|
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: 1001.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 1 MVQPYKHEPFTDFTVKENKKAFEDALQQVKSQLGQDHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQ 80
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 81 AASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVESR 160
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 161 PGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGE 240
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 241 VGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKC 320
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 321 SSGSRAVVHQDVYDEVLERVVARTKELSVGNaAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYFIEP 400
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGN-PEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 401 TVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVG 480
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500 510
....*....|....*....|....*....|....*
gi 2513828894 481 YQPFGGFKMSGTDSKAGGPDYIALHMQAKTISEMY 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: 868.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 5 YKHEPFTDFTVKENKKAFEDALQQVKSQLGQDHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASN 84
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 85 SFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIdKGKHVESRPGER 164
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL-RGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 165 NRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDY 244
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 245 LIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGS 324
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 325 RAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDD--SKGYFIEPTV 402
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLElaAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 403 FADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQ 482
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|...
gi 2513828894 483 PFGGFKMSGTDSKAGGPDYIALHMQAKTISEMY 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: 834.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 5 YKHEPFTDFTVKENKKAFEDALQQVKSQLGQDHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASN 84
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 85 SFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVESRPGER 164
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 165 NRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDY 244
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 245 LIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGS 324
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 325 RAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYFIEPTVFA 404
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 405 DLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPF 484
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500 510
....*....|....*....|....*....|.
gi 2513828894 485 GGFKMSGTDSKAGGPDYIALHMQAKTISEMY 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: 560.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 35 QDHHLLVDGERI--LTDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRK 112
Cdd:COG1012 4 PEYPLFIGGEWVaaASGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 113 HELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTT 192
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 193 VAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASv 272
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 273 rqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNA 352
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 353 AESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKG-DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDF 430
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 431 DDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAiVGYQPFGGFKMSGTDSKaGGPDYIALHMQAKT 510
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
...
gi 2513828894 511 ISE 513
Cdd:COG1012 475 VTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-511 |
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: 548.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 48 TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPW 127
Cdd:pfam00171 5 ESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 128 KEADADTAEAIDFLEYYARQMLEIDkGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPA 207
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLD-GETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEM 287
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA------QNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 288 GGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSA 367
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 368 YEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:pfam00171 317 LERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYqPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGF-GREGGPYGLEEYTEVKTV 459
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-513 |
3.88e-178 |
|
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: 510.20 E-value: 3.88e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 19 KKAFEDALQQVKSQLGQDHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARA 98
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 99 GLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEID-KGKHVESRPGERNRYVYQPIGVTVV 177
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRyPAVEVVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 178 IPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFT 257
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 258 GSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVL 337
Cdd:cd07083 241 GSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 338 ERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEI 417
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 418 FGPV--VCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSK 495
Cdd:cd07083 401 FGPVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAK 480
|
490
....*....|....*...
gi 2513828894 496 AGGPDYIALHMQAKTISE 513
Cdd:cd07083 481 TGGPHYLRRFLEMKAVAE 498
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-511 |
9.58e-159 |
|
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: 458.21 E-value: 9.58e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 76 EKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGK 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 156 HVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVP 235
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 236 GSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGF 315
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA------ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 316 SGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDS- 393
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 394 KGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNrN 473
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN-D 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 2513828894 474 CTGAIVGYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07078 394 YSVGAEPSAPFGGVKQSGI-GREGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-513 |
7.29e-157 |
|
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: 456.66 E-value: 7.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 21 AFEDALQQVKSQLGQdHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGL 100
Cdd:cd07125 18 ALADALKAFDEKEWE-AIPIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 101 LLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPP 180
Cdd:cd07125 97 LEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 181 WNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSR 260
Cdd:cd07125 177 WNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGST 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 261 DVGLRIMEKASVRQNGQNHLkqvIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERV 340
Cdd:cd07125 257 ETAKLINRALAERDGPILPL---IAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEML 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 341 VARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYFIEPTVFADlaPESRMQQEEIFGP 420
Cdd:cd07125 334 KGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 421 ---VVCFtKAKDFDDAIEIANNTEYGLTGAVIS-DNRQHLEIAARdFHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKA 496
Cdd:cd07125 412 ilhVIRF-KAEDLDEAIEDINATGYGLTLGIHSrDEREIEYWRER-VEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKA 489
|
490
....*....|....*..
gi 2513828894 497 GGPDYIALHMQAKTISE 513
Cdd:cd07125 490 GGPNYLLRFGNEKTVSL 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
40-511 |
2.10e-153 |
|
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: 446.31 E-value: 2.10e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYL 119
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 120 VYEVGKPWKEADADTAEAIDFLEYYARQMLEIdKGKHVES-RPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVA 198
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRL-SGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 199 GNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqN 278
Cdd:cd07097 163 GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA------A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 279 HLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVY 358
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 359 MGPVVDQSAYEKIMSYMEVGKEEG-RLMTGG---KGDDsKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAI 434
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGaKLVYGGerlKRPD-EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2513828894 435 EIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGaiVGYQ-PFGGFKMSGTDSKAGGPDYIALHMQAKTI 511
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
54-499 |
1.95e-144 |
|
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: 423.68 E-value: 1.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADAD 133
Cdd:cd07131 18 SRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYA---RQMleidKGKHVESR-PGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASN 209
Cdd:cd07131 98 VQEAIDMAQYAAgegRRL----FGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAED 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 210 SPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGG 289
Cdd:cd07131 174 TPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALEMGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 290 KDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYE 369
Cdd:cd07131 248 KNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 370 KIMSYMEVGKEEG-RLMTGG----KGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGL 444
Cdd:cd07131 328 KVLNYNEIGKEEGaTLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 445 TGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVgYQPFGGFKMSGTDSKAGGP 499
Cdd:cd07131 408 SSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGT 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
55-491 |
3.79e-135 |
|
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: 398.73 E-value: 3.79e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:cd07103 2 INPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMLEIDkGKHVESR-PGERNRYVYQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPASNSPV 212
Cdd:cd07103 81 DYAASFLEWFAEEARRIY-GRTIPSPaPGKRILVIKQPVGVVAAITPWNFPAA-MITRKIAPaLAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 213 IAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDT 292
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 293 VVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISD 451
Cdd:cd07103 313 ALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2513828894 452 NRQHLEIAARDFHVGNLYFNrncTGAIVGYQ-PFGGFKMSG 491
Cdd:cd07103 393 DLARAWRVAEALEAGMVGIN---TGLISDAEaPFGGVKESG 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-511 |
1.50e-129 |
|
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: 384.61 E-value: 1.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADA- 132
Cdd:cd07093 1 NFNPA-TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 133 DTAEAIDFLEYYARQMLEIDkGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMagtT--VAP-LVAGNTVVMKPASN 209
Cdd:cd07093 80 DIPRAAANFRFFADYILQLD-GESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLL---TwkIAPaLAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 210 SPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVrqngqnHLKQVIAEMGG 289
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP------NLKPVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 290 KDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYE 369
Cdd:cd07093 230 KNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 370 KIMSYMEVGKEEG-RLMTGGKGDDS----KGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGL 444
Cdd:cd07093 310 KVLGYVELARAEGaTILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 445 TGAVISDNRQHLEIAARDFHVG----NLYFNRNCTgaivgyQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07093 390 AAYVWTRDLGRAHRVARRLEAGtvwvNCWLVRDLR------TPFGGVKASGI-GREGGDYSLEFYTELKNV 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-506 |
1.66e-129 |
|
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: 385.08 E-value: 1.66e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 41 VDGERIL--TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAY 118
Cdd:cd07088 2 INGEFVPssSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 119 LVYEVGKPWKEADADTAEAIDFLEYYARQMLEIdKGKHVES-RPGErNRYVY-QPIGVTVVIPPWNLALAIMAgTTVAP- 195
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRI-EGEIIPSdRPNE-NIFIFkVPIGVVAGILPWNFPFFLIA-RKLAPa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 196 LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqn 275
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 276 gqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAES 355
Cdd:cd07088 234 --ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 356 NVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDS-KGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDA 433
Cdd:cd07088 312 ATDMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 434 IEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQpfGGFKMSGT---DSKAGGPDYIALHM 506
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHGLEEYLQTKV 465
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
54-491 |
4.59e-127 |
|
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: 378.86 E-value: 4.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFE--SWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKE-A 130
Cdd:cd07091 23 TINPA-TEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 131 DADTAEAIDFLEYYAR-------QMLEIDKGKHVESRPgernryvyQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTV 202
Cdd:cd07091 102 KGDVALSIKCLRYYAGwadkiqgKTIPIDGNFLAYTRR--------EPIGVCGQIIPWNFPL-LMLAWKLAPaLAAGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 203 VMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngQNHLKQ 282
Cdd:cd07091 173 VLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA-----KSNLKK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 283 VIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPV 362
Cdd:cd07091 248 VTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 363 VDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTE 441
Cdd:cd07091 328 VSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTE 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 442 YGLTGAVISDNRQHLEIAARDFHVGNLYFNrncTGAIVGYQ-PFGGFKMSG 491
Cdd:cd07091 408 YGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-515 |
1.28e-125 |
|
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: 376.93 E-value: 1.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 6 KHEPFTDFTVK-ENKKAFEDALQQVKSqLGQDHHLLVDGERILTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASN 84
Cdd:cd07123 2 VNEPVLSYAPGsPERAKLQEALAELKS-LTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 85 SFESWRKWSAEARAGLLLRASAIMR-RRKHELSAYLVYEVGKPWKEADADTA-EAIDFLEYYARQMLEIDKGKHVESRPG 162
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 163 ERNRYVYQPI-GVTVVIPPWNLAlAIMAGTTVAPLVAGNTVVMKPASNSpVIAAKFV-EILEEAGLPKGVLNFVPGSGGE 240
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTA-VLSNYLVyKILEEAGLPPGVINFVPGDGPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 241 VGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKC 320
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 321 SSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKE--EGRLMTGGKGDDSKGYFI 398
Cdd:cd07123 319 SAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 399 EPTVFADLAPESRMQQEEIFGPVVCFT--KAKDFDDAIEIANNT-EYGLTGAVISDNRQHLEIAARDFH--VGNLYFNRN 473
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDK 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2513828894 474 CTGAIVGYQPFGGFKMSGTDSKAGGPDYIALHMQAKTISEMY 515
Cdd:cd07123 479 PTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
50-491 |
7.91e-125 |
|
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: 373.44 E-value: 7.91e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 50 DRIVSTNPANTEQVVgRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKE 129
Cdd:cd07086 13 ETFTSRNPANGEPIA-RVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 130 ADADTAEAIDFLEYYA---RQMleidKGKHVES-RPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMK 205
Cdd:cd07086 92 GLGEVQEMIDICDYAVglsRML----YGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 206 PASNSPVIAAKFVEILEEA----GLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqngQNHLK 281
Cdd:cd07086 168 PSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETV------ARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 282 QVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGP 361
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 362 VVDQSAYEKIMSYMEVGKEEG-RLMTGGKG--DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIAN 438
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGgTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 439 NTEYGLTGAVISDNRQHLEIAARDF--HVGNLYFNRNCTGAIVGyQPFGGFKMSG 491
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
39-491 |
1.42e-124 |
|
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: 372.22 E-value: 1.42e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGERIL--TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELS 116
Cdd:cd07138 1 FYIDGAWVApaGTETIDVINPA-TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 117 AYLVYEVGKPWKEADADTAE-AIDFLEYYARQMLEIDkgkhVESRPGeRNRYVYQPIGVTVVIPPWNLALAIMAGTTVAP 195
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGlGIGHLRAAADALKDFE----FEERRG-NSLVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 196 LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqn 275
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 276 gqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAES 355
Cdd:cd07138 231 --DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 356 NVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKG---DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFD 431
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGPGrpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 432 DAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNrnctGAIVGYQ-PFGGFKMSG 491
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSG 445
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
56-512 |
6.31e-119 |
|
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: 357.31 E-value: 6.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFES-WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:cd07109 3 DPS-TGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMleiDK--GKHVESRPGERNRYVYQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPASNSP 211
Cdd:cd07109 82 EAAARYFEYYGGAA---DKlhGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQ-ITGRSVAPaLAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 212 VIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKD 291
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA------ENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGnAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGG---KGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGA 447
Cdd:cd07109 311 EGFVARARARGaRIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 448 VISDN--RQHLeiAARDFHVGNLYFnrNCTGAIVGYQ-PFGGFKMSGTDSKAGgpdYIALH--MQAKTIS 512
Cdd:cd07109 391 VWTRDgdRALR--VARRLRAGQVFV--NNYGAGGGIElPFGGVKKSGHGREKG---LEALYnyTQTKTVA 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
80-511 |
1.87e-118 |
|
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: 353.07 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 80 QAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVES 159
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 160 RPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGG 239
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 240 EVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQK 319
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAA------ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 320 CSSGSRAVVHQDVYDEVLERVVartkelsvgnaaesnvymgpvvdqsayekimsymevgkeegrlmtggkgddskgyfie 399
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 400 pTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAiV 479
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-G 334
|
410 420 430
....*....|....*....|....*....|..
gi 2513828894 480 GYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd06534 335 PEAPFGGVKNSGI-GREGGPYGLEEYTRTKTV 365
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
75-499 |
2.93e-118 |
|
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: 354.91 E-value: 2.93e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 75 AEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEY---YARQMlei 151
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREaagLPRRP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 152 dKGKHVES-RPGERNRYVYQPIGVTVVIPPWN--LALAIMAgttVAP-LVAGNTVVMKPASNSPVIAA-KFVEILEEAGL 226
Cdd:cd07104 79 -EGEILPSdVPGKESMVRRVPLGVVGVISPFNfpLILAMRS---VAPaLALGNAVVLKPDSRTPVTGGlLIAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 227 PKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVE 306
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDLAVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 307 AIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLM 385
Cdd:cd07104 229 AAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 386 TGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHV 465
Cdd:cd07104 309 TGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 2513828894 466 GNLYFNR---NCtGAIVgyqPFGGFKMSGTdSKAGGP 499
Cdd:cd07104 386 GMVHINDqtvND-EPHV---PFGGVKASGG-GRFGGP 417
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
56-511 |
3.06e-118 |
|
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: 355.59 E-value: 3.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEA-DADT 134
Cdd:cd07115 3 NPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMLEIDkGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSPVI 213
Cdd:cd07115 82 PRAADTFRYYAGWADKIE-GEVIPVRGPFLNYTVREPVGVVGAIVPWNFPL-MFAAWKVAPaLAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMekasvrQNGQNHLKQVIAEMGGKDTV 293
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIM------QGAAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMS 373
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 374 YMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07115 314 YVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2513828894 453 RQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07115 394 LGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGF-GREMGREALDEYTEVKSV 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-511 |
2.08e-116 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 351.08 E-value: 2.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:cd07114 1 SINPA-TGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYA-------RQMLEIDKGKHVesrpgerNRYVYQPIGVTVVIPPWNLALAIMAgTTVAP-LVAGNTVV 203
Cdd:cd07114 80 AQVRYLAEWYRYYAgladkieGAVIPVDKGDYL-------NFTRREPLGVVAAITPWNSPLLLLA-KKLAPaLAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 204 MKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQV 283
Cdd:cd07114 152 LKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA------ENLAPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 284 IAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVV 363
Cdd:cd07114 226 TLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 364 DQSAYEKIMSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIAN 438
Cdd:cd07114 306 TERQLEKVERYVARAREEGaRVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 439 NTEYGLTGAVISDN--RQHLeiAARDFHVGNLYFNrncTGAIVGYQ-PFGGFKMSGTDsKAGGPDYIALHMQAKTI 511
Cdd:cd07114 386 DSEYGLAAGIWTRDlaRAHR--VARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIG-RENGIEAIREYTQTKSV 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
39-511 |
2.72e-116 |
|
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: 351.11 E-value: 2.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGERI--LTDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKHE 114
Cdd:cd07139 1 LFIGGRWVapSGSETIDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 115 LSAYLVYEVGKP-WKEADADTAEAIDFLEYYARQmleIDKGKHVESRP---GERNRYVYQPIGVTVVIPPWNLALAIMAG 190
Cdd:cd07139 80 LARLWTAENGMPiSWSRRAQGPGPAALLRYYAAL---ARDFPFEERRPgsgGGHVLVRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 191 TTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKA 270
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 271 SVRqngqnhLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVG 350
Cdd:cd07139 236 GER------LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 351 NAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKG--DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKA 427
Cdd:cd07139 310 DPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 428 KDFDDAIEIANNTEYGLTGAVISDNRQH-LEIAARdFHVGNLYFNrnctGAIVGYQ-PFGGFKMSGTdSKAGGPDYIALH 505
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERgLAVARR-IRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDAY 463
|
....*.
gi 2513828894 506 MQAKTI 511
Cdd:cd07139 464 LETKSI 469
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
6-513 |
1.02e-115 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 351.78 E-value: 1.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 6 KHEPFTDFTVKENKK-AFEDALQQVKSQLgQDHHLLVDGERILTDD-RIVSTNPANTEQVVGRVSKATQELAEKAMQAAs 83
Cdd:TIGR01236 1 ANEPVLPFRPGSPERdLLRKSLKELKSSS-LEIPLVIGGEEVYDSNeRIPQVNPHNHQAVLAKATNATEEDAMKAVEAA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 84 nsFESWRKWSA---EARAGLLLRASAIMR-RRKHELSAYLVYEVGK-PWK-EADAdTAEAIDFLEY---YARQMLEidkg 154
Cdd:TIGR01236 79 --LDAKKDWSNlpfYDRAAIFLKAADLLSgPYRYEILAATMLGQSKtVYQaEIDA-VAELIDFFRFnvkYARELYA---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 155 KHVESRPGERNRYVYQPI-GVTVVIPPWNLAlAIMAGTTVAPLVAGNTVVMKPaSNSPVIAAKFV-EILEEAGLPKGVLN 232
Cdd:TIGR01236 152 QQPISAPGEWNRTEYRPLeGFVYAISPFNFT-AIAGNLAGAPALMGNTVVWKP-SQTAALSNYLLmRILEEAGLPPGVIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 233 FVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSA 312
Cdd:TIGR01236 230 FVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 313 FGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGK---EEGRLMTGGK 389
Cdd:TIGR01236 310 FEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKkdpEALTILYGGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 390 GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKD--FDDAIEIANNT-EYGLTGAVISDNRQHLEIAAR--DFH 464
Cdd:TIGR01236 390 YDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVDSTsQYGLTGAVFAKDRKAILEADKklRFA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2513828894 465 VGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKAGGPDYIALHMQAKTISE 513
Cdd:TIGR01236 470 AGNFYINDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKE 518
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-491 |
9.76e-115 |
|
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: 347.76 E-value: 9.76e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPANtEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADAD 133
Cdd:cd07119 19 NPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYArQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSPV 212
Cdd:cd07119 98 IDDVANCFRYYA-GLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPL-LQAAWKLAPaLAAGNTVVIKPSEVTPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 213 IAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDT 292
Cdd:cd07119 176 TTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA------GNVKKVALELGGKNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 293 VVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07119 250 NIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGK---GDD-SKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGA 447
Cdd:cd07119 330 SYIQLGKEEGaRLVCGGKrptGDElAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2513828894 448 VISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07119 410 VWTKDIARANRVARRLRAGTVWI--NDYHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
56-491 |
1.65e-114 |
|
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: 346.26 E-value: 1.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTA 135
Cdd:cd07110 3 NPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYYARQMLEIDKGKHVE---SRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSP 211
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAKAERAvplPSEDFKARVRREPVGVVGLITPWNFPL-LMAAWKVAPaLAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 212 VIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKD 291
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA------QDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGGK--GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAV 448
Cdd:cd07110 315 LSFIARGKEEGaRLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2513828894 449 ISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSG 435
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-512 |
4.06e-114 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 361.44 E-value: 4.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 12 DFTVKENKKAFEDALQQVKSQLGQDHhLLVDGerilTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRK 91
Cdd:PRK11904 529 NLNDRSELEPLAAAIAAFLEKQWQAG-PIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSR 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 92 WSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQM-LEIDKGKHVESRPGERNRYVYQ 170
Cdd:PRK11904 604 TPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQArRLFGAPEKLPGPTGESNELRLH 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 171 PIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPK 250
Cdd:PRK11904 684 GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 251 TALISFTGSRDVGLRIMEKASVRQNGQNHLkqvIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQ 330
Cdd:PRK11904 764 IAGVAFTGSTETARIINRTLAARDGPIVPL---IAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQE 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 331 DVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDS--KGYFIEPTVF----- 403
Cdd:PRK11904 841 DIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGteNGHFVAPTAFeidsi 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 404 ADLapesrmqQEEIFGP---VVCFtKAKDFDDAIEIANNTEYGLTGAVISDNRQH-LEIAARdFHVGNLYFNRNCTGAIV 479
Cdd:PRK11904 921 SQL-------EREVFGPilhVIRY-KASDLDKVIDAINATGYGLTLGIHSRIEETaDRIADR-VRVGNVYVNRNQIGAVV 991
|
490 500 510
....*....|....*....|....*....|...
gi 2513828894 480 GYQPFGGFKMSGTDSKAGGPDYIALHMQAKTIS 512
Cdd:PRK11904 992 GVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
54-515 |
8.96e-114 |
|
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: 344.36 E-value: 8.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADAD 133
Cdd:cd07107 1 VINPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYARQMLEIdKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVI 213
Cdd:cd07107 80 VMVAAALLDYFAGLVTEL-KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAEMGGKDTV 293
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSA-FGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGA 447
Cdd:cd07107 312 HYIDSAKREGaRLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 448 VISDNRQHLEIAARDFHVGNLYFN---RNCTGAivgyqPFGGFKMSGTDSKAGGPDYIAlHMQAKTISEMY 515
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIGREECLEELLS-YTQEKNVNVRL 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-511 |
2.59e-113 |
|
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: 343.43 E-value: 2.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEA- 130
Cdd:cd07112 6 TINPA-TGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 131 DADTAEAIDFLEYYARQmleIDK--GKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPA 207
Cdd:cd07112 85 AVDVPSAANTFRWYAEA---IDKvyGEVAPTGPDALALITREPLGVVGAVVPWNFPL-LMAAWKIAPaLAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqnGQNHLKQVIAEM 287
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS-----GQSNLKRVWLEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 288 GGKD-TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQS 366
Cdd:cd07112 236 GGKSpNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 367 AYEKIMSYMEVGKEEG-RLMTGGKGD--DSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYG 443
Cdd:cd07112 316 HFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 444 LTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGtdskaGGPDYiALH-----MQAKTI 511
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSG-----NGRDK-SLHaldkyTELKTT 460
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
54-491 |
4.45e-113 |
|
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: 342.39 E-value: 4.45e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADAD 133
Cdd:cd07150 3 DLNPADGS-VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYARQMLEIdKGKHVES-RPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVA-PLVAGNTVVMKPASNSP 211
Cdd:cd07150 82 TTFTPELLRAAAGECRRV-RGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPL-ILATKKVAfALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 212 VIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVrqngqnHLKQVIAEMGGKD 291
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR------HLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVIS 450
Cdd:cd07150 314 KRQVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2513828894 451 DNRQHLEIAARDFHVGNLYFNrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHIN-DPTILDEAHVPFGGVKASG 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
60-492 |
8.55e-113 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 341.50 E-value: 8.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAID 139
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 140 FLEYYARQMLEIdKGKHV--ESRPGERNR---YVYQPIGVTVVIPPWNLALAIMAgTTVAP-LVAGNTVVMKPASNSPVI 213
Cdd:cd07149 88 TLRLSAEEAKRL-AGETIpfDASPGGEGRigfTIREPIGVVAAITPFNFPLNLVA-HKVGPaIAAGNAVVLKPASQTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqnhLKQVIAEMGGKDTV 293
Cdd:cd07149 166 ALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMS 373
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 374 YMEVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07149 318 WVEEAVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2513828894 453 RQHLEIAARDFHVGNLYFNRNCTgAIVGYQPFGGFKMSGT 492
Cdd:cd07149 395 LQKALKAARELEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
55-491 |
2.83e-111 |
|
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: 337.58 E-value: 2.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMLEI-----DKGKHVESRpgernryvYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASN 209
Cdd:cd07106 81 GGAVAWLRYTASLDLPDeviedDDTRRVELR--------RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 210 SPVIAAKFVEILEEAgLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGG 289
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA------KTLKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 290 KDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYE 369
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 370 KIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAV 448
Cdd:cd07106 305 KVKELVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2513828894 449 ISDNRQHLEIAARDFHVGNLYFNRNctGAIVGYQPFGGFKMSG 491
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
40-512 |
1.19e-109 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 351.93 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGERILTDDRIVsTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYL 119
Cdd:COG4230 561 LIAGEAASGEARPV-RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 120 VYEVGKPWKEADADTAEAIDFLEYYARQmleidkgkhVESRPGerNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAG 199
Cdd:COG4230 640 VREAGKTLPDAIAEVREAVDFCRYYAAQ---------ARRLFA--APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 200 NTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNH 279
Cdd:COG4230 709 NTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVP 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 280 LkqvIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSsgsrAV----VHQDVYDEVLERVVARTKELSVGNAAES 355
Cdd:COG4230 789 L---IAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCS----ALrvlcVQEDIADRVLEMLKGAMAELRVGDPADL 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 356 NVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDS--KGYFIEPTVF-----ADLapesrmqQEEIFGP---VVCFt 425
Cdd:COG4230 862 STDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcaNGTFVAPTLIeidsiSDL-------EREVFGPvlhVVRY- 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 426 KAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKAGGPDYIALH 505
Cdd:COG4230 934 KADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRF 1013
|
....*..
gi 2513828894 506 MQAKTIS 512
Cdd:COG4230 1014 ATERTVT 1020
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
56-511 |
1.58e-109 |
|
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: 333.44 E-value: 1.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWrKWS--AEARAGLLLRASAIMRRRKHELSAYLVYEVGKP-WKEADA 132
Cdd:cd07089 3 NPA-TEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWStdAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 133 DTAEAIDFLEYYARQmleIDKGKHVESRPGE-------RNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMK 205
Cdd:cd07089 81 QVDGPIGHLRYFADL---ADSFPWEFDLPVPalrggpgRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 206 PASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIA 285
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 286 EMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQ 365
Cdd:cd07089 232 ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 366 SAYEKIMSYMEVGKEEG-RLMTGGKGDDS--KGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEY 442
Cdd:cd07089 312 AQRDRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDY 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 443 GLTGAVIS-DNRQHLEIAARdFHVGNLYFNrncTGAIVG-YQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07089 392 GLSGGVWSaDVDRAYRVARR-IRTGSVGIN---GGGGYGpDAPFGGYKQSGL-GRENGIEGLEEFLETKSI 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
52-491 |
7.00e-109 |
|
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: 332.84 E-value: 7.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 52 IVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFES-WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKE- 129
Cdd:cd07144 25 IKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 130 ADADTAEAIDFLEYYARQMLEIdKGKHVESRPgERNRY-VYQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPA 207
Cdd:cd07144 104 ALGDLDEIIAVIRYYAGWADKI-QGKTIPTSP-NKLAYtLHEPYGVCGQIIPWNYPLA-MAAWKLAPaLAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqnGQNhLKQVIAEM 287
Cdd:cd07144 181 ENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA-----AQN-LKAVTLEC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 288 GGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELS-VGNAAESNVYMGPVVDQS 366
Cdd:cd07144 255 GGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDDTVVGPQVSKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 367 AYEKIMSYMEVGKEEG-RLMTGGKG---DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEY 442
Cdd:cd07144 335 QYDRVLSYIEKGKKEGaKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTY 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2513828894 443 GLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIvgYQPFGGFKMSG 491
Cdd:cd07144 415 GLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
56-514 |
2.16e-108 |
|
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: 330.42 E-value: 2.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTA 135
Cdd:cd07090 3 EPA-TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYYA--RQMLEidkGKHVESRPGernRYVY---QPIGVTVVIPPWNLALAImAGTTVAP-LVAGNTVVMKPASN 209
Cdd:cd07090 82 SSADCLEYYAglAPTLS---GEHVPLPGG---SFAYtrrEPLGVCAGIGAWNYPIQI-ASWKSAPaLACGNAMVYKPSPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 210 SPVIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGG 289
Cdd:cd07090 155 TPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 290 KDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYE 369
Cdd:cd07090 228 KSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 370 KIMSYMEVGKEEG-RLMTGGKGDDSK-----GYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYG 443
Cdd:cd07090 308 KVLGYIESAKQEGaKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 444 LTGAVISDN--RQHLEIAArdFHVGNLYFNR-NCTGAIVgyqPFGGFKMSGTdSKAGGPDYIALHMQAKTI-SEM 514
Cdd:cd07090 388 LAAGVFTRDlqRAHRVIAQ--LQAGTCWINTyNISPVEV---PFGGYKQSGF-GRENGTAALEHYTQLKTVyVEM 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
55-491 |
2.39e-108 |
|
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: 330.48 E-value: 2.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWK-EADAD 133
Cdd:cd07108 2 INPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYARQMLEIdKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVI 213
Cdd:cd07108 81 AAVLADLFRYFGGLAGEL-KGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAEMGGKDTV 293
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR------LIPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSA-FGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKE--EGRLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:cd07108 313 GYIDLGLStsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFNRNctGAIVGYQPFGGFKMSG 491
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSG 435
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
21-502 |
1.08e-107 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 347.24 E-value: 1.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 21 AFEDALQQVKSQLGQDHHLLVDGEriLTDDRIVSTNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGL 100
Cdd:PRK11905 540 ALDEALNAFAAKTWHAAPLLAGGD--VDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAI 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 101 LLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQmleidkGKHVESRPGERnryvyqPIGVTVVIPP 180
Cdd:PRK11905 618 LERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQ------ARRLLNGPGHK------PLGPVVCISP 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 181 WNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSR 260
Cdd:PRK11905 686 WNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGST 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 261 DVGLRImekasvRQNGQNHLKQ---VIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVL 337
Cdd:PRK11905 766 EVARLI------QRTLAKRSGPpvpLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 338 ERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGK--GDDSKGYFIEPTVF-----ADLapes 410
Cdd:PRK11905 840 TMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPlpAETEKGTFVAPTLIeidsiSDL---- 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 411 rmqQEEIFGPV---VCFtKAKDFDDAIEIANNTEYGLTGAV---ISDNRQHleIAARdFHVGNLYFNRNCTGAIVGYQPF 484
Cdd:PRK11905 916 ---EREVFGPVlhvVRF-KADELDRVIDDINATGYGLTFGLhsrIDETIAH--VTSR-IRAGNIYVNRNIIGAVVGVQPF 988
|
490
....*....|....*...
gi 2513828894 485 GGFKMSGTDSKAGGPDYI 502
Cdd:PRK11905 989 GGEGLSGTGPKAGGPLYL 1006
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
52-492 |
1.88e-106 |
|
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: 325.46 E-value: 1.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 52 IVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:cd07145 1 IEVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYARQMLEIdKGKH--VESRPGERNRYVY---QPIGVTVVIPPWNLALAIMAgTTVAP-LVAGNTVVMK 205
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVL-RGETipVDAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFA-HKIAPaIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 206 PASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIA 285
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 286 EMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQ 365
Cdd:cd07145 232 ELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 366 SAYEKIMSYMEVGKEEG-RLMTGGKGDDskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGL 444
Cdd:cd07145 312 EAVERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2513828894 445 TGAVISDN-RQHLEIaARDFHVGNLYFNrNCTGAIVGYQPFGGFKMSGT 492
Cdd:cd07145 390 QASVFTNDiNRALKV-ARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
56-492 |
2.14e-105 |
|
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: 323.53 E-value: 2.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFE---SWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEA-D 131
Cdd:cd07141 28 NPA-TGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYARQMleiDKgKHVESRPGERNRYVY---QPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPA 207
Cdd:cd07141 107 VDLPGAIKVLRYYAGWA---DK-IHGKTIPMDGDFFTYtrhEPVGVCGQIIPWNFPL-LMAAWKLAPaLACGNTVVLKPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqnGQNHLKQVIAEM 287
Cdd:cd07141 182 EQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA-----GKSNLKRVTLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 288 GGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSA 367
Cdd:cd07141 257 GGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 368 YEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:cd07141 337 FKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAA 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGT 492
Cdd:cd07141 417 AVFTKDIDKAITFSNALRAGTVWV--NCYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
43-491 |
3.60e-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: 322.33 E-value: 3.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 43 GERILTDdrivsTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYE 122
Cdd:cd07151 8 SERTIDV-----LNPYTGE-TLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 123 VGKPWKEADADTAEAIDFLEYYARQMLEIDkGKHVESR-PGERNRYVYQPIGVTVVIPPWN--LALAIMAgttVAP-LVA 198
Cdd:cd07151 82 SGSTRIKANIEWGAAMAITREAATFPLRME-GRILPSDvPGKENRVYREPLGVVGVISPWNfpLHLSMRS---VAPaLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 199 GNTVVMKPASNSPVIAAK-FVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngq 277
Cdd:cd07151 158 GNAVVLKPASDTPITGGLlLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 278 NHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNV 357
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 358 YMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEI 436
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 437 ANNTEYGLTGAVISDNRQH-----LEIAARDFHVGNLYFNRNctgAIVgyqPFGGFKMSG 491
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERgvqfaRRIDAGMTHINDQPVNDE---PHV---PFGGEKNSG 442
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
39-491 |
2.20e-104 |
|
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: 320.83 E-value: 2.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGERI--LTDDRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELS 116
Cdd:cd07559 3 NFINGEWVapSKGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 117 AYLVYEVGKPWKEA-DADTAEAIDFLEYYArQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP 195
Cdd:cd07559 82 VAETLDNGKPIRETlAADIPLAIDHFRYFA-GVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPL-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 196 -LVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrq 274
Cdd:cd07559 160 aLAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 275 ngqNHLKQVIAEMGGK-------DtvVVDKEANIETAVEAIVVsAFGF-SGQKCSSGSRAVVHQDVYDEVLERVVARTKE 346
Cdd:cd07559 236 ---ENLIPVTLELGGKspniffdD--AMDADDDFDDKAEEGQL-GFAFnQGEVCTCPSRALVQESIYDEFIERAVERFEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 347 LSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPV 421
Cdd:cd07559 310 IKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 422 VCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWV--NCYHQYPAHAPFGGYKKSG 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
48-491 |
2.23e-103 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 318.75 E-value: 2.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 48 TDDRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPW 127
Cdd:PRK13252 20 SGETFEVINPATGE-VLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 128 KEAD-ADTAEAIDFLEYYA--RQMLEidkGKHVESRPGErnrYVY---QPIGVTVVIPPWNLALAImAGTTVAP-LVAGN 200
Cdd:PRK13252 99 QETSvVDIVTGADVLEYYAglAPALE---GEQIPLRGGS---FVYtrrEPLGVCAGIGAWNYPIQI-ACWKSAPaLAAGN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 201 TVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGgEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHL 280
Cdd:PRK13252 172 AMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA------ASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 281 KQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMG 360
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 361 PVVDQSAYEKIMSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIE 435
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGaRLLCGGErlteGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2513828894 436 IANNTEYGLTGAVISD--NRQHLEIAArdFHVGNLYFNR-NCTGAIVgyqPFGGFKMSG 491
Cdd:PRK13252 405 RANDTEYGLAAGVFTAdlSRAHRVIHQ--LEAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
60-511 |
1.60e-102 |
|
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: 315.97 E-value: 1.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFE--SWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD-ADTAE 136
Cdd:cd07142 28 NGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 137 AIDFLEYYARQMLEIdkgkHVESRPGERNRYVY---QPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSPV 212
Cdd:cd07142 108 AARLFRYYAGWADKI----HGMTLPADGPHHVYtlhEPIGVVGQIIPWNFPL-LMFAWKVGPaLACGNTIVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 213 IAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngQNHLKQVIAEMGGKDT 292
Cdd:cd07142 183 SALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA-----KSNLKPVTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 293 VVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKIL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISD 451
Cdd:cd07142 338 SYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 452 NRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07142 418 NIDTANTLSRALKAGTVWV--NCYDVFDASIPFGGYKMSGI-GREKGIYALNNYLQVKAV 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
39-491 |
5.87e-102 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 315.52 E-value: 5.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGE--RILTDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSF-----ESWRKWSAEARAGLLLRASAIMRRR 111
Cdd:PLN02467 10 LFIGGEwrEPVLGKRIPVVNPA-TEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 112 KHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEID-KGKHVESRPGE--RNRYVYQPIGVTVVIPPWNLALaIM 188
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDaKQKAPVSLPMEtfKGYVLKEPLGVVGLITPWNYPL-LM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 189 AGTTVAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIM 267
Cdd:PLN02467 168 ATWKVAPaLAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 268 EKASvrqngQNhLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKEL 347
Cdd:PLN02467 248 TAAA-----QM-VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 348 SVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGK--GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCF 424
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGaTILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2513828894 425 TKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWI--NCSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
57-491 |
6.96e-101 |
|
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: 311.19 E-value: 6.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 57 PAnTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:cd07118 4 PA-HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIA 214
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 215 AKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVV 294
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA------RNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 295 VDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSY 374
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 375 MEVGKEEG-RLMTGGKGDDS-KGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07118 317 VDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2513828894 453 RQHLEIAARDFHVGNLYFNRnctgAIVGYQ--PFGGFKMSG 491
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNT----FLDGSPelPFGGFKQSG 433
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
56-492 |
4.13e-100 |
|
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: 308.87 E-value: 4.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKE-ADADT 134
Cdd:cd07092 3 DPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYA---RQMLEIDKGKHVESRPGERNRyvyQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPASNS 210
Cdd:cd07092 82 PGAVDNFRFFAgaaRTLEGPAAGEYLPGHTSMIRR---EPIGVVAQIAPWNYPLM-MAAWKIAPaLAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 211 PVIAAKFVEILEEaGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGK 290
Cdd:cd07092 158 PLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA------DTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 291 DTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEK 370
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 371 IMSYMEVGKEEGRLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVIS 450
Cdd:cd07092 311 VAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2513828894 451 DNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGT 492
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWV--NTHIPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-513 |
4.36e-100 |
|
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: 309.83 E-value: 4.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 38 HLLVDGERIL--TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHEL 115
Cdd:cd07085 2 KLFINGEWVEskTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 116 SAYLVYEVGKPWKEADADTAEAIDFLEYyARQMLEIDKGKHVE-SRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVA 194
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 195 PLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrq 274
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 275 ngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAE 354
Cdd:cd07085 236 ---ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 355 SNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDD----SKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKD 429
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 430 FDDAIEIANNTEYGlTGAVI--SDNRqhleiAARDF----HVGNLYFNrnctgaI-----VGYQPFGGFKmsgtDSKAG- 497
Cdd:cd07085 393 LDEAIAIINANPYG-NGAAIftRSGA-----AARKFqrevDAGMVGIN------VpipvpLAFFSFGGWK----GSFFGd 456
|
490 500
....*....|....*....|
gi 2513828894 498 ----GPDYIALHMQAKTISE 513
Cdd:cd07085 457 lhfyGKDGVRFYTQTKTVTS 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
39-491 |
6.52e-100 |
|
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: 309.46 E-value: 6.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGERI--LTDDRIVSTNPANtEQVVGRVSKATQELAEKAMQAASNSFE-SW-RKWSAEARAGLLLRASAIMRRRKHE 114
Cdd:cd07143 9 LFINGEFVdsVHGGTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 115 LSAYLVYEVGKPWKEADA-DTAEAIDFLEYYArQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTV 193
Cdd:cd07143 88 LASIEALDNGKTFGTAKRvDVQASADTFRYYG-GWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPL-LMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 194 APLVA-GNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASv 272
Cdd:cd07143 166 APALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 273 rqngQNHLKQVIAEMGGKDTVVVDKEANIEtavEAIVVSAFGF---SGQKCSSGSRAVVHQDVYDEVLERVVARTKELSV 349
Cdd:cd07143 245 ----KSNLKKVTLELGGKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 350 GNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAK 428
Cdd:cd07143 318 GDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 429 DFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07143 398 TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWV--NCYNLLHHQVPFGGYKQSG 458
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
40-491 |
8.21e-98 |
|
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: 303.72 E-value: 8.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGERILTD-DRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRK-WSAEARAGLLLRASAIMRRRKHELSA 117
Cdd:cd07082 5 LINGEWKESSgKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 118 YLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDkGKHV--ESRPGERNRYVY---QPIGVTVVIPPWNLALAImAGTT 192
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLD-GDSLpgDWFPGTKGKIAQvrrEPLGVVLAIGPFNYPLNL-TVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 193 VAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAS 271
Cdd:cd07082 162 LIPaLIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 272 VrqngqnhlKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGN 351
Cdd:cd07082 242 M--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 352 AAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDdsKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDF 430
Cdd:cd07082 314 PWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 431 DDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIvGYQPFGGFKMSG 491
Cdd:cd07082 392 EEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
56-509 |
2.29e-97 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 303.54 E-value: 2.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTA 135
Cdd:PLN02278 46 NPATGE-VIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYYArqmleiDKGKHV------ESRPGERNRYVYQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPAS 208
Cdd:PLN02278 125 YGASFLEYFA------EEAKRVygdiipSPFPDRRLLVLKQPVGVVGAITPWNFPLA-MITRKVGPaLAAGCTVVVKPSE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 209 NSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMG 288
Cdd:PLN02278 198 LTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATVKRVSLELG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 289 GKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAY 368
Cdd:PLN02278 272 GNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 369 EKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGA 447
Cdd:PLN02278 352 QKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAY 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 448 VISDNRQHLEIAARDFHVGNLYFNrncTGAIVGYQ-PFGGFKMSGTdSKAGGPDYIALHMQAK 509
Cdd:PLN02278 432 IFTRDLQRAWRVSEALEYGIVGVN---EGLISTEVaPFGGVKQSGL-GREGSKYGIDEYLEIK 490
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
75-491 |
1.76e-96 |
|
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: 298.60 E-value: 1.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 75 AEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYAR---QMLei 151
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeAFL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 152 dKGKHVESrPGERNRYVYQPIGVTVVIPPWN--LALAIMAgttVAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPK 228
Cdd:cd07100 79 -ADEPIET-DAGKAYVRYEPLGVVLGIMPWNfpFWQVFRF---AAPnLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 229 GVLNFVPGSGGEVgDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqnGQnHLKQVIAEMGGKDTVVVDKEANIETAVEAI 308
Cdd:cd07100 154 GVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEA-----GK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 309 VVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTG 387
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 388 GKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGN 467
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420
....*....|....*....|....*..
gi 2513828894 468 LYFNrnctgAIVGYQ---PFGGFKMSG 491
Cdd:cd07100 387 VFIN-----GMVKSDprlPFGGVKRSG 408
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-499 |
3.17e-95 |
|
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: 296.13 E-value: 3.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 62 QVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFL 141
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 142 eYYARQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSPV-----IAa 215
Cdd:cd07152 82 -HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPL-ILAMRSVAPaLALGNAVVLKPDPRTPVsggvvIA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 216 kfvEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVV 295
Cdd:cd07152 159 ---RLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG------RHLKKVSLELGGKNALIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 296 DKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYM 375
Cdd:cd07152 229 LDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 376 EVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQ 454
Cdd:cd07152 309 DDSVAAGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2513828894 455 H-LEIAARdFHVGNLYFNrNCTGAIVGYQPFGGFKMSGTDSKAGGP 499
Cdd:cd07152 386 RaMALADR-LRTGMLHIN-DQTVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
55-502 |
3.13e-93 |
|
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: 292.97 E-value: 3.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:TIGR01238 56 TNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQmleidkgkhVESRPGErnrYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIA 214
Cdd:TIGR01238 136 REAVDFCRYYAKQ---------VRDVLGE---FSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 215 AKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLkqvIAEMGGKDTVV 294
Cdd:TIGR01238 204 YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 295 VDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSY 374
Cdd:TIGR01238 281 VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 375 MEVGKEEGRLMTGGKGDDS----KGYFIEPTVFA--DLAPesrmQQEEIFGPV--VCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:TIGR01238 361 IEHMSQTQKKIAQLTLDDSracqHGTFVAPTLFEldDIAE----LSEEVFGPVlhVVRYKARELDQIVDQINQTGYGLTM 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKAGGPDYI 502
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYL 492
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-511 |
1.59e-92 |
|
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: 289.63 E-value: 1.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 54 STNPAnTEQVVGRVSKATQELAEKAMQAASNSFE--SWRKwSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:cd07120 1 SIDPA-TGEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYA---RQMleidKGKHVESRPGERNRYVYQPIGVTVVIPPWNlALAIMAGTTVAP-LVAGNTVVMKPA 207
Cdd:cd07120 79 FEISGAISELRYYAglaRTE----AGRMIEPEPGSFSLVLREPMGVAGIIVPWN-SPVVLLVRSLAPaLAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEA-GLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEkasvrqNGQNHLKQVIAE 286
Cdd:cd07120 154 GQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMA------AAAPTLKRLGLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 287 MGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQS 366
Cdd:cd07120 228 LGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 367 AYEKIMSYMEVGKEEGR--LMTGGKGDD--SKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEY 442
Cdd:cd07120 308 NVDRVDRMVERAIAAGAevVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2513828894 443 GLTGAVISDNRQHLEIAARDFHVGNLYFNRNctGAIVGYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWINDW--NKLFAEAEEGGYRQSGL-GRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
52-491 |
2.57e-92 |
|
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: 288.95 E-value: 2.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 52 IVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:cd07094 1 LDVHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYARQMLEIdKGKHV-----ESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKP 206
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERI-RGEEIpldatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 207 ASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqnhLKQVIAE 286
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRIALE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 287 MGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQS 366
Cdd:cd07094 231 LGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 367 AYEKIMSYMEVGKEEG-RLMTGGKGDDSkgyFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLT 445
Cdd:cd07094 311 AAERVERWVEEAVEAGaRLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2513828894 446 GAVISDNRQHLEIAARDFHVGNLYFNrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVN-DSSAFRTDWMPFGGVKESG 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
55-491 |
5.54e-92 |
|
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: 287.97 E-value: 5.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLR-ASAIMRRRKhELSAYLVYEVGKPWKEADAD 133
Cdd:cd07099 1 RNPA-TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRwKRALADHAD-ELAELLHAETGKPRADAGLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 TAEAIDFLEYYARQMLEIDKGKHVESR---PGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNS 210
Cdd:cd07099 79 VLLALEAIDWAARNAPRVLAPRKVPTGllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 211 PVIAAKFVEILEEAGLPKGVLNFVPGSGgEVGDYLIEHpKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAEMGGK 290
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER------LIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 291 DTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEK 370
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 371 IMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVI 449
Cdd:cd07099 311 VRRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2513828894 450 SDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
39-491 |
9.99e-92 |
|
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: 288.20 E-value: 9.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGERILT--DDRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELS 116
Cdd:cd07117 3 LFINGEWVKGssGETIDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 117 AYLVYEVGKPWKEA-DADTAEAIDFLEYYArQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP 195
Cdd:cd07117 82 MVETLDNGKPIRETrAVDIPLAADHFRYFA-GVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPF-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 196 -LVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrq 274
Cdd:cd07117 160 aLAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 275 ngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAE 354
Cdd:cd07117 236 ---KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 355 SNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKD 429
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2513828894 430 FDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWV--NTYNQIPAGAPFGGYKKSG 452
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
56-502 |
1.14e-91 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 304.97 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPANTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTA 135
Cdd:PRK11809 665 NPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYYARQMleidkgkhvesRPGERNRyVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAA 215
Cdd:PRK11809 745 EAVDFLRYYAGQV-----------RDDFDND-THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 216 KFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGQNHLKQVIAEMGGKDTVVV 295
Cdd:PRK11809 813 QAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPLIAETGGQNAMIV 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 296 DKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYM 375
Cdd:PRK11809 893 DSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHI 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 376 EVGKEEGRLMT----GGKGDDSKGYFIEPTV-----FADLapesrmqQEEIFGPV--VCFTKAKDFDDAIEIANNTEYGL 444
Cdd:PRK11809 973 QAMRAKGRPVFqaarENSEDWQSGTFVPPTLieldsFDEL-------KREVFGPVlhVVRYNRNQLDELIEQINASGYGL 1045
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2513828894 445 TGAV---ISDNRQHLEIAArdfHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKAGGPDYI 502
Cdd:PRK11809 1046 TLGVhtrIDETIAQVTGSA---HVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1103
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
60-511 |
1.26e-91 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 288.64 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFE--SWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADA-DTAE 136
Cdd:PLN02766 45 TGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 137 AIDFLEYYARQMLEIdkgkHVESRPGERNRYVY---QPIGVTVVIPPWNLAlAIMAGTTVAP-LVAGNTVVMKPASNSPV 212
Cdd:PLN02766 125 AAGLLRYYAGAADKI----HGETLKMSRQLQGYtlkEPIGVVGHIIPWNFP-STMFFMKVAPaLAAGCTMVVKPAEQTPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 213 IAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEkASVRQNgqnhLKQVIAEMGGKDT 292
Cdd:PLN02766 200 SALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ-AAATSN----LKQVSLELGGKSP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 293 VVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:PLN02766 275 LLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKIL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISD 451
Cdd:PLN02766 355 SYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTK 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 452 NRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGTdSKAGGPDYIALHMQAKTI 511
Cdd:PLN02766 435 DLDVANTVSRSIRAGTIWV--NCYFAFDPDCPFGGYKMSGF-GRDQGMDALDKYLQVKSV 491
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
75-491 |
8.31e-91 |
|
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: 284.08 E-value: 8.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 75 AEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKG 154
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 155 KHVESRPGERNRYVYQPIGVTVVIPPWNlALAIMAGTTVA-PLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNF 233
Cdd:cd07105 82 SIPSDKPGTLAMVVKEPVGVVLGIAPWN-APVILGTRAIAyPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 234 V---PGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVV 310
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA------KHLKPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 311 SAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGnaaesNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGK 389
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGaKLVVGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 390 GDDSK-GYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN-RQHLEIAARdFHVGN 467
Cdd:cd07105 310 ADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlARALAVAKR-IESGA 388
|
410 420
....*....|....*....|....*..
gi 2513828894 468 LYFNrnctGAIVGYQ---PFGGFKMSG 491
Cdd:cd07105 389 VHIN----GMTVHDEptlPHGGVKSSG 411
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-515 |
1.60e-90 |
|
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: 285.10 E-value: 1.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 41 VDGERIL--TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFES-WRKWSAEARAGLLLRASAIMRRRKHELSA 117
Cdd:cd07113 4 IDGRPVAgqSEKRLDITNPA-TEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 118 YLVYEVGKPWKEADA-DTAEAIDFLEYYARQMLEIDkGKHVE----SRPGERnryvY------QPIGVTVVIPPWNLALA 186
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKIN-GETLApsipSMQGER----YtaftrrEPVGVVAGIVPWNFSVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 187 IMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGgEVGDYLIEHPKTALISFTGSRDVGLRI 266
Cdd:cd07113 158 IAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 267 MEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKE 346
Cdd:cd07113 237 GRQAA------SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 347 LSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFT 425
Cdd:cd07113 311 FQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 426 KAKDFDDAIEIANNTEYGLTGAVISDN-RQHLEIAARdFHVGNLYFNRNCTgaIVGYQPFGGFKMSGTdSKAGGPDYIAL 504
Cdd:cd07113 391 PYEDEEELIQLINDTPFGLTASVWTNNlSKALRYIPR-IEAGTVWVNMHTF--LDPAVPFGGMKQSGI-GREFGSAFIDD 466
|
490
....*....|.
gi 2513828894 505 HMQAKTISEMY 515
Cdd:cd07113 467 YTELKSVMIRY 477
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
101-505 |
8.62e-90 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 280.85 E-value: 8.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 101 LLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEY---YARQMleidKGKHVES-RPGErNRYVY-QPIGVT 175
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYmaeWARRY----EGEIIQSdRPGE-NILLFkRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 176 VVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALIS 255
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 256 FTGSRDVGLRIMEKASvrqngQNHLKqVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDE 335
Cdd:PRK10090 156 MTGSVSAGEKIMAAAA-----KNITK-VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 336 VLERVVARTKELSVGN-AAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQ 413
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 414 QEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQpfGGFKMS--- 490
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgig 387
|
410
....*....|....*
gi 2513828894 491 GTDSKAGGPDYIALH 505
Cdd:PRK10090 388 GADGKHGLHEYLQTQ 402
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
36-491 |
2.49e-88 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 279.10 E-value: 2.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 36 DHHLLVDGERILTDDRIVS-TNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHE 114
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPvYNPATGE-VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 115 LSAYLVYEVGKPWKEADAD----TAEAIDFLEYYARQMleidKGKHV-ESRPGERNRYVYQPIGVTVVIPPWNLALaIMA 189
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDeipaIVDVFRFFAGAARCL----EGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPL-MMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 190 GTTVAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIME 268
Cdd:PRK13473 156 AWKLAPaLAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 269 KASVrqngqnHLKQVIAEMGGKDTVVVDKEANIETAVEAIVvsAFGF--SGQKCSSGSRAVVHQDVYDEVLERVVARTKE 346
Cdd:PRK13473 235 AAAD------SVKRTHLELGGKAPVIVFDDADLDAVVEGIR--TFGYynAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 347 LSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG--RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCF 424
Cdd:PRK13473 307 LKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2513828894 425 TKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:PRK13473 387 TPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWV--NTHFMLVSEMPHGGQKQSG 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
60-491 |
2.61e-88 |
|
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: 278.36 E-value: 2.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAID 139
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 140 FLEYYAR-------QMLEIDKGKHVESRPGERNRYvyqPIGVTVVIPPWNLALAIMAgTTVAP-LVAGNTVVMKPASNSP 211
Cdd:cd07147 88 TFRIAAEeatriygEVLPLDISARGEGRQGLVRRF---PIGPVSAITPFNFPLNLVA-HKVAPaIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 212 VIAAKFVEILEEAGLPKGVLNFVPGSGgEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqnGQnhlKQVIAEMGGKD 291
Cdd:cd07147 164 LSALILGEVLAETGLPKGAFSVLPCSR-DDADLLVTDERIKLLSFTGSPAVGWDLKARA-----GK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGGKgddSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVIS 450
Cdd:cd07147 315 EGWVNEAVDAGaKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2513828894 451 DNRQHLEIAARDFHVGNLYFN-----RnctgaiVGYQPFGGFKMSG 491
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSG 431
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
39-497 |
3.19e-88 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 280.93 E-value: 3.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 39 LLVDGEriLTDDRIVSTNPA---NTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRKH 113
Cdd:PLN02466 60 LLINGQ--FVDAASGKTFPTldpRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 114 ELSAYLVYEVGKPWKE-ADADTAEAIDFLEYYARQMLEIdkgkHVESRPGERNRYV---YQPIGVTVVIPPWNLALaIMA 189
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKI----HGLTVPADGPHHVqtlHEPIGVAGQIIPWNFPL-LMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 190 GTTVAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIME 268
Cdd:PLN02466 213 AWKVGPaLACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 269 KASvrqngQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELS 348
Cdd:PLN02466 293 LAA-----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 349 VGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKA 427
Cdd:PLN02466 368 VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKF 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 428 KDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSGTDSKAG 497
Cdd:PLN02466 448 KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWV--NCFDVFDAAIPFGGYKMSGIGREKG 515
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-500 |
7.42e-86 |
|
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: 273.12 E-value: 7.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 35 QDHHL--LVDGERILTDDR--IVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRR 110
Cdd:cd07111 18 HDRSFghFINGKWVKPENRksFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 111 RKHELSAYLVYEVGKPWKEA-DADTAEAIDFLEYYARQMLEIDkgkhvESRPGernryvYQPIGVTVVIPPWNLALAIMA 189
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLD-----TELAG------WKPVGVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 190 GTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGlRIMEK 269
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVG-RALRR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 270 ASVRQNgqnhlKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSV 349
Cdd:cd07111 244 ATAGTG-----KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 350 GNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGrLMTGGKGDD--SKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKA 427
Cdd:cd07111 319 GDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEG-ADVFQPGADlpSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2513828894 428 KDFDDAIEIANNTEYGLTGAVISDN-RQHLEIAARdFHVGNLYFnrNCTGAIVGYQPFGGFKMSGTdSKAGGPD 500
Cdd:cd07111 398 RTAKEAVALANNTPYGLAASVWSENlSLALEVALS-LKAGVVWI--NGHNLFDAAAGFGGYRESGF-GREGGKE 467
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
60-491 |
5.32e-85 |
|
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: 270.86 E-value: 5.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEA-DADTAEAI 138
Cdd:cd07116 25 TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAADIPLAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 139 DFLEYYArQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALaIMAGTTVAP-LVAGNTVVMKPASNSPVIAAKF 217
Cdd:cd07116 105 DHFRYFA-GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPL-LMATWKLAPaLAAGNCVVLKPAEQTPASILVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 218 VEILEEAgLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngQNhLKQVIAEMGGK------D 291
Cdd:cd07116 183 MELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS-----EN-IIPVTLELGGKspniffA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGfSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07116 256 DVMDADDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADlAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:cd07116 335 LSYIDIGKEEGaEVLTGGErnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGA 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFnrNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07116 414 GVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSG 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
40-502 |
7.17e-83 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 265.23 E-value: 7.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGERILTD--DRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSA 117
Cdd:PRK11241 14 LINGEWLDANngEVIDVTNPANGD-KLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 118 YLVYEVGKPWKEADADTAEAIDFLEYYARQMLEIDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLV 197
Cdd:PRK11241 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 198 AGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngq 277
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 278 NHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNV 357
Cdd:PRK11241 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 358 YMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEI 436
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 437 ANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNrncTGAIVG-YQPFGGFKMSG---TDSKAGGPDYI 502
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNeVAPFGGIKASGlgrEGSKYGIEDYL 473
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
37-515 |
1.40e-82 |
|
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: 264.74 E-value: 1.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 37 HHLLVDGERILTDD-RIVST-NPANtEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLLRASAIMRRRK 112
Cdd:cd07140 6 HQLFINGEFVDAEGgKTYNTiNPTD-GSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 113 HELSAYLVYEVGKPWKEA-DADTAEAIDFLEYYARQMLEIdKGKHVESRPGERNRYV----YQPIGVTVVIPPWNLALAI 187
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKI-QGKTIPINQARPNRNLtltkREPIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 188 MAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIM 267
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 268 EKASVrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKEL 347
Cdd:cd07140 244 KSCAV-----SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 348 SVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTK 426
Cdd:cd07140 319 KIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 427 AK--DFDDAIEIANNTEYGLTGAVIS-DNRQHLEIAARdFHVGNLYFNR-NCTGAIvgyQPFGGFKMSGTdSKAGGPDYI 502
Cdd:cd07140 399 FDdgDVDGVLQRANDTEYGLASGVFTkDINKALYVSDK-LEAGTVFVNTyNKTDVA---APFGGFKQSGF-GKDLGEEAL 473
|
490
....*....|...
gi 2513828894 503 ALHMQAKTISEMY 515
Cdd:cd07140 474 NEYLKTKTVTIEY 486
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
60-512 |
9.13e-81 |
|
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: 258.83 E-value: 9.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFEswrKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAID 139
Cdd:cd07146 8 TGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 140 FLEYYARQMLEIDkGKHVES--RPGERNRYVY---QPIGVTVVIPPWNLALAIMAgTTVAPLVA-GNTVVMKPASNSPVI 213
Cdd:cd07146 85 VLRFAAAEALRDD-GESFSCdlTANGKARKIFtlrEPLGVVLAITPFNHPLNQVA-HKIAPAIAaNNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhlKQVIaEMGGKDTV 293
Cdd:cd07146 163 AIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK-------RQLL-ELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMS 373
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 374 YMEVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07146 315 RVEEAIAQGaRVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2513828894 453 RQHLEIAARDFHVGNLYFNRnctgaIVGYQ----PFGGFKMSGTDSKAGGPDYIALHMQAKTIS 512
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNE-----VPGFRselsPFGGVKDSGLGGKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-513 |
9.53e-81 |
|
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: 258.78 E-value: 9.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 60 TEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAID 139
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 140 FLEYYARQMleidkGKHVESR------PG-ERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPV 212
Cdd:cd07101 85 VARYYARRA-----ERLLKPRrrrgaiPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 213 IAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHpkTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAEMGGKDT 292
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRR------LIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 293 VVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIM 372
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 373 SYMEVGKEEG-RLMTGGKGDDSKG-YFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVIS 450
Cdd:cd07101 312 AHVDDAVAKGaTVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 451 DNRQH-LEIAARdFHVGNLYFNRNCTGAIVGYQ-PFGGFKMSGTdSKAGGPDYIALHMQAKTISE 513
Cdd:cd07101 392 RDGARgRRIAAR-LRAGTVNVNEGYAAAWASIDaPMGGMKDSGL-GRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
56-472 |
2.78e-79 |
|
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: 254.86 E-value: 2.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAdadtA 135
Cdd:cd07102 2 SPI-DGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYYARQMLEIDKGKHVESRPGE----RNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSP 211
Cdd:cd07102 77 GEIRGMLERARYMISIAEEALADIRVPEkdgfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 212 VIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAEMGGKD 291
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKVGLELGGKD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 292 TVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKI 371
Cdd:cd07102 230 PAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 372 MSYMEVGKEEG-RLMTGGKG---DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGA 447
Cdd:cd07102 310 RAQIADAIAKGaRALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTAS 389
|
410 420
....*....|....*....|....*
gi 2513828894 448 VISDNRQHLEIAARDFHVGNLYFNR 472
Cdd:cd07102 390 VWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
40-457 |
5.78e-78 |
|
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: 252.13 E-value: 5.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGERILTDDRIVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYL 119
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 120 VYEVGKPWKEADADTAEAIDFLEY---YARQMleidKGKHVES-RPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAP 195
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFavgLSRQL----YGLTIPSeRPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 196 LVAGNTVVMKPASNSPVIAAK----FVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAS 271
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 272 VRqngqnhLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGN 351
Cdd:cd07130 236 AR------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 352 AAESNVYMGPVVDQSAYEKIMSYMEVGKEE-GRLMTGGKGDDSKGYFIEPTVfADLAPESRMQQEEIFGPVVCFTKAKDF 430
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420
....*....|....*....|....*..
gi 2513828894 431 DDAIEIANNTEYGLTGAVISDNRQHLE 457
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAF 415
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-503 |
8.72e-77 |
|
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: 247.96 E-value: 8.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 78 AMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFLEYYARQMLEidkgkhv 157
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHE------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 158 esRPGERNRYV--------YQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKG 229
Cdd:cd07095 78 --RTGERATPMaqgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 230 VLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIA-EMGGKDTVVVDKEANIETAVEAI 308
Cdd:cd07095 156 VLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 309 VVSAFGFSGQKCSSGSRAVVHQD-VYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSY----MEVGKEEGR 383
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAqqdlLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 384 LMTGGkgdDSKGYFIEPTVFaDLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDF 463
Cdd:cd07095 309 AMERL---VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2513828894 464 HVGNLYFNRNCTGAiVGYQPFGGFKMSGTD--SKAGGPDYIA 503
Cdd:cd07095 385 RAGIVNWNRPTTGA-SSTAPFGGVGLSGNHrpSAYYAADYCA 425
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-491 |
1.79e-76 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 249.80 E-value: 1.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 49 DDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWK 128
Cdd:PRK09407 31 GPTREVTAPF-TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 129 EADADTAEAIDFLEYYARQ---MLEIDKgkhvesRPG-----ERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGN 200
Cdd:PRK09407 110 HAFEEVLDVALTARYYARRapkLLAPRR------RAGalpvlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 201 TVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHpkTALISFTGSRDVGLRIMEKASVRqngqnhL 280
Cdd:PRK09407 184 AVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR------L 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 281 KQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMG 360
Cdd:PRK09407 256 IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 361 PVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKG-YFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIAN 438
Cdd:PRK09407 336 SLISEAQLETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 439 NTEYGLTGAVIS-DNRQHLEIAARdFHVGNLYFNRNCTGAIVGYQ-PFGGFKMSG 491
Cdd:PRK09407 416 DTPYGLNASVWTgDTARGRAIAAR-IRAGTVNVNEGYAAAWGSVDaPMGGMKDSG 469
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-491 |
3.96e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 239.25 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 52 IVSTNPANTEqVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:PRK09406 3 IATINPATGE-TVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEYYAR---QMLEiDKGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAiMAGTTVAP-LVAGNTVVMKPA 207
Cdd:PRK09406 82 AEALKCAKGFRYYAEhaeALLA-DEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLW-QVVRFAAPaLMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVgDYLIEHPKTALISFTGSRDVGlrimekASVRQNGQNHLKQVIAEM 287
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAV-EAILRDPRVAAATLTGSEPAG------RAVAAIAGDEIKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 288 GGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSA 367
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 368 YEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTG 446
Cdd:PRK09406 313 RDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2513828894 447 AVISDNRQHLEIAARDFHVGNLYFNrnctGAIVGYQ--PFGGFKMSG 491
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSG 435
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
27-491 |
3.41e-71 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 235.18 E-value: 3.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 27 QQVKSQLGQDHHLLVDGE-RILTDDRIVST-NPAnTEQVVGRVSKATQELAEKAMQAASNSFES--WRKWSAEARAGLLL 102
Cdd:PRK09847 10 QDKALSLAIENRLFINGEyTAAAENETFETvDPV-TQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 103 RASAIMRRRKHELSAYLVYEVGKPWKEA-DADTAEAIDFLEYYARQmleIDK--GKHVESRPGERNRYVYQPIGVTVVIP 179
Cdd:PRK09847 89 KLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEA---IDKvyGEVATTSSHELAMIVREPVGVIAAIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 180 PWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGS 259
Cdd:PRK09847 166 PWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 260 RDVGLRIMEKAsvrqnGQNHLKQVIAEMGGKDTVVVDKEA-NIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLE 338
Cdd:PRK09847 246 TRTGKQLLKDA-----GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 339 RVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYfIEPTVFADLAPESRMQQEEIF 418
Cdd:PRK09847 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIF 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 419 GPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVgyQPFGGFKMSG 491
Cdd:PRK09847 400 GPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG 470
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
40-495 |
2.27e-67 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 225.02 E-value: 2.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 40 LVDGE-RILTDDRIVS-TNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSA 117
Cdd:PLN00412 19 YADGEwRTSSSGKSVAiTNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 118 YLVYEVGKPWKEADADTAEAIDFLEYYARQMLEI-DKGK--HVESRPG-ERNRYVYQ---PIGVTVVIPPWNLALAiMAG 190
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRIlGEGKflVSDSFPGnERNKYCLTskiPLGVVLAIPPFNYPVN-LAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 191 TTVAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSrDVGLRIMEK 269
Cdd:PLN00412 177 SKIAPaLIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 270 ASvrqngqnhLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSV 349
Cdd:PLN00412 256 AG--------MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 350 GnAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDdskGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAK 428
Cdd:PLN00412 328 G-PPEDDCDITPVVSESSANFIEGLVMDAKEKGaTFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 429 DFDDAIEIANNTEYGLTGAVISdnrqhleiaaRDFHVGNLYFNRNCTGAIV---------GYQPFGGFKMSGTDSK 495
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFT----------RDINKAILISDAMETGTVQinsapargpDHFPFQGLKDSGIGSQ 469
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
51-491 |
3.73e-66 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 221.76 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 51 RIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKP-WK- 128
Cdd:PRK09457 16 AFESRNPV-SGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPlWEa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 129 --EADADTAE-AIDFLEYYARQmleidkGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMK 205
Cdd:PRK09457 95 atEVTAMINKiAISIQAYHERT------GEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 206 PASNSPVIAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMekasvRQNGQNHLKQVIA 285
Cdd:PRK09457 169 PSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLH-----RQFAGQPEKILAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 286 EMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVY-DEVLERVVARTKELSVGNA-AESNVYMGPVV 363
Cdd:PRK09457 243 EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQPFMGAVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 364 DQSAYEKIMS----YMEVGKE---EGRLMTGGKGDDSKGyFIEPTVFADLaPEsrmqqEEIFGPVVCFTKAKDFDDAIEI 436
Cdd:PRK09457 323 SEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTGLLTPG-IIDVTGVAEL-PD-----EEYFGPLLQVVRYDDFDEAIRL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 437 ANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAiVGYQPFGGFKMSG 491
Cdd:PRK09457 396 ANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
56-497 |
7.27e-64 |
|
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: 214.86 E-value: 7.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLL--LRASAImrRRKHELSAYLVYEVGKPWKEADAD 133
Cdd:cd07098 2 DPA-TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLrsLLKYIL--ENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 134 ----TAEAIDFLeyyarqmleIDKG-KHV--ESRPG------ERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGN 200
Cdd:cd07098 79 eilvTCEKIRWT---------LKHGeKALrpESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 201 TVVMKPASNSPVIAAKFVEILEEA----GLPKGVLNFVPGSGgEVGDYLIEHPKTALISFTGSRDVGLRIMEKASvrqng 276
Cdd:cd07098 150 AIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAA----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 277 qNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESN 356
Cdd:cd07098 224 -ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 357 VYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGK----GDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFD 431
Cdd:cd07098 303 VDVGAMISPARFDRLEELVADAVEKGaRLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 432 DAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSGTDSKAG 497
Cdd:cd07098 383 EAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-491 |
7.30e-64 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 215.11 E-value: 7.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 53 VSTNPANTEQVvGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADA 132
Cdd:PRK13968 10 ISVNPATGEQL-SVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 133 DTAEAIDFLEYYARQ---MLEidkgkhVESRPGERNRYV--YQPIGVTVVIPPWNLAL-AIMAGTtVAPLVAGNTVVMKP 206
Cdd:PRK13968 89 EVAKSANLCDWYAEHgpaMLK------AEPTLVENQQAVieYRPLGTILAIMPWNFPLwQVMRGA-VPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 207 ASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDyLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQVIAE 286
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAA------LKKCVLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 287 MGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQS 366
Cdd:PRK13968 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 367 AYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLT 445
Cdd:PRK13968 315 LRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2513828894 446 GAVISDNRQHLEIAARDFHVGNLYFNRNC-TGAIVGyqpFGGFKMSG 491
Cdd:PRK13968 395 ATIFTTDETQARQMAARLECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
63-508 |
1.05e-61 |
|
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: 209.20 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 63 VVGRVSKATQELAEKAMQAASNSFESWRKW-SAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTAEAIDFL 141
Cdd:cd07148 11 PIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 142 EYYARQM-----LEIDKGkHVESRPGERNRYVYQPIGVTVVIPPWN--LALAIMagtTVAPLVA-GNTVVMKPASNSPVI 213
Cdd:cd07148 91 ELAADELgqlggREIPMG-LTPASAGRIAFTTREPIGVVVAISAFNhpLNLIVH---QVAPAIAaGCPVIVKPALATPLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 214 AAKFVEILEEAGLPKGVLNFVPgSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhlKQVIAEMGGKDTV 293
Cdd:cd07148 167 CLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-------TRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 294 VVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMS 373
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 374 YMEVGKEEG-RLMTGGKGDDSKGYfiEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07148 319 WVNEAVAAGaRLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2513828894 453 rqhLEIAARDfhVGNLyfnrNCTGAIVG--------YQPFGGFKMSGTDSkaGGPDYIALHMQA 508
Cdd:cd07148 397 ---LDVALKA--VRRL----DATAVMVNdhtafrvdWMPFAGRRQSGYGT--GGIPYTMHDMTQ 449
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
52-497 |
1.88e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 193.90 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 52 IVSTNPANTeQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD 131
Cdd:PLN02315 36 VSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 132 ADTAEAIDFLEY---YARQMleidKGKHVES-RPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPA 207
Cdd:PLN02315 115 GEVQEIIDMCDFavgLSRQL----NGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 208 SNSPVIA---AKFV-EILEEAGLPKGVLNFVPGsGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRqngqnhLKQV 283
Cdd:PLN02315 191 PTTPLITiamTKLVaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 284 IAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYMGPVV 363
Cdd:PLN02315 264 LLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 364 DQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYFIEPTVfADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEY 442
Cdd:PLN02315 344 TPESKKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2513828894 443 GLTGAVISDNRQHL--EIAARDFHVGNLYFNRNCTGAIVGyQPFGGFKMSGTDSKAG 497
Cdd:PLN02315 423 GLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
56-465 |
2.18e-54 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 193.04 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 56 NPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADTA 135
Cdd:PLN02419 135 NPA-TQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 136 EAIDFLEYyARQMLEIDKGKHVESRPGERNRY-VYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIA 214
Cdd:PLN02419 214 RGLEVVEH-ACGMATLQMGEYLPNVSNGVDTYsIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGAS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 215 AKFVEILEEAGLPKGVLNFVPGSGGEVgDYLIEHPKTALISFTGSRDVGLRIMEKASVRQngqnhlKQVIAEMGGKDTVV 294
Cdd:PLN02419 293 VILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG------KRIQSNMGAKNHGL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 295 VDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVyDEVLERVVARTKELSVGNAAESNVYMGPVVDQSAYEKIMSY 374
Cdd:PLN02419 366 VLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 375 MEVGKEEG-RLMTGGKG----DDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVI 449
Cdd:PLN02419 445 IQSGVDDGaKLLLDGRDivvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIF 524
|
410
....*....|....*.
gi 2513828894 450 SDNRQhleiAARDFHV 465
Cdd:PLN02419 525 TSSGA----AARKFQM 536
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
84-491 |
2.26e-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: 188.50 E-value: 2.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 84 NSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD----ADTAEAIDF-LEYYARQMleidKGKHVE 158
Cdd:cd07087 9 ETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVVLGEIDHaLKHLKKWM----KPRRVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 159 ----SRPGeRNRYVYQPIGVTVVIPPWN--LALAImagttvAPLV----AGNTVVMKPASNSPVIAAKFVEILEEAgLPK 228
Cdd:cd07087 85 vpllLQPA-KAYVIPEPLGVVLIIGPWNypLQLAL------APLIgaiaAGNTVVLKPSELAPATSALLAKLIPKY-FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 229 GVLNFVPGsGGEVGDYLIEHPkTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAI 308
Cdd:cd07087 157 EAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAA------KHLTPVTLELGGKSPCIVDKDANLEVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 309 VVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYmGPVVDQSAYEKIMSYMEVGKeegrLMTGG 388
Cdd:cd07087 229 AWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLDDGK----VVIGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 389 KGDDSKGYfIEPTVFADLAPESRMQQEEIFG---PVVCFTkakDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHV 465
Cdd:cd07087 304 QVDKEERY-IAPTILDDVSPDSPLMQEEIFGpilPILTYD---DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420
....*....|....*....|....*.
gi 2513828894 466 GNLYFNRNCTGAIVGYQPFGGFKMSG 491
Cdd:cd07087 380 GGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
89-491 |
5.45e-46 |
|
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: 166.25 E-value: 5.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 89 WRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAD--------ADTAEAIDFLEYYARQMleidKGKHVESR 160
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKKWMKPK----RVRTPLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 161 PGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVpgSGGE 240
Cdd:cd07134 90 FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE--GDAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 241 VGDYLIEHPKTAlISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKC 320
Cdd:cd07134 168 VAQALLELPFDH-IFFTGSPAVGKIVMAAAA------KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 321 SSGSRAVVHQDVYDEVLERVVARTKE-LSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEG-RLMTGGKGDDSKGYfI 398
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGaKVEFGGQFDAAQRY-I 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 399 EPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAI 478
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFL 399
|
410
....*....|...
gi 2513828894 479 VGYQPFGGFKMSG 491
Cdd:cd07134 400 NPNLPFGGVNNSG 412
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
166-491 |
1.24e-45 |
|
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: 165.76 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 166 RYVYQPIGVTVVIPPWN--LALAImagttvAPLV----AGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGsGG 239
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNypFQLAL------APLIgaiaAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 240 EVGDYLIEHpKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQK 319
Cdd:cd07136 167 EENQELLDQ-KFDYIFFTGSVRVGKIVMEAAA------KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 320 CSSGSRAVVHQDVYDEVLERVVARTKELsVGNAAESNVYMGPVVDQSAYEKIMSYMevgkEEGRLMTGGKGDDsKGYFIE 399
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLL----DNGKIVFGGNTDR-ETLYIE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 400 PTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEiaardfhvgnlYFNRNCT---G 476
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEK-----------KVLENLSfggG 382
|
330 340
....*....|....*....|...
gi 2513828894 477 AI--------VGYQPFGGFKMSG 491
Cdd:cd07136 383 CIndtimhlaNPYLPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
110-491 |
7.84e-45 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 164.43 E-value: 7.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 110 RRKHELSAYlVYEVGKPWKEADADTAeaiDFLEYYARQMLEIdkgkHVESRPGERnrYV-YQPIGVTVVIPPWN----LA 184
Cdd:PTZ00381 57 LGRHPFETK-MTEVLLTVAEIEHLLK---HLDEYLKPEKVDT----VGVFGPGKS--YIiPEPLGVVLVIGAWNyplnLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 185 LAIMAGTtvapLVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGsGGEVGDYLIEHPkTALISFTGSRDVGL 264
Cdd:PTZ00381 127 LIPLAGA----IAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 265 RIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVART 344
Cdd:PTZ00381 200 LVMQAAA------ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 345 KELSVGNAAESNVYmGPVVDQSAYEKIMSYMEVGKeeGRLMTGGKGDDSKGYfIEPTVFADLAPESRMQQEEIFGPVVCF 424
Cdd:PTZ00381 274 KEFFGEDPKKSEDY-SRIVNEFHTKRLAELIKDHG--GKVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPI 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2513828894 425 TKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGGFKMSG 491
Cdd:PTZ00381 350 LTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
170-492 |
5.41e-44 |
|
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: 160.85 E-value: 5.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 170 QPIGVTVVIPPWN----LALAIMAGTtvapLVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGSGGEVGdYL 245
Cdd:cd07135 107 EPLGVVLIIGPWNypvlLALSPLVGA----IAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT-AL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 246 IEHpKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSR 325
Cdd:cd07135 181 LEQ-KFDKIFYTGSGRVGRIIAEAAA------KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 326 AVVHQDVYDEVLERVVARTKELSVGNAAESNVYmGPVVDQSAYEKIMSYMEVGKeeGRLMTGGKGDDSKgYFIEPTVFAD 405
Cdd:cd07135 254 VLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLDTTK--GKVVIGGEMDEAT-RFIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 406 LAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNR---QHL--EIAARDFHVGNLYFNRNCTGAivg 480
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKseiDHIltRTRSGGVVINDTLIHVGVDNA--- 406
|
330
....*....|..
gi 2513828894 481 yqPFGGFKMSGT 492
Cdd:cd07135 407 --PFGGVGDSGY 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-491 |
2.67e-35 |
|
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: 136.97 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 76 EKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEAdadTAEAIDFLEYYARQMLEiDKGK 155
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEA---VLSEILLVKNEIKYAIS-NLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 156 HVESRPGERNR-------YVY-QPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPViAAKFVEILeeagLP 227
Cdd:cd07132 77 WMKPEPVKKNLatllddvYIYkEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPA-TAKLLAEL----IP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 228 KGVLN----FVPGsGGEVGDYLIEHpKTALISFTGSRDVGLRIMEKASVrqngqnHLKQVIAEMGGKDTVVVDKEANIET 303
Cdd:cd07132 152 KYLDKecypVVLG-GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAK------HLTPVTLELGGKSPCYVDKSCDIDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 304 AVEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAAESNVYmGPVVDQSAYEKIMSYMEvgkeEGR 383
Cdd:cd07132 224 AARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKLLS----GGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 384 LMTGGKGDDSKGYfIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQhleiaardf 463
Cdd:cd07132 299 VAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK--------- 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 2513828894 464 hVGNLYFNRNCTG----------AIVGYQPFGGFKMSG 491
Cdd:cd07132 369 -VINKILSNTSSGgvcvndtimhYTLDSLPFGGVGNSG 405
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
168-497 |
1.89e-32 |
|
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: 128.68 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 168 VYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPViAAKFVEILEEAGLPKGVLNFVPGsGGEVGDYLIE 247
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPA-TSALLAKLIPEYLDTKAIKVIEG-GVPETTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 248 HpKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGF-SGQKCSSGSRA 326
Cdd:cd07137 176 Q-KWDKIFFTGSPRVGRIIMAAAA------KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 327 VVHQDVYDEVLERVVARTKELSVGNAAESNvYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKGDDSKGYfIEPTVFADL 406
Cdd:cd07137 249 LVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLY-IEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 407 APESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGG 486
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
330
....*....|.
gi 2513828894 487 FKMSGTDSKAG 497
Cdd:cd07137 407 VGESGFGAYHG 417
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
76-504 |
4.31e-32 |
|
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: 128.12 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 76 EKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEA-----DADTAEAIDFLEYYARQMLE 150
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicgDQVQLRARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 151 IdkGKHVESRPGERNRYVYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAG-LPKG 229
Cdd:cd07084 82 P--GNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 230 VLNFVPGSgGEVGDYLIEHPKTALISFTGSRDVGLRIMEKAsvrqngqnHLKQVIAEMGGKDTVVVDKEANIETAV-EAI 308
Cdd:cd07084 160 DVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--------KQARIYLELAGFNWKVLGPDAQAVDYVaWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 309 VVSAFGFSGQKCSSGSRAVVHQD-----VYDEVLERVVARTKELSVgnaaesnvyMGPVVDQSAYEKImsyMEVGKEEGR 383
Cdd:cd07084 231 VQDMTACSGQKCTAQSMLFVPENwsktpLVEKLKALLARRKLEDLL---------LGPVQTFTTLAMI---AHMENLLGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 384 LMT-GGK------GDDSKGYFIEPTVFADLAPESRMQQ---EEIFGPVVCFTKAKDFD--DAIEIANNTEYGLTGAVISD 451
Cdd:cd07084 299 VLLfSGKelknhsIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQlaLVLELLERMHGSLTAAIYSN 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2513828894 452 NRQHL-EIAARDFHVGNLYF-NRNCTGAIVGYQPFGGFKMSGTDSKAGGPDYIAL 504
Cdd:cd07084 379 DPIFLqELIGNLWVAGRTYAiLRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
93-438 |
8.42e-32 |
|
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: 126.83 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 93 SAEARAGLLLRASAIMRRRKHELSAYLvyevgkpwkEAD-----------ADTAEAIDFLEYYARQMLEIDKGKHVESRP 161
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAI---------SADfghrsrhetllAEILPSIAGIKHARKHLKKWMKPSRRHVGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 162 ---GERNRYVYQPIGVTVVIPPWN--LALAImaGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKgVLNFVPG 236
Cdd:cd07133 89 lflPAKAEVEYQPLGVVGIIVPWNypLYLAL--GPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 237 sGGEVG--------DYLIehpktalisFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAI 308
Cdd:cd07133 166 -GADVAaafsslpfDHLL---------FTGSTAVGRHVMRAAA------ENLTPVTLELGGKSPAIIAPDADLAKAAERI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 309 VVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELsVGNAAESNVYMGpVVDQSAYEKIMSYMEVGKEEG-RLMT- 386
Cdd:cd07133 230 AFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTS-IINERHYARLQGLLEDARAKGaRVIEl 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 387 -GGKGDDSKGYFIEPTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIAN 438
Cdd:cd07133 308 nPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYIN 360
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
48-474 |
1.84e-31 |
|
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: 127.39 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 48 TDDRIVSTNPAnTEQVVGRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAyLVYEVGKPW 127
Cdd:cd07128 13 TGDGRTLHDAV-TGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA-LSAATGATR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 128 KEADADTAEAIDFLEYYA---RQMLEiDKGKHVE------SRPGE-RNRYVYQPI-GVTVVI-----PPWNLALAImagt 191
Cdd:cd07128 91 RDSWIDIDGGIGTLFAYAslgRRELP-NAHFLVEgdveplSKDGTfVGQHILTPRrGVAVHInafnfPVWGMLEKF---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 192 tvAP-LVAGNTVVMKPASNSPVIAAKFVEILEEAG-LPKGVLNFVPGSGGEVGDYLIEHPktaLISFTGSRDVGLRIMEK 269
Cdd:cd07128 166 --APaLLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQD---VVAFTGSAATAAKLRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 270 ASVRQNGQnhlkQVIAEMGGKDTVVVDKEANIETA-----VEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVART 344
Cdd:cd07128 241 PNIVARSI----RFNAEADSLNAAILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 345 KELSVGNAAESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGK-------GDDSKGYFIEPTVF--ADLAPESRMQQE 415
Cdd:cd07128 317 AKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLlcDDPDAATAVHDV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2513828894 416 EIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLE---IAARDFHvGNLYF-NRNC 474
Cdd:cd07128 397 EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARelvLGAAPYH-GRLLVlNRDS 458
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
76-481 |
1.58e-27 |
|
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: 114.95 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 76 EKAMQAASNSFESWRKWSAEARAGLLLR-ASAIMRRRKhELSAYLVYEVGKP--------------------------WK 128
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAiADEIEALGD-ELVARAHAETGLPearlqgelgrttgqlrlfadlvregsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 129 EADADTAEAidfleyyARQMLeidkgkhveSRPGERNRYVyqPIGVTVVIPPWN--LALAIMAGTTVAPLVAGNTVVMKP 206
Cdd:cd07129 81 DARIDPADP-------DRQPL---------PRPDLRRMLV--PLGPVAVFGASNfpLAFSVAGGDTASALAAGCPVVVKA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 207 ASNSPVIAAKFVEI----LEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRIMEKASVRQNGqnhlKQ 282
Cdd:cd07129 143 HPAHPGTSELVARAiraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP----IP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 283 VIAEMGGKDTVVVDKEA---NIETAVEAIVVSAFGFSGQKCSSGSRAVVHQdvyDEVLERVVARTKELSvgNAAESNVYM 359
Cdd:cd07129 219 FYAELGSVNPVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPA---GPAGDAFIAALAEAL--AAAPAQTML 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 360 GPVVdQSAYEKimsymevGKEE-----GRLMTGGKGDDSKGYFIEPTVFAD-----LAPESrmQQEEIFGPVVCFTKAKD 429
Cdd:cd07129 294 TPGI-AEAYRQ-------GVEAlaaapGVRVLAGGAAAEGGNQAAPTLFKVdaaafLADPA--LQEEVFGPASLVVRYDD 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 430 FDDAIEIANNTEYGLTGAVI---SDNRQHLEIAAR-DFHVGNLYFNRNCTGAIVGY 481
Cdd:cd07129 364 AAELLAVAEALEGQLTATIHgeeDDLALARELLPVlERKAGRLLFNGWPTGVEVCP 419
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
55-460 |
3.69e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.80 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 55 TNPANTEQVVgRVSKATQELAEKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWKEADADT 134
Cdd:PRK11903 24 FDPVTGEELV-RVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 135 AEAIDFLEYYARQMLEIDKGKHVESRPGER--------NRYVYQPI-GVTVVI-----PPWNLAlaimagTTVAP-LVAG 199
Cdd:PRK11903 103 DGGIFTLGYYAKLGAALGDARLLRDGEAVQlgkdpafqGQHVLVPTrGVALFInafnfPAWGLW------EKAAPaLLAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 200 NTVVMKPASNSPVIAAKFVEILEEAG-LPKGVLNFVPGSGGEVGDYLIEHPktaLISFTGSRDVGLRIMEKASVRQNGQn 278
Cdd:PRK11903 177 VPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFD---VVSFTGSAETAAVLRSHPAVVQRSV- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 279 hlkQVIAEMGGKDTVVVDKEANIETA-----VEAIVVSAFGFSGQKCSSGSRAVVHQDVYDEVLERVVARTKELSVGNAA 353
Cdd:PRK11903 253 ---RVNVEADSLNSALLGPDAAPGSEafdlfVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 354 ESNVYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKG------DDSKGYFIEPTVF----ADLAPesRMQQEEIFGPVVC 423
Cdd:PRK11903 330 NDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdaDPAVAACVGPTLLgasdPDAAT--AVHDVEVFGPVAT 407
|
410 420 430
....*....|....*....|....*....|....*..
gi 2513828894 424 FTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAA 460
Cdd:PRK11903 408 LLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
170-491 |
1.85e-26 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 112.13 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 170 QPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLnfVPGSGGEVGDYLIEHP 249
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVK--VIEGGPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 250 KTAlISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVD---KEANIETAVEAIVVSAFGF-SGQKCSSGSR 325
Cdd:PLN02203 185 WDK-IFFTGSPRVGRIIMTAAA------KHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 326 AVVHQDVYDEVLERVVARTKELSVGNAAESNvYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGkGDDSKGYFIEPTVFAD 405
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGG-SIDEKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 406 LAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNrnctGAIVGYQ--- 482
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN----DAIIQYAcds 411
|
330
....*....|
gi 2513828894 483 -PFGGFKMSG 491
Cdd:PLN02203 412 lPFGGVGESG 421
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
168-497 |
8.83e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 107.44 E-value: 8.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 168 VYQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAgLPKGVLNFVPGSGGEVGDYLIE 247
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 248 hpKTALISFTGSRDVGLRIMEKASvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGF-SGQKCSSGSRA 326
Cdd:PLN02174 188 --KWDKIFYTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 327 VVHQDVYDEVLERVVARTKELSVGNAAESNvYMGPVVDQSAYEKIMSYMEVGKEEGRLMTGGKgDDSKGYFIEPTVFADL 406
Cdd:PLN02174 260 LTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 407 APESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGLTGAVISDNRQHLEIAARDFHVGNLYFNRNCTGAIVGYQPFGG 486
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGG 417
|
330
....*....|.
gi 2513828894 487 FKMSGTDSKAG 497
Cdd:PLN02174 418 VGESGMGAYHG 428
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
57-437 |
1.63e-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: 94.85 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 57 PANTEQVVGRVSKATQELA--------EKAMQAASNSFESWRKWSAEARAGLLLRASAIMRRRKHELSAYLVYEVGKPWK 128
Cdd:cd07127 60 PGASGWVGGEVSPYGVELGvtypqcdpDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 129 EA-DADTAEAID----FLEYYARQMLEIdKGKHVESRPGERN-------RYVYQPIGVTVVI-----PPWNLALAIMAGt 191
Cdd:cd07127 140 MAfQAGGPHAQDrgleAVAYAWREMSRI-PPTAEWEKPQGKHdplamekTFTVVPRGVALVIgcstfPTWNGYPGLFAS- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 192 tvapLVAGNTVVMKPASNSPVIAAKFV----EILEEAGL-PKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDVGLRI 266
Cdd:cd07127 218 ----LATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 267 meKASVRQngqnhlKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSRAVVHQD---------VYDEVL 337
Cdd:cd07127 294 --EANARQ------AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 338 ERVVARTKELsVGNAAESNVYMGPVVDQSAYEKImsymevgkEEGRLMtGGKGDDSKGY----FIE-----PTVFADLAP 408
Cdd:cd07127 366 ADLAAAIDGL-LADPARAAALLGAIQSPDTLARI--------AEARQL-GEVLLASEAVahpeFPDarvrtPLLLKLDAS 435
|
410 420
....*....|....*....|....*....
gi 2513828894 409 ESRMQQEEIFGPVVCFTKAKDFDDAIEIA 437
Cdd:cd07127 436 DEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
170-457 |
9.05e-15 |
|
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: 76.54 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 170 QPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKP---ASNSPVIAAKFV-EILEEAGLPKGVLNFVPGSGGEVGDYL 245
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAGAPENLIGWIDNPSIELAQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 246 IEHPKTALISFTGSrdvglrimekASVRQNGQNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFGFSGQKCSSGSR 325
Cdd:cd07081 174 MKFPGIGLLLATGG----------PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 326 AVVHQDVYDEVLERVVARTKELSVGNAAES-------NVYMGP-VVDQSAYeKI--MSYMEVgKEEGRLMtggkgddskg 395
Cdd:cd07081 244 VIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRdIVGQDAY-KIaaAAGLKV-PQETRIL---------- 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2513828894 396 yFIEPTVFAdlapESRMQQEEIFGPVVCFTKAKDFDDAIEIA----NNTEYGLTGAVISDNRQHLE 457
Cdd:cd07081 312 -IGEVTSLA----EHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
171-452 |
2.17e-14 |
|
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: 75.61 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 171 PIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEAGLPKGVLNFVPGSGGEVGDYLIE-HP 249
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 250 KTALisFTGSRdvglRIMEKASVRQNGqnhlkQVIAEMGGKDTVVVDKE-ANIETAVEAIVVSAFGFSGQKCSSGSRAVV 328
Cdd:cd07126 222 RMTL--FTGSS----KVAERLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 329 HQDVYDEVLervVARTKELSvGNAAESNVYMGPVVDQSAyEKIMSYME--VGKEEGRLMTGGK----GDDSKGY-FIEPT 401
Cdd:cd07126 291 HENWVQAGI---LDKLKALA-EQRKLEDLTIGPVLTWTT-ERILDHVDklLAIPGAKVLFGGKpltnHSIPSIYgAYEPT 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 402 -VFADLApESRMQQ------EEIFGPVVCFTKAKD--FDDAIEIANNTEYGLTGAVISDN 452
Cdd:cd07126 366 aVFVPLE-EIAIEEnfelvtTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
117-452 |
3.06e-14 |
|
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: 74.57 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 117 AYLVYEVGKPWKEAD-ADTAEAIDFLEYYARQMLEIDKGK----------------HVESRPGERNRYVYQ---PIGVTV 176
Cdd:cd07077 26 ANALYDTRQRLASEAvSERGAYIRSLIANWIAMMGCSESKlyknidtergitasvgHIQDVLLPDNGETYVrafPIGVTM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 177 VIPPWNLALAIMAGTTVApLVAGNTVVMKPASNSPV----IAAKFVEILEeAGLPKGVLNFVPGSGGEVGDYLIEHPKTA 252
Cdd:cd07077 106 HILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFtnraLALLFQAADA-AHGPKILVLYVPHPSDELAEELLSHPKID 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 253 LISFTGSRDVgLRIMEKASvrqngqNHlKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAFgFSGQKCSSGSRAVVHQDV 332
Cdd:cd07077 184 LIVATGGRDA-VDAAVKHS------PH-IPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVDDV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 333 YDEVLERVVARTKELSVgnaaesNVYMGPvvdqsayeKIMSYMevgkeegrlmtggkgddskgyfieptVFADLAPESRm 412
Cdd:cd07077 255 LDPLYEEFKLKLVVEGL------KVPQET--------KPLSKE--------------------------TTPSFDDEAL- 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2513828894 413 qqeEIFGPVVCFTKAKDFDDAIEIANNT--EYG--LTGAVISDN 452
Cdd:cd07077 294 ---ESMTPLECQFRVLDVISAVENAWMIieSGGgpHTRCVYTHK 334
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
170-478 |
3.23e-12 |
|
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: 68.29 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 170 QPIGVTV-VIPPWNLALAIMAGTTVApLVAGNTVVMKP---ASNSPVIAAKFV-EILEEAGLPKGVLNFVPGSGGEVGDY 244
Cdd:cd07122 94 EPVGVIAaLIPSTNPTSTAIFKALIA-LKTRNAIIFSPhprAKKCSIEAAKIMrEAAVAAGAPEGLIQWIEEPSIELTQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 245 LIEHPKTALISFTGSRdvglrIMEKASvRQNGqnhlKQVIAEMGGKDTVVVDKEANIETAVEAIVVS-AFGFsGQKCSSG 323
Cdd:cd07122 173 LMKHPDVDLILATGGP-----GMVKAA-YSSG----KPAIGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 324 SRAVVHQDVYDEVLERVVARtkelsvgnaaesNVYmgpVVDQSAYEKIMSYMEvgkEEGRLMTG---GKGddskgyfieP 400
Cdd:cd07122 242 QSVIVDDEIYDEVRAELKRR------------GAY---FLNEEEKEKLEKALF---DDGGTLNPdivGKS---------A 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 401 TVFADLA-------------PESRMQQEEIF-----GPVVCFTKAKDFDDAIEIAN-NTEYGLTG--AVI-SDNRQHLEI 458
Cdd:cd07122 295 QKIAELAgievpedtkvlvaEETGVGPEEPLsreklSPVLAFYRAEDFEEALEKAReLLEYGGAGhtAVIhSNDEEVIEE 374
|
330 340
....*....|....*....|.
gi 2513828894 459 AARDFHVGNLYFNRNCT-GAI 478
Cdd:cd07122 375 FALRMPVSRILVNTPSSlGGI 395
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
169-461 |
2.48e-10 |
|
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: 62.64 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 169 YQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEA----GLPKGVLNFVPGSGGEVGDY 244
Cdd:cd07121 95 YAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 245 LIEHPKTALISFTGSRDVGLRIMekasvrqngqNHLKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAfGFSGQ-KCSSG 323
Cdd:cd07121 175 LMAHPDINLLVVTGGPAVVKAAL----------SSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 324 SRAVVHQDVYDEVLERVVaRTKELSVGNAAESNvyMGPVVDQSAYEKIMSYMEVGKEEGRL--MTGGKGDDSKgyfiePT 401
Cdd:cd07121 244 KEVIAVDSVADYLIAAMQ-RNGAYVLNDEQAEQ--LLEVVLLTNKGATPNKKWVGKDASKIlkAAGIEVPADI-----RL 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2513828894 402 VFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGL--TGAVISDNRQHLEIAAR 461
Cdd:cd07121 316 IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMAR 377
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
169-461 |
2.32e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.45 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 169 YQPIGVTVVIPPWNLALAIMAGTTVAPLVAGNTVVMKPASNSPVIAAKFVEILEEA----GLPKGVLNFVPGSGGEVGDY 244
Cdd:PRK15398 127 YAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 245 LIEHPKTALISFTGSRDVGlrimekASVRQNGqnhlKQVIAEMGGKDTVVVDKEANIETAVEAIVVSAfGFSGQ-KCSSG 323
Cdd:PRK15398 207 LMKHPGIALLVVTGGPAVV------KAAMKSG----KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 324 SRAVVHQDVYDEVLERVVARTKELSVGNAAESnvyMGPVV--DQSAYEKIMsymeVGKEEGRLM--TGGKGDDSKgyfie 399
Cdd:PRK15398 276 KEVIVVDSVADELMRLMEKNGAVLLTAEQAEK---LQKVVlkNGGTVNKKW----VGKDAAKILeaAGINVPKDT----- 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2513828894 400 PTVFADLAPESRMQQEEIFGPVVCFTKAKDFDDAIEIANNTEYGL--TGAVISDNRQHLEIAAR 461
Cdd:PRK15398 344 RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMAR 407
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
200-452 |
2.50e-08 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 56.73 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 200 NTVVMKP---ASNSPVIAAKFV-EILEEAGLPKGVLNFVPGSGGEVGDYLIEHPKTALISFTGSRDvglriMEKAsvrqn 275
Cdd:PRK13805 137 NPIIFSFhprAQKSSIAAAKIVlDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPG-----MVKA----- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 276 gqnhlkqviAEMGGKDT---------VVVDKEANIETAVEAIVVS-AFGfSGQKCSSGSRAVVHQDVYDEVLERVVAR-- 343
Cdd:PRK13805 207 ---------AYSSGKPAlgvgagnvpAYIDKTADIKRAVNDILLSkTFD-NGMICASEQAVIVDDEIYDEVKEEFASHga 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 344 ---TKE---------LSVGNAAESnvymGPVVDQSAYeKI--MSYMEVGKEEGRLMTGGKGDDSKgyfiEPtvfadLAPE 409
Cdd:PRK13805 277 yflNKKelkklekfiFGKENGALN----ADIVGQSAY-KIaeMAGFKVPEDTKILIAEVKGVGES----EP-----LSHE 342
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2513828894 410 SRMqqeeifgPVVCFTKAKDFDDAIEIANN-TEYGLTG--AVISDN 452
Cdd:PRK13805 343 KLS-------PVLAMYKAKDFEDAVEKAEKlVEFGGLGhtAVIYTN 381
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
158-349 |
9.69e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.51 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 158 ESRPgerNryvyqpigVTVVIppwnLALAIMAGttvaplvagNTVVMKP---ASNS-PVIAAKFVEILEEAGLPKGVLNF 233
Cdd:PRK00197 124 ESRP---N--------VTVDA----AALCLKSG---------NAVILRGgseAIHSnRALVAVIQEALEEAGLPADAVQL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513828894 234 VPGSG-GEVGdyliehpktALISFTGSRDV-------GL--RIMEKASVrqngqnhlkQVIAEMGGKDTVVVDKEANIET 303
Cdd:PRK00197 180 VETTDrAAVG---------ELLKLDGYVDViiprggaGLirRVVENATV---------PVIEHGDGICHIYVDESADLDK 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2513828894 304 AVeAIVVSAfgfsgqK------CSSGSRAVVHQDVYDEVLERVVARTKELSV 349
Cdd:PRK00197 242 AL-KIVLNA------KtqrpsvCNALETLLVHEAIAEEFLPKLAEALAEAGV 286
|
|
| |
