTKgkiaqVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 196 GTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEK 275
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 276 ASKvqpgqkwlKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKV 355
Cdd:cd07082 240 HPM--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 356 GNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADdsKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKAR 434
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267504047 435 DFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIvGYHPFGGFNMSG 497
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
53-465 |
3.76e-96 |
|
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: 299.22 E-value: 3.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 53 TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGK- 131
Cdd:cd07151 7 TSERTIDVLNPYTG-ETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 132 ------PWNEADADTAEAidfLEFYARQmlklkDGVPVQSR-EGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVT 204
Cdd:cd07151 86 rikaniEWGAAMAITREA---ATFPLRM-----EGRILPSDvPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 205 GNTILLKPADATPVVAAK-FVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgq 283
Cdd:cd07151 158 GNAVVLKPASDTPITGGLlLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRH---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 284 kwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVST 363
Cdd:cd07151 234 --LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 364 YMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEI 442
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420
....*....|....*....|...
gi 1267504047 443 ANNTDYALTGALLSSTpahIERA 465
Cdd:cd07151 389 ANDTEYGLSGAVFTSD---LERG 408
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-497 |
4.25e-96 |
|
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: 298.89 E-value: 4.25e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW-NEADAD 139
Cdd:cd07108 2 INPATG-QVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 140 TAEAIDFLEFYARQMLKLK-DGVPvqsreGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADA 215
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKgETLP-----FGPDVLTYTvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 216 TPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKAS-KVQPgqkwlkrVIAEMG 294
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAdRLIP-------VSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 295 GKDTVVVDKDADLDLAASSIVYSA-FGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07108 228 GKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKE--EGRLMTGG----EADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTD 447
Cdd:cd07108 308 FAKVCGYIDLGLStsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1267504047 448 YALTGALLSSTPAHIERAKEEFHVGNLYFNRGctGAIVGYHPFGGFNMSG 497
Cdd:cd07108 388 YGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSG 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
58-498 |
1.56e-95 |
|
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: 297.34 E-value: 1.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 58 IVSINPANkVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD 137
Cdd:cd07145 1 IEVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 138 ADTAEAIDFLEFYARQMLKLKDG-VPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPA 213
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGEtIPVDAYEYNERRIAFTvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 214 DATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEM 293
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTG 452
Cdd:cd07145 314 VERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1267504047 453 ALLSSTPAHIERAKEEFHVGNLYFNrGCTGAIVGYHPFGGFNMSGT 498
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
61-517 |
8.72e-95 |
|
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: 295.75 E-value: 8.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07090 2 IEPATG-EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYArqmlklkdGVpVQSREGE-----ENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKP 212
Cdd:cd07090 81 DSSADCLEYYA--------GL-APTLSGEhvplpGGSFAYTrrePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 213 ADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAE 292
Cdd:cd07090 152 SPFTPLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG------IKHVTLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 293 MGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEA 372
Cdd:cd07090 225 LGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 373 SYNKVLSYIEIGKEEG-RLMTGGEADDSK-----GYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNT 446
Cdd:cd07090 305 HLEKVLGYIESAKQEGaKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDT 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267504047 447 DYALTGALLSSTPAHIERAKEEFHVGNLYFNR-GCTGAIVgyhPFGGFNMSGTdSKAGGPDYLILHMQAKTT 517
Cdd:cd07090 385 TYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGF-GRENGTAALEHYTQLKTV 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
68-497 |
1.88e-94 |
|
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: 294.73 E-value: 1.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFL 147
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 EFYARQMLKLKD-GVPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKF 223
Cdd:cd07094 90 RLAAEEAERIRGeEIPLDATQGSDNRLAWTirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 224 VEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKvqpgqkwlKRVIAEMGGKDTVVVDK 303
Cdd:cd07094 170 AKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 304 DADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEI 383
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 384 GKEEG-RLMTGGEADDSkgyFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHI 462
Cdd:cd07094 322 AVEAGaRLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1267504047 463 ERAKEEFHVGNLYFNRGcTGAIVGYHPFGGFNMSG 497
Cdd:cd07094 399 FKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
45-497 |
5.82e-94 |
|
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: 294.32 E-value: 5.82e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 45 LVIGEELI--TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEV-RANILFRAADIIRRRKHEF 121
Cdd:cd07144 10 LFINNEFVksSDGETIKTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEeRGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 122 SSYLVKEAGKPWNE-ADADTAEAIDFLEFYARQMLKLKdGVPVQSregEENKFNYI---PLGVGIIISPFNFPLAIMAGT 197
Cdd:cd07144 89 AAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQ-GKTIPT---SPNKLAYTlhePYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 198 AAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGcRIYEKAS 277
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG-RLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 278 kvqpGQKwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTK-TLKVG 356
Cdd:cd07144 244 ----AQN-LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 357 NPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEA---DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCK 432
Cdd:cd07144 319 SPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 433 ARDFDHMMEIANNTDYALTGALLSS--TPAHieRAKEEFHVGNLYFNR---GCTGAivgyhPFGGFNMSG 497
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKdiRRAH--RVARELEAGMVWINSsndSDVGV-----PFGGFKMSG 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
61-498 |
1.51e-93 |
|
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: 293.10 E-value: 1.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTF---NTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA- 136
Cdd:cd07141 27 INPATG-EKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 137 DADTAEAIDFLEFYARQMLKLK-DGVPVqsrEGEEnkFNYI---PLGV-GIIIsPFNFPLAIMAGTAAAAIVTGNTILLK 211
Cdd:cd07141 106 LVDLPGAIKVLRYYAGWADKIHgKTIPM---DGDF--FTYTrhePVGVcGQII-PWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 212 PADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVIA 291
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSN-----LKRVTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 292 EMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHE 371
Cdd:cd07141 255 ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 372 ASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYAL 450
Cdd:cd07141 335 EQFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGL 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 451 TGALLSStpaHIERA---KEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGT 498
Cdd:cd07141 415 AAAVFTK---DIDKAitfSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
53-516 |
1.41e-92 |
|
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: 290.25 E-value: 1.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 53 TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFN--TWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAG 130
Cdd:cd07139 11 SGSETIDVVSPATE-EVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARLWTAENG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 131 KP-WNEADADTAEAIDFLEFYArqmlKLKDGVPV----QSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTG 205
Cdd:cd07139 90 MPiSWSRRAQGPGPAALLRYYA----ALARDFPFeerrPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 206 NTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGCRIYEKAskvqpGQKw 285
Cdd:cd07139 166 CTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC-----GER- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 286 LKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYM 365
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 366 GPVSHEASYNKVLSYIEIGKEEG-RLMTGGE--ADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEI 442
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGaRLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 443 ANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgctGAIVGYH-PFGGFNMSGTdSKAGGPDYLILHMQAKT 516
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDAYLETKS 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
61-498 |
3.19e-92 |
|
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: 288.84 E-value: 3.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNE-ADAD 139
Cdd:cd07092 2 VDPATG-EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 140 TAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVV 219
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 220 AAKFVEVMEEaGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTV 299
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT------LKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 300 VVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLS 379
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 380 YIEIGKEEGRLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTP 459
Cdd:cd07092 314 FVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1267504047 460 AHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGT 498
Cdd:cd07092 394 GRAMRLSARLDFGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-508 |
4.34e-91 |
|
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: 287.58 E-value: 4.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 24 NKKEFKKALETVHSQLGKDYPL--VIGEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPE 101
Cdd:TIGR01238 17 NESELKPLEAQIHAWADKTWQAapIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 102 VRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMlklKDGVPVQSREgeenkfnyiPLGVG 181
Cdd:TIGR01238 97 ERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQV---RDVLGEFSVE---------SRGVF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 182 IIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVS 261
Cdd:TIGR01238 165 VCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 262 FTGSREVGCRIYEKASKVQPGQKWLkrvIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDI 341
Cdd:TIGR01238 245 FTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 342 VLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGR----LMTGGEADDSKGYFIQPTIFaDVDEKAR 417
Cdd:TIGR01238 322 VLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKkiaqLTLDDSRACQHGTFVAPTLF-ELDDIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 418 LmQEEIFGPV--VAFCKARDFDHMMEIANNTDYALTGALLS---STPAHIERAKEefhVGNLYFNRGCTGAIVGYHPFGG 492
Cdd:TIGR01238 401 L-SEEVFGPVlhVVRYKARELDQIVDQINQTGYGLTMGVHSrieTTYRWIEKHAR---VGNCYVNRNQVGAVVGVQPFGG 476
|
490
....*....|....*.
gi 1267504047 493 FNMSGTDSKAGGPDYL 508
Cdd:TIGR01238 477 QGLSGTGPKAGGPHYL 492
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
53-497 |
7.38e-91 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 286.39 E-value: 7.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 53 TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKP 132
Cdd:PRK13252 19 TSGETFEVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 133 WNEAD-ADTAEAIDFLEFYArqmlklkdGVpVQSREGE-----ENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIV 203
Cdd:PRK13252 98 IQETSvVDIVTGADVLEYYA--------GL-APALEGEqiplrGGSFVYTrrePLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 204 TGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgq 283
Cdd:PRK13252 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 284 kwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVST 363
Cdd:PRK13252 244 --LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 364 YMGPVSHEASYNKVLSYIEIGKEEG-RLMTGG----EADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDH 438
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGerltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267504047 439 MMEIANNTDYALTGALLSS--TPAHieRAKEEFHVGNLYFNR-GCTGAIVgyhPFGGFNMSG 497
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTAdlSRAH--RVIHQLEAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
44-515 |
2.37e-90 |
|
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: 284.79 E-value: 2.37e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 44 PLVIGEELI--TTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEF 121
Cdd:cd07085 2 KLFINGEWVesKTTEWLDVYNPATG-EVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 122 SSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAA 201
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 202 IVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqp 281
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 282 gqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDV 361
Cdd:cd07085 238 ----GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 362 STYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGE----ADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDF 436
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRgvkvPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 437 DHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGctgaI---VGYHPFGGFNmsgtDSKAGgpdylILHMQ 513
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVP----IpvpLAFFSFGGWK----GSFFG-----DLHFY 460
|
..
gi 1267504047 514 AK 515
Cdd:cd07085 461 GK 462
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
43-497 |
3.62e-90 |
|
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: 284.24 E-value: 3.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 43 YPLVIGEELIT--TDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHE 120
Cdd:cd07559 1 YDNFINGEWVApsKGEYFDNYNPVNG-KVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 121 FSSYLVKEAGKPWNEA-DADTAEAIDFLEFYArqmlklkdGVpVQSREGE-----ENKFNYI---PLGV-GIIIsPFNFP 190
Cdd:cd07559 80 LAVAETLDNGKPIRETlAADIPLAIDHFRYFA--------GV-IRAQEGSlseidEDTLSYHfhePLGVvGQII-PWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 191 LAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGC 270
Cdd:cd07559 150 LLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 271 RIYEKASKVqpgqkwLKRVIAEMGGK-------DtvVVDKDADLDLAASSIVySAFGF-SGQKCSAGSRAVVHQDVYDIV 342
Cdd:cd07559 229 LIMQYAAEN------LIPVTLELGGKspniffdD--AMDADDDFDDKAEEGQ-LGFAFnQGEVCTCPSRALVQESIYDEF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 343 LEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGE----ADDSKGYFIQPTIFADVDEKAR 417
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 418 LMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07559 380 IFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
68-505 |
1.51e-89 |
|
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: 281.49 E-value: 1.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFL 147
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 eFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVA-AKFVEV 226
Cdd:cd07152 82 -HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 227 MEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDAD 306
Cdd:cd07152 161 FEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRH------LKKVSLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 307 LDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKE 386
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 387 EG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERA 465
Cdd:cd07152 314 AGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1267504047 466 KEEFHVGNLYFNRGcTGAIVGYHPFGGFNMSGTDSKAGGP 505
Cdd:cd07152 391 ADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
61-497 |
9.19e-89 |
|
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: 280.95 E-value: 9.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNT-WKKE-NPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA 138
Cdd:cd07143 27 YNPSTG-KLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 -DTAEAIDFLEFYArqmlKLKDGVPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPAD 214
Cdd:cd07143 106 vDVQASADTFRYYG----GWADKIHGQVIETDIKKLTYTrhePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 215 ATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVIAEMG 294
Cdd:cd07143 182 LTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN-----LKKVTLELG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 295 GKDTVVVDKDADLDlaaSSIVYSAFGF---SGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHE 371
Cdd:cd07143 257 GKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 372 ASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYAL 450
Cdd:cd07143 334 IQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGL 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1267504047 451 TGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07143 414 AAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
81-497 |
2.93e-88 |
|
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: 277.80 E-value: 2.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 81 AEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYAR---QMLKL 157
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 158 KdgvPVQSrEGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVL 237
Cdd:cd07100 81 E---PIET-DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 238 NFIPgVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYS 317
Cdd:cd07100 157 QNLL-IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKN------LKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 318 AFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEA 396
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 397 DDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYF 476
Cdd:cd07100 310 PDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420
....*....|....*....|....
gi 1267504047 477 NrgctgAIVGYH---PFGGFNMSG 497
Cdd:cd07100 390 N-----GMVKSDprlPFGGVKRSG 408
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
60-503 |
4.43e-88 |
|
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: 278.99 E-value: 4.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFN--TWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD 137
Cdd:cd07142 23 TIDPRNG-EVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 138 -ADTAEAIDFLEFYARQMLKLK------DGvPVQSREGEEnkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILL 210
Cdd:cd07142 102 yAEVPLAARLFRYYAGWADKIHgmtlpaDG-PHHVYTLHE------PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 211 KPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVI 290
Cdd:cd07142 175 KPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN-----LKPVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 291 AEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSH 370
Cdd:cd07142 250 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 371 EASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYA 449
Cdd:cd07142 330 KEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYG 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1267504047 450 LTGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAG 503
Cdd:cd07142 410 LAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
68-497 |
1.71e-87 |
|
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: 276.43 E-value: 1.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFL 147
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 EFYAR-------QMLKLkDGVPV-QSREGEENKFnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVV 219
Cdd:cd07147 90 RIAAEeatriygEVLPL-DISARgEGRQGLVRRF---PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 220 AAKFVEVMEEAGLPKGVLNFIPgVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKvqpgqkwlKRVIAEMGGKDTV 299
Cdd:cd07147 166 ALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--------KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 300 VVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLS 379
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 380 YIEIGKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSST 458
Cdd:cd07147 317 WVNEAVDAGaKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1267504047 459 PAHIERAKEEFHVGNLYFN-----RgctgaiVGYHPFGGFNMSG 497
Cdd:cd07147 394 LEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSG 431
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
46-508 |
1.54e-85 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 288.03 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 46 VIGEELITTDEKIVsINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYL 125
Cdd:PRK11809 650 MLEDPVAAGEMSPV-INPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 126 VKEAGKPWNEADADTAEAIDFLEFYArqmlklkdgvpVQSREGEENKfNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTG 205
Cdd:PRK11809 729 VREAGKTFSNAIAEVREAVDFLRYYA-----------GQVRDDFDND-THRPLGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 206 NTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGcRIYEK--ASKVQPgQ 283
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRnlAGRLDP-Q 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 284 KWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVST 363
Cdd:PRK11809 875 GRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLST 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 364 YMGPVSHEASYNKVLSYIEIGKEEGRLMT----GGEADDSKGYFIQPTI--FADVDEkarlMQEEIFGPV---VAFcKAR 434
Cdd:PRK11809 955 DIGPVIDAEAKANIERHIQAMRAKGRPVFqaarENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVlhvVRY-NRN 1029
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267504047 435 DFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 508
Cdd:PRK11809 1030 QLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1103
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
68-503 |
4.88e-85 |
|
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: 270.00 E-value: 4.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALstfNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFL 147
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAA---SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 EFYARQMLKLkDGVPVQSREGEENKFNYI-----PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAK 222
Cdd:cd07146 87 RFAAAEALRD-DGESFSCDLTANGKARKIftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 223 FVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASkvqpgqkwLKRVIAEMGGKDTVVVD 302
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 303 KDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIE 382
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 383 IGKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAH 461
Cdd:cd07146 318 EAIAQGaRVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1267504047 462 IERAKEEFHVGNLYFNRGctgaiVGYH----PFGGFNMSGTDSKAG 503
Cdd:cd07146 395 IKRLVERLDVGTVNVNEV-----PGFRselsPFGGVKDSGLGGKEG 435
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
61-508 |
1.14e-84 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 270.79 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:PLN02278 45 YNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYA-----------------RQMLKLKDgvpvqsregeenkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIV 203
Cdd:PLN02278 124 AYGASFLEYFAeeakrvygdiipspfpdRRLLVLKQ-----------------PVGVVGAITPWNFPLAMITRKVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 204 TGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgq 283
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 284 kwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVST 363
Cdd:PLN02278 263 --VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 364 YMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEI 442
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267504047 443 ANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGyhPFGGFNMSGT---DSKAGGPDYL 508
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLgreGSKYGIDEYL 487
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
61-497 |
4.75e-84 |
|
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: 267.67 E-value: 4.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKVEIIgRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA 138
Cdd:cd07118 2 RSPAHGVVVA-RYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLKL---------KDGVPVQSREgeenkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTIL 209
Cdd:cd07118 81 EIEGAADLWRYAASLARTLhgdsynnlgDDMLGLVLRE---------PIGVVGIITPWNFPFLILSQKLPFALAAGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 210 LKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRV 289
Cdd:cd07118 152 VKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARN------LKKV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 290 IAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVS 369
Cdd:cd07118 226 SLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAII 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 370 HEASYNKVLSYIEIGKEEG-RLMTGGEADDS-KGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTD 447
Cdd:cd07118 306 NEAQLAKITDYVDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTV 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1267504047 448 YALTGALLSSTPAHIERAKEEFHVGNLYFNRgctgAIVGYH--PFGGFNMSG 497
Cdd:cd07118 386 YGLSAGVWSKDIDTALTVARRIRAGTVWVNT----FLDGSPelPFGGFKQSG 433
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
61-497 |
5.85e-83 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 266.21 E-value: 5.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNT-----WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNE 135
Cdd:PLN02467 28 VNPATE-ETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 136 ADADTAEAIDFLEFYARQM--LKLKDGVPVqSREGEENKFNYI--PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLK 211
Cdd:PLN02467 107 AAWDMDDVAGCFEYYADLAeaLDAKQKAPV-SLPMETFKGYVLkePLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 212 PADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIA 291
Cdd:PLN02467 186 PSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQM------VKPVSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 292 EMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHE 371
Cdd:PLN02467 260 ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 372 ASYNKVLSYIEIGKEEG-RLMTGGEADD--SKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDY 448
Cdd:PLN02467 340 GQYEKVLKFISTAKSEGaTILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHY 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1267504047 449 ALTGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:PLN02467 420 GLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
107-511 |
1.08e-82 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 262.75 E-value: 1.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 107 LFRAADIIRRRKHEFSSYLVKEAGKPWNEADAD---TAEAIDFLEFYARQMlklkDGVPVQSREGEENKFNY-IPLGVGI 182
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEvafTADYIDYMAEWARRY----EGEIIQSDRPGENILLFkRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 183 IISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSF 262
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 263 TGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIV 342
Cdd:PRK10090 157 TGSVSAGEKIMAAAAKN------ITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 343 LEKAVALTKTLKVGNPEDVSTY-MGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQ 420
Cdd:PRK10090 231 VNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 421 EEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHpfGGFNMS---G 497
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgigG 388
|
410
....*....|....
gi 1267504047 498 TDSKAGGPDYLILH 511
Cdd:PRK10090 389 ADGKHGLHEYLQTQ 402
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
68-521 |
3.04e-82 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 264.38 E-value: 3.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFN--TWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADA-DTAEAI 144
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 145 DFLEFYARQMLKLKDGVPVQSREgeenKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAA 221
Cdd:PLN02766 127 GLLRYYAGAADKIHGETLKMSRQ----LQGYTlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 222 KFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVIAEMGGKDTVVV 301
Cdd:PLN02766 203 FYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN-----LKQVSLELGGKSPLLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 302 DKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYI 381
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 382 EIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPA 460
Cdd:PLN02766 358 EHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLD 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 461 HIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTdSKAGGPDYLILHMQAKTTSTAL 521
Cdd:PLN02766 438 VANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGF-GRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
55-498 |
6.10e-82 |
|
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: 262.76 E-value: 6.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 55 DEKIVSI-NPANKvEIIGRVSKTNQELAEKAMQTALSTF-NTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKP 132
Cdd:cd07113 13 SEKRLDItNPATE-QVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 133 WNEADA-DTAEAIDFLEFYARQMLKLKD---GVPVQSREGEE-NKFNYI-PLGVGIIISPFNFPLAIMAGTAAAAIVTGN 206
Cdd:cd07113 92 IHLSRAfEVGQSANFLRYFAGWATKINGetlAPSIPSMQGERyTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 207 TILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwL 286
Cdd:cd07113 172 TIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASD------L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 287 KRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMG 366
Cdd:cd07113 245 TRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 367 PVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANN 445
Cdd:cd07113 325 PLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLIND 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 446 TDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgctgaivgYH-------PFGGFNMSGT 498
Cdd:cd07113 405 TPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---------MHtfldpavPFGGMKQSGI 455
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
42-517 |
5.55e-81 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 260.23 E-value: 5.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 42 DYPLVIGEELITTDEKIVSI-NPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHE 120
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVyNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 121 FSSYLVKEAGKPWNEADAD----TAEAIDFLEFYARQMlklkDGvpvqSREGE--ENKFNYI---PLGVGIIISPFNFPL 191
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDeipaIVDVFRFFAGAARCL----EG----KAAGEylEGHTSMIrrdPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 192 AIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCR 271
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 272 IYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTK 351
Cdd:PRK13473 232 VLSAAADS------VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 352 TLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG--RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVA 429
Cdd:PRK13473 306 TLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 430 FCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVG----NLYFnrgctgAIVGYHPFGGFNMS--GTD-SKA 502
Cdd:PRK13473 386 VTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGctwvNTHF------MLVSEMPHGGQKQSgyGKDmSLY 459
|
490
....*....|....*.
gi 1267504047 503 GGPDYLIL-HMQAKTT 517
Cdd:PRK13473 460 GLEDYTVVrHVMVKHT 475
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
43-497 |
3.06e-80 |
|
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: 258.54 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 43 YPLVIGEELITT--DEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHE 120
Cdd:cd07117 1 YGLFINGEWVKGssGETIDSYNPANG-ETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 121 FSSYLVKEAGKPWNEA-DADTAEAIDFLEFYArqmlklkdGVpVQSREGEENKFN--------YIPLGVGIIISPFNFPL 191
Cdd:cd07117 80 LAMVETLDNGKPIRETrAVDIPLAADHFRYFA--------GV-IRAEEGSANMIDedtlsivlREPIGVVGQIIPWNFPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 192 AIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCR 271
Cdd:cd07117 151 LMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 272 IYEKASKvqpgqkwlkRVIA---EMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVA 348
Cdd:cd07117 230 VAIAAAK---------KLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 349 LTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGG----EADDSKGYFIQPTIFADVDEKARLMQEEI 423
Cdd:cd07117 301 KFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267504047 424 FGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07117 381 FGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
60-450 |
5.90e-79 |
|
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: 254.58 E-value: 5.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFN--TWKkENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD 137
Cdd:cd07120 1 SIDPATG-EVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 138 ADTAEAIDFLEFYArQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATP 217
Cdd:cd07120 79 FEISGAISELRYYA-GLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 218 VVAAKFVEVMEEA-GLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGK 296
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT------LKRLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 297 DTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNK 376
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 377 VLSYIEIGKEEGR--LMTGGEADD--SKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYAL 450
Cdd:cd07120 312 VDRMVERAIAAGAevVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGL 389
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
84-497 |
1.72e-78 |
|
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: 252.58 E-value: 1.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 84 AMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMlklkdgvpv 163
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAY--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 164 QSREGEENKFN--------YIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKG 235
Cdd:cd07095 76 HERTGERATPMaqgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 236 VLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKvQPGqkwlkRVIA-EMGGKDTVVVDKDADLDLAASSI 314
Cdd:cd07095 156 VLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAG-RPG-----KILAlEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 315 VYSAFGFSGQKCSAGSRAVVHQD-VYDIVLEKAVALTKTLKVGNPEDVSTYMGP-VSHEASYNKVLSYIEIGKEEGRLMT 392
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPlIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 393 GGEADDSKGYFIQPTIFaDVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVG 472
Cdd:cd07095 309 AMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420
....*....|....*....|....*
gi 1267504047 473 NLYFNRGCTGAiVGYHPFGGFNMSG 497
Cdd:cd07095 388 IVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
61-490 |
2.01e-77 |
|
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: 250.24 E-value: 2.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKVEIIGRVSKTNQELAEKAmQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWneadADT 140
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAAL-ERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPI----AQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYARQMLKLKDGVPVQSREGEENKFN-YI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADAT 216
Cdd:cd07102 76 GGEIRGMLERARYMISIAEEALADIRVPEKDGFErYIrrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 217 PVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIyEKASkvqpgQKWLKRVIAEMGGK 296
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAI-QRAA-----AGRFIKVGLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 297 DTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNK 376
Cdd:cd07102 229 DPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 377 VLSYIEIGKEEG-RLMTGGE---ADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTG 452
Cdd:cd07102 309 VRAQIADAIAKGaRALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267504047 453 ALLSSTPAHIERAKEEFHVGNLYFNR------------------GCTGAIVGYHPF 490
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNRcdyldpalawtgvkdsgrGVTLSRLGYDQL 444
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
61-497 |
2.03e-76 |
|
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: 247.90 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 61 INPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADT 140
Cdd:cd07099 1 RNPATG-EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 141 AEAIDFLEFYARQMLKLKDGVPVQSREGEENKFN---YIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATP 217
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKAtveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 218 VVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHpKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKD 297
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTG-DGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER------LIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 298 TVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKV 377
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 378 LSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLS 456
Cdd:cd07099 312 RRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1267504047 457 STPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 497
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
81-457 |
1.98e-75 |
|
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: 244.41 E-value: 1.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 81 AEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKLKDG 160
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 161 VPVQSREGE------EnkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPK 234
Cdd:cd07105 82 SIPSDKPGTlamvvkE------PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 235 GVLNFI---PGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKvqpgqkWLKRVIAEMGGKDTVVVDKDADLDLAA 311
Cdd:cd07105 156 GVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 312 SSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGnpedvSTYMGPVSHEASYNKVLSYIEIGKEEG-RL 390
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGaKL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 391 MTGGEADDSK-GYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSS 457
Cdd:cd07105 305 VVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTR 372
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
68-521 |
7.74e-75 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 246.26 E-value: 7.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNE-ADADTAEAI 144
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKAELPMFA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 145 DFLEFYARQMLKLKdGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFV 224
Cdd:PLN02466 164 RLFRYYAGWADKIH-GLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 225 EVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVIAEMGGKDTVVVDKD 304
Cdd:PLN02466 243 KLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN-----LKPVTLELGGKSPFIVCED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 305 ADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIG 384
Cdd:PLN02466 318 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 385 KEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIE 463
Cdd:PLN02466 398 VESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTAN 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 464 RAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTdSKAGGPDYLILHMQAKTTSTAL 521
Cdd:PLN02466 478 TLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGI-GREKGIYSLNNYLQVKAVVTPL 532
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
72-497 |
1.65e-72 |
|
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: 238.51 E-value: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 72 RVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA-DADTAEAIDFLEFY 150
Cdd:cd07116 31 EVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAADIPLAIDHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 151 ArqmlklkdGVpVQSREG-----EENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAK 222
Cdd:cd07116 111 A--------GC-IRAQEGsiseiDENTVAYHfhePLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 223 FVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGK------ 296
Cdd:cd07116 182 LMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN------IIPVTLELGGKspniff 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 297 DTVVVDKDADLDLAASSIVYSAFGfSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNK 376
Cdd:cd07116 255 ADVMDADDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 377 VLSYIEIGKEEG-RLMTGGEA----DDSKGYFIQPTIFADvDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALT 451
Cdd:cd07116 334 ILSYIDIGKEEGaEVLTGGERnelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1267504047 452 GALLSSTPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 497
Cdd:cd07116 413 AGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
60-497 |
9.41e-72 |
|
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: 236.62 E-value: 9.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA- 136
Cdd:cd07140 25 TINPTDG-SVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 137 DADTAEAIDFLEFYARQMLKLK-DGVPV-QSREGEENKFNYI-PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPA 213
Cdd:cd07140 104 KTHVGMSIQTFRYFAGWCDKIQgKTIPInQARPNRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 214 DATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwLKRVIAEM 293
Cdd:cd07140 184 QVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSN-----LKKVSLEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07140 259 GGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKAR--DFDHMMEIANNTDYAL 450
Cdd:cd07140 339 LDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDGVLQRANDTEYGL 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1267504047 451 TGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGyhPFGGFNMSG 497
Cdd:cd07140 419 ASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
60-508 |
2.73e-70 |
|
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: 232.67 E-value: 2.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA-DA 138
Cdd:cd07111 41 TINPATG-EVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 139 DTAEAIDFLEFYARQMLKLKDGVPvqsregeenkfNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPV 218
Cdd:cd07111 120 DIPLVARHFYHHAGWAQLLDTELA-----------GWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 219 VAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGcRIYEKASKvqpgqKWLKRVIAEMGGKDT 298
Cdd:cd07111 189 TALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVG-RALRRATA-----GTGKKLSLELGGKSP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 299 VVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVL 378
Cdd:cd07111 262 FIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 379 SYIEIGKEEGRLMTGGEAD-DSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSS 457
Cdd:cd07111 342 ELVEEGRAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSE 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 458 TPAHIERAKEEFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTdSKAGGPDYL 508
Cdd:cd07111 422 NLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGF-GREGGKEGL 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
62-508 |
1.10e-68 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 228.25 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 62 NPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTA 141
Cdd:PRK11241 32 NPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 142 EAIDFLEFYARQMLKL-KDGVPvqsreGEENKFNYI----PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADAT 216
Cdd:PRK11241 111 YAASFIEWFAEEGKRIyGDTIP-----GHQADKRLIvikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 217 PVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGK 296
Cdd:PRK11241 186 PFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD------IKKVSLELGGN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 297 DTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNK 376
Cdd:PRK11241 260 APFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 377 VLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALL 455
Cdd:PRK11241 340 VEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFY 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267504047 456 SSTPAHIERAKEEFHVGNLYFNRGCTGAIVGyhPFGGFNMSG---TDSKAGGPDYL 508
Cdd:PRK11241 420 ARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
68-519 |
1.30e-68 |
|
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: 227.19 E-value: 1.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKpwNEADA-----DTAE 142
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK--ARRHAfeevlDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 143 AIdflEFYARQMLKL------KDGVPVQSREGEenkfNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADAT 216
Cdd:cd07101 85 VA---RYYARRAERLlkprrrRGAIPVLTRTTV----NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 217 PVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHpkTRFVSFTGSREVGCRIYEKASkvqpgqkwlKRVI---AEM 293
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG---------RRLIgcsLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDSKG-YFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALT 451
Cdd:cd07101 307 LDRVTAHVDDAVAKGaTVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267504047 452 GALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYH-PFGGFNMSGTdSKAGGPDYLILHMQAKTTST 519
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGL-GRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
46-464 |
3.16e-68 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 226.70 E-value: 3.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 46 VIGEELITTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYL 125
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 126 VKEAGKPWNEADADTAEAIDFLEF---YARQMlklkDGVPVQS-REGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAA 201
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFavgLSRQL----YGLTIPSeRPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 202 IVTGNTILLKPADATPVVAAK----FVEVMEEAGLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGCRIyekAS 277
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQV---GQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 278 KVQpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGN 357
Cdd:cd07130 233 AVA---ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 358 PEDVSTYMGPVSHEASYNKVLSYIEIGKEE-GRLMTGGEADDSKGYFIQPTIfADVDEKARLMQEEIFGPVVAFCKARDF 436
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420
....*....|....*....|....*...
gi 1267504047 437 DHMMEIANNTDYALTGALLSSTPAHIER 464
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
58-497 |
7.02e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 214.99 E-value: 7.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 58 IVSINPANkveiiGRVSKT----NQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW 133
Cdd:PRK09406 3 IATINPAT-----GETVKTftalTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 134 NEADADTAEAIDFLEFYARQMLKLKDGVPVQSRE-GEENKF-NYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLK 211
Cdd:PRK09406 78 ASAKAEALKCAKGFRYYAEHAEALLADEPADAAAvGASRAYvRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 212 PADATPVVAAKFVEVMEEAGLPKGVLnfipgVTPEIG----DYLVQHPKTRFVSFTGSREVGCRIYEKAskvqpGQKwLK 287
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCF-----QTLLVGsgavEAILRDPRVAAATLTGSEPAGRAVAAIA-----GDE-IK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 288 RVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGP 367
Cdd:PRK09406 227 KTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 368 VSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNT 446
Cdd:PRK09406 307 LATEQGRDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANAT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1267504047 447 DYALTGALLSSTPAHIERAKEEFHVGNLYFNrgctGAIVGYH--PFGGFNMSG 497
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSG 435
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
60-497 |
2.14e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 212.06 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 60 SINPANKVEIiGRVSKTNQELAEKAMQTALSTFNT--WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA- 136
Cdd:PRK09847 39 TVDPVTQAPL-AKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 137 DADTAEAIDFLEFYARQMLKLKDGVPVQSrEGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADAT 216
Cdd:PRK09847 118 RDDIPGAARAIRWYAEAIDKVYGEVATTS-SHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 217 PVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKAskvqpGQKWLKRVIAEMGGK 296
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA-----GDSNMKRVWLEAGGK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 297 DTVVVDKDA-DLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYN 375
Cdd:PRK09847 272 SANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHAD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 376 KVLSYIEIGKEEGRLMTGGEADDSKGYfIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALL 455
Cdd:PRK09847 352 SVHSFIREGESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVW 430
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1267504047 456 SSTPAHIERAKEEFHVGNLYFNRGCTGAIVgyHPFGGFNMSG 497
Cdd:PRK09847 431 TRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG 470
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
54-519 |
6.06e-62 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 210.51 E-value: 6.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 54 TDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPW 133
Cdd:TIGR01722 14 SGTYIPVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 134 NEADADTAEAIDFLEfYARQMLKLKDGVPVQSREGEENKFNY-IPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKP 212
Cdd:TIGR01722 93 SDALGDVARGLEVVE-HACGVNSLLKGETSTQVATRVDVYSIrQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 213 ADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIgDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwlKRVIAE 292
Cdd:TIGR01722 172 SEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG------KRVQAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 293 MGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVyDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEA 372
Cdd:TIGR01722 245 GGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 373 SYNKVLSYIEIGKEEG-RLMTGGEADDSKGY----FIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTD 447
Cdd:TIGR01722 324 AKDRVASLIAGGAAEGaEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASP 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267504047 448 YALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTgAIVGYHPFGGFNMS-GTDSKAGGPDYLILHMQAKTTST 519
Cdd:TIGR01722 404 YGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIP-VPLPYFSFTGWKDSfFGDHHIYGKQGTHFYTRGKTVTT 475
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
52-497 |
7.44e-62 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 209.72 E-value: 7.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 52 ITTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGK 131
Cdd:PRK13968 3 ITPATHAISVNPATG-EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 132 PWNEADADTAEAIDFLEFYARQ---MLKLKDGVPvqsrEGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTI 208
Cdd:PRK13968 82 PINQARAEVAKSANLCDWYAEHgpaMLKAEPTLV----ENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 209 LLKPADATPVVAAKFVEVMEEAGLPKGVLNFI----PGVTPEIGDylvqhPKTRFVSFTGSREVGCRIYEKASKVqpgqk 284
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLnadnDGVSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAA----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 285 wLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTY 364
Cdd:PRK13968 228 -LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 365 MGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIA 443
Cdd:PRK13968 307 LGPMARFDLRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 444 NNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGC-TGAIVGyhpFGGFNMSG 497
Cdd:PRK13968 387 NDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
48-497 |
2.54e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 206.35 E-value: 2.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 48 GEELITTDEKIVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVK 127
Cdd:PRK09457 7 GDWIAGQGEAFESRNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 128 EAGKPWNEADADTAEAIDflefyarqmlklKDGVPVQS---REGEENK--------FNYIPLGVGIIISPFNFPLAIMAG 196
Cdd:PRK09457 86 ETGKPLWEAATEVTAMIN------------KIAISIQAyheRTGEKRSemadgaavLRHRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 197 TAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKA 276
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 277 SKvQPGqkwlkRVIA-EMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVY-DIVLEKAVALTKTLK 354
Cdd:PRK09457 233 AG-QPE-----KILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 355 VGNP-EDVSTYMGPVSHEASYNKVLS----YIEIGKEEGRLMTGGEADDSkgyFIQPTIFaDVDEKARLMQEEIFGPVVA 429
Cdd:PRK09457 307 VGRWdAEPQPFMGAVISEQAAQGLVAaqaqLLALGGKSLLEMTQLQAGTG---LLTPGII-DVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 430 FCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAiVGYHPFGGFNMSG 497
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
68-514 |
6.12e-60 |
|
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: 204.57 E-value: 6.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTF---NTWKKenPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAI 144
Cdd:cd07148 10 KPIGEVPTVDWAAIDKALDTAHALFldrNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 145 DFLEFYARQMLKLK-DGVPVQSREGEENKFNYI---PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVA 220
Cdd:cd07148 88 DGVELAADELGQLGgREIPMGLTPASAGRIAFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 221 AKFVEVMEEAGLPKGVLNFIPgVTPEIGDYLVQHPKTRFVSFTGSREVGCRIyekASKVQPGqkwlKRVIAEMGGKDTVV 300
Cdd:cd07148 168 LAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWML---RSKLAPG----TRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 301 VDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSY 380
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 381 IEIGKEEG-RLMTGGEADDSKGYfiQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTP 459
Cdd:cd07148 320 VNEAVAAGaRLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1267504047 460 AHIERAKEEFHVGNLYFNRGcTGAIVGYHPFGGFNMSGTDSkaGGPDYLILHMQA 514
Cdd:cd07148 398 DVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYGT--GGIPYTMHDMTQ 449
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
68-497 |
7.38e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 205.88 E-value: 7.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 68 EIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKpwNEADA-----DTAE 142
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK--ARRHAfeevlDVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 143 AIDFlefYARQMLKL------KDGVPVQSREGEenkfNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADAT 216
Cdd:PRK09407 121 TARY---YARRAPKLlaprrrAGALPVLTKTTE----LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 217 PVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHpkTRFVSFTGSREVGCRIYEKASkvqpgqkwlKRVI---AEM 293
Cdd:PRK09407 194 PLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG---------RRLIgfsLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDSKG-YFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALT 451
Cdd:PRK09407 343 LETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1267504047 452 GALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYH-PFGGFNMSG 497
Cdd:PRK09407 423 ASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSG 469
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
48-452 |
3.35e-58 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 200.75 E-value: 3.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 48 GEELITTDEKIVSINPANKVEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVK 127
Cdd:PLN00412 22 GEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 128 EAGKPWNEADADTAEAIDFLEFYARQMLKL--------KDGVPVQSRegeeNKF---NYIPLGVGIIISPFNFPLAIMAG 196
Cdd:PLN00412 102 EIAKPAKDAVTEVVRSGDLISYTAEEGVRIlgegkflvSDSFPGNER----NKYcltSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 197 TAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSrEVGCRIYEKA 276
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 277 SKVqPGQkwlkrviAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVG 356
Cdd:PLN00412 257 GMV-PLQ-------MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 357 NPEDVSTyMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADdskGYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARD 435
Cdd:PLN00412 329 PPEDDCD-ITPVVSESSANFIEGLVMDAKEKGaTFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410
....*....|....*..
gi 1267504047 436 FDHMMEIANNTDYALTG 452
Cdd:PLN00412 405 VEEGIHHCNASNFGLQG 421
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
171-508 |
1.11e-54 |
|
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: 190.59 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEA----GLPKGVLNFIPGvTPE 246
Cdd:cd07098 114 ARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTC-LPE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 247 IGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKC 326
Cdd:cd07098 193 TAEALTSHPVIDHITFIGSPPVGKKVMAAAAES------LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 327 SAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGE----ADDSKG 401
Cdd:cd07098 267 IGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGaRLLAGGKryphPEYPQG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 402 YFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCT 481
Cdd:cd07098 347 HYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGV 426
|
330 340
....*....|....*....|....*..
gi 1267504047 482 GAIVGYHPFGGFNMSGTDsKAGGPDYL 508
Cdd:cd07098 427 NYYVQQLPFGGVKGSGFG-RFAGEEGL 452
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
176-498 |
8.04e-51 |
|
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: 179.72 E-value: 8.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 176 IPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGdYLVQHp 255
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT-ALLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 256 KTRFVSFTGSREVGCRIYEKASkvqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVH 335
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAA------KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 336 QDVYDIVLEkavALTKTLK--VGNPEDVSTYMGPVSHEASYNKVLSYIEIGKeeGRLMTGGEADDSKgYFIQPTIFADVD 413
Cdd:cd07135 258 PSVYDEFVE---ELKKVLDefYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--GKVVIGGEMDEAT-RFIPPTIVSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 414 EKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNR-----GCTGAivgyh 488
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtlihvGVDNA----- 406
|
330
....*....|
gi 1267504047 489 PFGGFNMSGT 498
Cdd:cd07135 407 PFGGVGDSGY 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
58-462 |
2.90e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 176.95 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 58 IVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD 137
Cdd:PLN02315 36 VSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 138 ADTAEAIDFLEFYARQMLKLKDGVPVQSREGEENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATP 217
Cdd:PLN02315 115 GEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 218 VVA---AKFV-EVMEEAGLPKGVLNFIPGVTpEIGDYLVQHPKTRFVSFTGSREVGcRIYEKASKVQPGQKWLkrviaEM 293
Cdd:PLN02315 195 LITiamTKLVaEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVG-LMVQQTVNARFGKCLL-----EL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 294 GGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEAS 373
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPES 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 374 YNKVLSYIEIGKEEG-RLMTGGEADDSKGYFIQPTIfADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTG 452
Cdd:PLN02315 348 KKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410
....*....|
gi 1267504047 453 ALLSSTPAHI 462
Cdd:PLN02315 427 SIFTRNPETI 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
33-477 |
1.79e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 176.86 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 33 ETVHSQLGKDYPLVIGEELITTDEK--IVSINPANKvEIIGRVSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRA 110
Cdd:PLN02419 104 QSTQPQMPPRVPNLIGGSFVESQSSsfIDVINPATQ-EVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 111 ADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEfYARQMLKLKDG--VPVQSrEGEENKFNYIPLGVGIIISPFN 188
Cdd:PLN02419 183 QELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVE-HACGMATLQMGeyLPNVS-NGVDTYSIREPLGVCAGICPFN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 189 FPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGvTPEIGDYLVQHPKTRFVSFTGSREV 268
Cdd:PLN02419 261 FPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHG-TNDTVNAICDDEDIRAVSFVGSNTA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 269 GCRIYEKASKVQpgqkwlKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVY---DIVLEK 345
Cdd:PLN02419 340 GMHIYARAAAKG------KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVER 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 346 AvaltKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGE----ADDSKGYFIQPTIFADVDEKARLMQ 420
Cdd:PLN02419 414 A----KALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRdivvPGYEKGNFIGPTILSGVTPDMECYK 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267504047 421 EEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFN 477
Cdd:PLN02419 490 EEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
91-497 |
9.50e-46 |
|
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: 165.78 E-value: 9.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 91 TFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD----ADTAEAIDFLEFYARQMLKLKD-GVPVQS 165
Cdd:cd07087 10 TFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVVLGEIDHALKHLKKWMKPRRvSVPLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 166 REGEeNKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTP 245
Cdd:cd07087 90 QPAK-AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 246 EIGDYLvqhpKTRF--VSFTGSREVGCRIYEKASkvqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSG 323
Cdd:cd07087 168 VATALL----AEPFdhIFFTGSPAVGKIVMEAAA------KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 324 QKCSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYmGPVSHEASYNKVLSYIeigkEEGRLMTGGEADDSKGYf 403
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLL----DDGKVVIGGQVDKEERY- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 404 IQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGA 483
Cdd:cd07087 312 IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHA 391
|
410
....*....|....
gi 1267504047 484 IVGYHPFGGFNMSG 497
Cdd:cd07087 392 AIPNLPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
73-497 |
1.81e-41 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 155.19 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 73 VSKTNQELAEKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEAD-ADTAEAIDFLEFYA 151
Cdd:PTZ00381 1 QEPDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 152 RQMLKLKDGVPVQSrEG----EENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVM 227
Cdd:PTZ00381 81 KHLDEYLKPEKVDT-VGvfgpGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 228 EEAgLPKGVLNFIPGVTPEIGDYLvqhpKTRF--VSFTGSREVGCRIYEKASKvqpgqkWLKRVIAEMGGKDTVVVDKDA 305
Cdd:PTZ00381 160 TKY-LDPSYVRVIEGGVEVTTELL----KEPFdhIFFTGSPRVGKLVMQAAAE------NLTPCTLELGGKSPVIVDKSC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 306 DLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEkavaltkTLKvgnpEDVSTYMGP-VSHEASYNKVL--SYIE 382
Cdd:PTZ00381 229 NLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE-------ALK----EAIKEFFGEdPKKSEDYSRIVneFHTK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 383 -----IGKEEGRLMTGGEADDSKGYfIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSS 457
Cdd:PTZ00381 298 rlaelIKDHGGKVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1267504047 458 TPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 497
Cdd:PTZ00381 377 DKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
175-497 |
3.17e-41 |
|
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: 153.81 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 175 YIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQh 254
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQ- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 255 pKTRFVSFTGSREVGCRIYEKASKvqpgqkWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRAVV 334
Cdd:cd07136 176 -KFDYIFFTGSVRVGKIVMEAAAK------HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 335 HQDVYDIVLEKAVALTKTLKVGNPEDVSTYmGPVSHEASYNKVLSYIEIGKeegrLMTGGEADDsKGYFIQPTIFADVDE 414
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGK----IVFGGNTDR-ETLYIEPTILDNVTW 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 415 KARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSStpahiERAKEEFHVGNLYFNRGCTGAIVgYH------ 488
Cdd:cd07136 323 DDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSE-----DKKVEKKVLENLSFGGGCINDTI-MHlanpyl 396
|
....*....
gi 1267504047 489 PFGGFNMSG 497
Cdd:cd07136 397 PFGGVGNSG 405
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-506 |
1.70e-37 |
|
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: 143.53 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 95 WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA-DADTAEAIDFLEFYARQMLKLKDGV---PVQSREgEE 170
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAeNICGDQVQLRARAFVIYSYRIPHEPgnhLGQGLK-QQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAG-LPKGVLNFIPGvTPEIGD 249
Cdd:cd07084 94 SHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLING-DGKTMQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 250 YLVQHPKTRFVSFTGSREVGCRIYEKASKVqpgqkwlkRVIAEMGGKDTVVVDKDAD-LDLAASSIVYSAFGFSGQKCSA 328
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSRVAEKLALDAKQA--------RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 329 GSRAVVHQDVY-DIVLEKAVALTKTLKVGnpedvSTYMGPVsheaSYNKVLSYI-EIGKEEGRLMTGG-------EADDS 399
Cdd:cd07084 245 QSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPV----QTFTTLAMIaHMENLLGSVLLFSgkelknhSIPSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 400 KGYFIQPTIFADVDE---KARLMQEEIFGPV--VAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHV-GN 473
Cdd:cd07084 316 YGACVASALFVPIDEilkTYELVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVaGR 395
|
410 420 430
....*....|....*....|....*....|....
gi 1267504047 474 LYF-NRGCTGAIVGYHPFGGFNMSGTDSKAGGPD 506
Cdd:cd07084 396 TYAiLRGRTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
95-497 |
2.70e-35 |
|
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: 136.97 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 95 WKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPwnEADADTAEAIDFLEFYARQMLKLKDGV-PVQSR-----EG 168
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP--AAEVDLTEILPVLSEINHAIKHLKKWMkPKRVRtplllFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 169 EENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVtpEIG 248
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDA--EVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 249 DYLVQHPktrF--VSFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKC 326
Cdd:cd07134 170 QALLELP---FdhIFFTGSPAVGKIVMAAAAKH------LASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 327 SAGSRAVVHQDVYDIVLEKAVA-LTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEG-RLMTGGEADDSKGYfI 404
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAeIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGaKVEFGGQFDAAQRY-I 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 405 QPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrGCTGAI 484
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-DVVLHF 398
|
410
....*....|....
gi 1267504047 485 VGYH-PFGGFNMSG 497
Cdd:cd07134 399 LNPNlPFGGVNNSG 412
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
82-497 |
8.00e-34 |
|
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: 133.12 E-value: 8.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 82 EKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA--------DADTAEAIDFL------ 147
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpewmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 148 EFYARQMLKLKDGVPVQSRegeenkfnyiPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVvAAKFVEVM 227
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKE----------PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPA-TAKLLAEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 228 eeagLPKGVLN----FIPGVTPEIGDYLvqhpKTRF--VSFTGSREVGCRIYEKASKvqpgqkWLKRVIAEMGGKDTVVV 301
Cdd:cd07132 150 ----IPKYLDKecypVVLGGVEETTELL----KQRFdyIFYTGSTSVGKIVMQAAAK------HLTPVTLELGGKSPCYV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 302 DKDADLDLAASSIVYSAFGFSGQKCSAGSRAVVHQDVYDIVLEKavaLTKTLK--VGNPEDVSTYMGPVSHEASYNKVLS 379
Cdd:cd07132 216 DKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEA---LKKTLKefYGEDPKESPDYGRIINDRHFQRLKK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 380 YIEigkeEGRLMTGGEADDSKGYfIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTP 459
Cdd:cd07132 293 LLS----GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNK 367
|
410 420 430
....*....|....*....|....*....|....*...
gi 1267504047 460 AHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 497
Cdd:cd07132 368 KVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
103-465 |
2.23e-32 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 130.21 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 103 RANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQMLKL------KDGVPVQSreGEENKFN-- 174
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALgdarllRDGEAVQL--GKDPAFQgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 175 --YIPL-GVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAG-LPKGVLNFIPGVTpeiGDY 250
Cdd:PRK11903 143 hvLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS---AGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 251 LVQHPKTRFVSFTGSREVGCRIYEKASKVQPGQkwlkRVIAEMGGKDTVVVDKDAD-----LDLAASSIVYSAFGFSGQK 325
Cdd:PRK11903 220 LDHLQPFDVVSFTGSAETAAVLRSHPAVVQRSV----RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 326 CSAGSRAVVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGG------EADDS 399
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGggfalvDADPA 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267504047 400 KGYFIQPTIF--ADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERA 465
Cdd:PRK11903 376 VAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
175-497 |
9.64e-28 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 115.27 E-value: 9.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 175 YIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKgVLNFIPGvTPEIG------ 248
Cdd:cd07133 99 YQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTG-GADVAaafssl 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 249 --DYLVqhpktrfvsFTGSREVGCRIYEKASKVqpgqkwLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKC 326
Cdd:cd07133 177 pfDHLL---------FTGSTAVGRHVMRAAAEN------LTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 327 SAGSRAVVHQDVYDIVLEKAVALTKTL---KVGNPEdvstYMGPVShEASYNKVLSYIEIGKEEG-RLMTGGEA--DDSK 400
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPD----YTSIIN-ERHYARLQGLLEDARAKGaRVIELNPAgeDFAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 401 GYFIQPTIFADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgc 480
Cdd:cd07133 317 TRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--- 393
|
330 340
....*....|....*....|...
gi 1267504047 481 tgaIVGYH------PFGGFNMSG 497
Cdd:cd07133 394 ---DTLLHvaqddlPFGGVGASG 413
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
177-503 |
2.04e-27 |
|
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: 114.43 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 177 PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEiGDYLVQHpK 256
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPE-TTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 257 TRFVSFTGSREVGcRIYEKASKvqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGF-SGQKCSAGSRAVVH 335
Cdd:cd07137 178 WDKIFFTGSPRVG-RIIMAAAA-----KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 336 QDVYDIVLEkavALTKTLK--VGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDSKGYfIQPTIFADVD 413
Cdd:cd07137 252 ESFAPTLID---ALKNTLEkfFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLY-IEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 414 EKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGF 493
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGV 407
|
330
....*....|
gi 1267504047 494 NMSGTDSKAG 503
Cdd:cd07137 408 GESGFGAYHG 417
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
179-464 |
1.35e-26 |
|
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: 113.13 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 179 GVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAG-LPKGVLNFIPGVTpeiGDYLVQHPKT 257
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSV---GDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 258 RFVSFTGSREVGCRIYEKASKVQPGqkwlKRVIAEMGGKDTVVVDKDA-----DLDLAASSIVYSAFGFSGQKCSAGSRA 332
Cdd:cd07128 223 DVVAFTGSAATAAKLRAHPNIVARS----IRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 333 VVHQDVYDIVLEKAVALTKTLKVGNPEDVSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGG-------EADDSKGYFIQ 405
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrfevvGADAEKGAFFP 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 406 PTIF--ADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIER 464
Cdd:cd07128 379 PTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
177-497 |
1.15e-22 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 100.96 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 177 PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVlNFIPGvTPEIGDYLVQHPK 256
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 257 TRfVSFTGSREVGCRIYEKASkvqpgqKWLKRVIAEMGGKDTVVVD---KDADLDLAASSIVYSAFGF-SGQKCSAGSRA 332
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAA------KHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 333 VVHQDVYDIVLEkavALTKTLK---VGNPEDvSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEADDsKGYFIQPTIF 409
Cdd:PLN02203 259 LVEERFAPILIE---LLKSTIKkffGENPRE-SKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDE-KKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 410 ADVDEKARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNrgctGAIVGYH- 488
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN----DAIIQYAc 409
|
330
....*....|..
gi 1267504047 489 ---PFGGFNMSG 497
Cdd:PLN02203 410 dslPFGGVGESG 421
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
177-503 |
3.15e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 96.65 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 177 PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAgLPKGVLNFIPGVTPEIGDYLVQhpK 256
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 257 TRFVSFTGSREVGCRIYEKASkvqpgqKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGF-SGQKCSAGSRAVVH 335
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 336 QDVYDIVLEKAVALTKTLKVGNPEDvSTYMGPVSHEASYNKVLSYIEIGKEEGRLMTGGEaDDSKGYFIQPTIFADVDEK 415
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 416 ARLMQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIERAKEEFHVGNLYFNRGCTGAIVGYHPFGGFNM 495
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....*...
gi 1267504047 496 SGTDSKAG 503
Cdd:PLN02174 421 SGMGAYHG 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
98-464 |
8.03e-19 |
|
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: 89.09 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 98 ENPE---VRANILFRAADIIRRRKHE--FSSYLVKEAGKPWNEADADTAEAIDFLE-FYARQMLKLKDGVPVQ-SREGEE 170
Cdd:cd07126 56 KNPErylLYGDVSHRVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLEnFAGDQVRFLARSFNVPgDHQGQQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 171 NKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDy 250
Cdd:cd07126 136 SSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 251 LVQHPKTRFVSFTGSRevgcRIYEKASKVQPGqkwlkRVIAEMGGKDTVVVDKD-ADLDLAASSIVYSAFGFSGQKCSAG 329
Cdd:cd07126 215 ILLEANPRMTLFTGSS----KVAERLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 330 SRAVVHQDVYDI-VLEKAVALTKTLKVgnpEDVStyMGPV---SHEASYNKVLSYIEIGKEE----GRLMTGGEADDSKG 401
Cdd:cd07126 286 SILFAHENWVQAgILDKLKALAEQRKL---EDLT--IGPVltwTTERILDHVDKLLAIPGAKvlfgGKPLTNHSIPSIYG 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267504047 402 YfIQPT-IFADVDEKA-----RLMQEEIFGP--VVAFCKARDFDHMMEIANNTDYALTGALLSSTPAHIER 464
Cdd:cd07126 361 A-YEPTaVFVPLEEIAieenfELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQE 430
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
84-467 |
1.33e-18 |
|
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: 88.69 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 84 AMQTALSTfntWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEA-DADTAEAID----FLEFYARQMLKLK 158
Cdd:cd07127 92 AARAAMPG---WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfQAGGPHAQDrgleAVAYAWREMSRIP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 159 DGVPVQSREGE------ENKFNYIPLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKPADATPVVAAKFV----EVME 228
Cdd:cd07127 169 PTAEWEKPQGKhdplamEKTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVqvarEVLA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 229 EAGL-PKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASKVQpgqkwlkrVIAEMGGKDTVVVDKDADL 307
Cdd:cd07127 249 EAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDSTDDL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 308 DLAASSIVYSAFGFSGQKCSAGSRAVVHQD---------VYDIVLEK-AVALTKTLkvGNPEDVSTYMGPVSHEAsynkV 377
Cdd:cd07127 321 KAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADlAAAIDGLL--ADPARAAALLGAIQSPD----T 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 378 LSYIEIGKEEGRLMTGGEA----DDSKGYFIQPTIFA-DVDEKARLMQEEiFGPVVAFCKARDFDHMMEIANN---TDYA 449
Cdd:cd07127 395 LARIAEARQLGEVLLASEAvahpEFPDARVRTPLLLKlDASDEAAYAEER-FGPIAFVVATDSTDHSIELAREsvrEHGA 473
|
410
....*....|....*...
gi 1267504047 450 LTGALLSSTPAHIERAKE 467
Cdd:cd07127 474 MTVGVYSTDPEVVERVQE 491
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
82-487 |
6.82e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 70.65 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 82 EKAMQTALSTFNTWKKENPEVRANILFRAADIIRRRKHEFSSYLVKEAGKPWNEADADTAEAIDFLEFYARQmlkLKDGV 161
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADL---VREGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 162 PVQSREGEEN-----------KFNYIPLGVGIIISPFNFPLAIMAG--TAAAAIVTGNTILLKPADATP----VVAAKFV 224
Cdd:cd07129 79 WLDARIDPADpdrqplprpdlRRMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPgtseLVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 225 EVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVGCRIYEKASK-VQPgqkwlKRVIAEMGGKDTVVVDK 303
Cdd:cd07129 159 AALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArPEP-----IPFYAELGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 304 DA---DLDLAASSIVYSAFGFSGQKC-SAGSRAVVHQDVYDIVLEkavALTKTLKVGNPedvSTYMGPVSHEAsYNKVLS 379
Cdd:cd07129 234 GAlaeRGEAIAQGFVGSLTLGAGQFCtNPGLVLVPAGPAGDAFIA---ALAEALAAAPA---QTMLTPGIAEA-YRQGVE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 380 yiEIGKEEGRLMTGGEADDSKGYFIQPTIFAdVDEKARL----MQEEIFGPVVAFCKARDFDHMMEIANNTDYALTGALL 455
Cdd:cd07129 307 --ALAAAPGVRVLAGGAAAEGGNQAAPTLFK-VDAAAFLadpaLQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIH 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 1267504047 456 SSTpAHIERAKE-----EFHVGNLYFNRGCTGAIVGY 487
Cdd:cd07129 384 GEE-DDLALAREllpvlERKAGRLLFNGWPTGVEVCP 419
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
177-345 |
2.22e-11 |
|
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: 65.71 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 177 PLGVGIIISPFNFPLAIMAGTAAAaIVTGNTILLKP---ADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLVQ 253
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 254 HPKTRFVSFTGSREVgcriYEKASKVQPGqkwlKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFgFSGQKCSAGSRAV 333
Cdd:cd07077 179 HPKIDLIVATGGRDA----VDAAVKHSPH----IPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLY 249
|
170
....*....|..
gi 1267504047 334 VHQDVYDIVLEK 345
Cdd:cd07077 250 VVDDVLDPLYEE 261
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
177-345 |
9.91e-10 |
|
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: 60.74 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 177 PLGVGIIISPFNFPLAIMAGTAAAAIVTGNTILLKP----ADATPVVAAKFVEVMEEAGLPKGVLNFIPGVTPEIGDYLV 252
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 253 QHPKTRFVSFTGSREVgcriyekaskVQPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAFGFSGQKCSAGSRA 332
Cdd:cd07081 175 KFPGIGLLLATGGPAV----------VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170
....*....|...
gi 1267504047 333 VVHQDVYDIVLEK 345
Cdd:cd07081 245 IVVDSVYDEVMRL 257
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
205-443 |
1.68e-07 |
|
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: 53.39 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 205 GNTILLKPADATPVVAAKFVEVMEEA----GLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVgcriyekaskVQ 280
Cdd:cd07121 125 GNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAV----------VK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 281 PGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAfGFSGQ-KCSAGSRAVVHQDVYD-------------IVLEKA 346
Cdd:cd07121 195 AALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADyliaamqrngayvLNDEQA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 347 VALTKTLKVGNPEDVStymgpvsheasyNKVLsyieIGKEEGRL--MTGGEADDSKgyfiqPTIFADVDEKARLMQEEIF 424
Cdd:cd07121 274 EQLLEVVLLTNKGATP------------NKKW----VGKDASKIlkAAGIEVPADI-----RLIIVETDKDHPFVVEEQM 332
|
250
....*....|....*....
gi 1267504047 425 GPVVAFCKARDFDHMMEIA 443
Cdd:cd07121 333 MPILPVVRVKNFDEAIELA 351
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
204-484 |
1.93e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 204 TGNTILLKP---ADATPVVAAKFV-EVMEEAGLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSrevgcriyekASKV 279
Cdd:cd07122 122 TRNAIIFSPhprAKKCSIEAAKIMrEAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG----------PGMV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 280 QPGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYS-AFGFsGQKCSAGSRAVVHQDVYDIVLE-----KAVALTKTL 353
Cdd:cd07122 192 KAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRAelkrrGAYFLNEEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 354 KvgnpEDVSTYM----GPVSHEAsynkvlsyieIGKEEGRL--MTGGEADDSKGYFIQPtiFADVDEKARLMQEEIFgPV 427
Cdd:cd07122 271 K----EKLEKALfddgGTLNPDI----------VGKSAQKIaeLAGIEVPEDTKVLVAE--ETGVGPEEPLSREKLS-PV 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267504047 428 VAFCKARDFDHMMEIAN-NTDYA---LTGALLSSTPAHIERAKEEFHVGNLYFNR-GCTGAI 484
Cdd:cd07122 334 LAFYRAEDFEEALEKAReLLEYGgagHTAVIHSNDEEVIEEFALRMPVSRILVNTpSSLGGI 395
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
205-443 |
1.18e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 47.97 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 205 GNTILLKPADATPVVAAKFVEVMEEA----GLPKGVLNFIPGVTPEIGDYLVQHPKTRFVSFTGSREVgcriyekaskVQ 280
Cdd:PRK15398 157 GNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAV----------VK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 281 PGQKWLKRVIAEMGGKDTVVVDKDADLDLAASSIVYSAfGFSGQ-KCSAGSRAVVHQDVYD-----IVLEKAVALtktlk 354
Cdd:PRK15398 227 AAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIAEKEVIVVDSVADelmrlMEKNGAVLL----- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267504047 355 vgNPEDVSTYMGPVSHEASY-NKVLsyieIGKEEGRLM--TGGEADDSKgyfiqPTIFADVDEKARLMQEEIFGPVVAFC 431
Cdd:PRK15398 301 --TAEQAEKLQKVVLKNGGTvNKKW----VGKDAAKILeaAGINVPKDT-----RLLIVETDANHPFVVTELMMPVLPVV 369
|
250
....*....|..
gi 1267504047 432 KARDFDHMMEIA 443
Cdd:PRK15398 370 RVKDVDEAIALA 381
|
|
| |
