|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1-515 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 1031.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 1 MVRTYQHEPFTNFKDEKNQELFQEALSYVNTQLGKTYPLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMN 80
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 81 AALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSR 160
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 161 PGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSI 240
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 241 IGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKC 320
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 321 SAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESvDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNGFFVQP 400
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 401 TVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVG 480
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500 510
....*....|....*....|....*....|....*
gi 1154270283 481 YQPFGGFNMSGTDSKAGGPDYLLLHMQAKTTSEMF 515
Cdd:PRK03137 480 YHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-515 |
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: 891.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 5 YQHEPFTNFKDEKNQELFQEALSYVNTQLGKTYPLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALE 84
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 85 AFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELtKGQPVNSRPGEY 164
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL-RGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 165 NQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDY 244
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 245 LVEHPKTRFVSFTGSREVGCRIYERAAKVQSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGS 324
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 325 RAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGE--GDSSNGFFVQPTV 402
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEvlELAAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 403 FGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQ 482
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|...
gi 1154270283 483 PFGGFNMSGTDSKAGGPDYLLLHMQAKTTSEMF 515
Cdd:cd07124 480 PFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-515 |
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: 848.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 5 YQHEPFTNFKDEKNQELFQEALSYVNTQLGKTYPLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALE 84
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 85 AFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSRPGEY 164
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 165 NQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDY 244
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 245 LVEHPKTRFVSFTGSREVGCRIYERAAKVQSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGS 324
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 325 RAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNGFFVQPTVFG 404
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 405 NIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPF 484
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500 510
....*....|....*....|....*....|.
gi 1154270283 485 GGFNMSGTDSKAGGPDYLLLHMQAKTTSEMF 515
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
35-513 |
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: 565.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 35 KTYPLIINGERIE--TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRK 112
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPATG-EVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 113 HEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTA 192
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 193 IAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAK 272
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 273 vqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNP 352
Cdd:COG1012 243 ------NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 353 ESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEG-DSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDF 430
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 431 DHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAiVGYQPFGGFNMSGTDSKaGGPDYLLLHMQAKT 510
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
...
gi 1154270283 511 TSE 513
Cdd:COG1012 475 VTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
42-510 |
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: 560.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 42 NGERIEtdekttSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVK 121
Cdd:pfam00171 5 ESETIE------VINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 122 EAGKPWNEADADTAEAIDFIEYYGRQMLELTkGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNT 201
Cdd:pfam00171 78 ENGKPLAEARGEVDRAIDVLRYYAGLARRLD-GETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 202 ILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLK 281
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 282 RVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGP 361
Cdd:pfam00171 231 RVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 362 VIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNT 440
Cdd:pfam00171 311 LISKAQLERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDT 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 441 DYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYqPFGGFNMSGTdSKAGGPDYLLLHMQAKT 510
Cdd:pfam00171 391 EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGF-GREGGPYGLEEYTEVKT 458
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
20-515 |
0e+00 |
|
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: 521.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 20 ELFQEALSYVNTQLGKTYPLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRAN 99
Cdd:cd07083 2 RAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 100 ILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQP-VNSRPGEYNQYNYVPLGVGVII 178
Cdd:cd07083 82 LLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGLGAGVVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 179 SPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTG 258
Cdd:cd07083 162 SPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 259 SREVGCRIYERAAKVQSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVE 338
Cdd:cd07083 242 SLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 339 KVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIF 418
Cdd:cd07083 322 RLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 419 GPVVAVC--KARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKA 496
Cdd:cd07083 402 GPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKT 481
|
490
....*....|....*....
gi 1154270283 497 GGPDYLLLHMQAKTTSEMF 515
Cdd:cd07083 482 GGPHYLRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-510 |
3.25e-163 |
|
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: 469.77 E-value: 3.25e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 76 EKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQ 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 156 PVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIP 235
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 236 GKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGF 315
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE------NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 316 SGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEG-DSS 393
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRlEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 394 NGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRG 473
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1154270283 474 CTGAiVGYQPFGGFNMSGTdSKAGGPDYLLLHMQAKT 510
Cdd:cd07078 395 SVGA-EPSAPFGGVKQSGI-GREGGPYGLEEYTEPKT 429
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
15-513 |
3.18e-159 |
|
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: 462.82 E-value: 3.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 15 DEK-NQELFQEALSYVNTQLGKTYPlIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWK 93
Cdd:cd07125 11 DLEvPLEALADALKAFDEKEWEAIP-IINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 94 AEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSRPGEYNQYNYVPLG 173
Cdd:cd07125 90 VEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 174 VGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRF 253
Cdd:cd07125 170 VFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 254 VSFTGSREVGCRIYERAAKVQSGQIwlkRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVY 333
Cdd:cd07125 250 VIFTGSTETAKLINRALAERDGPIL---PLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 334 DEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNGFFVQPTVFGNIHQDarLM 413
Cdd:cd07125 327 ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIF--DL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 414 KEEIFGPVVAVC--KARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07125 405 TTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSG 484
|
490 500
....*....|....*....|..
gi 1154270283 492 TDSKAGGPDYLLLHMQAKTTSE 513
Cdd:cd07125 485 TGPKAGGPNYLLRFGNEKTVSL 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
37-510 |
2.22e-144 |
|
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: 423.20 E-value: 2.22e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFS 116
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 117 AYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAI 196
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 197 VTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQsg 276
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 277 qiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVD 356
Cdd:cd07097 239 ----ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 357 TYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE-GDSSN-GFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHM 433
Cdd:cd07097 315 VDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGErLKRPDeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154270283 434 LEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGaiVGYQ-PFGGFNMSGTDSKAGGPDYLLLHMQAKT 510
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALEFYTTIKT 470
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
38-503 |
1.01e-139 |
|
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: 413.14 E-value: 1.01e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 38 PLIINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLR-RRKHEFS 116
Cdd:cd07123 34 PLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 117 AYLVKEAGKPWNEADADTA-EAIDFIEYYGRQMLELTKGQPVNSRPGEYNQYNYVPL-GVGVIISPFNFPlAIMAGTAIA 194
Cdd:cd07123 114 AATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 195 AIVTGNTILLKPADaTPVVAAKFV-ELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKV 273
Cdd:cd07123 193 PALMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 274 QSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPE 353
Cdd:cd07123 272 LDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 354 SVDTYMGPVIHQASFDKIMKYIEIGRTEGDL--LVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVA--VCKARD 429
Cdd:cd07123 352 DFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAeiIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTvyVYPDSD 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 430 FDHMLEIANNT-DYGLTGAVLSNTRANIERAREEFH--VGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYLL 503
Cdd:cd07123 432 FEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLL 508
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-499 |
2.99e-139 |
|
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: 410.20 E-value: 2.99e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIE--TDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAY 118
Cdd:cd07131 3 IGGEWVDsaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 119 LVKEAGKPWNEADADTAEAIDFIEYY---GRQMleltKGQPVNSRPGEYNQYNY-VPLGVGVIISPFNFPLAIMAGTAIA 194
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAageGRRL----FGETVPSELPNKDAMTRrQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 195 AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQ 274
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 275 sgqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPES 354
Cdd:cd07131 239 ------KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 355 VDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE----GDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARD 429
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGaTLLLGGErltgGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVgYQPFGGFNMSGTDSKAGGP 499
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGT 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
41-491 |
5.18e-126 |
|
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: 376.52 E-value: 5.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIETDEKT-TSINPSNKKEVIGyVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYL 119
Cdd:cd07086 3 IGGEWVGSGGETfTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 120 VKEAGKPWNEADADTAEAIDFIEYY---GRQMleltKGQPVNS-RPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAA 195
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAvglSRML----YGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 196 IVTGNTILLKPADATPVVAAKFVELMEEA----GLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERAA 271
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 272 KVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGN 351
Cdd:cd07086 237 RR------FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 352 PESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEG--DSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKAR 428
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154270283 429 DFDHMLEIANNTDYGLTGAVLSNTRANIERAREEF--HVGNLYFNRGCTGAIVGyQPFGGFNMSG 491
Cdd:cd07086 391 SLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
39-491 |
1.21e-125 |
|
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: 375.39 E-value: 1.21e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIE-TDEKT-TSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWK--AEDRANILFRAAAMLRRRKHE 114
Cdd:cd07091 6 LFINNEFVDsVSGKTfPTINPATE-EVICQVAEADEEDVDAAVKAARAAFETGWWRKmdPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNE-ADADTAEAIDFIEYYGRQMLELTkGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAI 193
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQ-GKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 AAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKV 273
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 274 QsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPE 353
Cdd:cd07091 244 N-----LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 354 SVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDH 432
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 433 MLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgcTGAIVGYQ-PFGGFNMSG 491
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-512 |
1.30e-125 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 391.87 E-value: 1.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 12 NFKDEKNQELFQEAlsyVNTQLGKTY--PLIINGerieTDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDW 89
Cdd:PRK11904 529 NLNDRSELEPLAAA---IAAFLEKQWqaGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAW 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 90 KKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQM-LELTKGQPVNSRPGEYNQYN 168
Cdd:PRK11904 602 SRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQArRLFGAPEKLPGPTGESNELR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 169 YVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEH 248
Cdd:PRK11904 682 LHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTAD 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 249 PKTRFVSFTGSREVGCRIyERAAKVQSGQIwlkrV--IAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRA 326
Cdd:PRK11904 762 PRIAGVAFTGSTETARII-NRTLAARDGPI----VplIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVL 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 327 VIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGE--GDSSNGFFVQPTVF- 403
Cdd:PRK11904 837 FVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPlpAGTENGHFVAPTAFe 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 404 -GNIHQdarlMKEEIFGPV--VAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVG 480
Cdd:PRK11904 917 iDSISQ----LEREVFGPIlhVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVG 992
|
490 500 510
....*....|....*....|....*....|..
gi 1154270283 481 YQPFGGFNMSGTDSKAGGPDYLLLHMQAKTTS 512
Cdd:PRK11904 993 VQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
55-491 |
3.55e-125 |
|
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: 373.31 E-value: 3.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07103 2 INPATG-EVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGRQMLELTkGQPVNSR-PGEYNQYNYVPLGVGVIISPFNFPLAIMA---GTAIAAivtGNTILLKPADAT 210
Cdd:cd07103 81 DYAASFLEWFAEEARRIY-GRTIPSPaPGKRILVIKQPVGVVAAITPWNFPAAMITrkiAPALAA---GCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGK 290
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT------VKRVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVL 449
Cdd:cd07103 311 VEALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1154270283 450 SNTRANIERAREEFHVGNLYFNRGCTGAIVgyQPFGGFNMSG 491
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESG 430
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-506 |
2.52e-124 |
|
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: 371.60 E-value: 2.52e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIE--TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAY 118
Cdd:cd07088 2 INGEFVPssSGETIDVLNPATG-EVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 119 LVKEAGKPWNEADADTAEAIDFIEYYGRQMLELtKGQPVNS-RPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIV 197
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRI-EGEIIPSdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 198 TGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgq 277
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEN---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 278 iwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDT 357
Cdd:cd07088 236 --ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 358 YMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSS-NGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLE 435
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154270283 436 IANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQpfGGFNMSGT---DSKAGGPDYLLLHM 506
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHGLEEYLQTKV 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
81-510 |
1.06e-122 |
|
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: 363.86 E-value: 1.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 81 AALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNSR 160
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 161 PGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSI 240
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 241 IGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKC 320
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN------LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 321 SAGSRAVIHEDVYDEVVEKVVsltktlkvgnpesvdtymgpvihqasfdkimkyieigrtegdllvggegdssngffvqp 400
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 401 TVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAiVG 480
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GP 335
|
410 420 430
....*....|....*....|....*....|
gi 1154270283 481 YQPFGGFNMSGTdSKAGGPDYLLLHMQAKT 510
Cdd:cd06534 336 EAPFGGVKNSGI-GREGGPYGLEEYTRTKT 364
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-511 |
2.74e-121 |
|
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: 363.41 E-value: 2.74e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEAD 131
Cdd:cd07114 1 SINPATG-EPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 132 ADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYN-YVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADAT 210
Cdd:cd07114 80 AQVRYLAEWYRYYA-GLADKIEGAVIPVDKGDYLNFTrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGK 290
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEG-DLLVGGE----GDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLT 445
Cdd:cd07114 313 VERYVARAREEGaRVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 446 GAVLSNTRANIERAREEFHVGNLYFNrgcTGAIVGYQ-PFGGFNMSGTDsKAGGPDYLLLHMQAKTT 511
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIG-RENGIEAIREYTQTKSV 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
62-492 |
5.21e-121 |
|
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: 362.68 E-value: 5.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 EYYGRQMLELTkGQ--PVNSRPGEYNQYNY---VPLGVGVIISPFNFPLAIMA---GTAIAAivtGNTILLKPADATPVV 213
Cdd:cd07149 90 RLSAEEAKRLA-GEtiPFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAhkvGPAIAA---GNAVVLKPASQTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 214 AAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAkvqsgqiwLKRVIAEMGGKDTV 293
Cdd:cd07149 166 ALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 294 LVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMK 373
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 374 YIEIGRTEG-DLLVGGEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNT 452
Cdd:cd07149 318 WVEEAVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1154270283 453 RANIERAREEFHVGNLYFNRGCTgAIVGYQPFGGFNMSGT 492
Cdd:cd07149 395 LQKALKAARELEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
40-512 |
1.52e-120 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 380.82 E-value: 1.52e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 40 IINGERiETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYL 119
Cdd:COG4230 561 LIAGEA-ASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 120 VKEAGKPWNEADADTAEAIDFIEYYGRQmleltkgqpvnSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTG 199
Cdd:COG4230 640 VREAGKTLPDAIAEVREAVDFCRYYAAQ-----------ARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 200 NTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGcRIYERA-AKVQSGQI 278
Cdd:COG4230 709 NTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETA-RLINRTlAARDGPIV 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 279 WLkrvIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAgSRAV-IHEDVYDEVVEKVVSLTKTLKVGNPESVDT 357
Cdd:COG4230 788 PL---IAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRVLcVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 358 YMGPVIHQASFDKIMKYIEIGRTEGDLL--VGGEGDSSNGFFVQPTVF--GNIHQdarlMKEEIFGPVVAVC--KARDFD 431
Cdd:COG4230 864 DVGPVIDAEARANLEAHIERMRAEGRLVhqLPLPEECANGTFVAPTLIeiDSISD----LEREVFGPVLHVVryKADELD 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 432 HMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYLLLHMQAKTT 511
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
.
gi 1154270283 512 S 512
Cdd:COG4230 1020 T 1020
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
75-499 |
1.53e-119 |
|
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: 358.00 E-value: 1.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 75 AEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIeyygRQMLELT-- 152
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL----REAAGLPrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 153 -KGQPVNS-RPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLKPADATPVVAA-KFVELMEEAGLPK 228
Cdd:cd07104 78 pEGEILPSdVPGKESMVRRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDSRTPVTGGlLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 229 GVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSI 308
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 309 VYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVG 387
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 388 GEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNtraNIERAR---EEFH 464
Cdd:cd07104 311 GTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTR---DLERAMafaERLE 384
|
410 420 430
....*....|....*....|....*....|....*...
gi 1154270283 465 VGNLYFNrGCT---GAIVgyqPFGGFNMSGTdSKAGGP 499
Cdd:cd07104 385 TGMVHIN-DQTvndEPHV---PFGGVKASGG-GRFGGP 417
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-511 |
3.28e-117 |
|
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: 353.02 E-value: 3.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADA- 132
Cdd:cd07093 1 NFNPATG-EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 133 DTAEAIDFIEYYGrqmlELTKGQPVNSRPGEYNQYNYV---PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADA 209
Cdd:cd07093 80 DIPRAAANFRFFA----DYILQLDGESYPQDGGALNYVlrqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 210 TPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGG 289
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 290 KDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFD 369
Cdd:cd07093 230 KNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 370 KIMKYIEIGRTEGD-LLVGG----EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGL 444
Cdd:cd07093 310 KVLGYVELARAEGAtILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 445 TGAVLSNTRANIERAREEFHVG----NLYFNRGCTgaivgyQPFGGFNMSGTdSKAGGPDYLLLHMQAKTT 511
Cdd:cd07093 390 AAYVWTRDLGRAHRVARRLEAGtvwvNCWLVRDLR------TPFGGVKASGI-GREGGDYSLEFYTELKNV 453
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
37-502 |
5.32e-117 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 372.28 E-value: 5.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGErieTDEKTTSI-NPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEF 115
Cdd:PRK11905 556 APLLAGGD---VDGGTRPVlNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPEL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 116 SAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQPVNsrpgeynqynyvPLGVGVIISPFNFPLAIMAGTAIAA 195
Cdd:PRK11905 633 FALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHK------------PLGPVVCISPWNFPLAIFTGQIAAA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 196 IVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQS 275
Cdd:PRK11905 701 LVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSG 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 276 GQIWLkrvIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESV 355
Cdd:PRK11905 781 PPVPL---IAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 356 DTYMGPVIHQASFDKIMKYIEIGRTEGDLL--VGGEGDSSNGFFVQPTVF--GNIHQdarlMKEEIFGPVVAVC--KARD 429
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAGRLVhqLPLPAETEKGTFVAPTLIeiDSISD----LEREVFGPVLHVVrfKADE 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYL 502
Cdd:PRK11905 934 LDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYL 1006
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-491 |
1.88e-115 |
|
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: 348.55 E-value: 1.88e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 56 NPsNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTA 135
Cdd:cd07150 5 NP-ADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 136 EAIDFIeyygRQMLELT---KGQPVNS-RPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLKPADAT 210
Cdd:cd07150 84 FTPELL----RAAAGECrrvRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPL-ILATKKVAfALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGK 290
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRH------LKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEG-DLLVGGEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVL 449
Cdd:cd07150 313 IKRQVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 450 SNtraNIERA-------------------REEFHVgnlyfnrgctgaivgyqPFGGFNMSG 491
Cdd:cd07150 390 TN---DLQRAfklaerlesgmvhindptiLDEAHV-----------------PFGGVKASG 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
54-491 |
7.30e-113 |
|
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: 341.91 E-value: 7.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAF-VDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADA 132
Cdd:cd07109 1 VFDPSTG-EVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 133 DTAEAIDFIEYYGRQMLELtKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPV 212
Cdd:cd07109 80 DVEAAARYFEYYGGAADKL-HGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 213 VAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDT 292
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 293 VLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESvDTYMGPVIHQASFDKIM 372
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 373 KYIEIGRTEG-DLLVGG---EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAV 448
Cdd:cd07109 312 GFVARARARGaRIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1154270283 449 LSNTRANIERAREEFHVGNLYFNRGCTGAIVGYqPFGGFNMSG 491
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-491 |
1.17e-112 |
|
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: 341.79 E-value: 1.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIETDEKTTS--INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAY 118
Cdd:cd07138 3 IDGAWVAPAGTETIdvINPATE-EVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 119 LVKEAGKPWNEADADTAE-AIDFIEYYgrqmLELTKGQPVNSRPGEYNQYnYVPLGVGVIISPFNFPLAIMAGTAIAAIV 197
Cdd:cd07138 82 ITLEMGAPITLARAAQVGlGIGHLRAA----ADALKDFEFEERRGNSLVV-REPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 198 TGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgq 277
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 278 iwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDT 357
Cdd:cd07138 233 --VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 358 YMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEG---DSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHM 433
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGPGrpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154270283 434 LEIANNTDYGLTGAVLSntrANIERARE---EFHVGNLYFNrgctGAIVGYQ-PFGGFNMSG 491
Cdd:cd07138 391 IAIANDTPYGLAGYVWS---ADPERARAvarRLRAGQVHIN----GAAFNPGaPFGGYKQSG 445
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
54-491 |
4.77e-112 |
|
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: 339.80 E-value: 4.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSnKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEA-DA 132
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 133 DTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPV 212
Cdd:cd07115 80 DVPRAADTFRYYA-GWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 213 VAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIyeraakVQSGQIWLKRVIAEMGGKDT 292
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKI------MQGAAGNLKRVSLELGGKSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 293 VLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIM 372
Cdd:cd07115 233 NIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 373 KYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSN 451
Cdd:cd07115 313 DYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1154270283 452 TRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
41-491 |
1.56e-111 |
|
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: 339.29 E-value: 1.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIETDEKTTS--INPSNKkEVIGYVSLANQELAEKAMNAALEAF--VDWKKWKAEDRANILFRAAAMLRRRKHEFS 116
Cdd:cd07119 2 IDGEWVEAASGKTRdiINPANG-EVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 117 AYLVKEAGKPWNEADADTAEAIDFIEYYGrQMLELTKGQpVNSRPGeyNQYNYV---PLGVGVIISPFNFPLaIMAGTAI 193
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYA-GLATKETGE-VYDVPP--HVISRTvrePVGVCGLITPWNYPL-LQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 A-AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAK 272
Cdd:cd07119 156 ApALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 273 VqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNP 352
Cdd:cd07119 236 N------VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 353 ESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGG-----EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKA 427
Cdd:cd07119 310 LDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGgkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERF 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 428 RDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVG-------NLYFNRGctgaivgyqPFGGFNMSG 491
Cdd:cd07119 390 DTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGtvwindyHPYFAEA---------PWGGYKQSG 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
37-491 |
3.01e-108 |
|
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: 330.69 E-value: 3.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERIETDEKTTSI-NPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKK-WKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07082 2 FKYLINGEWKESSGKTIEVySPIDG-EVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEADADTAEAIDFIEY----YGRQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAG 190
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDtieeLKRLDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 191 TAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERA 270
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 271 AKvqsgqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVG 350
Cdd:cd07082 241 PM--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 351 NPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNgfFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARD 429
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIvGYQPFGGFNMSG 491
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
55-510 |
5.18e-106 |
|
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: 324.20 E-value: 5.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKkWK--AEDRANILFRAAAMLRRRKHEFSAYLVKEAGKP-WNEAD 131
Cdd:cd07089 2 INPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGD-WStdAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 132 ADTAEAIDFIEYYGRQ--MLELTKGQPVNSRPGEYNQ--YNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPA 207
Cdd:cd07089 80 MQVDGPIGHLRYFADLadSFPWEFDLPVPALRGGPGRrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 208 DATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEM 287
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 288 GGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQAS 367
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 368 FDKIMKYIEIGRTEGDLLV--GGEGDS-SNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGL 444
Cdd:cd07089 314 RDRVEGYIARGRDEGARLVtgGGRPAGlDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 445 TGAVLSntrANIERARE---EFHVGNLYFNRGCTGAIvgYQPFGGFNMSGTdSKAGGPDYLLLHMQAKT 510
Cdd:cd07089 394 SGGVWS---ADVDRAYRvarRIRTGSVGINGGGGYGP--DAPFGGYKQSGL-GRENGIEGLEEFLETKS 456
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
40-502 |
7.23e-106 |
|
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: 325.33 E-value: 7.23e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 40 IINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYL 119
Cdd:TIGR01238 41 IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 120 VKEAGKPWNEADADTAEAIDFIEYYGRQMLEltkgqpvnsrpgEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTG 199
Cdd:TIGR01238 121 VREAGKTIHNAIAEVREAVDFCRYYAKQVRD------------VLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 200 NTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQSGQIW 279
Cdd:TIGR01238 189 NTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 280 LkrvIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYM 359
Cdd:TIGR01238 269 L---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 360 GPVIHQASFDKIMKYIE----IGRTEGDLLVGGEGDSSNGFFVQPTVFGNIHQDArlMKEEIFGPVVAVC--KARDFDHM 433
Cdd:TIGR01238 346 GPVIDAEAKQNLLAHIEhmsqTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVryKARELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 434 LEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYL 502
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYL 492
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
54-511 |
1.24e-105 |
|
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: 323.17 E-value: 1.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD 133
Cdd:cd07107 1 VINPATG-QVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYYGRQMLELtKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVV 213
Cdd:cd07107 80 VMVAAALLDYFAGLVTEL-KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 214 AAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTV 293
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 294 LVDRDADLELAASSIVYSA-FGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIM 372
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 373 KYIEIGRTEGDLLVGGEG-----DSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGA 447
Cdd:cd07107 312 HYIDSAKREGARLVTGGGrpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 448 VLSNTRANIERAREEFHVGNLYFNRGCT---GAivgyqPFGGFNMSGTDSKAgGPDYLLLHMQAKTT 511
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINGSSRhflGA-----PFGGVKNSGIGREE-CLEELLSYTQEKNV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
42-461 |
1.87e-105 |
|
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: 323.10 E-value: 1.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 42 NGERIETDekttsINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVK 121
Cdd:cd07151 7 TSERTIDV-----LNPYTG-ETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 122 EAGK-------PWNEADADTAEAIDF-IEYYGRQMLELTkgqpvnsrPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAI 193
Cdd:cd07151 81 ESGStrikaniEWGAAMAITREAATFpLRMEGRILPSDV--------PGKENRVYREPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 AAIVTGNTILLKPADATPVVAAK-FVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAK 272
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGGLlLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 273 VqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNP 352
Cdd:cd07151 233 H------LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 353 ESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFD 431
Cdd:cd07151 307 SDPDTVVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE 383
|
410 420 430
....*....|....*....|....*....|
gi 1154270283 432 HMLEIANNTDYGLTGAVLSntrANIERARE 461
Cdd:cd07151 384 EALELANDTEYGLSGAVFT---SDLERGVQ 410
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
55-491 |
7.98e-105 |
|
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: 321.23 E-value: 7.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSnKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPW-NEADAD 133
Cdd:cd07108 2 INPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYYGRQMLELtKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVV 213
Cdd:cd07108 81 AAVLADLFRYFGGLAGEL-KGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 214 AAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTV 293
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR------LIPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 294 LVDRDADLELAASSIVYSA-FGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIM 372
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 373 KYIEIGRT--EGDLLVGG----EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTG 446
Cdd:cd07108 313 GYIDLGLStsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1154270283 447 AVLSNTRANIERAREEFHVGNLYFNRGctGAIVGYQPFGGFNMSG 491
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSG 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
55-514 |
1.44e-104 |
|
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: 320.79 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07090 2 IEPATG-EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGRQMLELTkGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVA 214
Cdd:cd07090 81 DSSADCLEYYAGLAPTLS-GEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 215 AKFVELMEEAGLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVL 294
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG------IKHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 295 VDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKY 374
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 375 IEIGRTEG-DLLVGGEGDSS-----NGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAV 448
Cdd:cd07090 313 IESAKQEGaKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 449 LSNtraNIERAR---EEFHVGNLYFNR-GCTGAIVgyqPFGGFNMSGTdSKAGGPDYLLLHMQAKTT-SEM 514
Cdd:cd07090 393 FTR---DLQRAHrviAQLQAGTCWINTyNISPVEV---PFGGYKQSGF-GRENGTAALEHYTQLKTVyVEM 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
55-492 |
3.64e-104 |
|
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: 319.68 E-value: 3.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07145 4 RNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGRQMLELTkGQPVNSRPGEYNQYNYV-----PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADA 209
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLR-GETIPVDAYEYNERRIAftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 210 TPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGG 289
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 290 KDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFD 369
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 370 KIMKYIEIGRTEG-DLLVGGEGDssNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAV 448
Cdd:cd07145 316 RMENLVNDAVEKGgKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1154270283 449 LSNtraNIERA---REEFHVGNLYFNrGCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07145 394 FTN---DINRAlkvARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-510 |
3.46e-103 |
|
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: 317.54 E-value: 3.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 38 PLIINGERIE--TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEF 115
Cdd:cd07085 2 KLFINGEWVEskTTEWLDVYNPATG-EVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 116 SAYLVKEAGKPWNEADADTAEAIDFIEYyGRQMLELTKGQPVNSRPGEYNQYNY-VPLGVGVIISPFNFPLAIMAGTAIA 194
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLENVARGIDTYSYrQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 195 AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIgDYLVEHPKTRFVSFTGSREVGCRIYERAAKvq 274
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAA-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 275 SGqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPES 354
Cdd:cd07085 237 NG----KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 355 VDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDS----SNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARD 429
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGctgaI---VGYQPFGGFNmsgtDSKAG-----GPDY 501
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVP----IpvpLAFFSFGGWK----GSFFGdlhfyGKDG 464
|
....*....
gi 1154270283 502 LLLHMQAKT 510
Cdd:cd07085 465 VRFYTQTKT 473
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
55-491 |
4.72e-103 |
|
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: 316.39 E-value: 4.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07106 2 INPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGR-----QMLELTKGQPVNSRpgeynqynYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADA 209
Cdd:cd07106 81 GGAVAWLRYTASldlpdEVIEDDDTRRVELR--------RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 210 TPVVAAKFVELMEEAgLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGG 289
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 290 KDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFD 369
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 370 KIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAV 448
Cdd:cd07106 305 KVKELVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1154270283 449 LSNtraNIERARE---EFHVGNLYFNRgcTGAIVGYQPFGGFNMSG 491
Cdd:cd07106 385 WSS---DLERAEAvarRLEAGTVWINT--HGALDPDAPFGGHKQSG 425
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
34-491 |
1.16e-102 |
|
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: 316.66 E-value: 1.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 34 GKTY--P--LIINGERIET--DEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWK-KWKAEDRANILFRAAA 106
Cdd:cd07144 1 GKSYdqPtgLFINNEFVKSsdGETIKTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 107 MLRRRKHEFSAYLVKEAGKPWNE-ADADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPL 185
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYA-GWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 186 AIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCR 265
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 266 IYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTK 345
Cdd:cd07144 239 VMKAAAQN------LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 346 -TLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGD-LLVGGEGDS---SNGFFVQPTVFGNIHQDARLMKEEIFGP 420
Cdd:cd07144 313 qNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAkLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 421 VVAVCKARDFDHMLEIANNTDYGLTGAVLSNtraNIERAR---EEFHVGNLYFNR---GCTGAivgyqPFGGFNMSG 491
Cdd:cd07144 393 VVVISKFKTYEEAIKKANDTTYGLAAAVFTK---DIRRAHrvaRELEAGMVWINSsndSDVGV-----PFGGFKMSG 461
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
55-491 |
2.55e-102 |
|
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: 314.67 E-value: 2.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07110 2 INPATE-ATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGRQMLELTKGQPVnSRPGEYNQYN----YVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLKPADA 209
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAER-AVPLPSEDFKarvrREPVGVVGLITPWNFPL-LMAAWKVApALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 210 TPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGG 289
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 290 KDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFD 369
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 370 KIMKYIEIGRTEG-DLLVGGE--GDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTG 446
Cdd:cd07110 313 KVLSFIARGKEEGaRLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1154270283 447 AVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07110 393 AVISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
39-491 |
1.67e-101 |
|
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: 313.70 E-value: 1.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTTS--INPSNKKeVIGYVSLANQELAEKAMNAALEAF-VDW-KKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07143 9 LFINGEFVDSVHGGTVkvYNPSTGK-LITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEADA-DTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAI 193
Cdd:cd07143 88 LASIEALDNGKTFGTAKRvDVQASADTFRYYG-GWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 AAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKV 273
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 274 QsgqiwLKRVIAEMGGKDTVLVDRDADLElaaSSIVYSAFGF---SGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVG 350
Cdd:cd07143 247 N-----LKKVTLELGGKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 351 NPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARD 429
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
38-502 |
4.68e-101 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 330.78 E-value: 4.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 38 PLIinGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSA 117
Cdd:PRK11809 649 PML--EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMG 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 118 YLVKEAGKPWNEADADTAEAIDFIEYYGRQMleltkgqpvnsRPgEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIV 197
Cdd:PRK11809 727 LLVREAGKTFSNAIAEVREAVDFLRYYAGQV-----------RD-DFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALA 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 198 TGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGcRIYERA-AKVQSG 276
Cdd:PRK11809 795 AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNlAGRLDP 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 277 QIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVD 356
Cdd:PRK11809 874 QGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLS 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 357 TYMGPVIHQASFDKIMKYIEIGRTEG----DLLVGGEGDSSNGFFVQPTV--FGNIHQdarlMKEEIFGPVVAVCKAR-- 428
Cdd:PRK11809 954 TDIGPVIDAEAKANIERHIQAMRAKGrpvfQAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrn 1029
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154270283 429 DFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYL 502
Cdd:PRK11809 1030 QLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1103
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
50-511 |
7.19e-101 |
|
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: 311.07 E-value: 7.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 50 EKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPW 127
Cdd:cd07112 2 ETFATINPATG-RVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 128 NEA-DADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLK 205
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYA-EAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPL-LMAAWKIApALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 206 PADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAkvQSGqiwLKRVIA 285
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG--QSN---LKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 286 EMGGKDTVLVDRDA-DLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIH 364
Cdd:cd07112 234 ECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 365 QASFDKIMKYIEIGRTEG-DLLVGGEGDS--SNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTD 441
Cdd:cd07112 314 EAHFDKVLGYIESGKAEGaRLVAGGKRVLteTGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154270283 442 YGLTGAVLSntrANIERARE---EFHVGNLYFNrgCTGAIVGYQPFGGFNMSGtdskaGGPDyLLLH-----MQAKTT 511
Cdd:cd07112 394 YGLAASVWT---SDLSRAHRvarRLRAGTVWVN--CFDEGDITTPFGGFKQSG-----NGRD-KSLHaldkyTELKTT 460
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
28-492 |
4.41e-100 |
|
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: 310.05 E-value: 4.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 28 YVNTQLGKTYPliingerietdekttSINPSNKkEVIGYVSLANQELAEKAMNAALEAF---VDWKKWKAEDRANILFRA 104
Cdd:cd07141 15 WHDSVSGKTFP---------------TINPATG-EKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 105 AAMLRRRKHEFSAYLVKEAGKPWNEA-DADTAEAIDFIEYY-GRQMLELTKGQPVNsrpGEYNQYN-YVPLGV-GVIIsP 180
Cdd:cd07141 79 ADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYaGWADKIHGKTIPMD---GDFFTYTrHEPVGVcGQII-P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 181 FNFPLaIMAGTAIA-AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGS 259
Cdd:cd07141 155 WNFPL-LMAAWKLApALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 260 REVGCRIYERAAKVQsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEK 339
Cdd:cd07141 234 TEVGKLIQQAAGKSN-----LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 340 VVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIF 418
Cdd:cd07141 309 SVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIF 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 419 GPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNtraNIERARE---EFHVGNLYFNrgCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07141 389 GPVQQIFKFKTIDEVIERANNTTYGLAAAVFTK---DIDKAITfsnALRAGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
36-491 |
3.06e-99 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 307.96 E-value: 3.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 36 TYPLIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKH 113
Cdd:PRK13252 6 LQSLYIDGAYVEATSGETfeVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 114 EFSAYLVKEAGKPWNEAD-ADTAEAIDFIEYYG--RQMLEltkGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAG 190
Cdd:PRK13252 85 ELAALETLDTGKPIQETSvVDIVTGADVLEYYAglAPALE---GEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 191 TAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERA 270
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 271 AKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVG 350
Cdd:PRK13252 241 AAS------LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 351 NPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGG----EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVC 425
Cdd:PRK13252 315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGerltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 426 KARDFDHMLEIANNTDYGLTGAVLSntrANIERAREEFH---VGNLYFNR-GCTGAIVgyqPFGGFNMSG 491
Cdd:PRK13252 395 TFDDEDEVIARANDTEYGLAAGVFT---ADLSRAHRVIHqleAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
39-510 |
6.06e-99 |
|
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: 306.42 E-value: 6.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIE--TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07139 1 LFIGGRWVApsGSETIDVVSPATE-EVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKP-WNEADADTAEAIDFIEYYgrqmLELTKGQPVNS-RPGEYNQYNYV---PLGVGVIISPFNFPLAIMA 189
Cdd:cd07139 80 LARLWTAENGMPiSWSRRAQGPGPAALLRYY----AALARDFPFEErRPGSGGGHVLVrrePVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 190 GTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGkGSIIGDYLVEHPKTRFVSFTGSREVGCRIYER 269
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 270 AAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKV 349
Cdd:cd07139 235 CGER------LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 350 GNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEG--DSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCK 426
Cdd:cd07139 309 GDPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 427 ARDFDHMLEIANNTDYGLTGAVLSN-TRANIERAReEFHVGNLYFNrgctGAIVGYQ-PFGGFNMSGTdSKAGGPDYLLL 504
Cdd:cd07139 389 YDDEDDAVRIANDSDYGLSGSVWTAdVERGLAVAR-RIRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDA 462
|
....*.
gi 1154270283 505 HMQAKT 510
Cdd:cd07139 463 YLETKS 468
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
62-491 |
9.59e-99 |
|
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: 305.51 E-value: 9.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 --------EYYGRQMleltkgqPVNSRPGEYNQYNYV---PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADAT 210
Cdd:cd07094 90 rlaaeeaeRIRGEEI-------PLDATQGSDNRLAWTirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKvqsgqiwlKRVIAEMGGK 290
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEG-DLLVGGEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVL 449
Cdd:cd07094 315 VERWVEEAVEAGaRLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1154270283 450 SNTRANIERAREEFHVGNLYFNRGcTGAIVGYQPFGGFNMSG 491
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
55-492 |
3.11e-98 |
|
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: 304.25 E-value: 3.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNE-ADAD 133
Cdd:cd07092 2 VDPATG-EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYYGRQMLELTkgqpvNSRPGEYnQYNYV------PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPA 207
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLE-----GPAAGEY-LPGHTsmirrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 208 DATPVVAAKFVELMEEaGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEM 287
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT------LKRVHLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 288 GGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQAS 367
Cdd:cd07092 228 GGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 368 FDKIMKYIEIGRTEGDLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGA 447
Cdd:cd07092 308 RERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1154270283 448 VLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-499 |
1.75e-97 |
|
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: 301.91 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 eYYGRQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLKPADATPVVA-AKFVE 219
Cdd:cd07152 82 -HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 220 LMEEAGLPKGVLNFIPGkGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDA 299
Cdd:cd07152 160 LFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRH------LKKVSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 300 DLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGR 379
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 380 TEG-DLLVGGEGDssnGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSntrANIER 458
Cdd:cd07152 313 AAGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIIS---RDVGR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1154270283 459 AR---EEFHVGNLYFNRGcTGAIVGYQPFGGFNMSGTDSKAGGP 499
Cdd:cd07152 387 AMalaDRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
55-491 |
2.21e-95 |
|
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: 296.94 E-value: 2.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKKEVIGYVSlANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADA 132
Cdd:cd07118 2 RSPAHGVVVARYAE-GTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 133 DTAEAIDFIEY---------------YGRQMLELTKGQPVnsrpgeynqynyvplGVGVIISPFNFPLAIMAGTAIAAIV 197
Cdd:cd07118 81 EIEGAADLWRYaaslartlhgdsynnLGDDMLGLVLREPI---------------GVVGIITPWNFPFLILSQKLPFALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 198 TGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgq 277
Cdd:cd07118 146 AGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARN---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 278 iwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDT 357
Cdd:cd07118 222 --LKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPET 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 358 YMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSS-NGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLE 435
Cdd:cd07118 300 KVGAIINEAQLAKITDYVDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 436 IANNTDYGLTGAVLSNTRAN-IERAReEFHVGNLYFNRgctgAIVGYQ--PFGGFNMSG 491
Cdd:cd07118 380 LANDTVYGLSAGVWSKDIDTaLTVAR-RIRAGTVWVNT----FLDGSPelPFGGFKQSG 433
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
37-491 |
6.89e-95 |
|
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: 296.56 E-value: 6.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERIE--TDEKTTSINPSNKKeVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07559 1 YDNFINGEWVApsKGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGRQMLeltkgqpvnSRPGEYNQYN--------YVPLGV-GVIIsPFNFP 184
Cdd:cd07559 80 LAVAETLDNGKPIRETlAADIPLAIDHFRYFAGVIR---------AQEGSLSEIDedtlsyhfHEPLGVvGQII-PWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 185 LaIMAGTAIA-AIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVG 263
Cdd:cd07559 150 L-LMAAWKLApALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 264 CRIYERAAKVqsgqiwLKRVIAEMGGK------DTVLvDRDADLELAASSIVySAFGF-SGQKCSAGSRAVIHEDVYDEV 336
Cdd:cd07559 228 RLIMQYAAEN------LIPVTLELGGKspniffDDAM-DADDDFDDKAEEGQ-LGFAFnQGEVCTCPSRALVQESIYDEF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 337 VEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE----GDSSNGFFVQPTVFGNIHQDAR 411
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 412 LMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07559 380 IFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
39-497 |
7.73e-94 |
|
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: 293.63 E-value: 7.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07142 6 LFINGQFVDAASGKTfpTIDPRNG-EVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEAD-ADTAEAIDFIEYY-GRQMLELTKGQPVNsrpGEYNQYN-YVPLGVGVIISPFNFPLAIMAGT 191
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYaGWADKIHGMTLPAD---GPHHVYTlHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 192 AIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAA 271
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 272 KVQsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGN 351
Cdd:cd07142 242 KSN-----LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 352 PESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDF 430
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 431 DHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTDSKAG 497
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
75-491 |
1.88e-93 |
|
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: 290.90 E-value: 1.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 75 AEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYY---GRQMLel 151
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYaenAEAFL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 152 tKGQPVNSrPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVL 231
Cdd:cd07100 79 -ADEPIET-DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 232 N--FIPGKGSiigDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIV 309
Cdd:cd07100 157 QnlLIDSDQV---EAIIADPRVRGVTLTGSERAGRAVAAEAGKN------LKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 310 YSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGG 388
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 389 EGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNL 468
Cdd:cd07100 308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420
....*....|....*....|....*.
gi 1154270283 469 YFNrgctgAIVGYQ---PFGGFNMSG 491
Cdd:cd07100 388 FIN-----GMVKSDprlPFGGVKRSG 408
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
41-502 |
4.30e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 289.67 E-value: 4.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIET-DEKTTSI-NPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAY 118
Cdd:PLN02278 29 IGGKWTDAyDGKTFPVyNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 119 LVKEAGKPWNEADADTAEAIDFIEYY-----------------GRQMLELTkgQPVnsrpgeynqynyvplGVGVIISPF 181
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFaeeakrvygdiipspfpDRRLLVLK--QPV---------------GVVGAITPW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 182 NFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSRE 261
Cdd:PLN02278 171 NFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 262 VGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVV 341
Cdd:PLN02278 251 VGKKLMAGAAAT------VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 342 SLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGP 420
Cdd:PLN02278 325 KAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 421 VVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGyqPFGGFNMSGT---DSKAG 497
Cdd:PLN02278 405 VAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLgreGSKYG 482
|
....*
gi 1154270283 498 GPDYL 502
Cdd:PLN02278 483 IDEYL 487
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
62-491 |
1.37e-91 |
|
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: 286.83 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 EY--------YGRQMleltkgqPVNSRPGEYNQYNYV---PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADAT 210
Cdd:cd07147 90 RIaaeeatriYGEVL-------PLDISARGEGRQGLVrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSiIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKvqsgqiwlKRVIAEMGGK 290
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSRD-DADLLVTDERIKLLSFTGSPAVGWDLKARAGK--------KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEG-DLLVGGEgdsSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVL 449
Cdd:cd07147 314 VEGWVNEAVDAGaKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1154270283 450 SNTRANIERAREEFHVGNLYFN-----RgctgaiVGYQPFGGFNMSG 491
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSG 431
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
39-491 |
5.04e-91 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 287.01 E-value: 5.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFV-----DWKKWKAEDRANILFRAAAMLRRR 111
Cdd:PLN02467 10 LFIGGEWREPVLGKRipVVNPATE-ETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 112 KHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKGQ--PVnSRPGEYNQYNYV--PLGVGVIISPFNFPLaI 187
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkaPV-SLPMETFKGYVLkePLGVVGLITPWNYPL-L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 188 MAGTAIA-AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRI 266
Cdd:PLN02467 167 MATWKVApALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 267 YERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKT 346
Cdd:PLN02467 247 MTAAAQM------VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 347 LKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE--GDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVA 423
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGaTILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154270283 424 VCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
36-491 |
7.74e-91 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 285.65 E-value: 7.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 36 TYPLIINGERIETDEKTTSI-NPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVyNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEADAD----TAEAIDFIEYYGRQMleltKGqpvnSRPGEY--NQYNYV---PLGVGVIISPFNFPL 185
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDeipaIVDVFRFFAGAARCL----EG----KAAGEYleGHTSMIrrdPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 186 AIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCR 265
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 266 IYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTK 345
Cdd:PRK13473 232 VLSAAADS------VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 346 TLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG--DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVA 423
Cdd:PRK13473 306 TLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154270283 424 VCKARDFDHMLEIANNTDYGLTGAVLSN--TRANIERAREEFhvgnlyfnrGCT-----GAIVGYQPFGGFNMSG 491
Cdd:PRK13473 386 VTPFDDEDQAVRWANDSDYGLASSVWTRdvGRAHRVSARLQY---------GCTwvnthFMLVSEMPHGGQKQSG 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
62-497 |
3.10e-90 |
|
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: 283.48 E-value: 3.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALeafVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAA---SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 EYYGRQMLELTkGQPVNSRPGEYNQYNYV-----PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAK 216
Cdd:cd07146 87 RFAAAEALRDD-GESFSCDLTANGKARKIftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 217 FVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAkvqsgqiwLKRVIAEMGGKDTVLVD 296
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 297 RDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIE 376
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 377 igRTEGD---LLVGGEgdsSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTR 453
Cdd:cd07146 318 --EAIAQgarVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1154270283 454 ANIERAREEFHVGNLYFNRGctgaiVGYQ----PFGGFNMSGTDSKAG 497
Cdd:cd07146 393 DTIKRLVERLDVGTVNVNEV-----PGFRselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
62-491 |
7.40e-89 |
|
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: 279.88 E-value: 7.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07099 7 EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 EYYGRQMLELTKGQPVNSRPGEYNQYN---YVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFV 218
Cdd:cd07099 87 DWAARNAPRVLAPRKVPTGLLMPNKKAtveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 219 ELMEEAGLPKGVLNFIPGKGSIiGDYLVEHpKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRD 298
Cdd:cd07099 167 EAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAAER------LIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 299 ADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIG 378
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 379 RTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIE 457
Cdd:cd07099 319 VAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430
....*....|....*....|....*....|....
gi 1154270283 458 RAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
55-484 |
3.12e-87 |
|
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: 275.66 E-value: 3.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADT 134
Cdd:cd07102 1 ISPIDG-SVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 135 AEAIDFIEYYGRQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVA 214
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 215 AKFVELMEEAGLPKGVLNFIPGKGSIIGDyLVEHPKTRFVSFTGSREVGCRIyERAAKVQsgqiwLKRVIAEMGGKDTVL 294
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAI-QRAAAGR-----FIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 295 VDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKY 374
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 375 IEIGRTEG--DLLVGGEGDSSN--GFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLS 450
Cdd:cd07102 313 IADAIAKGarALIDGALFPEDKagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1154270283 451 NTRANIERAREEFHVGNLYFNR------------------GCTGAIVGYQPF 484
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNRcdyldpalawtgvkdsgrGVTLSRLGYDQL 444
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
37-491 |
1.22e-86 |
|
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: 275.14 E-value: 1.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRK 112
Cdd:cd07140 6 HQLFINGEFVDAEGGKTynTINPTDG-SVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 113 HEFSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGRQMLELT-KGQPVN-SRPGEYNQYNYV-PLGVGVIISPFNFPLAIM 188
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQgKTIPINqARPNRNLTLTKRePIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 189 AGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYE 268
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 269 RAAKVQsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLK 348
Cdd:cd07140 245 SCAVSN-----LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 349 VGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLV-GGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKA 427
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVyGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154270283 428 R--DFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRgctgaivgYQ------PFGGFNMSG 491
Cdd:cd07140 400 DdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--------YNktdvaaPFGGFKQSG 463
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-448 |
2.69e-86 |
|
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: 273.45 E-value: 2.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAFV--DWKKwKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEAD 131
Cdd:cd07120 1 SIDPATG-EVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 132 ADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATP 211
Cdd:cd07120 79 FEISGAISELRYYA-GLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 212 VVAAKFVELMEEA-GLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGK 290
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT------LKRLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 291 DTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDK 370
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 371 IMKYIEIGRTEGD--LLVGGEGDS--SNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTG 446
Cdd:cd07120 312 VDRMVERAIAAGAevVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
..
gi 1154270283 447 AV 448
Cdd:cd07120 392 SV 393
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
37-491 |
8.64e-86 |
|
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: 272.79 E-value: 8.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERI--ETDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07117 1 YGLFINGEWVkgSSGETIDSYNPANG-ETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGRQMLeltkgqpvnSRPGEYNQYN--------YVPLGVGVIISPFNFPL 185
Cdd:cd07117 80 LAMVETLDNGKPIRETrAVDIPLAADHFRYFAGVIR---------AEEGSANMIDedtlsivlREPIGVVGQIIPWNFPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 186 aIMAGTAIA-AIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGC 264
Cdd:cd07117 151 -LMAAWKLApALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 265 RIYERAAKvqsgqiwlkRVIA---EMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVV 341
Cdd:cd07117 229 DVAIAAAK---------KLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 342 SLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGG----EGDSSNGFFVQPTVFGNIHQDARLMKEE 416
Cdd:cd07117 300 EKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEE 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154270283 417 IFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSN--TRA-NIERAREefhVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07117 380 IFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKdiNRAlRVARAVE---TGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
75-461 |
1.71e-84 |
|
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: 267.91 E-value: 1.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 75 AEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTKG 154
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 155 QPVNSRPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAIA-AIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNF 233
Cdd:cd07105 82 SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPV-ILGTRAIAyPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 234 I---PGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVY 310
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 311 SAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGnpesvDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE 389
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGaKLVVGGL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154270283 390 GD-SSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSntrANIERARE 461
Cdd:cd07105 310 ADeSPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFT---RDLARALA 379
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-492 |
3.35e-84 |
|
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: 268.54 E-value: 3.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERI--ETDEKTTSINPSNKKeVIGYVSLANQELAEKAMNAALEAFVD-WKKWKAEDRANILFRAAAMLRRRKHEFSA 117
Cdd:cd07113 4 IDGRPVagQSEKRLDITNPATEQ-VIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 118 YLVKEAGKPWNEADA-DTAEAIDFIEYYGRQMLELTkGQPVN----SRPGE-YNQYNY-VPLGVGVIISPFNFPLAIMAG 190
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKIN-GETLApsipSMQGErYTAFTRrEPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 191 TAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERA 270
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 271 AKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVG 350
Cdd:cd07113 241 ASD------LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 351 NPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLV-GGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARD 429
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVrGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYED 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154270283 430 FDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFN-RGCTGAIVgyqPFGGFNMSGT 492
Cdd:cd07113 395 EEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGI 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
101-505 |
3.87e-84 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 266.22 E-value: 3.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 101 LFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD---TAEAIDFIEYYGRQMleltKGQPVNS-RPGEyNQYNY-VPLGVG 175
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEvafTADYIDYMAEWARRY----EGEIIQSdRPGE-NILLFkRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 176 VIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVS 255
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 256 FTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDE 335
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKN------ITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 336 VVEKVVSLTKTLKVGNP-ESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLM 413
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 414 KEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQpfGGFNMS--- 490
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgig 387
|
410
....*....|....*
gi 1154270283 491 GTDSKAGGPDYLLLH 505
Cdd:PRK10090 388 GADGKHGLHEYLQTQ 402
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
39-510 |
5.25e-84 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 269.00 E-value: 5.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:PLN02766 23 LFINGEFVDAASGKTfeTRDPRTG-EVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEADA-DTAEAIDFIEYYGR-------QMLELTkgqpvnsrpGEYNQYNY-VPLGVGVIISPFNFPL 185
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGaadkihgETLKMS---------RQLQGYTLkEPIGVVGHIIPWNFPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 186 AIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCR 265
Cdd:PLN02766 173 TMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 266 IYERAAKVQsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTK 345
Cdd:PLN02766 253 IMQAAATSN-----LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 346 TLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAV 424
Cdd:PLN02766 328 DWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 425 CKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTdSKAGGPDYLLL 504
Cdd:PLN02766 408 MKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGF-GRDQGMDALDK 484
|
....*.
gi 1154270283 505 HMQAKT 510
Cdd:PLN02766 485 YLQVKS 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
42-458 |
3.26e-82 |
|
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: 263.30 E-value: 3.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 42 NGERIETDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVK 121
Cdd:cd07130 4 DGEWGGGGGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 122 EAGKPWNEADADTAEAIDFIEY---YGRQMleltKGQPVNS-RPGE--YNQYNyvPLGVGVIISPFNFPLAIMAGTAIAA 195
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFavgLSRQL----YGLTIPSeRPGHrmMEQWN--PLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 196 IVTGNTILLKPADATPVVAAK----FVELMEEAGLPKGVLNFIPGkGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAA 271
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 272 KvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGN 351
Cdd:cd07130 236 A------RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 352 PESVDTYMGPVIHQASFDKIMKYIEIGRTE-GDLLVGGEGDSSNGFFVQPTVFGNIHQDArLMKEEIFGPVVAVCKARDF 430
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTIVEGLSDAP-IVKEETFAPILYVLKFDTL 388
|
410 420
....*....|....*....|....*...
gi 1154270283 431 DHMLEIANNTDYGLTGAVLSNTRANIER 458
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
39-497 |
7.27e-81 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 261.67 E-value: 7.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTT--SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVD--WKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:PLN02466 60 LLINGQFVDAASGKTfpTLDPRTG-EVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNE-ADADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAI 193
Cdd:PLN02466 139 LAALETWDNGKPYEQsAKAELPMFARLFRYYA-GWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 AAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKV 273
Cdd:PLN02466 218 PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 274 QsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPE 353
Cdd:PLN02466 298 N-----LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 354 SVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDH 432
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDE 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154270283 433 MLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTDSKAG 497
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKG 515
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-512 |
1.15e-80 |
|
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: 259.64 E-value: 1.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 24 EALSYVNTQlGKTYPLIINGE--RIETDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANIL 101
Cdd:cd07111 10 CALAWLDAH-DRSFGHFINGKwvKPENRKSFPTINPATG-EVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 102 FRAAAMLRRRKHEFSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGRQMLELtkgqpvnsrpgEYNQYNYVPLGVGVIISP 180
Cdd:cd07111 88 YRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL-----------DTELAGWKPVGVVGQIVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 181 FNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSiIGDYLVEHPKTRFVSFTGSR 260
Cdd:cd07111 157 WNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 261 EVGcRIYERAAkvqSGqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKV 340
Cdd:cd07111 236 EVG-RALRRAT---AG--TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 341 VSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFG 419
Cdd:cd07111 310 KERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGaDVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 420 PVVAVCKARDFDHMLEIANNTDYGLTGAVLSNtraNIERARE---EFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTdSKA 496
Cdd:cd07111 390 PVLVVLTFRTAKEAVALANNTPYGLAASVWSE---NLSLALEvalSLKAGVVWIN--GHNLFDAAAGFGGYRESGF-GRE 463
|
490
....*....|....*.
gi 1154270283 497 GGPDYLLLHMQAKTTS 512
Cdd:cd07111 464 GGKEGLYEYLRPSWEP 479
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-491 |
4.83e-79 |
|
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: 253.73 E-value: 4.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 78 AMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTkGQPV 157
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERT-GERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 158 NSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGK 237
Cdd:cd07095 84 TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 238 GSiIGDYLVEHPKTRFVSFTGSREVGCRIYERAAkvqsGQIWlkRVIA-EMGGKDTVLVDRDADLELAASSIVYSAFGFS 316
Cdd:cd07095 164 RE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFA----GRPG--KILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 317 GQKCSAGSRAVIHED-VYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSN 394
Cdd:cd07095 237 GQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGgEPLLAMERLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 395 GFFVQPtvfgNIHQ---DARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFN 471
Cdd:cd07095 317 TAFLSP----GIIDvtdAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN 392
|
410 420
....*....|....*....|
gi 1154270283 472 RGCTGAiVGYQPFGGFNMSG 491
Cdd:cd07095 393 RPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
62-513 |
5.77e-78 |
|
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: 251.84 E-value: 5.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFI 141
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 142 EYYGRQMLELTK------GQPVNSRPGEynqyNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAA 215
Cdd:cd07101 87 RYYARRAERLLKprrrrgAIPVLTRTTV----NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 216 KFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHpkTRFVSFTGSREVGCRIYERAAkvqsgqiwlKRVI---AEMGGKDT 292
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG---------RRLIgcsLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 293 VLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIM 372
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 373 KYIEIGRTEG-DLLVGGEGDSSNG-FFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLS 450
Cdd:cd07101 312 AHVDDAVAKGaTVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154270283 451 ntrANIERAR---EEFHVGNLYFNRGCTGAIVGYQ-PFGGFNMSGTdSKAGGPDYLLLHMQAKTTSE 513
Cdd:cd07101 392 ---RDGARGRriaARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGL-GRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
37-491 |
6.90e-75 |
|
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: 244.28 E-value: 6.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 37 YPLIINGERIE--TDEKTTSINPSNKKeVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:cd07116 1 YDNFIGGEWVApvKGEYFDNITPVTGK-VFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLaIMAGTAI 193
Cdd:cd07116 80 LAVAETWDNGKPVRETlAADIPLAIDHFRYFA-GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPL-LMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 A-AIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAK 272
Cdd:cd07116 158 ApALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 273 VqsgqiwLKRVIAEMGGK------DTVLVDRDADLELAASSIVYSAFGfSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKT 346
Cdd:cd07116 237 N------IIPVTLELGGKspniffADVMDADDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 347 LKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGE-----GDSSNGFFVQPTVFGniHQDARLMKEEIFGP 420
Cdd:cd07116 310 IKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGaEVLTGGErnelgGLLGGGYYVPTTFKG--GNKMRIFQEEIFGP 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 421 VVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07116 388 VLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
62-491 |
7.10e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 240.17 E-value: 7.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKpwNEADA-----DTAE 136
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK--ARRHAfeevlDVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 137 AIDfieYYGRQMLELTKGQ------PVNSRPGEYnqynYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADAT 210
Cdd:PRK09407 121 TAR---YYARRAPKLLAPRrragalPVLTKTTEL----RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 211 PVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHpkTRFVSFTGSREVGCRIYERAAkvqsgqiwlKRVI---AEM 287
Cdd:PRK09407 194 PLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG---------RRLIgfsLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 288 GGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQAS 367
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 368 FDKIMKYIEIGRTEG-DLLVGGEGDSSNG-FFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLT 445
Cdd:PRK09407 343 LETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1154270283 446 GAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQ-PFGGFNMSG 491
Cdd:PRK09407 423 ASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSG 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-502 |
1.03e-71 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 236.34 E-value: 1.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 41 INGERIETDE-KTTSINPSNKKEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYL 119
Cdd:PRK11241 15 INGEWLDANNgEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 120 VKEAGKPWNEADADTAEAIDFIEYYG----RQMLELTKGQPVNSRPGEYNQynyvPLGVGVIISPFNFPLAIMAGTAIAA 195
Cdd:PRK11241 95 TLEQGKPLAEAKGEISYAASFIEWFAeegkRIYGDTIPGHQADKRLIVIKQ----PIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 196 IVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqs 275
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 276 gqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESV 355
Cdd:PRK11241 249 ----IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 356 DTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHML 434
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 435 EIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGyqPFGGFNMSG---TDSKAGGPDYL 502
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
39-512 |
2.26e-69 |
|
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: 229.77 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIE--TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFS 116
Cdd:TIGR01722 3 HWIGGKFAEgaSGTYIPVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 117 AYLVKEAGKPWNEADADTAEAIDFIEYyGRQMLELTKGQPVNSRPGEYNQYNY-VPLGVGVIISPFNFPLAIMAGTAIAA 195
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEH-ACGVNSLLKGETSTQVATRVDVYSIrQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 196 IVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIgDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQs 275
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 276 gqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVyDEVVEKVVSLTKTLKVGNPESV 355
Cdd:TIGR01722 239 -----KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 356 DTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDS----SNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDF 430
Cdd:TIGR01722 313 GAEMGPLITPQAKDRVASLIAGGAAEGaEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 431 DHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTgAIVGYQPFGGFNMS-GTDSKAGGPDYLLLHMQAK 509
Cdd:TIGR01722 393 EEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIP-VPLPYFSFTGWKDSfFGDHHIYGKQGTHFYTRGK 471
|
...
gi 1154270283 510 TTS 512
Cdd:TIGR01722 472 TVT 474
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-459 |
1.64e-68 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 228.10 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 19 QELFQEALSyvntqlGKTYPLIINGE-RIETDEKTTSI-NPSNKKEVIGyVSLANQELAEKAMNAALEAFVDWKK---WK 93
Cdd:PLN00412 4 TGFFAEILD------GDVYKYYADGEwRTSSSGKSVAItNPSTRKTQYK-VQACTQEEVNKAMESAKAAQKAWAKtplWK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 94 aedRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYYGRQMLE-LTKGQPVNSR--PG-EYNQY-- 167
Cdd:PLN00412 77 ---RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRiLGEGKFLVSDsfPGnERNKYcl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 168 -NYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLV 246
Cdd:PLN00412 154 tSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 247 EHPKTRFVSFTGSrEVGCRIYERAakvqsGQIWLKrviAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRA 326
Cdd:PLN00412 234 MHPGVNCISFTGG-DTGIAISKKA-----GMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 327 VIHEDVYDEVVEKVVSLTKTLKVGNPESvDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNgfFVQPTVFGNI 406
Cdd:PLN00412 305 LVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN--LIWPLLLDNV 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1154270283 407 HQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLsnTRaNIERA 459
Cdd:PLN00412 382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVF--TR-DINKA 431
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
55-508 |
8.90e-67 |
|
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: 222.29 E-value: 8.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 55 INPSNKKeVIGYVSLANQELAEKAMNAALEAFVDWKKW-KAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD 133
Cdd:cd07148 4 VNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYYGRQMLELTKGQ-PVNSRPGEYNQYNYV---PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADA 209
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGREiPMGLTPASAGRIAFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 210 TPVVAAKFVELMEEAGLPKGVLNFIPGKgSIIGDYLVEHPKTRFVSFTGSREVGCRIyerAAKVQSGQiwlkRVIAEMGG 289
Cdd:cd07148 163 TPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWML---RSKLAPGT----RCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 290 KDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFD 369
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 370 KIMKYIEIGRTEGDLLVGGEGDSSNGFFvQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVL 449
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 450 SNTRANIERAREEFHVGNLYFNRGcTGAIVGYQPFGGFNMSGTDSkaGGPDYLLLHMQA 508
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYGT--GGIPYTMHDMTQ 449
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
39-491 |
2.32e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 219.44 E-value: 2.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIE-TDEKTTSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSA 117
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 118 YLVKEAGKPWNEADADTAEAIDFIEYYGRQMLELTkGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIV 197
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAISIQAYHERT-GEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 198 TGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGkGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKvQSGQ 277
Cdd:PRK09457 161 AGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAG-QPEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 278 IwlkrVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVY-DEVVEKVVSLTKTLKVGNPESVD 356
Cdd:PRK09457 239 I----LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 357 T-YMGPVIHQASFDKIMK----YIEIGRT---EGDLLVGGEGdssngfFVQPTVFgNIHQDARLMKEEIFGPVVAVCKAR 428
Cdd:PRK09457 315 QpFMGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG------LLTPGII-DVTGVAELPDEEYFGPLLQVVRYD 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154270283 429 DFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAiVGYQPFGGFNMSG 491
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
54-491 |
2.41e-65 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 218.96 E-value: 2.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD 133
Cdd:PRK13968 11 SVNPATG-EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYY---GRQMLElTKGQPVnsrpgEYNQ--YNYVPLGVGVIISPFNFPL-AIMAGtAIAAIVTGNTILLKPA 207
Cdd:PRK13968 90 VAKSANLCDWYaehGPAMLK-AEPTLV-----ENQQavIEYRPLGTILAIMPWNFPLwQVMRG-AVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 208 DATPVVAAKFVELMEEAGLPKGVLNFI----PGKGSIIGDylvehPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRV 283
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLnadnDGVSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAA------LKKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 284 IAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVI 363
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 364 HQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDY 442
Cdd:PRK13968 312 RFDLRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1154270283 443 GLTGAVLSNTRANIERAREEFHVGNLYFNRGC-TGAIVGyqpFGGFNMSG 491
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-491 |
4.50e-65 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 219.00 E-value: 4.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 39 LIINGERIETDEKTT--SINPSNKKEvIGYVSLANQELAEKAMNAALEAFV--DWKKWKAEDRANILFRAAAMLRRRKHE 114
Cdd:PRK09847 22 LFINGEYTAAAENETfeTVDPVTQAP-LAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 115 FSAYLVKEAGKPWNEA-DADTAEAIDFIEYYGrQMLELTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAI 193
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYA-EAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 194 AAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAakv 273
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 274 qsGQIWLKRVIAEMGGKDTVLVDRDA-DLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNP 352
Cdd:PRK09847 257 --GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 353 ESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEgDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDH 432
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGR-NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 433 MLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVgyQPFGGFNMSG 491
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG 470
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
54-491 |
1.96e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 216.14 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 54 SINPSNKKEVIGYVSLANQELaEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD 133
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEV-DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 134 TAEAIDFIEYYGRQMLELTKGQPVNSRP-GEYNQY-NYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATP 211
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALLADEPADAAAvGASRAYvRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 212 VVAAKFVELMEEAGLPKGVLNFIpgkgsIIGDYLVE----HPKTRFVSFTGSREVGcriyeRAAKVQSGQIwLKRVIAEM 287
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFQTL-----LVGSGAVEailrDPRVAAATLTGSEPAG-----RAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 288 GGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQAS 367
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 368 FDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTG 446
Cdd:PRK09406 313 RDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1154270283 447 AVLSNTRANIERAREEFHVGNLYFNrgctGAIVGYQ--PFGGFNMSG 491
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSG 435
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
62-503 |
4.70e-63 |
|
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: 212.93 E-value: 4.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 62 EVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADAD----TAEA 137
Cdd:cd07098 7 QHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGeilvTCEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 138 IDFIEYYGRQMLeltkgQPvNSRPGEYN------QYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATP 211
Cdd:cd07098 87 IRWTLKHGEKAL-----RP-ESRPGGLLmfykraRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 212 VVAAKFVELMEEA----GLPKGVLNFIPGKGSIiGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEM 287
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES------LTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 288 GGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQAS 367
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 368 FDKIMKYIEIGRTEG-DLLVGGEGDSS----NGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDY 442
Cdd:cd07098 314 FDRLEELVADAVEKGaRLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154270283 443 GLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDsKAGGPDYLL 503
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLR 453
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
53-456 |
1.78e-57 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 199.29 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 53 TSINPSNKKeVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADA 132
Cdd:PLN02315 37 SSVNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 133 DTAEAIDFIEY---YGRQMleltKGQPVNS-RPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPAD 208
Cdd:PLN02315 116 EVQEIIDMCDFavgLSRQL----NGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 209 ATPVVA---AKFV-ELMEEAGLPKGVLNFIPGkGSIIGDYLVEHPKTRFVSFTGSREVGcRIYERAAKVQSGQIWLkrvi 284
Cdd:PLN02315 192 TTPLITiamTKLVaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG-LMVQQTVNARFGKCLL---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 285 aEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIH 364
Cdd:PLN02315 266 -ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 365 QASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGFFVQPTVFgNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYG 443
Cdd:PLN02315 345 PESKKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410
....*....|...
gi 1154270283 444 LTGAVLSNTRANI 456
Cdd:PLN02315 424 LSSSIFTRNPETI 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
32-471 |
3.56e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 197.66 E-value: 3.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 32 QLGKTYPLIINGERIETDEKT--TSINPSNKkEVIGYVSLANQELAEKAMNAALEAFVDWKKWKAEDRANILFRAAAMLR 109
Cdd:PLN02419 109 QMPPRVPNLIGGSFVESQSSSfiDVINPATQ-EVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 110 RRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYY-GRQMLELTKGQPvNSRPGEYNQYNYVPLGVGVIISPFNFPLAIM 188
Cdd:PLN02419 188 KNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHAcGMATLQMGEYLP-NVSNGVDTYSIREPLGVCAGICPFNFPAMIP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 189 AGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIgDYLVEHPKTRFVSFTGSREVGCRIYE 268
Cdd:PLN02419 267 LWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 269 RAAKVQsgqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIHEDVyDEVVEKVVSLTKTLK 348
Cdd:PLN02419 346 RAAAKG------KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALK 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 349 VGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEG-DLLVGGEGDSSNGF----FVQPTVFGNIHQDARLMKEEIFGPVVA 423
Cdd:PLN02419 419 VTCGSEPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLV 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1154270283 424 VCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFN 471
Cdd:PLN02419 499 CMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
170-492 |
5.21e-55 |
|
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: 190.51 E-value: 5.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 170 VPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGdYLVEHp 249
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT-ALLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 250 KTRFVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAVIH 329
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAK------HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 330 EDVYDEVVEKvvsLTKTLK--VGNPESVDTYMGPVIHQASFDKIMKYIEigRTEGDLLVGGEGDSSNGFFvQPTVFGNIH 407
Cdd:cd07135 258 PSVYDEFVEE---LKKVLDefYPGGANASPDYTRIVNPRHFNRLKSLLD--TTKGKVVIGGEMDEATRFI-PPTIVSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 408 QDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNR-----GCTGAivgyq 482
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtlihvGVDNA----- 406
|
330
....*....|
gi 1154270283 483 PFGGFNMSGT 492
Cdd:cd07135 407 PFGGVGDSGY 416
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
95-491 |
5.34e-54 |
|
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: 187.73 E-value: 5.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 95 EDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEAD-ADTAEAIDFIEYYGRQMLELTKGQPVN----SRPGEyNQYNY 169
Cdd:cd07087 20 EWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALKHLKKWMKPRRVSvpllLQPAK-AYVIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 170 VPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLvehp 249
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 250 KTRF--VSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRAV 327
Cdd:cd07087 174 AEPFdhIFFTGSPAVGKIVMEAAAK------HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 328 IHEDVYDEVVEKVVSLTKTLKVGNPESVDTYmGPVIHQASFDKIMKYIEigrtEGDLLVGGEGDSSNgFFVQPTVFGNIH 407
Cdd:cd07087 248 VHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLD----DGKVVIGGQVDKEE-RYIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 408 QDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGF 487
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGV 401
|
....
gi 1154270283 488 NMSG 491
Cdd:cd07087 402 GNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
84-491 |
6.36e-49 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 175.60 E-value: 6.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 84 EAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEAD-ADTAEAIDFIEYYGRQMLELTKGQPVN---- 158
Cdd:PTZ00381 18 ESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEYLKPEKVDtvgv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 159 SRPGE-YNQYNyvPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGK 237
Cdd:PTZ00381 98 FGPGKsYIIPE--PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 238 GSIIGDYLVEHPKTRFvsFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSG 317
Cdd:PTZ00381 175 VEVTTELLKEPFDHIF--FTGSPRVGKLVMQAAAE------NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 318 QKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYmGPVIHQASFDKIMKYIEigRTEGDLLVGGEGDSSNGFf 397
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDY-SRIVNEFHTKRLAELIK--DHGGKVVYGGEVDIENKY- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 398 VQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGA 477
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHL 402
|
410
....*....|....
gi 1154270283 478 IVGYQPFGGFNMSG 491
Cdd:PTZ00381 403 LNPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
169-491 |
5.47e-47 |
|
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: 169.22 E-value: 5.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 169 YVPLGVGVIISPFNFP--LAIMAgtAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGKGSIIGDYLv 246
Cdd:cd07136 98 YEPYGVVLIIAPWNYPfqLALAP--LIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 247 ehpKTRF--VSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGS 324
Cdd:cd07136 174 ---DQKFdyIFFTGSVRVGKIVMEAAAK------HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 325 RAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYmGPVIHQASFDKIMKYIEigrtEGDLLVGGEGDsSNGFFVQPTVFG 404
Cdd:cd07136 245 YVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLD----NGKIVFGGNTD-RETLYIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 405 NIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANierarEEFHVGNLYFNRGCTG-AIV---- 479
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKV-----EKKVLENLSFGGGCINdTIMhlan 393
|
330
....*....|..
gi 1154270283 480 GYQPFGGFNMSG 491
Cdd:cd07136 394 PYLPFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
89-491 |
9.57e-45 |
|
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: 162.78 E-value: 9.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 89 WKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPwnEADADTAE---AIDFIEYYGRQMLELTKGQPVNSR---PG 162
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP--AAEVDLTEilpVLSEINHAIKHLKKWMKPKRVRTPlllFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 163 EYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGsiIG 242
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAE--VA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 243 DYLVEHPktrF--VSFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKC 320
Cdd:cd07134 170 QALLELP---FdhIFFTGSPAVGKIVMAAAAKH------LASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 321 SAGSRAVIHEDVYDEVVEKVVSLTKtlKV-----GNPESVDtyMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNG 395
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIE--KFygkdaARKASPD--LARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 396 FFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgct 475
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN---- 392
|
410 420
....*....|....*....|
gi 1154270283 476 GAIVGYQ----PFGGFNMSG 491
Cdd:cd07134 393 DVVLHFLnpnlPFGGVNNSG 412
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
76-500 |
7.03e-44 |
|
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: 160.87 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 76 EKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEA-----DADTAEAIDFIEYYGRqmLE 150
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicgDQVQLRARAFVIYSYR--IP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 151 LTKGQPVNSRPGEYNQYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAG-LPKG 229
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 230 VLNFIPGKGSiIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVqsgqiwlkRVIAEMGGKDTVLVDRDAD-LELAASSI 308
Cdd:cd07084 160 DVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--------RIYLELAGFNWKVLGPDAQaVDYVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 309 VYSAFGFSGQKCSAGSRAVIHEDVYDE-VVEKVVSLTKTLKVGnpesvDTYMGPVIhqaSFDKIMKYIEIGRTEG-DLLV 386
Cdd:cd07084 231 VQDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQ---TFTTLAMIAHMENLLGsVLLF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 387 GG------EGDSSNGFFVQPTVFGNIHQDAR---LMKEEIFGPV--VAVCKARDFDHMLEIANNTDYGLTGAVLSNTRAN 455
Cdd:cd07084 303 SGkelknhSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIF 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1154270283 456 IERAREEFHV-GNLYF-NRGCTGAIVGYQPFGGFNMSGTDSKAGGPD 500
Cdd:cd07084 383 LQELIGNLWVaGRTYAiLRGRTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
94-491 |
9.49e-36 |
|
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: 138.00 E-value: 9.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 94 AEDRANILFRAAAMLRRRKHEFSAYLVKEAGkpwNEADADT--AE---AIDFIEYYGRQMLELTKGQPVNSRP---GEYN 165
Cdd:cd07133 19 LEERRDRLDRLKALLLDNQDALAEAISADFG---HRSRHETllAEilpSIAGIKHARKHLKKWMKPSRRHVGLlflPAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 166 QYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKgVLNFIPGkGSIIG--- 242
Cdd:cd07133 96 EVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTG-GADVAaaf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 243 -----DYLVehpktrfvsFTGSREVGCRIYERAAKVqsgqiwLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSG 317
Cdd:cd07133 174 sslpfDHLL---------FTGSTAVGRHVMRAAAEN------LTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 318 QKCSAGSRAVIHEDVYDEVVEKVVSLTKTL---KVGNPEsvdtyMGPVIHQASFDKIMKYIEIGRTEG----DLLVGGEG 390
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPD-----YTSIINERHYARLQGLLEDARAKGarviELNPAGED 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 391 DSSNGFFVqPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYF 470
Cdd:cd07133 314 FAATRKLP-PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI 392
|
410 420
....*....|....*....|.
gi 1154270283 471 NRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07133 393 NDTLLHVAQDDLPFGGVGASG 413
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
171-497 |
5.56e-35 |
|
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: 136.00 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 171 PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIPGkGSIIGDYLVEHpK 250
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 251 TRFVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGF-SGQKCSAGSRAVIH 329
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAK------HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 330 EDVYDEVVEKVVSLTKTLKVGNPESVDTyMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNgFFVQPTVFGNIHQD 409
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKN-LYIEPTILLDPPLD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 410 ARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFNM 489
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGE 409
|
....*...
gi 1154270283 490 SGTDSKAG 497
Cdd:cd07137 410 SGFGAYHG 417
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-491 |
6.10e-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: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 76 EKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEAD-ADTAEAIDFIEYYGRQMLELTKG 154
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 155 QPVNSRPGeyNQYNYV-----PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAakfvELMEEAgLPKG 229
Cdd:cd07132 81 EPVKKNLA--TLLDDVyiykePLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAEL-IPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 230 VLN--FIpgkgSIIGDY-----LVEHpktRF--VSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDAD 300
Cdd:cd07132 154 LDKecYP----VVLGGVeetteLLKQ---RFdyIFYTGSTSVGKIVMQAAAK------HLTPVTLELGGKSPCYVDKSCD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 301 LELAASSIVYSAFGFSGQKCSAGSRAVIHEDVYDEVVEKvvsLTKTLK--VGNPESVDTYMGPVIHQASFDKIMKYIEIG 378
Cdd:cd07132 221 IDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEA---LKKTLKefYGEDPKESPDYGRIINDRHFQRLKKLLSGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 379 RtegdLLVGGEGDSSNGfFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIER 458
Cdd:cd07132 298 K----VAIGGQTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINK 372
|
410 420 430
....*....|....*....|....*....|...
gi 1154270283 459 AREEFHVGNLYFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07132 373 ILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
95-459 |
3.84e-33 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 132.14 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 95 EDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEADADTAEAIDFIEYY---GRQMLE---LTKGQPVN-SRPGEY-NQ 166
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYaklGAALGDarlLRDGEAVQlGKDPAFqGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 167 YNYVPL-GVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAG-LPKGVLNFIPGKGSIIGDY 244
Cdd:PRK11903 143 HVLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 245 LVEHPktrFVSFTGSREVGCRIYERAAKVQSGQiwlkRVIAEMGGKDTVLVDRDAD-----LELAASSIVYSAFGFSGQK 319
Cdd:PRK11903 223 LQPFD---VVSFTGSAETAAVLRSHPAVVQRSV----RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 320 CSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEG------DSS 393
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdaDPA 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154270283 394 NGFFVQPTVFGNIHQDA--RLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERA 459
Cdd:PRK11903 376 VAACVGPTLLGASDPDAatAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
40-451 |
3.55e-27 |
|
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: 114.51 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 40 IINGERIETDEKTTSINPSNKKEVIGYVSLANQELAEKAMNAA------LEafvdwKKWKAEDR----ANILFRAAAMLR 109
Cdd:cd07126 2 LVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRqcpksgLH-----NPLKNPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 110 RRKHE-FSAYLVKE-AGKPWNEADADTAEAIDFIE-YYGRQMLELTKGQPVnsrPGEY-----NQYNYvPLGVGVIISPF 181
Cdd:cd07126 77 KPEVEdFFARLIQRvAPKSDAQALGEVVVTRKFLEnFAGDQVRFLARSFNV---PGDHqgqqsSGYRW-PYGPVAIITPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 182 NFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLPKGVLNFIPGKGSIIGDYLVEhPKTRFVSFTGSRe 261
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSS- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 262 vgcRIYERAAKVQSGQIWLkrviaEMGGKDTVLVDRD-ADLELAASSIVYSAFGFSGQKCSAGSRAVIHED-VYDEVVEK 339
Cdd:cd07126 231 ---KVAERLALELHGKVKL-----EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 340 VVSLTKTLKVGnpesvDTYMGPVI---HQASFDKIMKYIEIGRTEgdLLVGGE---GDSSNGFF--VQPT-VF-----GN 405
Cdd:cd07126 303 LKALAEQRKLE-----DLTIGPVLtwtTERILDHVDKLLAIPGAK--VLFGGKpltNHSIPSIYgaYEPTaVFvpleeIA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1154270283 406 IHQDARLMKEEIFGP--VVAVCKARDFDHMLEIANNTDYGLTGAVLSN 451
Cdd:cd07126 376 IEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSN 423
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
96-458 |
6.72e-27 |
|
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: 113.90 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 96 DRANILFRAAAMLRRRKHEFSAYLVKEAGkpwNEADA--DTAEAIDFIEYY---GRQMLE----LTKGQPVN-SRPGEY- 164
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYALSAATGA---TRRDSwiDIDGGIGTLFAYaslGRRELPnahfLVEGDVEPlSKDGTFv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 165 NQYNYVPL-GVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAG-LPKGVLNFIPGKGsiiG 242
Cdd:cd07128 137 GQHILTPRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSV---G 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 243 DyLVEHPKTR-FVSFTGSREVGCRIYERAAKVQSGQiwlkRVIAEMG-------GKDTVLVDRDADL---ELAASSIVYS 311
Cdd:cd07128 214 D-LLDHLGEQdVVAFTGSAATAAKLRAHPNIVARSI----RFNAEADslnaailGPDATPGTPEFDLfvkEVAREMTVKA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 312 afgfsGQKCSAGSRAVIHEDVYDEVVEKVVSLTKTLKVGNPESVDTYMGPVIHQASFDKIMKYIEIGRTEGDLLVGG--- 388
Cdd:cd07128 289 -----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdr 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154270283 389 ----EGDSSNGFFVQPTVF--GNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIER 458
Cdd:cd07128 364 fevvGADAEKGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
171-491 |
3.01e-26 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 111.74 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 171 PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPvVAAKFVELMEEAGLPKGVLNFIPGkGSIIGDYLVEHPK 250
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-ATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 251 TRfVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVD---RDADLELAASSIVYSAFGF-SGQKCSAGSRA 326
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAAK------HLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 327 VIHEDVYDEVVEKVVSLTKTLKVGNPESVDtYMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNgFFVQPTVFGNI 406
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK-LFIEPTILLNP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 407 HQDARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNrgctGAIVGYQ---- 482
Cdd:PLN02203 337 PLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN----DAIIQYAcdsl 412
|
....*....
gi 1154270283 483 PFGGFNMSG 491
Cdd:PLN02203 413 PFGGVGESG 421
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
171-497 |
7.11e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.52 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 171 PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAgLPKGVLNFIpgKGSIIGDYLVEHPK 250
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVV--EGAVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 251 TRFVSFTGSREVGCRIYERAAKvqsgqiWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGF-SGQKCSAGSRAVIH 329
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAK------HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 330 EDVYDEVVEKVVSLTKTLKVGNP-ESVDtyMGPVIHQASFDKIMKYIEIGRTEGDLLVGGEGDSSNgFFVQPTVFGNIHQ 408
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPmESKD--MSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDREN-LKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 409 DARLMKEEIFGPVVAVCKARDFDHMLEIANNTDYGLTGAVLSNTRANIERAREEFHVGNLYFNRGCTGAIVGYQPFGGFN 488
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVG 419
|
....*....
gi 1154270283 489 MSGTDSKAG 497
Cdd:PLN02174 420 ESGMGAYHG 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
76-481 |
1.81e-24 |
|
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: 106.09 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 76 EKAMNAALEAFVDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKP--------------------------WNE 129
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPearlqgelgrttgqlrlfadlvregsWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 130 ADADTAEAidfieyyGRQML---ELTKGQpvnsrpgeynqynyVPLGVGVIISPFNFPLAI-MAG--TAiAAIVTGNTIL 203
Cdd:cd07129 82 ARIDPADP-------DRQPLprpDLRRML--------------VPLGPVAVFGASNFPLAFsVAGgdTA-SALAAGCPVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 204 LKPADATPVVAAKFVELMEEA----GLPKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQSGqiw 279
Cdd:cd07129 140 VKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 280 lKRVIAEMGGKDTVLV------DRDADL--ELAASsivySAFGfSGQKC-SAGSRAVIHEDVYDEVVEKVVSLTKTLKVG 350
Cdd:cd07129 217 -IPFYAELGSVNPVFIlpgalaERGEAIaqGFVGS----LTLG-AGQFCtNPGLVLVPAGPAGDAFIAALAEALAAAPAQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 351 npesvdTYMGPVIHQAsFDKIMKYIEiGRTEGDLLVGGEGDsSNGFFVQPTVFGNIHQDAR---LMKEEIFGPVVAVCKA 427
Cdd:cd07129 291 ------TMLTPGIAEA-YRQGVEALA-AAPGVRVLAGGAAA-EGGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRY 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154270283 428 RDFDHMLEIANNTDYGLTGAVLSNTRANiERARE-----EFHVGNLYFNRGCTGAIVGY 481
Cdd:cd07129 362 DDAAELLAVAEALEGQLTATIHGEEDDL-ALAREllpvlERKAGRLLFNGWPTGVEVCP 419
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
78-461 |
7.64e-20 |
|
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: 92.54 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 78 AMNAALEafvDWKKWKAEDRANILFRAAAMLRRRKHEFSAYLVKEAGKPWNEA-DADTAEAID----FIEYYGRQMLELT 152
Cdd:cd07127 92 AARAAMP---GWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfQAGGPHAQDrgleAVAYAWREMSRIP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 153 kGQPVNSRPGEYN-------QYNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFV----ELM 221
Cdd:cd07127 169 -PTAEWEKPQGKHdplamekTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVqvarEVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 222 EEAGL-PKGVLNFIPGKGSIIGDYLVEHPKTRFVSFTGSREVGCRIYERAAKVQsgqiwlkrVIAEMGGKDTVLVDRDAD 300
Cdd:cd07127 248 AEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDSTDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 301 LELAASSIVYSAFGFSGQKCSAGSRAVIHED---------VYDEVVEKVVSLTKTLkVGNPESVDTYMGPVIHQASFDKI 371
Cdd:cd07127 320 LKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 372 MKYIEIGRTEGDLLVGGEGDSSNGFFVQPTVFGNIHQDARLMKEEIFGPVVAVCKARDFDHMLEIANNT--DYG-LTGAV 448
Cdd:cd07127 399 AEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGV 478
|
410
....*....|...
gi 1154270283 449 LSNTRANIERARE 461
Cdd:cd07127 479 YSTDPEVVERVQE 491
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
170-355 |
1.12e-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: 66.48 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 170 VPLGVGVIISPFNFPLAIMAgTAIAAIVTGNTILLKPADATPVVAAKFVELMEEA---GLPKGVLNFIPGKGSIIGDYLV 246
Cdd:cd07077 99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 247 EHPKTRFVSFTGSREVgcriyERAAKVQSGQIwlkRVIAEMGGKDTVLVDRDADLELAASSIVYSAFgFSGQKCSAGSRA 326
Cdd:cd07077 178 SHPKIDLIVATGGRDA-----VDAAVKHSPHI---PVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNL 248
|
170 180
....*....|....*....|....*....
gi 1154270283 327 VIHEDVYDEVVEKVVSLTKTLKVGNPESV 355
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVVEGLKVPQET 277
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
171-437 |
1.23e-09 |
|
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: 60.36 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 171 PLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEA----GLPKGVLNFIPGKGSIIGDYLV 246
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 247 EHPKTRFVSFTGSREVgcriyeraakVQSGQIWLKRVIAEMGGKDTVLVDRDADLELAASSIVYSAFGFSGQKCSAGSRA 326
Cdd:cd07081 175 KFPGIGLLLATGGPAV----------VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 327 VIHEDVYDEVVEKVVSLTKTLKVGNPEsvdtymgpvihQASFDKIMKYIEIGRTegdlLVG---GEGDSSNGFFVQPTVF 403
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQGAYKLTAEEL-----------QQVQPVILKNGDVNRD----IVGqdaYKIAAAAGLKVPQETR 309
|
250 260 270
....*....|....*....|....*....|....*....
gi 1154270283 404 GNIHQDARLMKEEIFG-----PVVAVCKARDFDHMLEIA 437
Cdd:cd07081 310 ILIGEVTSLAEHEPFAheklsPVLAMYRAANFADADAKA 348
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
170-478 |
1.48e-09 |
|
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: 60.20 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 170 VPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELM----EEAGLPKGVLNFIPGKGSIIGDYL 245
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 246 VEHPKTRFVSFTGSREVgcriyERAAkVQSGqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYS-AFGFsGQKCSAGS 324
Cdd:cd07122 174 MKHPDVDLILATGGPGM-----VKAA-YSSG----KPAIGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 325 RAVIHEDVYDEVVEKVVS-----LTKTLKvgnpESVDTYM--------GPVIHQaSFDKIMKYIEIGRTEGDLLVGGEGD 391
Cdd:cd07122 243 SVIVDDEIYDEVRAELKRrgayfLNEEEK----EKLEKALfddggtlnPDIVGK-SAQKIAELAGIEVPEDTKVLVAEET 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 392 SsngffvqptvfgnIHQDARLMKEEIFgPVVAVCKARDFDHMLEIA----NNTDYGLTGAVLSNTRANIERAREEFHVGN 467
Cdd:cd07122 318 G-------------VGPEEPLSREKLS-PVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSR 383
|
330
....*....|..
gi 1154270283 468 LYFNR-GCTGAI 478
Cdd:cd07122 384 ILVNTpSSLGGI 395
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
167-458 |
4.49e-08 |
|
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: 55.32 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 167 YNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEA----GLPKGVLNFIpGKGSI-I 241
Cdd:cd07121 93 VEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTV-EEPTIeT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 242 GDYLVEHPKTRFVSFTGSREVGcriyeRAAkVQSGqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAfGFSGQKCS 321
Cdd:cd07121 172 TNELMAHPDINLLVVTGGPAVV-----KAA-LSSG----KKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNLPC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 322 AGSRAVIHED-VYDEVVEKVVS-------------LTKTLKVGNPESV--DTYMGpvihqASFDKIMKYIEIGRTEGDLL 385
Cdd:cd07121 241 IAEKEVIAVDsVADYLIAAMQRngayvlndeqaeqLLEVVLLTNKGATpnKKWVG-----KDASKILKAAGIEVPADIRL 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154270283 386 VGGEGDSSNGFFVqptvfgnihqdarlmkEEIFGPVVAVCKARDFDHMLEIANNTDYGL--TGAVLSNtraNIER 458
Cdd:cd07121 316 IIVETDKDHPFVV----------------EEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK---NVEN 371
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
167-437 |
2.13e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 50.29 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 167 YNYVPLGVGVIISPFNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEA----GLPKGVLNFIpGKGSI-I 241
Cdd:PRK15398 125 IEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTV-AEPTIeT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 242 GDYLVEHPKTRFVSFTGSREVGcriyerAAKVQSGqiwlKRVIAEMGGKDTVLVDRDADLELAASSIVYSAfGFSGQ-KC 320
Cdd:PRK15398 204 AQRLMKHPGIALLVVTGGPAVV------KAAMKSG----KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPC 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 321 SAGSRAVIHEDVYDEVVEKVVSlTKTLKVgNPESVDTYMGPVIHQASF----------DKIMKYIEIGRTEGDLLVGGEG 390
Cdd:PRK15398 273 IAEKEVIVVDSVADELMRLMEK-NGAVLL-TAEQAEKLQKVVLKNGGTvnkkwvgkdaAKILEAAGINVPKDTRLLIVET 350
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1154270283 391 DSSNGFFVqptvfgnihqdarlmkEEIFGPVVAVCKARDFDHMLEIA 437
Cdd:PRK15398 351 DANHPFVV----------------TELMMPVLPVVRVKDVDEAIALA 381
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
154-229 |
2.40e-03 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 40.22 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154270283 154 GQPVNSRPGEYNQ-YNYVPLGVGVIIS-P----FNFPLAIMAGTAIAAIVTGNTILLKPADATPVVAAKFVELMEEAGLP 227
Cdd:cd08190 286 GLVKDYRPPGYPVdHPHVPHGLSVALTaPavfrFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIP 365
|
..
gi 1154270283 228 KG 229
Cdd:cd08190 366 NG 367
|
|
| |
