|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-516 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 863.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 2 TVEPFRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALE 81
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 82 AAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRyPAVEVVP 161
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLA-DGKPVES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 162 YPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGE 241
Cdd:PRK03137 160 RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 242 EVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK 321
Cdd:PRK03137 240 EVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 *SAASRLILTQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAP 401
Cdd:PRK03137 320 CSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 402 TVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVG 481
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500 510
....*....|....*....|....*....|....*
2J40_B 482 VQPFGGFKLSGTNAKTGALDYLRLFLEMKAVAERF 516
Cdd:PRK03137 480 YHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
6-516 |
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: 800.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 6 FRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWK 85
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 86 AFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEvvPYPGE 165
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE--MVPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGA 245
Cdd:cd07124 159 DNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHPRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAA 325
Cdd:cd07124 239 YLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSAC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 326 SRLILTQGAYEPVLERVLKRAERLSVGPAEEN-PDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEG--EGYFIAPT 402
Cdd:cd07124 319 SRVIVHESVYDEFLERLVERTKALKVGDPEDPeVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELaaEGYFVQPT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGV 482
Cdd:cd07124 399 IFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGR 478
|
490 500 510
....*....|....*....|....*....|....
2J40_B 483 QPFGGFKLSGTNAKTGALDYLRLFLEMKAVAERF 516
Cdd:cd07124 479 QPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
20-516 |
0e+00 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 780.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 20 RRAMREALRRVREEFGRHYPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRS 99
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 100 RLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEDNESFYVPLGAGVV 179
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 180 IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFT 259
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 260 GSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVL 339
Cdd:cd07083 241 GSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 340 ERVLKRAERLSVGPAEEN-PDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEI 418
Cdd:cd07083 321 ERLLKRAERLSVGPPEENgTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 419 FGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNAK 496
Cdd:cd07083 401 FGPVLSVIRYKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAK 480
|
490 500
....*....|....*....|
2J40_B 497 TGALDYLRLFLEMKAVAERF 516
Cdd:cd07083 481 TGGPHYLRRFLEMKAVAERF 500
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
6-516 |
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: 636.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 6 FRNEPIETFQTEEARRAMREALRRVREEFGRHYPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWK 85
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 86 AFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAvEVVPYPGE 165
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGK-PVNSREGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGA 245
Cdd:TIGR01237 160 TNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHPRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAA 325
Cdd:TIGR01237 240 YLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 326 SRLILTQGAYEPVLERVLKRAERLSVGPAEE-NPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAPTVF 404
Cdd:TIGR01237 320 SRAVVHEKVYDEVVERFVEITESLKVGPPDSaDVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 405 TEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQP 484
Cdd:TIGR01237 400 ADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQP 479
|
490 500 510
....*....|....*....|....*....|..
2J40_B 485 FGGFKLSGTNAKTGALDYLRLFLEMKAVAERF 516
Cdd:TIGR01237 480 FGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
36-516 |
2.55e-177 |
|
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: 507.36 E-value: 2.55e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 36 RHYPLYIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRK 113
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINP-ATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 114 RELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPyPGEDNESFYVPLGAGVVIAPWNFPVAIFTGM 193
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDA-PGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 194 IVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAG 273
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 274 RlapgqtWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG- 352
Cdd:COG1012 242 E------NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGd 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 353 PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE-GYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD 430
Cdd:COG1012 316 PLDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 431 FAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlVGVQPFGGFKLSGTNAKTGAlDYLRLFLEMK 510
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGR-EGLEEYTETK 473
|
....*.
2J40_B 511 AVAERF 516
Cdd:COG1012 474 TVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
87-512 |
3.84e-174 |
|
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: 498.59 E-value: 3.84e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVvpYPGED 166
Cdd:pfam00171 42 FPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS--DPGRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAY 246
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:pfam00171 200 LVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVF 404
Cdd:pfam00171 274 RLLVHESIYDEFVEKLVEAAKKLKVGdPLDPDTDMGPLISKAQLERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 405 TEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVqP 484
Cdd:pfam00171 354 ANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-P 432
|
410 420
....*....|....*....|....*...
2J40_B 485 FGGFKLSGTNAKTGAlDYLRLFLEMKAV 512
Cdd:pfam00171 433 FGGFKQSGFGREGGP-YGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
87-512 |
1.12e-163 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 470.92 E-value: 1.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPaVEVVPYPGED 166
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE-VIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAY 246
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHPRIRFINFTGSLEVGLKIYEAAGRlapgqtWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAE------NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE-GYFIAPTV 403
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGnPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGGkGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 404 FTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlVGVQ 483
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA-EPSA 402
|
410 420
....*....|....*....|....*....
2J40_B 484 PFGGFKLSGTNaKTGALDYLRLFLEMKAV 512
Cdd:cd07078 403 PFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-512 |
2.85e-137 |
|
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: 405.19 E-value: 2.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVD--TKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEA 118
Cdd:cd07131 2 YIGGEWVDsaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 119 TLVYEVGKNWVEASADVAEAIDFIEYYARAAlryRYPAVEVVP--YPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVG 196
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEG---RRLFGETVPseLPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 197 PVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLa 276
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 277 pgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAE 355
Cdd:cd07131 238 -----NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGdGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 356 ENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG----EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD 430
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGaTLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 431 FAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVqPFGGFKLSGTNAKTGALDYLRLFLEMK 510
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALDAFTEWK 471
|
..
2J40_B 511 AV 512
Cdd:cd07131 472 AV 473
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
38-512 |
7.69e-135 |
|
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: 398.93 E-value: 7.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 38 YPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELE 117
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 118 ATLVYEVGKNWVEASADVAEAIDFIEYYARAALR---YRYPAVEvvpyPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMI 194
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRlsgETLPSTR----PGVEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 195 VGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGR 274
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 275 LapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVGPA 354
Cdd:cd07097 237 R------GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 355 -EENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG--EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD 430
Cdd:cd07097 311 lDEGVDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 431 FAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVqPFGGFKLSGTNAKTGALDYLRLFLEMK 510
Cdd:cd07097 391 YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEAALEFYTTIK 469
|
..
2J40_B 511 AV 512
Cdd:cd07097 470 TV 471
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
14-514 |
8.07e-135 |
|
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: 400.42 E-value: 8.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 14 FQTEEARRAMREALRRVREEFGRHYPLYIGGEwVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDW 93
Cdd:cd07125 10 FDLEVPLEALADALKAFDEKEWEAIPIINGEE-TETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 94 PQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyRYPAVEVVPYPGEDNESFYVP 173
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARE-LFSDPELPGPTGELNGLELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 174 LGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRI 253
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 254 RFINFTGSLEVGLKIYEAagrLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQG 333
Cdd:cd07125 248 DGVIFTGSTETAKLINRA---LAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 334 AYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAPTVFTEVppKAR 412
Cdd:cd07125 325 IAERFIEMLKGAMASLKVGdPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 413 IAQEEIFGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSR-KREHLEWARReFHVGNLYFNRKITGALVGVQPFGGFK 489
Cdd:cd07125 403 DLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRdEREIEYWRER-VEAGNLYINRNITGAIVGRQPFGGWG 481
|
490 500
....*....|....*....|....*
2J40_B 490 LSGTNAKTGALDYLRLFLEMKAVAE 514
Cdd:cd07125 482 LSGTGPKAGGPNYLLRFGNEKTVSL 506
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
87-512 |
1.78e-122 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 363.47 E-value: 1.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVeVVPYPGED 166
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPEL-PSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAY 246
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAAEN------LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLkraerlsvgpaeenpdlgpvvsaeqerkvlsyieigknegqlvlggkrlegegyfiapTVFTE 406
Cdd:cd06534 240 RLLVHESIYDEFVEKLV----------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 407 VPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlVGVQPFG 486
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEAPFG 340
|
410 420
....*....|....*....|....*.
2J40_B 487 GFKLSGTNAKtGALDYLRLFLEMKAV 512
Cdd:cd06534 341 GVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
90-513 |
1.18e-115 |
|
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: 348.84 E-value: 1.18e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 90 WKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYpavEVVPY-PGEDNE 168
Cdd:cd07109 36 WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHG---ETIPLgPGYFVY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 169 SFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLV 248
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 249 EHPRIRFINFTGSLEVGLKIYEAAGRLAPGQTwfkrayVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRL 328
Cdd:cd07109 193 AHPGVDHISFTGSVETGIAVMRAAAENVVPVT------LELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 329 ILTQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG---EGYFIAPTVF 404
Cdd:cd07109 267 LVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARARARGaRIVAGGRIAEGapaGGYFVAPTLL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 405 TEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR--KREHleWARREFHVGNLYFNRkiTGALVGV 482
Cdd:cd07109 347 DDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRdgDRAL--RVARRLRAGQVFVNN--YGAGGGI 422
|
410 420 430
....*....|....*....|....*....|..
2J40_B 483 Q-PFGGFKLSGTNAKTGaLDYLRLFLEMKAVA 513
Cdd:cd07109 423 ElPFGGVKKSGHGREKG-LEALYNYTQTKTVA 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
41-492 |
5.37e-107 |
|
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: 327.60 E-value: 5.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVD-TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELeAT 119
Cdd:cd07086 2 VIGGEWVGsGGETFTSRNP-ANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEAL-GR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 120 LV-YEVGKNWVEASADVAEAIDFIEYyarAALRYRYPAVEVVP--YPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVG 196
Cdd:cd07086 80 LVsLEMGKILPEGLGEVQEMIDICDY---AVGLSRMLYGLTIPseRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 197 PVAVGNTVIAKPAEDAVVVGAKVFEIFHEA----GFPPGVVNFLPGVGEeVGAYLVEHPRIRFINFTGSLEVGLKIYEAA 272
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 273 GRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG 352
Cdd:cd07086 236 ARR------FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 353 -PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG--EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRV 428
Cdd:cd07086 310 dPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 429 KDFAEALEVANDTPYGLTGGVYSRK-REHLEWAR-REFHVGNLYFNRKITGALVGVqPFGGFKLSG 492
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDlREAFRWLGpKGSDCGIVNVNIPTSGAEIGG-AFGGEKETG 454
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
87-513 |
3.11e-106 |
|
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: 324.90 E-value: 3.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASA-DVAEAIDFIEYYARAALRYRYPAVEVVPypGE 165
Cdd:cd07093 32 FPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYILQLDGESYPQDG--GA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGA 245
Cdd:cd07093 110 LNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAA 325
Cdd:cd07093 190 ALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 326 SRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLE----GEGYFI 399
Cdd:cd07093 264 SRILVQRSIYDEFLERFVERAKALKVGdPLDPDTEVGPLISKEHLEKVLGYVELARAEGaTILTGGGRPElpdlEGGYFV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 400 APTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVG----NLYFNRKI 475
Cdd:cd07093 344 EPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGtvwvNCWLVRDL 423
|
410 420 430
....*....|....*....|....*....|....*...
2J40_B 476 TgalvgvQPFGGFKLSGTnAKTGALDYLRLFLEMKAVA 513
Cdd:cd07093 424 R------TPFGGVKASGI-GREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
37-512 |
1.92e-105 |
|
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: 323.39 E-value: 1.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 37 HYPLYIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKdW---PQEDRSRLLLKAAALMRR 111
Cdd:cd07091 3 PTGLFINNEFVDsvSGKTFPTINP-ATEEVICQVAEADEEDVDAAVKAARAAFETGW-WrkmDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 112 RKRELEATLVYEVGKN-WVEASADVAEAIDFIEYYARAALRyrypaVEVVPYPGEDNESFY---VPLGAGVVIAPWNFPV 187
Cdd:cd07091 81 DRDELAALESLDNGKPlEESAKGDVALSIKCLRYYAGWADK-----IQGKTIPIDGNFLAYtrrEPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 188 AIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLK 267
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 268 IYEAAgrlapGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAE 347
Cdd:cd07091 236 IMEAA-----AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 348 RLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSV 425
Cdd:cd07091 311 KRVVGdPFDPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 426 IRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkiTGALVGVQ-PFGGFKLSGTNAKTGaLDYLR 504
Cdd:cd07091 391 LKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFGRELG-EEGLE 466
|
....*...
2J40_B 505 LFLEMKAV 512
Cdd:cd07091 467 EYTQVKAV 474
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-492 |
2.25e-105 |
|
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: 321.79 E-value: 2.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEyyARAALRYRyPAVEVVP--YPG 164
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR--EAAGLPRR-PEGEILPsdVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 EDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVF-EIFHEAGFPPGVVNFLPGVGEEV 243
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGGGSEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:cd07104 170 GDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRlegEGYFIAP 401
Cdd:cd07104 244 AAGRILVHESVYDEFVEKLVAKAKALPVGdPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTGGTY---EGLFYQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 402 TVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREH-LEWARReFHVGNLYFNrKITGALV 480
Cdd:cd07104 321 TVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERaMAFAER-LETGMVHIN-DQTVNDE 398
|
410
....*....|..
2J40_B 481 GVQPFGGFKLSG 492
Cdd:cd07104 399 PHVPFGGVKASG 410
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
41-512 |
3.59e-103 |
|
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: 317.72 E-value: 3.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTwKDWPQ---EDRSRLLLKAAALMRRRKRE 115
Cdd:cd07119 1 YIDGEWVEaaSGKTRDIINP-ANGEVIATVPEGTAEDAKRAIAAARRAFDS-GEWPHlpaQERAALLFRIADKIREDAEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 116 LEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyryPAVEVVPYPgEDNESFYV--PLGAGVVIAPWNFPVAIFTGM 193
Cdd:cd07119 79 LARLETLNTGKTLRESEIDIDDVANCFRYYAGLATK---ETGEVYDVP-PHVISRTVrePVGVCGLITPWNYPLLQAAWK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 194 IVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAG 273
Cdd:cd07119 155 LAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 274 RLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVGP 353
Cdd:cd07119 235 GN------VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 354 AE-ENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG----EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIR 427
Cdd:cd07119 309 GLdADTEMGPLVSAEHREKVLSYIQLGKEEGaRLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVER 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 428 VKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVG-------NLYFNRkitgalvgvQPFGGFKLSGTNAKTGAL 500
Cdd:cd07119 389 FDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGtvwindyHPYFAE---------APWGGYKQSGIGRELGPT 459
|
490
....*....|..
2J40_B 501 DyLRLFLEMKAV 512
Cdd:cd07119 460 G-LEEYQETKHI 470
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-512 |
2.46e-102 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 330.24 E-value: 2.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 19 ARRAMREALRRVREEFGRHYPLyIGGewvdTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDR 98
Cdd:PRK11904 535 ELEPLAAAIAAFLEKQWQAGPI-ING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEER 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 99 SRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAAlRYRYPAVEVVPYP-GEDNESFYVPLGAG 177
Cdd:PRK11904 610 AAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQA-RRLFGAPEKLPGPtGESNELRLHGRGVF 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 178 VVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFIN 257
Cdd:PRK11904 689 VCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVA 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 258 FTGSLEVGLKIYEA-AGRlapgqtwfKRAYV----ETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQ 332
Cdd:PRK11904 769 FTGSTETARIINRTlAAR--------DGPIVpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQE 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 333 GAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEG--EGYFIAPTVFtEVPp 409
Cdd:PRK11904 841 DIADRVIEMLKGAMAELKVGdPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGteNGHFVAPTAF-EID- 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 410 kaRIAQ--EEIFGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPF 485
Cdd:PRK11904 919 --SISQleREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPF 996
|
490 500
....*....|....*....|....*..
2J40_B 486 GGFKLSGTNAKTGALDYLRLFLEMKAV 512
Cdd:PRK11904 997 GGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
87-513 |
3.66e-102 |
|
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: 314.37 E-value: 3.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYrYPAVEVVPYPGED 166
Cdd:cd07103 32 FKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRI-YGRTIPSPAPGKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAY 246
Cdd:cd07103 111 ILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHPRIRFINFTGSLEVGLKIYEAAgrlAPGqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:cd07103 191 LCASPRVRKISFTGSTAVGKLLMAQA---ADT---VKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCAN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVF 404
Cdd:cd07103 265 RIYVHESIYDEFVEKLVERVKKLKVGNGlDEGTDMGPLINERAVEKVEALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 405 TEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkiTGALVGVQ- 483
Cdd:cd07103 345 TDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGIN---TGLISDAEa 421
|
410 420 430
....*....|....*....|....*....|
2J40_B 484 PFGGFKLSGtNAKTGALDYLRLFLEMKAVA 513
Cdd:cd07103 422 PFGGVKESG-LGREGGKEGLEEYLETKYVS 450
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
8-516 |
1.11e-101 |
|
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: 315.30 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 8 NEPIETFQT-EEARRAMREALRRVREEFgRHYPLYIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKA 86
Cdd:cd07123 3 NEPVLSYAPgSPERAKLQEALAELKSLT-VEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKR-ELEATLVYEVGKNWVEASADVA-EAIDFIEYYARAALR-YRYPavEVVPYP 163
Cdd:cd07123 82 RKEWARMPFEDRAAIFLKAADLLSGKYRyELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEElYAQQ--PLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 164 GEDNESFYVPL-GAGVVIAPWNFpVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEE 242
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 243 VGAYLVEHPRIRFINFTGSLEVGLKIYE-AAGRLAPGQTwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK 321
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKqIGENLDRYRT-YPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 *SAASRLILTQGAYEPVLERVLKRAERLSVGPAEE--NPdLGPVVSAEQERKVLSYIEIGKN--EGQLVLGGKRLEGEGY 397
Cdd:cd07123 318 CSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDfsNF-MGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGKCDDSVGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 398 FIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD--FAEALEVANDT-PYGLTGGVYSRKREHLEWARREFH--VGNLYFN 472
Cdd:cd07123 397 FVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDsdFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYIN 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
2J40_B 473 RKITGALVGVQPFGGFKLSGTNAKTGALDYLRLFLEMKAVAERF 516
Cdd:cd07123 477 DKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
90-512 |
5.63e-101 |
|
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: 311.41 E-value: 5.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 90 WKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRypaVEVVPYPGEDNES 169
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIE---GAVIPVDKGDYLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 170 F--YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYL 247
Cdd:cd07114 114 FtrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 248 VEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASR 327
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE----GYFIAP 401
Cdd:cd07114 268 LLVQRSIYDEFVERLVARARAIRVGdPLDPETQMGPLATERQLEKVERYVARAREEGaRVLTGGERPSGAdlgaGYFFEP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 402 TVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKrehlewARREFHVGnlyfnRKITGALVG 481
Cdd:cd07114 348 TILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD------LARAHRVA-----RAIEAGTVW 416
|
410 420 430 440
....*....|....*....|....*....|....*....|
2J40_B 482 VQ---------PFGGFKLSGTNAKTGaLDYLRLFLEMKAV 512
Cdd:cd07114 417 VNtyralspssPFGGFKDSGIGRENG-IEAIREYTQTKSV 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
40-513 |
8.30e-101 |
|
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: 311.36 E-value: 8.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELE 117
Cdd:cd07138 1 FYIDGAWVApaGTETIDVINP-ATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 118 ATLVYEVGK-NWVEASADVAEAIDFIEYYARAALRY----RYPAVEVVpypgednesfYVPLGAGVVIAPWNFPVaiftG 192
Cdd:cd07138 80 QAITLEMGApITLARAAQVGLGIGHLRAAADALKDFefeeRRGNSLVV----------REPIGVCGLITPWNWPL----N 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 193 MIVGPV----AVGNTVIAKPAEDAVVvGAKVF-EIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLK 267
Cdd:cd07138 146 QIVLKVapalAAGCTVVLKPSEVAPL-SAIILaEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 268 IYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAE 347
Cdd:cd07138 225 VAEAAADT------VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 348 RLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGG----KRLEGeGYFIAPTVFTEVPPKARIAQEEIFGP 421
Cdd:cd07138 299 AYVVGdPRDPATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGpgrpEGLER-GYFVKPTVFADVTPDMTIAREEIFGP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 422 VLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRkitGALVGVQPFGGFKLSGtNAKTGALD 501
Cdd:cd07138 378 VLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING---AAFNPGAPFGGYKQSG-NGREWGRY 453
|
490
....*....|..
2J40_B 502 YLRLFLEMKAVA 513
Cdd:cd07138 454 GLEEFLEVKSIQ 465
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
17-513 |
1.39e-100 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 327.28 E-value: 1.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 17 EEARRAMREALRRVREEFGRHYPLyIGGEWVDTKERMVsLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQE 96
Cdd:COG4230 538 EAVLAALSAALAAAAEKQWQAAPL-IAGEAASGEARPV-RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVE 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 97 DRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYrypavevvpypgEDNESFYVPLGA 176
Cdd:COG4230 616 ERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRL------------FAAPTVLRGRGV 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 177 GVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFI 256
Cdd:COG4230 684 FVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGV 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 257 NFTGSLEVGLKIYEA-AGRLAPGqtwfkrayV----ETGGKDAIIVDETA-------DfdlaaegVVVSAYGFQGQK*SA 324
Cdd:COG4230 764 AFTGSTETARLINRTlAARDGPI--------VpliaETGGQNAMIVDSSAlpeqvvdD-------VLASAFDSAGQRCSA 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 AsRLILTQgayEPVLERVLKR----AERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEG--EGY 397
Cdd:COG4230 829 L-RVLCVQ---EDIADRVLEMlkgaMAELRVGdPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcaNGT 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 398 FIAPTVFtEVPpkaRIAQ--EEIFGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNR 473
Cdd:COG4230 905 FVAPTLI-EID---SISDleREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR 980
|
490 500 510 520
....*....|....*....|....*....|....*....|
2J40_B 474 KITGALVGVQPFGGFKLSGTNAKTGALDYLRLFLEMKAVA 513
Cdd:COG4230 981 NIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVT 1020
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
87-493 |
5.15e-99 |
|
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: 306.06 E-value: 5.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyryPAVEVVP---YP 163
Cdd:cd07149 34 AKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKR---LAGETIPfdaSP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 164 G-EDNESFY--VPLGAGVVIAPWNFP---VAiftgMIVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFL 236
Cdd:cd07149 111 GgEGRIGFTirEPIGVVAAITPFNFPlnlVA----HKVGPaIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 237 PGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYG 316
Cdd:cd07149 187 TGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 317 FQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRleg 394
Cdd:cd07149 259 NAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGdPLDEDTDVGPMISEAEAERIEEWVEEAVEGGaRLLTGGKR--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 395 EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrK 474
Cdd:cd07149 336 DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIN-D 414
|
410
....*....|....*....
2J40_B 475 ITGALVGVQPFGGFKLSGT 493
Cdd:cd07149 415 SSTFRVDHMPYGGVKESGT 433
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
87-513 |
5.33e-98 |
|
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: 303.78 E-value: 5.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWkDW--PQEDRSRLLLKAAALMRRRKRELEATLVYEVGK-NWVEASADVAEAIDFIEYYARAALRYRYP-AVEVVPY 162
Cdd:cd07089 32 FDTG-DWstDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQVDGPIGHLRYFADLADSFPWEfDLPVPAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 163 PGEDNESFYVPLGAGVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVG 240
Cdd:cd07089 111 RGGPGRRVVRREPVGVVaaITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 241 EEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQ 320
Cdd:cd07089 191 NAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 321 K*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG--EG 396
Cdd:cd07089 265 GCALTTRLLVPRSRYDEVVEALAAAFEALPVGdPADPGTVMGPLISAAQRDRVEGYIARGRDEGaRLVTGGGRPAGldKG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 397 YFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREH-LEWARReFHVGNLYFNrki 475
Cdd:cd07089 345 FYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRaYRVARR-IRTGSVGIN--- 420
|
410 420 430
....*....|....*....|....*....|....*....
2J40_B 476 TGALVGVQ-PFGGFKLSGTNAKTGaLDYLRLFLEMKAVA 513
Cdd:cd07089 421 GGGGYGPDaPFGGYKQSGLGRENG-IEGLEEFLETKSIA 458
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
87-512 |
1.61e-97 |
|
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: 302.44 E-value: 1.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEA-SADVAEAIDFIEYYARAALRYrypAVEVVPY-PG 164
Cdd:cd07115 32 FEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTFRYYAGWADKI---EGEVIPVrGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 EDNESFYVPLGAGVVIAPWNFPVaIFTGMIVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEV 243
Cdd:cd07115 109 FLNYTVREPVGVVGAIVPWNFPL-MFAAWKVAPaLAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHPRIRFINFTGSLEVGLKIYEAAgrlapgQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:cd07115 188 GAALVEHPDVDKITFTGSTAVGRKIMQGA------AGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAP 401
Cdd:cd07115 262 AGSRLLVHESIYDEFLERFTSLARSLRPGdPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGaRLLTGGKRPGARGFFVEP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 402 TVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR--KREHLEWARreFHVGNLYFNrkITGAL 479
Cdd:cd07115 342 TIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRdlGRAHRVAAA--LKAGTVWIN--TYNRF 417
|
410 420 430
....*....|....*....|....*....|...
2J40_B 480 VGVQPFGGFKLSGTNAKTGAlDYLRLFLEMKAV 512
Cdd:cd07115 418 DPGSPFGGYKQSGFGREMGR-EALDEYTEVKSV 449
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
7-516 |
4.80e-97 |
|
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: 303.63 E-value: 4.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 7 RNEPIETF-QTEEARRAMREALRRVREEFgRHYPLYIGGEWV-DTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAW 84
Cdd:TIGR01236 1 ANEPVLPFrPGSPERDLLRKSLKELKSSS-LEIPLVIGGEEVyDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 85 KAFKTWKDWPQEDRSRLLLKAAALM--RRRKRELEATLVYEvGKNWVEASAD-VAEAIDFIEYYARAAlRYRYpAVEVVP 161
Cdd:TIGR01236 80 DAKKDWSNLPFYDRAAIFLKAADLLsgPYRYEILAATMLGQ-SKTVYQAEIDaVAELIDFFRFNVKYA-RELY-AQQPIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 162 YPGEDNESFYVPLGAGV-VIAPWNFpVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVG 240
Cdd:TIGR01236 157 APGEWNRTEYRPLEGFVyAISPFNF-TAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 241 EEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQ 320
Cdd:TIGR01236 236 VQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 321 K*SAASRLILTQGAYEPVLERVLKRAERLSVGPAEE-NPDLGPVVSAEQERKVLSYIEIGK---NEGQLVLGGKRLEGEG 396
Cdd:TIGR01236 316 KCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDfRGFMGAVIDEQSFDKIVKYIEDAKkdpEALTILYGGKYDDSQG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 397 YFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD--FAEALEVA-NDTPYGLTGGVYSRKREHLEWA--RREFHVGNLYF 471
Cdd:TIGR01236 396 YFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVdSTSQYGLTGAVFAKDRKAILEAdkKLRFAAGNFYI 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
2J40_B 472 NRKITGALVGVQPFGGFKLSGTNAKTGALDYLRLFLEMKAVAERF 516
Cdd:TIGR01236 476 NDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETF 520
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-504 |
5.73e-97 |
|
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: 301.49 E-value: 5.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEA 118
Cdd:cd07088 1 YINGEFVPssSGETIDVLNP-ATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 119 TLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYpavEVVP--YPGEDNESFYVPLGAGVVIAPWNFPVAIFtGMIVG 196
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEG---EIIPsdRPNENIFIFKVPIGVVAGILPWNFPFFLI-ARKLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 197 PVAV-GNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAgrl 275
Cdd:cd07088 156 PALVtGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAA--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 276 apgQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PA 354
Cdd:cd07088 233 ---AENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGdPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 355 EENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE-GYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFA 432
Cdd:cd07088 310 DAATDMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLD 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 433 EALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlvgVQPF-GGFKLSGT---NAKTGALDYLR 504
Cdd:cd07088 390 EAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEA---MQGFhAGWKKSGLggaDGKHGLEEYLQ 462
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
87-514 |
8.72e-96 |
|
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: 298.11 E-value: 8.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGED 166
Cdd:cd07110 32 FPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLDAKAERAVPLPSED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NES--FYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVG 244
Cdd:cd07110 112 FKArvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGRLApgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07110 192 APLAAHPGIDKISFTGSTATGSQVMQAAAQDI------KPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLE--GEGYFIA 400
Cdd:cd07110 266 TSRLLVHESIADAFLERLATAAEAIRVGdPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGaRLLCGGRRPAhlEKGYFIA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkiTGALV 480
Cdd:cd07110 346 PTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN---CSQPC 422
|
410 420 430
....*....|....*....|....*....|....*
2J40_B 481 GVQ-PFGGFKLSGTNAKTGALDyLRLFLEMKAVAE 514
Cdd:cd07110 423 FPQaPWGGYKRSGIGRELGEWG-LDNYLEVKQITR 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
40-512 |
8.75e-96 |
|
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: 298.33 E-value: 8.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVDTK-ERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAF--KTWKDWPQEDRSRLLLKAAALMRRRKREL 116
Cdd:cd07139 1 LFIGGRWVAPSgSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 117 EATLVYEVGK-NWVEASADVAEAIDFIEYYARAALRYryPAVEVVPYP-GEDNESFYVPLGAGVVIAPWNFPVAIFTGMI 194
Cdd:cd07139 81 ARLWTAENGMpISWSRRAQGPGPAALLRYYAALARDF--PFEERRPGSgGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 195 VGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGR 274
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 275 LapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-P 353
Cdd:cd07139 238 R------LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGdP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 354 AEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEG--EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD 430
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 431 FAEALEVANDTPYGLTGGVYSRKREH-LEWARReFHVGNLYFNrkitGALVGVQ-PFGGFKLSGTnAKTGALDYLRLFLE 508
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVERgLAVARR-IRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDAYLE 465
|
....
2J40_B 509 MKAV 512
Cdd:cd07139 466 TKSI 469
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
87-492 |
9.27e-96 |
|
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: 297.70 E-value: 9.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEyyaRAALRYRYPAVEVVP--YPG 164
Cdd:cd07150 34 FPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLR---AAAGECRRVRGETLPsdSPG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 EDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVG 244
Cdd:cd07150 111 TVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07150 191 DELVDDPRVRMVTFTGSTAVGREIAEKAGRH------LKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRleGEGYFIAPTV 403
Cdd:cd07150 265 ASRIIVEEPVYDEFVKKFVARASKLKVGdPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGK--YDGNFYQPTV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 404 FTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKrEHLEWARRE------FHVGNLYFNRKITG 477
Cdd:cd07150 343 LTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND-LQRAFKLAErlesgmVHINDPTILDEAHV 421
|
410
....*....|....*
2J40_B 478 alvgvqPFGGFKLSG 492
Cdd:cd07150 422 ------PFGGVKASG 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-508 |
2.66e-95 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 313.73 E-value: 2.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 17 EEARRAMREALRRVREEFGRHYPLyIGGEWVDTKERMVsLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQE 96
Cdd:PRK11905 535 EATLAALDEALNAFAAKTWHAAPL-LAGGDVDGGTRPV-LNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 97 DRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyrypavevvpypgEDNESFYVPLGA 176
Cdd:PRK11905 613 ERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARR-------------LLNGPGHKPLGP 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 177 GVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFI 256
Cdd:PRK11905 680 VVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGV 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 257 NFTGSLEVGLKIYEA-AGRLAPGqtwfkrayV----ETGGKDAIIVDETAdfdlAAEGVV--VSAYGFQ--GQK*SAASR 327
Cdd:PRK11905 760 MFTGSTEVARLIQRTlAKRSGPP--------VpliaETGGQNAMIVDSSA----LPEQVVadVIASAFDsaGQRCSALRV 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLErVLKRA-ERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVlggKRLE-----GEGYFIA 400
Cdd:PRK11905 828 LCLQEDVADRVLT-MLKGAmDELRIGdPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV---HQLPlpaetEKGTFVA 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFtEVpPKARIAQEEIFGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGA 478
Cdd:PRK11905 904 PTLI-EI-DSISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGA 981
|
490 500 510
....*....|....*....|....*....|
2J40_B 479 LVGVQPFGGFKLSGTNAKTGALDYLRLFLE 508
Cdd:PRK11905 982 VVGVQPFGGEGLSGTGPKAGGPLYLGRLVR 1011
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
42-510 |
3.13e-95 |
|
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: 297.98 E-value: 3.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 42 IGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLV 121
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 122 YEVGKNWVEASADVAEAIDFIEYYARaalryrypavEVVPYPGEDNESfyvPLGAGVVIAPWNFPVAIFTGMIVGPVAVG 201
Cdd:TIGR01238 122 REAGKTIHNAIAEVREAVDFCRYYAK----------QVRDVLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 202 NTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEA-AGRLAPGQT 280
Cdd:TIGR01238 189 NTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTlAQREDAPVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 281 WFkrayVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPD 359
Cdd:TIGR01238 269 LI----AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGvPHLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 360 LGPVVSAEQERKVLSYIE----IGKNEGQLVLGGKRLEGEGYFIAPTVFtEVPPKARIaQEEIFGPVLSVIRVK--DFAE 433
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEhmsqTQKKIAQLTLDDSRACQHGTFVAPTLF-ELDDIAEL-SEEVFGPVLHVVRYKarELDQ 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2J40_B 434 ALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNAKTGALDYLRLFLEMK 510
Cdd:TIGR01238 423 IVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
89-512 |
5.18e-95 |
|
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: 296.05 E-value: 5.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 89 TWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASA-DVAEAIDFIEYYARAaLRYRYPavEVVPyPGEDN 167
Cdd:cd07112 41 VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANTFRWYAEA-IDKVYG--EVAP-TGPDA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 168 ESFYVPLGAGVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGA 245
Cdd:cd07112 117 LALITREPLGVVgaVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgQTWFKRAYVETGGKDAIIV-DETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07112 197 ALGLHMDVDALAFTGSTEVGRRFLEYSG-----QSNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRL--EGEGYFIA 400
Cdd:cd07112 272 GSRLLVHESIKDEFLEKVVAAAREWKPGdPLDPATRMGALVSEAHFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVG----NLYFNRKIT 476
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGtvwvNCFDEGDIT 431
|
410 420 430
....*....|....*....|....*....|....*.
2J40_B 477 galvgvQPFGGFKLSGtNAKTGALDYLRLFLEMKAV 512
Cdd:cd07112 432 ------TPFGGFKQSG-NGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
39-491 |
4.23e-93 |
|
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: 291.73 E-value: 4.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 39 PLYIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKREL 116
Cdd:cd07085 2 KLFINGEWVEskTTEWLDVYNP-ATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 117 EATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPyPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVG 196
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVA-RGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 197 PVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAyLVEHPRIRFINFTGSLEVGLKIYEAAGRLa 276
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAAAN- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 277 pgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVGPA-E 355
Cdd:cd07085 238 -----GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGdD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 356 ENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGK--RLEG--EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKD 430
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRgvKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2J40_B 431 FAEALEVANDTPYG------LTGGVYSRKrehlewARREFHVGNLYFNRKITgALVGVQPFGGFKLS 491
Cdd:cd07085 393 LDEAIAIINANPYGngaaifTRSGAAARK------FQREVDAGMVGINVPIP-VPLAFFSFGGWKGS 452
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
87-512 |
4.77e-93 |
|
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: 290.74 E-value: 4.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYrypAVEVVPYPged 166
Cdd:cd07090 32 QKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTL---SGEHVPLP--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESF-Y---VPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEe 242
Cdd:cd07090 106 GGSFaYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGE- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 243 VGAYLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgqTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK* 322
Cdd:cd07090 185 TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 323 SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGE----- 395
Cdd:cd07090 259 SNGTRVFVQRSIKDEFTERLVERTKKIRIGdPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLcGGERVVPEdglen 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 396 GYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR--KREHLEWArrEFHVGNLYFNR 473
Cdd:cd07090 339 GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRdlQRAHRVIA--QLQAGTCWINT 416
|
410 420 430 440
....*....|....*....|....*....|....*....|
2J40_B 474 -KITGALVgvqPFGGFKLSGTNAKTGaLDYLRLFLEMKAV 512
Cdd:cd07090 417 yNISPVEV---PFGGYKQSGFGRENG-TAALEHYTQLKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-492 |
3.05e-91 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 287.16 E-value: 3.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 38 YPLYIGGEWVD--TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRE 115
Cdd:PRK13252 7 QSLYIDGAYVEatSGETFEVINP-ATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 116 LEATLVYEVGKNWVEAS-ADVAEAIDFIEYYARAAlryryPAVE--VVPYPGEDnesFY----VPLGAGVVIAPWNFPVA 188
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYAGLA-----PALEgeQIPLRGGS---FVytrrEPLGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 189 IFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEeVGAYLVEHPRIRFINFTGSLEVGLKI 268
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 269 Y-EAAGRLapgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAE 347
Cdd:PRK13252 237 MaAAAASL-------KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 348 RLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLE----GEGYFIAPTVFTEVPPKARIAQEEIFGP 421
Cdd:PRK13252 310 RIRIGdPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGP 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2J40_B 422 VLSVIRVKDFAEALEVANDTPYGLTGGVYSR--KREHLEWARREfhVGNLYFNrkiTGALVGVQ-PFGGFKLSG 492
Cdd:PRK13252 390 VMSVLTFDDEDEVIARANDTEYGLAAGVFTAdlSRAHRVIHQLE--AGICWIN---TWGESPAEmPVGGYKQSG 458
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
87-492 |
3.98e-90 |
|
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: 282.88 E-value: 3.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALryrypAVEVVpypgED 166
Cdd:cd07106 32 FPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLDL-----PDEVI----ED 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESF-----YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGvGE 241
Cdd:cd07106 103 DDTRrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 242 EVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK 321
Cdd:cd07106 181 ELGPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 *SAASRLILTQGAYEPVLERVLKRAERLSVGP-AEENPDLGPVVSAEQERKVLSYIE-IGKNEGQLVLGGKRLEGEGYFI 399
Cdd:cd07106 255 CAAIKRLYVHESIYDEFCEALVALAKAAVVGDgLDPGTTLGPVQNKMQYDKVKELVEdAKAKGAKVLAGGEPLDGPGYFI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 400 APTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKitGAL 479
Cdd:cd07106 335 PPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTH--GAL 412
|
410
....*....|...
2J40_B 480 VGVQPFGGFKLSG 492
Cdd:cd07106 413 DPDAPFGGHKQSG 425
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
87-492 |
7.28e-90 |
|
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: 282.71 E-value: 7.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNW-VEASADVAEAIDFIEYYARAALRYRYpavEVVPyPGE 165
Cdd:cd07108 32 FPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLAGELKG---ETLP-FGP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYV--PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEV 243
Cdd:cd07108 108 DVLTYTVrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEEC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHPRIRFINFTGSLEVGLKIYE-AAGRLAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSA-YGFQGQK 321
Cdd:cd07108 187 GAALVDHPDVDKVTFTGSTEVGKIIYRaAADRLIP-------VSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 *SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKN--EGQLVLGGK-RLEG--- 394
Cdd:cd07108 260 CTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGdPLDEATDIGAIISEKQFAKVCGYIDLGLStsGATVLRGGPlPGEGpla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 395 EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRK-REHLEWARReFHVGNLYFNR 473
Cdd:cd07108 340 DGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDlGRALRAAHA-LEAGWVQVNQ 418
|
410
....*....|....*....
2J40_B 474 KItGALVGvQPFGGFKLSG 492
Cdd:cd07108 419 GG-GQQPG-QSYGGFKQSG 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
87-493 |
2.12e-88 |
|
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: 278.85 E-value: 2.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAA--LRYRYPAVEVVPYpg 164
Cdd:cd07145 34 KDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAkvLRGETIPVDAYEY-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 edNESFYV-----PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGV 239
Cdd:cd07145 112 --NERRIAftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 240 GEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQG 319
Cdd:cd07145 190 GSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 320 QK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLegEGY 397
Cdd:cd07145 264 QVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGdPLDESTDLGPLISPEAVERMENLVNDAVEKGgKILYGGKRD--EGS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 398 FIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRK-REHLEWArREFHVGNLYFN---R 473
Cdd:cd07145 342 FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDiNRALKVA-RELEAGGVVINdstR 420
|
410 420
....*....|....*....|
2J40_B 474 KITGALvgvqPFGGFKLSGT 493
Cdd:cd07145 421 FRWDNL----PFGGFKKSGI 436
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
40-512 |
2.38e-88 |
|
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: 279.68 E-value: 2.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVDT--KERMVSLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFKTWK-DWPQEDRSRLLLKAAALMRRRKREL 116
Cdd:cd07144 10 LFINNEFVKSsdGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 117 EATLVYEVGKNW-VEASADVAEAIDFIEYYARAALRyrypaVEVVPYPGEDNESFY---VPLGAGVVIAPWNFPVAIFTG 192
Cdd:cd07144 89 AAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADK-----IQGKTIPTSPNKLAYtlhEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 193 MIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAA 272
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 273 GrlapgqTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRA-ERLSV 351
Cdd:cd07144 244 A------QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 352 G-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGG---KRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVI 426
Cdd:cd07144 318 GsPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 427 RVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlVGVqPFGGFKLSGTNAKTGALDyLRLF 506
Cdd:cd07144 398 KFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELGEYG-LETY 474
|
....*.
2J40_B 507 LEMKAV 512
Cdd:cd07144 475 TQTKAV 480
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
42-505 |
7.32e-88 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 294.19 E-value: 7.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 42 IGGEWVDTKERMVsLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLV 121
Cdd:PRK11809 651 LEDPVAAGEMSPV-INPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 122 YEVGKNWVEASADVAEAIDFIEYYArAALRyrypavevvpyPGEDNESfYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVG 201
Cdd:PRK11809 730 REAGKTFSNAIAEVREAVDFLRYYA-GQVR-----------DDFDNDT-HRPLGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 202 NTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEA-AGRLAP-GQ 279
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNlAGRLDPqGR 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 280 TWFKRAyvETGGKDAIIVDETAdfdlAAEGVVV----SAYGFQGQK*SAAsRLILTQgayEPVLERVLK----------- 344
Cdd:PRK11809 877 PIPLIA--ETGGQNAMIVDSSA----LTEQVVAdvlaSAFDSAGQRCSAL-RVLCLQ---DDVADRTLKmlrgamaecrm 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 345 -RAERLSVgpaeenpDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGE----GYFIAPTV-----FTEVppkaria 414
Cdd:PRK11809 947 gNPDRLST-------DIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEdwqsGTFVPPTLieldsFDEL------- 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 415 QEEIFGPVLSVIRVK--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSG 492
Cdd:PRK11809 1013 KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSG 1092
|
490
....*....|....
2J40_B 493 TNAKTGALDYL-RL 505
Cdd:PRK11809 1093 TGPKAGGPLYLyRL 1106
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
36-512 |
1.21e-87 |
|
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: 277.69 E-value: 1.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 36 RHYPLYIGGEWVDTKERMV--SLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQED---RSRLLLKAAALMR 110
Cdd:cd07141 5 KYTKIFINNEWHDSVSGKTfpTINP-ATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDaseRGRLLNKLADLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 111 RRKRELEATLVYEVGKNWVEAS-ADVAEAIDFIEYYARAALRYRYpavEVVPYPGEdnesFYV-----PLGAGVVIAPWN 184
Cdd:cd07141 84 RDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHG---KTIPMDGD----FFTytrhePVGVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 185 FPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEV 264
Cdd:cd07141 157 FPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 265 GLKIYEAAGRlapgqTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLK 344
Cdd:cd07141 237 GKLIQQAAGK-----SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 345 RAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPV 422
Cdd:cd07141 312 RAKKRVVGnPFDPKTEQGPQIDEEQFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 423 LSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkiTGALVGVQ-PFGGFKLSGTNAKTGAlD 501
Cdd:cd07141 392 QQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELGE-Y 467
|
490
....*....|.
2J40_B 502 YLRLFLEMKAV 512
Cdd:cd07141 468 GLQEYTEVKTV 478
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
88-492 |
2.78e-87 |
|
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: 276.11 E-value: 2.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyryPAVEVVPY--PGE 165
Cdd:cd07151 46 KEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLR---MEGRILPSdvPGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVF-EIFHEAGFPPGVVNFLPGVGEEVG 244
Cdd:cd07151 123 ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07151 203 DAFVEHPVPRLISFTGSTPVGRHIGELAGRH------LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRlegEGYFIAPT 402
Cdd:cd07151 277 INRIIVHEDVYDEFVEKFVERVKALPYGdPSDPDTVVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEA---EGNVLEPT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREH-LEWARR----EFHVGNLYFNRKitg 477
Cdd:cd07151 354 VLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERgVQFARRidagMTHINDQPVNDE--- 430
|
410
....*....|....*
2J40_B 478 ALVgvqPFGGFKLSG 492
Cdd:cd07151 431 PHV---PFGGEKNSG 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
93-512 |
3.12e-87 |
|
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: 275.76 E-value: 3.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 93 WPQ---EDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVpypGEDNES 169
Cdd:cd07118 37 WPRmsgAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNL---GDDMLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 170 FYVPLGAGVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYL 247
Cdd:cd07118 114 LVLREPIGVVgiITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 248 VEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASR 327
Cdd:cd07118 194 TEHPDVDMVSFTGSTRVGKAIAAAAARN------LKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLE-GEGYFIAPTVF 404
Cdd:cd07118 268 LLVHESIADAFVAAVVARSRKVRVGdPLDPETKVGAIINEAQLAKITDYVDAGRAEGaTLLLGGERLAsAAGLFYQPTIF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 405 TEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGalvGVQ- 483
Cdd:cd07118 348 TDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDG---SPEl 424
|
410 420
....*....|....*....|....*....
2J40_B 484 PFGGFKLSGTNAKTGaLDYLRLFLEMKAV 512
Cdd:cd07118 425 PFGGFKQSGIGRELG-RYGVEEYTELKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
37-492 |
9.37e-87 |
|
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: 275.22 E-value: 9.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 37 HYPLYIGGEWVDTKERMVS-LNPSAPsEVVGTTAKAGKAEAEAALEAAWKAFK-TWKDWPQEDRSRLLLKAAALMRRRKR 114
Cdd:cd07082 1 QFKYLINGEWKESSGKTIEvYSPIDG-EVIGSVPALSALEILEAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 115 ELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEDN-ESFY--VPLGAGVVIAPWNFPVAI-F 190
Cdd:cd07082 80 EVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVrrEPLGVVLAIGPFNYPLNLtV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 191 TGMIVGPVAvGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYE 270
Cdd:cd07082 160 SKLIPALIM-GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 271 AAGRlapgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLS 350
Cdd:cd07082 239 QHPM--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 351 VG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEgyFIAPTVFTEVPPKARIAQEEIFGPVLSVIRV 428
Cdd:cd07082 311 VGmPWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
2J40_B 429 KDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKiTGALVGVQPFGGFKLSG 492
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK-CQRGPDHFPFLGRKDSG 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
38-492 |
1.17e-86 |
|
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: 274.99 E-value: 1.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 38 YPLYIGGEWVD-TKERMV-SLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRE 115
Cdd:cd07559 1 YDNFINGEWVApSKGEYFdNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 116 LEATLVYEVGKNWVEA-SADVAEAIDFIEYYArAALRYRYPAVEVVpypgeDNES----FYVPLGagVV--IAPWNFPVA 188
Cdd:cd07559 80 LAVAETLDNGKPIRETlAADIPLAIDHFRYFA-GVIRAQEGSLSEI-----DEDTlsyhFHEPLG--VVgqIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 189 IFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKI 268
Cdd:cd07559 152 MAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 269 YEAAG-RLAPgqtwfkrAYVETGGKDAIIV-----DETADFDLAAEGVVVsayGF---QGQK*SAASRLILTQGAYEPVL 339
Cdd:cd07559 231 MQYAAeNLIP-------VTLELGGKSPNIFfddamDADDDFDDKAEEGQL---GFafnQGEVCTCPSRALVQESIYDEFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 340 ERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE----GYFIAPTVFTEVPPKARI 413
Cdd:cd07559 301 ERAVERFEAIKVGnPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 414 AQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLY---FNRKITGAlvgvqPFGGFKL 490
Cdd:cd07559 381 FQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWvncYHQYPAHA-----PFGGYKK 455
|
..
2J40_B 491 SG 492
Cdd:cd07559 456 SG 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
87-512 |
2.25e-86 |
|
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: 273.48 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYpavEVVPYPGED 166
Cdd:cd07107 32 FPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKG---ETIPVGGRN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 -NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGA 245
Cdd:cd07107 109 lHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSA-YGFQGQK*SA 324
Cdd:cd07107 188 ALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE----GYF 398
Cdd:cd07107 262 TSRLFVHESIYDEVLARVVERVAAIKVGdPTDPATTMGPLVSRQQYDRVMHYIDSAKREGaRLVTGGGRPEGPalegGFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 399 IAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR--KREHLewARREFHVGNLYFNRKIT 476
Cdd:cd07107 342 VEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNdiSQAHR--TARRVEAGYVWINGSSR 419
|
410 420 430
....*....|....*....|....*....|....*.
2J40_B 477 GALvGVqPFGGFKLSGTNAKTGaLDYLRLFLEMKAV 512
Cdd:cd07107 420 HFL-GA-PFGGVKNSGIGREEC-LEELLSYTQEKNV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-512 |
1.72e-84 |
|
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: 269.40 E-value: 1.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVDT--KERMVSLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFKTwkDWPQE----DRSRLLLKAAALMRRRK 113
Cdd:cd07143 9 LFINGEFVDSvhGGTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFET--DWGLKvsgsKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 114 RELEATLVYEVGKNWVE-ASADVAEAIDFIEYYARAALRYRYPAVEVvpypgeDNESF----YVPLGAGVVIAPWNFPVA 188
Cdd:cd07143 86 DYLASIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQVIET------DIKKLtytrHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 189 IFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKI 268
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 269 YEAAGRlapgqTWFKRAYVETGGKDAIIVDETADFDlaaEGVVVSAYGF---QGQK*SAASRLILTQGAYEPVLERVLKR 345
Cdd:cd07143 240 MEAAAK-----SNLKKVTLELGGKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFKEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 346 AERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVL 423
Cdd:cd07143 312 AKKLKVGdPFAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 424 SVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkiTGALVGVQ-PFGGFKLSGTNAKTGALDy 502
Cdd:cd07143 392 AVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN---CYNLLHHQvPFGGYKQSGIGRELGEYA- 467
|
490
....*....|
2J40_B 503 LRLFLEMKAV 512
Cdd:cd07143 468 LENYTQIKAV 477
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-492 |
1.88e-84 |
|
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: 267.99 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEvvpyPGED 166
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGERAT----PMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESF--YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEVG 244
Cdd:cd07095 89 GRAVlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEA-AGRlaPGqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:cd07095 168 EALAAHEGIDGLLFTGSAATGLLLHRQfAGR--PG----KILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAY-EPVLERVLKRAERLSVGP--AEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIA 400
Cdd:cd07095 242 CARRLIVPDGAVgDAFLERLVEAAKRLRIGApdAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFtEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlV 480
Cdd:cd07095 322 PGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-S 399
|
410
....*....|..
2J40_B 481 GVQPFGGFKLSG 492
Cdd:cd07095 400 STAPFGGVGLSG 411
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
87-492 |
4.94e-84 |
|
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: 266.63 E-value: 4.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYrypaVEVVPYPGED 166
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAF----LADEPIETDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESF--YVPLGAGVVIAPWNFP---VAIFtgmiVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPgVG 240
Cdd:cd07100 88 GKAYvrYEPLGVVLGIMPWNFPfwqVFRF----AAPnLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL-ID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 241 EEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQ 320
Cdd:cd07100 163 SDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKN------LKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 321 K*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYF 398
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGdPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGKRPDGPGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 399 IAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRkITGA 478
Cdd:cd07100 317 YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING-MVKS 395
|
410
....*....|....
2J40_B 479 LVGVqPFGGFKLSG 492
Cdd:cd07100 396 DPRL-PFGGVKRSG 408
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
40-492 |
7.41e-84 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 268.52 E-value: 7.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVD--TKERMVSLNPSAPSEV----VGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRK 113
Cdd:PLN02467 10 LFIGGEWREpvLGKRIPVVNPATEETIgdipAATAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 114 RELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEDNESFYV--PLGAGVVIAPWNFPVAIFT 191
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVLkePLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 192 GMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEA 271
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 272 AGRLApgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSV 351
Cdd:PLN02467 250 AAQMV------KPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 352 G-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEG--EGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIR 427
Cdd:PLN02467 324 SdPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILcGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
2J40_B 428 VKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkITGALVGVQPFGGFKLSG 492
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
36-512 |
2.11e-83 |
|
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: 266.67 E-value: 2.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 36 RHYPLYIGGEWVDTK--ERMVSLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFK--TWKDWPQEDRSRLLLKAAALMRR 111
Cdd:cd07142 2 KHTKLFINGQFVDAAsgKTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 112 RKRELEATLVYEVGKNWVEAS-ADVAEAIDFIEYYARAALRyrypaVEVVPYPGEDNESFYV---PLGAGVVIAPWNFPV 187
Cdd:cd07142 81 HADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADK-----IHGMTLPADGPHHVYTlhePIGVVGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 188 AIFTgMIVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGL 266
Cdd:cd07142 156 LMFA-WKVGPaLACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 267 KIYEAAGrlapgQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRA 346
Cdd:cd07142 235 IIMQLAA-----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 347 ERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLS 424
Cdd:cd07142 310 LKRVVGdPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 425 VIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrkITGALVGVQPFGGFKLSGTNAKTGAlDYLR 504
Cdd:cd07142 390 ILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGI-YALN 466
|
....*...
2J40_B 505 LFLEMKAV 512
Cdd:cd07142 467 NYLQVKAV 474
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
42-512 |
5.46e-82 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 263.47 E-value: 5.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 42 IGGEWVDTK--ERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEAT 119
Cdd:PLN02278 29 IGGKWTDAYdgKTFPVYNP-ATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 120 LVYEVGKNWVEASADVAEAIDFIEYYARAALRyryPAVEVVPYPGEDNESFYVPLGAGVV--IAPWNFPVAIFTGMiVGP 197
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKR---VYGDIIPSPFPDRRLLVLKQPVGVVgaITPWNFPLAMITRK-VGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 198 -VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLA 276
Cdd:PLN02278 184 aLAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 277 pgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVGP-AE 355
Cdd:PLN02278 264 ------KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDgFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 356 ENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEA 434
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 435 LEVANDTPYGLTGGVYSRKREHLeWarrefhvgnlYFNRKITGALVGVQ---------PFGGFKLSGT---NAKTGALDY 502
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRA-W----------RVSEALEYGIVGVNeglistevaPFGGVKQSGLgreGSKYGIDEY 486
|
490
....*....|
2J40_B 503 lrlfLEMKAV 512
Cdd:PLN02278 487 ----LEIKYV 492
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
88-498 |
1.41e-81 |
|
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: 260.69 E-value: 1.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIdfIEYYARAALRYRyPAVEVVPY-PGED 166
Cdd:cd07152 27 RAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAI--GELHEAAGLPTQ-PQGEILPSaPGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVaIFTGMIVGP-VAVGNTVIAKPAEDAVVVGAKVF-EIFHEAGFPPGVVNFLPGvGEEVG 244
Cdd:cd07152 104 SLARRVPLGVVGVISPFNFPL-ILAMRSVAPaLALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPAGVLHVLPG-GADAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07152 182 EALVEDPNVAMISFTGSTAVGRKVGEAAGRH------LKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRlegEGYFIAPT 402
Cdd:cd07152 256 AGRHLVHESVADAYTAKLAAKAKHLPVGdPATGQVALGPLINARQLDRVHAIVDDSVAAGaRLEAGGTY---DGLFYRPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKiTGALVGV 482
Cdd:cd07152 333 VLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ-TVNDEPH 411
|
410
....*....|....*.
2J40_B 483 QPFGGFKLSGTNAKTG 498
Cdd:cd07152 412 NPFGGMGASGNGSRFG 427
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
87-505 |
4.82e-81 |
|
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: 259.57 E-value: 4.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASAD-VAEAIDFIEYYARAALRYRYPAV-EVVPypg 164
Cdd:cd07092 32 FPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDeLPGAVDNFRFFAGAARTLEGPAAgEYLP--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 eDNESFYV--PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEaGFPPGVVNFLPGVGEE 242
Cdd:cd07092 109 -GHTSMIRrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGAS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 243 VGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK* 322
Cdd:cd07092 187 AGDALVAHPRVRMVSLTGSVRTGKKVARAAADT------LKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 323 SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAP 401
Cdd:cd07092 261 TAACRVYVHESVYDEFVAALVEAVSAIRVGdPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRAEGPGYFYEP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 402 TVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITgaLVG 481
Cdd:cd07092 341 TVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAA 418
|
410 420
....*....|....*....|....*..
2J40_B 482 VQPFGGFKLSGT---NAKTGALDYLRL 505
Cdd:cd07092 419 EMPHGGFKQSGYgkdLSIYALEDYTRI 445
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
90-513 |
1.84e-80 |
|
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: 258.31 E-value: 1.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 90 WKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPavEVVP----YPGE 165
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAP--RKVPtgllMPNK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEeVGA 245
Cdd:cd07099 112 KATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 246 YLVEHpRIRFINFTGSLEVGLKIYEAAG-RLAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07099 191 ALIDA-GVDKVAFTGSVATGRKVMAAAAeRLIP-------VVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCIS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGEGYFIAPT 402
Cdd:cd07099 263 VERVYVHESVYDEFVARLVAKARALRPGaDDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALtGGARSNGGGPFYEPT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGV 482
Cdd:cd07099 343 VLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPA 422
|
410 420 430
....*....|....*....|....*....|.
2J40_B 483 QPFGGFKLSGTNAKTGAlDYLRLFLEMKAVA 513
Cdd:cd07099 423 LPFGGVKDSGGGRRHGA-EGLREFCRPKAIA 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-512 |
1.96e-78 |
|
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: 252.11 E-value: 1.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVG--KNWVEAsaDVAEAIDFIEYYARAALRYRypaVEVVPYPG 164
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGatAAWAGF--NVDLAAGMLREAASLITQII---GGSIPSDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 EDNESFYVPLGAGVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFL---PGV 239
Cdd:cd07105 88 PGTLAMVVKEPVGVVlgIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPED 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 240 GEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRlapgqtWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQG 319
Cdd:cd07105 168 APEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 320 QK*SAASRLILTQGAYEPVLERVLKRAERLSVGPAeenpDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGK-RLEGEGY 397
Cdd:cd07105 242 QICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV----VLGSLVSAAAADRVKELVDDALSKGaKLVVGGLaDESPSGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 398 FIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRK-REHLEWARReFHVGNLYFNrkit 476
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlARALAVAKR-IESGAVHIN---- 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
2J40_B 477 GALVGVQ---PFGGFKLSGT---NAKTGaldyLRLFLEMKAV 512
Cdd:cd07105 393 GMTVHDEptlPHGGVKSSGYgrfNGKWG----IDEFTETKWI 430
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
38-497 |
5.30e-78 |
|
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: 252.38 E-value: 5.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 38 YPLYIGGEWVDTK--ERMVSLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRE 115
Cdd:cd07117 1 YGLFINGEWVKGSsgETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 116 LEATLVYEVGKNWVEA-SADVAEAIDFIEYYARAALRYRYPAVEVvpypGEDNESFYVPLGAGVV--IAPWNFPVAIFTG 192
Cdd:cd07117 80 LAMVETLDNGKPIRETrAVDIPLAADHFRYFAGVIRAEEGSANMI----DEDTLSIVLREPIGVVgqIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 193 MIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAA 272
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 273 G-RLAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSV 351
Cdd:cd07117 235 AkKLIP-------ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 352 G-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE----GYFIAPTVFTEVPPKARIAQEEIFGPVLSV 425
Cdd:cd07117 308 GnPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2J40_B 426 IRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLY---FNRKITGAlvgvqPFGGFKLSGTNAKT 497
Cdd:cd07117 388 IKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWvntYNQIPAGA-----PFGGYKKSGIGRET 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-504 |
9.19e-76 |
|
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: 246.92 E-value: 9.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 35 GRHYPLYIGGEWVDTKERMV--SLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRR 112
Cdd:cd07111 19 DRSFGHFINGKWVKPENRKSfpTINP-ATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 113 KRELEATLVYEVGKNWVEA-SADVAEAIDFIEYYARAA--LRYRYPAVEvvpypgednesfyvPLGAGVVIAPWNFPVAI 189
Cdd:cd07111 98 QRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAqlLDTELAGWK--------------PVGVVGQIVPWNFPLLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 190 FTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEeVGAYLVEHPRIRFINFTGSLEVGLKIY 269
Cdd:cd07111 164 LAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 270 EA-AGrlapgqtWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAER 348
Cdd:cd07111 243 RAtAG-------TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 349 LSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVI 426
Cdd:cd07111 316 LRVGdPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFqPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 427 RVKDFAEALEVANDTPYGLTGGVYSRK-REHLEWARReFHVGNLYFNRkiTGALVGVQPFGGFKLSGTN---AKTGALDY 502
Cdd:cd07111 396 TFRTAKEAVALANNTPYGLAASVWSENlSLALEVALS-LKAGVVWING--HNLFDAAAGFGGYRESGFGregGKEGLYEY 472
|
..
2J40_B 503 LR 504
Cdd:cd07111 473 LR 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
93-512 |
1.63e-75 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 246.66 E-value: 1.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 93 WPQ---EDRSRLLLKAAALMRRRKRELEATLVYEVGKNW-VEASADVAEAIDFIEYYARAALRYRYPAVEVV-PYPGEDN 167
Cdd:PLN02766 76 WPRmsgFERGRIMMKFADLIEEHIEELAALDTIDAGKLFaLGKAVDIPAAAGLLRYYAGAADKIHGETLKMSrQLQGYTL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 168 ESfyvPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYL 247
Cdd:PLN02766 156 KE---PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 248 VEHPRIRFINFTGSLEVGLKIYEAAGRlapgqTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASR 327
Cdd:PLN02766 233 ASHMDVDKVSFTGSTEVGRKIMQAAAT-----SNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFT 405
Cdd:PLN02766 308 VYVQEGIYDEFVKKLVEKAKDWVVGdPFDPRARQGPQVDKQQFEKILSYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 406 EVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVG----NLYFnrkitgALVG 481
Cdd:PLN02766 388 DVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGtiwvNCYF------AFDP 461
|
410 420 430
....*....|....*....|....*....|.
2J40_B 482 VQPFGGFKLSGtNAKTGALDYLRLFLEMKAV 512
Cdd:PLN02766 462 DCPFGGYKMSG-FGRDQGMDALDKYLQVKSV 491
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
37-492 |
2.27e-75 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 245.59 E-value: 2.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 37 HYPLYIGGEWVDTK-ERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRE 115
Cdd:PRK13473 2 QTKLLINGELVAGEgEKQPVYNP-ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 116 LEATLVYEVGKNWVEASAD-VAEAIDFIEYYARAALRYRYPAVevvpypGEdnesfYVPlG---------AGVV--IAPW 183
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKAA------GE-----YLE-GhtsmirrdpVGVVasIAPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 184 NFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLE 263
Cdd:PRK13473 149 NYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 264 VGLKIYEAAGRLApgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVL 343
Cdd:PRK13473 228 TGKHVLSAAADSV------KRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 344 KRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG--QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFG 420
Cdd:PRK13473 302 AAVATLKVGdPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFG 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2J40_B 421 PVLSVIRVKDFAEALEVANDTPYGLTGGVYSRK--REHLewARREFHVGNLYFNRKITgaLVGVQPFGGFKLSG 492
Cdd:PRK13473 382 PVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvgRAHR--VSARLQYGCTWVNTHFM--LVSEMPHGGQKQSG 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
97-510 |
2.36e-73 |
|
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: 239.57 E-value: 2.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 97 DRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEDNESFYV---P 173
Cdd:cd07146 41 QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTlreP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 174 LGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRI 253
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 254 RFINFTGSLEVGLKIYEAAGrlapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQG 333
Cdd:cd07146 201 DLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHES 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 334 AYEPVLERVLKRAERLSVG-PAEENPDLGPVVS---AEQ-ERKVLSYIEIGkneGQLVLGGKRlegEGYFIAPTVFTEVP 408
Cdd:cd07146 273 VADEFVDLLVEKSAALVVGdPMDPATDMGTVIDeeaAIQiENRVEEAIAQG---ARVLLGNQR---QGALYAPTVLDHVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 409 PKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrKITGALVGVQPFGGF 488
Cdd:cd07146 347 PDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGV 425
|
410 420
....*....|....*....|..
2J40_B 489 KLSGTNAKTGALDYLRLFLEMK 510
Cdd:cd07146 426 KDSGLGGKEGVREAMKEMTNVK 447
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
63-492 |
5.79e-72 |
|
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: 236.18 E-value: 5.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 63 EVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFI 142
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 143 EYYARAALRYRYpavEVVP---YPGEDNESFYV---PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVG 216
Cdd:cd07094 90 RLAAEEAERIRG---EEIPldaTQGSDNRLAWTirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 217 AKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgqtwFKRAYVETGGKDAII 296
Cdd:cd07094 167 LELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 297 VDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSY 375
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGdPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 376 IEIGKNEG-QLVLGGKRlegEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKR 454
Cdd:cd07094 319 VEEAVEAGaRLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430
....*....|....*....|....*....|....*...
2J40_B 455 EHLEWARREFHVGNLYFNRKiTGALVGVQPFGGFKLSG 492
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
102-503 |
1.31e-70 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 231.16 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 102 LLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYpavEVVPY--PGEDNESFYVPLGAGVV 179
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEG---EIIQSdrPGENILLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 180 IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFT 259
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 260 GSLEVGLKIYEAAgrlAPGQTwfkRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVL 339
Cdd:PRK10090 158 GSVSAGEKIMAAA---AKNIT---KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 340 ERVLKRAERLSVG-PAEEN-PDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQE 416
Cdd:PRK10090 232 NRLGEAMQAVQFGnPAERNdIAMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 417 EIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQpfGGFKLS---GT 493
Cdd:PRK10090 312 ETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgigGA 389
|
410
....*....|
2J40_B 494 NAKTGALDYL 503
Cdd:PRK10090 390 DGKHGLHEYL 399
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
98-492 |
4.01e-70 |
|
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: 230.98 E-value: 4.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 98 RSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyryPAVEVVP---YPGEDNESFYV-- 172
Cdd:cd07147 45 RAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATR---IYGEVLPldiSARGEGRQGLVrr 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 -PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPgVGEEVGAYLVEHP 251
Cdd:cd07147 122 fPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 252 RIRFINFTGSLEVGLKIYEAAGRlapgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILT 331
Cdd:cd07147 201 RIKLLSFTGSPAVGWDLKARAGK--------KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 332 QGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRlegEGYFIAPTVFTEVPP 409
Cdd:cd07147 273 RSVYDEFKSRLVARVKALKTGdPKDDATDVGPMISESEAERVEGWVNEAVDAGaKLLTGGKR---DGALLEPTILEDVPP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 410 KARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNrKITGALVGVQPFGGFK 489
Cdd:cd07147 350 DMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVK 428
|
...
2J40_B 490 LSG 492
Cdd:cd07147 429 DSG 431
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
90-512 |
4.03e-70 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 233.55 E-value: 4.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 90 WKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVE-ASADVAEAIDFIEYYARAALRYRYPAVevvpyPGEDN- 167
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTV-----PADGPh 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 168 --ESFYVPLGAGVVIAPWNFPVAIFtGMIVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVG 244
Cdd:PLN02466 188 hvQTLHEPIGVAGQIIPWNFPLLMF-AWKVGPaLACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGRlapgqTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:PLN02466 267 AALASHMDVDKLAFTGSTDTGKIVLELAAK-----SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPT 402
Cdd:PLN02466 342 GSRTFVHERVYDEFVEKAKARALKRVVGdPFKKGVEQGPQIDSEQFEKILRYIKSGVESGaTLECGGDRFGSKGYYIQPT 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFN-RKITGALVg 481
Cdd:PLN02466 422 VFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI- 500
|
410 420 430
....*....|....*....|....*....|.
2J40_B 482 vqPFGGFKLSGTNAKTGaLDYLRLFLEMKAV 512
Cdd:PLN02466 501 --PFGGYKMSGIGREKG-IYSLNNYLQVKAV 528
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
89-512 |
7.63e-70 |
|
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: 230.31 E-value: 7.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 89 TWKDWPQEdRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEvvPYPGEDNE 168
Cdd:cd07120 36 DWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIE--PEPGSFSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 169 SFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEA-GFPPGVVNFLPGVGEEVGAYL 247
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 248 VEHPRIRFINFTGSLEVGLKIYEAAgrlAPGqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASR 327
Cdd:cd07120 193 VASPDVDVISFTGSTATGRAIMAAA---APT---LKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLERVLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL--GGKRLEG--EGYFIAPT 402
Cdd:cd07120 267 VLVQRSIADEVRDRLAARLAAVKVGPGlDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVlrGGPVTEGlaKGAFLRPT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKitGALVGV 482
Cdd:cd07120 347 LLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDW--NKLFAE 424
|
410 420 430
....*....|....*....|....*....|
2J40_B 483 QPFGGFKLSGTNAKTGAlDYLRLFLEMKAV 512
Cdd:cd07120 425 AEEGGYRQSGLGRLHGV-AALEDFIEYKHI 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
90-516 |
4.45e-69 |
|
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: 229.25 E-value: 4.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 90 WKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKN-WVEASADVAEAIDFIEYYARAALRYRYPAVEV-VPYP-GED 166
Cdd:cd07113 54 WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSiHLSRAFEVGQSANFLRYFAGWATKINGETLAPsIPSMqGER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYV--PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEeVG 244
Cdd:cd07113 134 YTAFTRrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIyeaaGRLAPGQtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:cd07113 213 AQLISHPDVAKVSFTGSVATGKKI----GRQAASD--LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPT 402
Cdd:cd07113 287 PERFYVHRSKFDELVTKLKQALSSFQVGSPmDESVMFGPLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSrkrEHLEWARR---EFHVGNLYFN-RKITGA 478
Cdd:cd07113 367 LVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT---NNLSKALRyipRIEAGTVWVNmHTFLDP 443
|
410 420 430
....*....|....*....|....*....|....*...
2J40_B 479 LVgvqPFGGFKLSGTNAKTGAlDYLRLFLEMKAVAERF 516
Cdd:cd07113 444 AV---PFGGMKQSGIGREFGS-AFIDDYTELKSVMIRY 477
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
87-473 |
3.64e-68 |
|
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: 225.97 E-value: 3.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRyrypAVEVVPYPGED 166
Cdd:cd07102 31 QKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEE----ALADIRVPEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 N-ESF--YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEV 243
Cdd:cd07102 107 GfERYirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHL-SHET 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHPRIRFINFTGSLEVGLKIYEAAgrlAPGqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:cd07102 186 SAALIADPRIDHVSFTGSVAGGRAIQRAA---AGR---FIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRL---EGEGYF 398
Cdd:cd07102 260 SIERIYVHESIYDAFVEAFVAVVKGYKLGdPLDPSTTLGPVVSARAADFVRAQIADAIAKGaRALIDGALFpedKAGGAY 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2J40_B 399 IAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNR 473
Cdd:cd07102 340 LAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
40-492 |
2.95e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.45 E-value: 2.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVD-TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEA 118
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNP-VSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 119 TLVYEVGKNWVEASADVAEAIDFIE-----YY------------ARAALRYRypavevvpypgednesfyvPLGAGVVIA 181
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAisiqaYHertgekrsemadGAAVLRHR-------------------PHGVVAVFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 182 PWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEVGAYLVEHPRIRFINFTGS 261
Cdd:PRK09457 143 PYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 262 LEVGLKIYEA-AGRlaPGqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAY-EPVL 339
Cdd:PRK09457 222 ANTGYLLHRQfAGQ--PE----KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 340 ERVLKRAERLSVGP--AEENPDLGPVVSAEQERKVL-SYIEIGKNEGQLVLGGKRLEGEGYFIAPTVFtEVPPKARIAQE 416
Cdd:PRK09457 296 ARLVAVAKRLTVGRwdAEPQPFMGAVISEQAAQGLVaAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 417 EIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAlVGVQPFGGFKLSG 492
Cdd:PRK09457 375 EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
87-492 |
5.32e-66 |
|
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: 221.17 E-value: 5.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEAS-ADVAEAIDFIEYYArAALRYRYPAVEVVpypge 165
Cdd:cd07116 51 KEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA-GCIRAQEGSISEI----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNES----FYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGE 241
Cdd:cd07116 125 DENTvayhFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 242 EVGAYLVEHPRIRFINFTGSLEVGLKIYE-AAGRLAPgqtwfkrAYVETGGK------DAIIVDETADFDLAAEGVVVSA 314
Cdd:cd07116 204 EAGKPLASSKRIAKVAFTGETTTGRLIMQyASENIIP-------VTLELGGKspniffADVMDADDAFFDKALEGFVMFA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 315 YGfQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKR- 391
Cdd:cd07116 277 LN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGnPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLtGGERn 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 392 ----LEGEGYFIAPTVFTEvpPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVG 467
Cdd:cd07116 356 elggLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAG 433
|
410 420
....*....|....*....|....*
2J40_B 468 NLYFNrkITGALVGVQPFGGFKLSG 492
Cdd:cd07116 434 RVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
88-514 |
1.58e-65 |
|
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: 219.10 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPG-ED 166
Cdd:cd07101 32 RAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKPRRRRGAIPVlTR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAY 246
Cdd:cd07101 112 TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHprIRFINFTGSLEVGLKIYEAAGRLAPGqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:cd07101 192 IVDN--ADYVMFTGSTATGRVVAERAGRRLIG------CSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGEG-YFIAPTV 403
Cdd:cd07101 264 RIYVHESVYDEFVRRFVARTRALRLGAAlDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLaGGRARPDLGpYFYEPTV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 404 FTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQ 483
Cdd:cd07101 344 LTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASID 423
|
410 420 430
....*....|....*....|....*....|..
2J40_B 484 -PFGGFKLSGTNAKTGALDYLRlFLEMKAVAE 514
Cdd:cd07101 424 aPMGGMKDSGLGRRHGAEGLLK-YTETQTVAV 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
88-452 |
8.16e-64 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 215.78 E-value: 8.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVV--PYPGE 165
Cdd:PLN00412 67 KAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVsdSFPGN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESF----YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGE 241
Cdd:PLN00412 147 ERNKYcltsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 242 EVGAYLVEHPRIRFINFTGSlEVGLKIYEAAGrLAPGQTwfkrayvETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK 321
Cdd:PLN00412 227 EIGDFLTMHPGVNCISFTGG-DTGIAISKKAG-MVPLQM-------ELGGKDACIVLEDADLDLAAANIIKGGFSYSGQR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 *SAASRLILTQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRlegEGYFIA 400
Cdd:PLN00412 298 CTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGaTFCQEWKR---EGNLIW 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2J40_B 401 PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR 452
Cdd:PLN00412 375 PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTR 426
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
38-512 |
7.02e-63 |
|
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: 213.13 E-value: 7.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 38 YPLYIGGEWVDTK--ERMVSLNPSAPSeVVGTTAKAGKAEAEAALEAAWKAFKT--WKDWPQEDRSRLLLKAAALMRRRK 113
Cdd:cd07140 6 HQLFINGEFVDAEggKTYNTINPTDGS-VICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 114 RELEATLVYEVGKNWVEA-SADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEDNESFYV--PLGAGVVIAPWNFPVAIF 190
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKrePIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 191 TGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYE 270
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 271 AAgrlapGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLS 350
Cdd:cd07140 245 SC-----AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 351 VG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRV 428
Cdd:cd07140 320 IGdPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 429 K--DFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFN--RKITGAlvgvQPFGGFKLSGTNAKTGAlDYLR 504
Cdd:cd07140 400 DdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtyNKTDVA----APFGGFKQSGFGKDLGE-EALN 474
|
....*...
2J40_B 505 LFLEMKAV 512
Cdd:cd07140 475 EYLKTKTV 482
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-505 |
4.21e-62 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 210.92 E-value: 4.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVDTKE-RMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEAT 119
Cdd:PRK11241 14 LINGEWLDANNgEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 120 LVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYpavEVVPYPGEDNESFYV--PLGAGVVIAPWNFPVAIFTGMIVGP 197
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG---DTIPGHQADKRLIVIkqPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 198 VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRLap 277
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 278 gqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVGPA-EE 356
Cdd:PRK11241 249 ----IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGlEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 357 NPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEAL 435
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2J40_B 436 EVANDTPYGLTGGVYSRKrehlewARREFHVGNL--YFNRKITGALVG--VQPFGGFKLSG---TNAKTGALDYLRL 505
Cdd:PRK11241 405 AQANDTEFGLAAYFYARD------LSRVFRVGEAleYGIVGINTGIISneVAPFGGIKASGlgrEGSKYGIEDYLEI 475
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
92-512 |
3.72e-61 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 208.60 E-value: 3.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 92 DWPQE---DRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEA-SADVAEAIDFIEYYARAALRYrYPavEVVPyPGEDN 167
Cdd:PRK09847 74 DWSLSspaKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKV-YG--EVAT-TSSHE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 168 ESFYV--PLGAGVVIAPWNFPVaIFTGMIVGP-VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVG 244
Cdd:PRK09847 150 LAMIVrePVGVIAAIVPWNFPL-LLTCWKLGPaLAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgQTWFKRAYVETGGKDA-IIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:PRK09847 229 QALSRHNDIDAIAFTGSTRTGKQLLKDAG-----DSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGkRLEGEGYFIAPT 402
Cdd:PRK09847 304 AGTRLLLEESIADEFLALLKQQAQNWQPGhPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG-RNAGLAAAIGPT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALvgV 482
Cdd:PRK09847 383 IFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--T 460
|
410 420 430
....*....|....*....|....*....|
2J40_B 483 QPFGGFKLSGtNAKTGALDYLRLFLEMKAV 512
Cdd:PRK09847 461 VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
88-514 |
4.07e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 209.35 E-value: 4.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKN---WVEASADVAEAIDfieYYARAALRYRYPAVEVVPYPG 164
Cdd:PRK09407 68 RAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKArrhAFEEVLDVALTAR---YYARRAPKLLAPRRRAGALPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 165 -EDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEV 243
Cdd:PRK09407 145 lTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHprIRFINFTGSLEVGLKIYEAAGRLAPGQTwfkrayVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:PRK09407 225 GTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFS------LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLERVLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGEG-YFIA 400
Cdd:PRK09407 297 SIERIYVHESIYDEFVRAFVAAVRAMRLGAGyDYSADMGSLISEAQLETVSAHVDDAVAKGATVLaGGKARPDLGpLFYE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALV 480
Cdd:PRK09407 377 PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWG 456
|
410 420 430
....*....|....*....|....*....|....*
2J40_B 481 GVQ-PFGGFKLSGTNAKTGAlDYLRLFLEMKAVAE 514
Cdd:PRK09407 457 SVDaPMGGMKDSGLGRRHGA-EGLLKYTESQTIAT 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
171-514 |
1.18e-59 |
|
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: 203.69 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 171 YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEA----GFPPGVVNFLPGVGEeVGAY 246
Cdd:cd07098 118 YEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 247 LVEHPRIRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAA 325
Cdd:cd07098 197 LTSHPVIDHITFIGSPPVGKKVMAAAAEsLTP-------VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 326 SRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKR----LEGEGYFI 399
Cdd:cd07098 270 ERVIVHEKIYDKLLEILTDRVQALRQGpPLDGDVDVGAMISPARFDRLEELVADAVEKGaRLLAGGKRyphpEYPQGHYF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 400 APTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGAL 479
Cdd:cd07098 350 PPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYY 429
|
330 340 350
....*....|....*....|....*....|....*
2J40_B 480 VGVQPFGGFKLSGTNaKTGALDYLRLFLEMKAVAE 514
Cdd:cd07098 430 VQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTE 463
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
40-491 |
4.49e-59 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 202.80 E-value: 4.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVDTK--ERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELE 117
Cdd:TIGR01722 3 HWIGGKFAEGAsgTYIPVTNP-ATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 118 ATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPyPGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGP 197
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVA-TRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 198 VAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGaYLVEHPRIRFINFTGSLEVGLKIYEAAGRLAp 277
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 278 gqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTqGAYEPVLERVLKRAERLSVGPAEE- 356
Cdd:TIGR01722 239 -----KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 357 NPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGY----FIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDF 431
Cdd:TIGR01722 313 GAEMGPLITPQAKDRVASLIAGGAAEGaEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 432 AEALEVANDTPYG------LTGGVYSRKREHlewarrEFHVGNLYFNRKITGALvGVQPFGGFKLS 491
Cdd:TIGR01722 393 EEAIALINASPYGngtaifTRDGAAARRFQH------EIEVGQVGVNVPIPVPL-PYFSFTGWKDS 451
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
41-452 |
5.40e-58 |
|
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: 199.74 E-value: 5.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVDTKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATL 120
Cdd:cd07130 2 VYDGEWGGGGGVVTSISP-ANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 121 VYEVGKNWVEASADVAEAIDfIEYYARAALRYRYPAVEVVPYPGEDNESFYVPLGAGVVIAPWNFPVAIF--TGMIVgpV 198
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMID-ICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWgwNAAIA--L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 199 AVGNTVIAKPAED----AVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEA-AG 273
Cdd:cd07130 158 VCGNVVVWKPSPTtpltAIAVTKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAvAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 274 RlapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG- 352
Cdd:cd07130 237 R-------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGd 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 353 PAEENPDLGPVVSAEQERKVLSYIEIGKNE-GQLVLGGKRLEGEGYFIAPTVfTEVPPKARIAQEEIFGPVLSVIRVKDF 431
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420
....*....|....*....|.
2J40_B 432 AEALEVANDTPYGLTGGVYSR 452
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTT 409
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
40-515 |
2.04e-57 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 198.45 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 40 LYIGGEWVD-TKERMVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTwKDWPQ--EDRSRLLLKAAALMRRRKREL 116
Cdd:TIGR04284 3 LLIDGKLVAgSAGTFPTVNP-ATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRdtALRVRCLRQLRDALRAHVEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 117 EATLVYEVGK-NWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYP-GEDNESFYVPLGAGVV--IAPWNFPVAIFTG 192
Cdd:TIGR04284 81 RELTIAEVGApRMLTAGAQLEGPVDDLGFAADLAESYAWTTDLGVASPmGIPTRRTLRREAVGVVgaITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 193 MIVGPVAVGNTVIAKPAED----AVVVGAKVFEifhEAGFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKI 268
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDtpwcAAVLGELIAE---HTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 269 yeaagrLAPGQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAER 348
Cdd:TIGR04284 238 ------MADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 349 LSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGE--GYFIAPTVFTEVPPKARIAQEEIFGPVLS 424
Cdd:TIGR04284 312 IKPGdPADPGTVCGPVISARQRDRVQSYLDLAVAEGgRFACGGGRPADRdrGFFVEPTVIAGLDNNARVAREEIFGPVLT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 425 VIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKI-TGALVgvqPFGGFKLSGTNAKTGALDYl 503
Cdd:TIGR04284 392 VIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVwYSADA---PFGGYKQSGIGREMGVAGF- 467
|
490
....*....|..
2J40_B 504 RLFLEMKAVAER 515
Cdd:TIGR04284 468 EEYLETKLIATA 479
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
54-492 |
6.12e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 185.84 E-value: 6.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 54 VSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASA 133
Cdd:PRK13968 10 ISVNP-ATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 134 DVAEAIDFIEYYARAAlryryPA-VEVVPYPGEDNESF--YVPLGAGVVIAPWNFPV-AIFTGMIvgPVAV-GNTVIAKP 208
Cdd:PRK13968 89 EVAKSANLCDWYAEHG-----PAmLKAEPTLVENQQAVieYRPLGTILAIMPWNFPLwQVMRGAV--PILLaGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 209 AEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAyLVEHPRIRFINFTGSLEVGLKIYEAAGrlapgqTWFKRAYVE 288
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAG------AALKKCVLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 289 TGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAE 367
Cdd:PRK13968 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGdPRDEENALGPMARFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 368 QERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLT 446
Cdd:PRK13968 315 LRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
2J40_B 447 GGVYSRKREHLEWARREFHVGNLYFN-RKITGALVGvqpFGGFKLSG 492
Cdd:PRK13968 395 ATIFTTDETQARQMAARLECGGVFINgYCASDARVA---FGGVKKSG 438
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
87-492 |
6.51e-53 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 185.71 E-value: 6.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGEd 166
Cdd:PRK09406 36 FRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEPADAAAVGA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 167 NESF--YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPgvgeeVG 244
Cdd:PRK09406 115 SRAYvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-----VG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 245 AYLVE----HPRIRFINFTGSLEVGLKIYEAAGRLapgqtwFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQ 320
Cdd:PRK09406 190 SGAVEailrDPRVAAATLTGSEPAGRAVAAIAGDE------IKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 321 K*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL-GGKRLEGEGYF 398
Cdd:PRK09406 264 SCIAAKRFIVHADVYDAFAEKFVARMAALRVGdPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILcGGKRPDGPGWF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 399 IAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITG- 477
Cdd:PRK09406 344 YPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSy 423
|
410
....*....|....*.
2J40_B 478 -ALvgvqPFGGFKLSG 492
Cdd:PRK09406 424 pEL----PFGGVKRSG 435
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
39-516 |
1.92e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 176.48 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 39 PLYIGGEWVDTKER--MVSLNPsAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKREL 116
Cdd:PLN02419 115 PNLIGGSFVESQSSsfIDVINP-ATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 117 EATLVYEVGKNWVEASADVAEAIDFIEY---YARAALRYRYPAVEvvpyPGEDNESFYVPLGAGVVIAPWNFPVAIFTGM 193
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHacgMATLQMGEYLPNVS----NGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 194 IVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAyLVEHPRIRFINFTGSLEVGLKIYEAAG 273
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 274 rlAPGqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTqGAYEPVLERVLKRAERLSVG- 352
Cdd:PLN02419 349 --AKG----KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFV-GDAKSWEDKLVERAKALKVTc 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 353 PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGY----FIAPTVFTEVPPKARIAQEEIFGPVLSVIR 427
Cdd:PLN02419 422 GSEPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQ 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 428 VKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALvgvqPFggFKLSGTNAK-TGALDY---- 502
Cdd:PLN02419 502 ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPL----PF--FSFTGNKASfAGDLNFygka 575
|
490
....*....|....*
2J40_B 503 -LRLFLEMKAVAERF 516
Cdd:PLN02419 576 gVDFFTQIKLVTQKQ 590
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
87-502 |
1.94e-48 |
|
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: 173.37 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDW-PQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGE 165
Cdd:cd07148 34 FLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPAS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 166 DNESFYV---PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPgVGEE 242
Cdd:cd07148 114 AGRIAFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 243 VGAYLVEHPRIRFINFTGSLEVGLKIyeaAGRLAPGQtwfkRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK* 322
Cdd:cd07148 193 VAEKLVTDPRVAFFSFIGSARVGWML---RSKLAPGT----RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 323 SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYfiA 400
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLVVGdPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGaRLLCGGKRLSDTTY--A 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 401 PTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKiTGALV 480
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRV 422
|
410 420
....*....|....*....|..
2J40_B 481 GVQPFGGFKLSGTNakTGALDY 502
Cdd:cd07148 423 DWMPFAGRRQSGYG--TGGIPY 442
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
41-499 |
4.37e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 162.70 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVDTKERMVSLNPSApSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEATL 120
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 121 VYEVGKNWVEASADVAEAIDFIEYyarAALRYRYPAVEVVPY--PGEDNESFYVPLGAGVVIAPWNFPVAIFTGMIVGPV 198
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDF---AVGLSRQLNGSIIPSerPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 199 AVGNTVIAKPAED----AVVVGAKVFEIFHEAGFPPGVVNFLPGvGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAgr 274
Cdd:PLN02315 180 VCGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 275 lapgQTWFKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-P 353
Cdd:PLN02315 257 ----NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGdP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 354 AEENPDLGPVVSAEQERKVLSYIEIGKNEG-QLVLGGKRLEGEGYFIAPTVfTEVPPKARIAQEEIFGPVLSVIRVKDFA 432
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2J40_B 433 EALEVANDTPYGLTGGVYSRKREHL-EW-ARREFHVGNLYFNRKITGALVGvQPFGGFKLSGTNAKTGA 499
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIfKWiGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
87-492 |
7.46e-44 |
|
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: 160.38 E-value: 7.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEAS----ADVAEAIDFIEYYARAALRYRYPAVEVVPY 162
Cdd:cd07087 11 FLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVVLGEIDHALKHLKKWMKPRRVSVPLLLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 163 PGEdneSFYV--PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGvG 240
Cdd:cd07087 91 PAK---AYVIpePLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-G 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 241 EEVGAYLVEHPrIRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQG 319
Cdd:cd07087 166 VEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKhLTP-------VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 320 QK*SAASRLILTQGAYEPVLERvLKRAERLSVGP-AEENPDLGPVVSAEQERKVLSYIeigkNEGQLVLGGKRLEGEGYf 398
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEE-LKKAIKEFYGEdPKESPDYGRIINERHFDRLASLL----DDGKVVIGGQVDKEERY- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 399 IAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGA 478
Cdd:cd07087 312 IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHA 391
|
410
....*....|....
2J40_B 479 LVGVQPFGGFKLSG 492
Cdd:cd07087 392 AIPNLPFGGVGNSG 405
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
172-498 |
2.67e-40 |
|
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: 150.83 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 172 VPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGAyLVEHp 251
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTA-LLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 252 RIRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLIL 330
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKhLTP-------VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 331 TQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEigKNEGQLVLGGKRLEGEgYFIAPTVFTEVPPK 410
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD--TTKGKVVIGGEMDEAT-RFIPPTIVSDVSWD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 411 ARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKL 490
Cdd:cd07135 334 DSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGD 413
|
....*...
2J40_B 491 SGTNAKTG 498
Cdd:cd07135 414 SGYGAYHG 421
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
170-492 |
6.91e-40 |
|
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: 149.96 E-value: 6.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 170 FYVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGVGEEVGAYLve 249
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 250 HPRIRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrayV--ETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAAS 326
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKhLTP---------VtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 327 RLILTQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKnegqLVLGGKRLEGEGYfIAPTVFTE 406
Cdd:cd07136 245 YVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK----IVFGGNTDRETLY-IEPTILDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 407 VPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREF------------HVGNLYFnrk 474
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLsfgggcindtimHLANPYL--- 396
|
330
....*....|....*...
2J40_B 475 itgalvgvqPFGGFKLSG 492
Cdd:cd07136 397 ---------PFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
171-492 |
7.08e-40 |
|
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: 149.68 E-value: 7.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 171 YVPLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGvGEEVGAYLVEH 250
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 251 PrirF--INFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASR 327
Cdd:cd07134 176 P---FdhIFFTGSPAVGKIVMAAAAKhLAS-------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 328 LILTQGAYEPVLERVLKRAERL--SVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEGEGYFIAPTVFT 405
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIAPTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 406 EVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPF 485
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPF 405
|
....*..
2J40_B 486 GGFKLSG 492
Cdd:cd07134 406 GGVNNSG 412
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
106-495 |
3.17e-39 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 149.02 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 106 AALMRRRKRELEATLVYEvgknWVEASADVAEAIDFIEYYARAalryRYPAVEVVPYPGEdNESFYVPLGAGVVIAPWNF 185
Cdd:PTZ00381 51 EAVHKDLGRHPFETKMTE----VLLTVAEIEHLLKHLDEYLKP----EKVDTVGVFGPGK-SYIIPEPLGVVLVIGAWNY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 186 PvaIFTGMI--VGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLPGvGEEVGAYLVEHPrIRFINFTGSLE 263
Cdd:PTZ00381 122 P--LNLTLIplAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 264 VGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVLERv 342
Cdd:PTZ00381 197 VGKLVMQAAAEnLTP-------CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEA- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 343 LKRAERLSVGPAEEN-PDLGPVVSAEQERKVLSYIEIGKneGQLVLGGKRLEGEGYfIAPTVFTEVPPKARIAQEEIFGP 421
Cdd:PTZ00381 269 LKEAIKEFFGEDPKKsEDYSRIVNEFHTKRLAELIKDHG--GKVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGP 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2J40_B 422 VLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKLSGTNA 495
Cdd:PTZ00381 346 ILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGA 419
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
98-512 |
5.31e-35 |
|
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: 136.21 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 98 RSRLLLKAAALMRRRKRELEATLVYEVGKNWVEAsADVAEAIDFIEYYARAALRYRY---PAVEVVPYPGEDNESFYVPL 174
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIphePGNHLGQGLKQQSHGYRWPY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 175 GAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAG-FPPGVVNFLPGVGeEVGAYLVEHPRI 253
Cdd:cd07084 102 GPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG-KTMQALLLHPNP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 254 RFINFTGSLEVGLKIYEAAGrlapgqtwFKRAYVETGGKDAIIVDETAD-FDLAAEGVVVSAYGFQGQK*SAASRL-ILT 331
Cdd:cd07084 181 KMVLFTGSSRVAEKLALDAK--------QARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLfVPE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 332 QGAYEPVLERVLKRAERLSVGPAeenpdlgpVVSAEQERKVLSYIEIGKNEGQLVL--GGKRL------EGEGYFIAPTV 403
Cdd:cd07084 253 NWSKTPLVEKLKALLARRKLEDL--------LLGPVQTFTTLAMIAHMENLLGSVLlfSGKELknhsipSIYGACVASAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 404 FTEVPP---KARIAQEEIFGPVLSVIRVKDFAEA--LEVANDTPYGLTGGVYSRKREHL-EWARREFHVGNLYF-NRKIT 476
Cdd:cd07084 325 FVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLqELIGNLWVAGRTYAiLRGRT 404
|
410 420 430
....*....|....*....|....*....|....*.
2J40_B 477 GALVGVQPFGGFKLSGTNAKTGALDYLRLFLEMKAV 512
Cdd:cd07084 405 GVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
173-495 |
1.19e-33 |
|
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: 132.35 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVG---AKVF------EIFHeagfppgVVNflpgVGEEV 243
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllAELIpkyldkECYP-------VVL----GGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHpRIRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK* 322
Cdd:cd07132 169 TTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKhLTP-------VTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 323 SAASRLILTQGAYEPVLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKnegqLVLGGKRLEGEGYfIAPT 402
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGK----VAIGGQTDEKERY-IAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 403 VFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGV 482
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDS 395
|
330
....*....|...
2J40_B 483 QPFGGFKLSGTNA 495
Cdd:cd07132 396 LPFGGVGNSGMGA 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
173-512 |
2.26e-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: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFhEAGFPPGVVNFLPGvGEEVGAYLVEHpR 252
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 253 IRFINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILT 331
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKhLTP-------VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNNGQACIAPDYVLV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 332 QGAYEPVLERVLKRAERLSVGP-AEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRLEgEGYFIAPTVFTEVPPK 410
Cdd:cd07137 251 EESFAPTLIDALKNTLEKFFGEnPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE-KNLYIEPTILLDPPLD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 411 ARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKL 490
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGE 409
|
330 340
....*....|....*....|..
2J40_B 491 SGTNAKTGALDYlRLFLEMKAV 512
Cdd:cd07137 410 SGFGAYHGKFSF-DAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
160-492 |
2.60e-27 |
|
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: 114.12 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 160 VPYPGEDNESFYVPLGagVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAgFPPGVVNFLP 237
Cdd:cd07133 88 LLFLPAKAEVEYQPLG--VVgiIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 238 GvGEEVGAYLVEHPrirF--INFTGSLEVGLKIYEAAGR-LAPgqtwfkrayV--ETGGKDAIIVDETADFDLAAEGVVV 312
Cdd:cd07133 165 G-GADVAAAFSSLP---FdhLLFTGSTAVGRHVMRAAAEnLTP---------VtlELGGKSPAIIAPDADLAKAAERIAF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 313 SAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLsVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVL---GG 389
Cdd:cd07133 232 GKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTSIINERHYARLQGLLEDARAKGARVIelnPA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 390 KRLEGEGYFIAPTVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNL 469
Cdd:cd07133 311 GEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV 390
|
330 340
....*....|....*....|...
2J40_B 470 YFNRKITGALVGVQPFGGFKLSG 492
Cdd:cd07133 391 TINDTLLHVAQDDLPFGGVGASG 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
173-515 |
8.40e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.52 E-value: 8.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFhEAGFPPGVVNFLPGVGEEVGAYLVEhpR 252
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ--K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 253 IRFINFTGSLEVGLKIYEAAG-RLAPgqtwfkrAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILT 331
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAkHLTP-------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 332 QGAYEP-VLERVLKRAERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKRlEGEGYFIAPTVFTEVPPK 410
Cdd:PLN02174 262 TKEYAPkVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEK-DRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 411 ARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLEWARREFHVGNLYFNRKITGALVGVQPFGGFKL 490
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|....*
2J40_B 491 SGTNAKTGALDYlRLFLEMKAVAER 515
Cdd:PLN02174 421 SGMGAYHGKFSF-DAFSHKKAVLYR 444
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
41-458 |
1.37e-21 |
|
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: 97.73 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 41 YIGGEWVDTKERMVSLNPSAPSEVVGTTAKAGKAEAEAALEAAWKAFKTWKDWPQEDRSRLLLKAAALMRRRKRELEAtL 120
Cdd:cd07128 4 YVAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA-L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 121 VYEVGKNWVEASADVAEAIDFIEYYARAALRYRYPAVEVVPYPGED---NESF-----YVPL-GAGVVIAPWNFPVaifT 191
Cdd:cd07128 83 SAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPlskDGTFvgqhiLTPRrGVAVHINAFNFPV---W 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 192 GMIvGPVAV----GNTVIAKPAEDAVVVGAKVFEIFHEAG-FPPGVVNFLPG-VGEevgayLVEHPRIR-FINFTGSLEV 264
Cdd:cd07128 160 GML-EKFAPallaGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGsVGD-----LLDHLGEQdVVAFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 265 GLKIYEAAGRLAPGQtwfkRAYVETGGKDAIIVDETA-----DFDLAAEGVVVSAYGFQGQK*SAASRLILTQGAYEPVL 339
Cdd:cd07128 234 AAKLRAHPNIVARSI----RFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 340 ERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGK-------RLEGEGYFIAPTVFTEVPPKA 411
Cdd:cd07128 310 EALKARLAKVVVGdPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLLCDDPDA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
2J40_B 412 RIA--QEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHLE 458
Cdd:cd07128 390 ATAvhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAR 438
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
173-515 |
3.95e-21 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 96.33 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 PLGAGVVIAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAkvfeiFHEAGFP----PGVVNFLPGvGEEVGAYLV 248
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 249 EHPRIRfINFTGSLEVGLKIYEAAGR-LAPgqtwfkrAYVETGGKDAIIVD---ETADFDLAAEGVVVSAYGFQGQK*SA 324
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKhLTP-------VALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCAGQACI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 325 ASRLILTQGAYEPVLERVLKRA-ERLSVGPAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGGKrLEGEGYFIAPTV 403
Cdd:PLN02203 254 AIDYVLVEERFAPILIELLKSTiKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGS-IDEKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 404 FTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSR----KREHLEwarrEFHVGNLYFNRKITGAL 479
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNneklKRRILS----ETSSGSVTFNDAIIQYA 408
|
330 340 350
....*....|....*....|....*....|....*.
2J40_B 480 VGVQPFGGFKLSGTNAKTGALDYlRLFLEMKAVAER 515
Cdd:PLN02203 409 CDSLPFGGVGESGFGRYHGKYSF-DTFSHEKAVLRR 443
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
87-481 |
2.25e-20 |
|
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: 93.76 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 87 FKTWKDWPQEDRSRLLLKAAALMRRRKREL-----------EATLVYEVGK--NWVEASADVAEAIDFIEyyaraaLRYR 153
Cdd:cd07129 12 FESYRALSPARRAAFLEAIADEIEALGDELvarahaetglpEARLQGELGRttGQLRLFADLVREGSWLD------ARID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 154 YPAVEVVPYPGEDNESFYVPLGAGVVIAPWNFPVAIFT--GMIVGPVAVGNTVIAK--PA--EDAVVVGAKVFEIFHEAG 227
Cdd:cd07129 86 PADPDRQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRATG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 228 FPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYE-AAGRLAPgqtwfKRAYVETGGKDAIIVDETAdfdLA 306
Cdd:cd07129 166 LPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDaAAARPEP-----IPFYAELGSVNPVFILPGA---LA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 307 AEGVVVsAYGFqgqk*sAASrliLTQGA-------------YEPVLERVLKR-AERLSVGPAEenPDLGP-VVSAEQERK 371
Cdd:cd07129 238 ERGEAI-AQGF------VGS---LTLGAgqfctnpglvlvpAGPAGDAFIAAlAEALAAAPAQ--TMLTPgIAEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 372 VlsyiEIGKNEGQLVLGGKRLEGEGYFIAPTVFtEVPPKARIA----QEEIFGPVLSVIRVKDFAEALEVANDTPYGLTG 447
Cdd:cd07129 306 E----ALAAAPGVRVLAGGAAAEGGNQAAPTLF-KVDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEALEGQLTA 380
|
410 420 430
....*....|....*....|....*....|....*...
2J40_B 448 GVYSRKREHLEWAR----REFHVGNLYFNRKITGALVG 481
Cdd:cd07129 381 TIHGEEDDLALAREllpvLERKAGRLLFNGWPTGVEVC 418
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
96-457 |
4.36e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 90.15 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 96 EDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASADVAEAIDFIEYYAR-------AALRYRYPAVEVVPYPGEDNE 168
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaalgdARLLRDGEAVQLGKDPAFQGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 169 SFYVPL-GAGVVIAPWNFP---------VAIFTGMivgpvavgnTVIAKPAEDAVVVGAKVFEIFHEAG-FPPGVVNFLP 237
Cdd:PRK11903 143 HVLVPTrGVALFINAFNFPawglwekaaPALLAGV---------PVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 238 GVGeevgAYLVEHPR-IRFINFTGSLEVGlkiyeAAGRLAPGQTW-FKRAYVETGGKDAIIV--DETAD---FDLAAEGV 310
Cdd:PRK11903 214 GSS----AGLLDHLQpFDVVSFTGSAETA-----AVLRSHPAVVQrSVRVNVEADSLNSALLgpDAAPGseaFDLFVKEV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 311 VVSAYGFQGQK*SAASRLILTQGAYEPVLERVLKRAERLSVG-PAEENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLGG 389
Cdd:PRK11903 285 VREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGnPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDG 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 390 KRLE------GEGYFIAPTVF-TEVPPKARIAQE-EIFGPVLSVIRVKDFAEALEVANDTPYGLTGGVYSRKREHL 457
Cdd:PRK11903 365 GGFAlvdadpAVAACVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFL 440
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
88-458 |
4.40e-16 |
|
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: 80.99 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 88 KTWKDWPQEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEA-SADVAEAID----FIEYYARAALRYRYPAVEVVPY 162
Cdd:cd07127 98 PGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfQAGGPHAQDrgleAVAYAWREMSRIPPTAEWEKPQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 163 PGED----NESFY-VPLGAGVVIAPWNFPV-AIFTGMIVGpVAVGNTVIAKPAEDAVVVGAKVF----EIFHEAGFPPGV 232
Cdd:cd07127 178 GKHDplamEKTFTvVPRGVALVIGCSTFPTwNGYPGLFAS-LATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 233 VNFLP-GVGEEVGAYLVEHPRIRFINFTGSLEVGLKIYEAAGRlapgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVV 311
Cdd:cd07127 257 VTLAAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--------AQVYTEKAGVNTVVVDSTDDLKAMLRNLA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 312 VSAYGFQGQK*SAASRL------ILT-QGA--YEPVLERVLKRAERLSVGPAEENPDLGPVVSAEqerkVLSYIEIGKNE 382
Cdd:cd07127 329 FSLSLYSGQMCTTPQNIyvprdgIQTdDGRksFDEVAADLAAAIDGLLADPARAAALLGAIQSPD----TLARIAEARQL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 383 GQLVLGGKRLEGEGYfiaPTVFTEVP--------PKARIAQEEiFGPVLSVIRVKDFAEALEVANDTPY---GLTGGVYS 451
Cdd:cd07127 405 GEVLLASEAVAHPEF---PDARVRTPlllkldasDEAAYAEER-FGPIAFVVATDSTDHSIELARESVRehgAMTVGVYS 480
|
....*..
2J40_B 452 RKREHLE 458
Cdd:cd07127 481 TDPEVVE 487
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-451 |
1.15e-15 |
|
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: 79.46 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 104 KAAALMRRRKRE-LEATLVYEVG-KNWVEASADVAEAIDFIEYYARAALRYRYPAVeVVP--YPGEDNESFYVPLGAGVV 179
Cdd:cd07126 70 RVAHELRKPEVEdFFARLIQRVApKSDAQALGEVVVTRKFLENFAGDQVRFLARSF-NVPgdHQGQQSSGYRWPYGPVAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 180 IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPPGVVNFLPGVGEEVGAYLVEhPRIRFINFT 259
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 260 GSLEVglkiyeaAGRLApgQTWFKRAYVETGGKD-AIIVDETADFDLAAEGVVVSAYGFQGQK*SAASRLILTQG-AYEP 337
Cdd:cd07126 228 GSSKV-------AERLA--LELHGKVKLEDAGFDwKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 338 VLERVLKRAERLSVgpaeENPDLGPVVSAEQERkVLSYIE-IGKNEGQLVL-GGKRLEGEGYfiaPTVFTEVPPKA---- 411
Cdd:cd07126 299 ILDKLKALAEQRKL----EDLTIGPVLTWTTER-ILDHVDkLLAIPGAKVLfGGKPLTNHSI---PSIYGAYEPTAvfvp 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2J40_B 412 ----------RIAQEEIFGPVLSVIRVKDFAE--ALEVANDTPYGLTGGVYS 451
Cdd:cd07126 371 leeiaieenfELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVS 422
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
177-463 |
6.79e-11 |
|
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: 64.18 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 177 GVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPP-GVVNFLPGVGE---EVGAYLVEH 250
Cdd:cd07121 99 GVIgaITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAgGPDNLVVTVEEptiETTNELMAH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 251 PRIRFINFTGslevGLKIYEAAgrLAPGqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAyGFQ------GQK--- 321
Cdd:cd07121 179 PDINLLVVTG----GPAVVKAA--LSSG----KKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDnnlpciAEKevi 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 322 --*SAASRLI---LTQGAYEPVLERVLKRAERLSVGPAEENPDlgpvvsaeqeRKVlsyieIGKNEGQL-------VLGG 389
Cdd:cd07121 248 avDSVADYLIaamQRNGAYVLNDEQAEQLLEVVLLTNKGATPN----------KKW-----VGKDASKIlkaagieVPAD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2J40_B 390 KRLegegyfiaptVFTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGL--TGGVYSRKREHLEWARRE 463
Cdd:cd07121 313 IRL----------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARA 378
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
95-458 |
2.28e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 62.67 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 95 QEDRSRLLLKAAALMRRRKRELEATLVYEVGKNWVEASadvaeaidFIEYYARAALRYRYPAVEVVPYPGEDNESFYV-- 172
Cdd:cd07081 20 QEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK--------VIKNHFAAEYIYNVYKDEKTCGVLTGDENGGTli 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 173 ---PLGAGVVIAPWNFPVA--IFTGMIVgpVAVGNTVIAKP---AEDAVVVGAK-VFEIFHEAGFPPGVVNFLPGVGEEV 243
Cdd:cd07081 92 iaePIGVVASITPSTNPTStvIFKSLIS--LKTRNSIIFSPhprAKKVTQRAATlLLQAAVAAGAPENLIGWIDNPSIEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 244 GAYLVEHPRIRFINFTGslevGLKIYEAAGRLApgqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAYGFQGQK*S 323
Cdd:cd07081 170 AQRLMKFPGIGLLLATG----GPAVVKAAYSSG------KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 324 AASRLILTQGAYEPVLER-------VLKRAERLSVGPA-EENPDLGPVVSAEQERKVLSYIEIGKNEGQLVLggkrlege 395
Cdd:cd07081 240 SEQSVIVVDSVYDEVMRLfegqgayKLTAEELQQVQPViLKNGDVNRDIVGQDAYKIAAAAGLKVPQETRIL-------- 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2J40_B 396 gyFIAPTVFTEVPPKAriaqEEIFGPVLSVIRVKDFAEALEVA----NDTPYGLTGGVYSRKREHLE 458
Cdd:cd07081 312 --IGEVTSLAEHEPFA----HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIE 372
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
177-463 |
1.36e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 60.30 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 177 GVV--IAPWNFPVAIFTGMIVGPVAVGNTVIAKPAEDAVVVGAKVFEIFHEAGFPP-GVVNFLPGVGE---EVGAYLVEH 250
Cdd:PRK15398 131 GVIgaVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAgGPENLVVTVAEptiETAQRLMKH 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 251 PRIRFINFTGslevGLKIYEAAgrLAPGqtwfKRAYVETGGKDAIIVDETADFDLAAEGVVVSAyGFQ------GQK*-- 322
Cdd:PRK15398 211 PGIALLVVTG----GPAVVKAA--MKSG----KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDnnlpciAEKEvi 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 323 ---SAASRLI---LTQGAYEpVLERVLKRAERLSVGPAEE-NPDLgpvvsaeqerkvlsyieIGKNEGQLvlggkrLEGE 395
Cdd:PRK15398 280 vvdSVADELMrlmEKNGAVL-LTAEQAEKLQKVVLKNGGTvNKKW-----------------VGKDAAKI------LEAA 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2J40_B 396 GYFIAPTV---FTEVPPKARIAQEEIFGPVLSVIRVKDFAEALEVANDTPYGL--TGGVYSRKREHLEWARRE 463
Cdd:PRK15398 336 GINVPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARA 408
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
172-462 |
1.04e-07 |
|
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: 54.03 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 172 VPLG--AGVViaPWNFPV--AIFTGMIvgpvAV--GNTVIAKPAEDAVVVGAKVFEIFHEA----GFPPGVVNFLPGVGE 241
Cdd:cd07122 94 EPVGviAALI--PSTNPTstAIFKALI----ALktRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 242 EVGAYLVEHPRIRFINFTGslevglkiyeaagrlapGQTWFKRAYveTGGKDAI---------IVDETADFDLAAEGVVV 312
Cdd:cd07122 168 ELTQELMKHPDVDLILATG-----------------GPGMVKAAY--SSGKPAIgvgpgnvpaYIDETADIKRAVKDIIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 313 SAyGF-QGQK*SAASRLILTQGAYEPVLERVLKRAerlsvgpaeenpdlGPVVSAEQERKVLSYIE----------IGKN 381
Cdd:cd07122 229 SK-TFdNGTICASEQSVIVDDEIYDEVRAELKRRG--------------AYFLNEEEKEKLEKALFddggtlnpdiVGKS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 382 EGQL--VLGGKRLEGEGYFIAPtvFTEVPPKARIAQEEIFgPVLSVIRVKDFAEALEVAND--TPYGL--TGGVYSRKRE 455
Cdd:cd07122 294 AQKIaeLAGIEVPEDTKVLVAE--ETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKAREllEYGGAghTAVIHSNDEE 370
|
....*...
2J40_B 456 H-LEWARR 462
Cdd:cd07122 371 ViEEFALR 378
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
148-458 |
2.83e-07 |
|
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: 52.61 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 148 AALRYRYPAVEVVP-YPGEDNESFYV---PLGAGVVIAPWNFPVAIFTGMIVGpVAVGNTVIAKPAEDAVVVGAKVFEIF 223
Cdd:cd07077 71 DTERGITASVGHIQdVLLPDNGETYVrafPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 224 HEA---GFPPGVVNFLPGVGEEVGAYLVEHPRIRFINFTGslevGLKIYEAAGRLAPGqtwfKRAYVETGGKDAIIVDET 300
Cdd:cd07077 150 QAAdaaHGPKILVLYVPHPSDELAEELLSHPKIDLIVATG----GRDAVDAAVKHSPH----IPVIGFGAGNSPVVVDET 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 301 ADFDLAAEGVVVSAYgFQGQK*SAASRLILTQGAYEPVLERVlkraerlsvgpaeenpdlgpvvsaeqerkvlsyieigk 380
Cdd:cd07077 222 ADEERASGSVHDSKF-FDQNACASEQNLYVVDDVLDPLYEEF-------------------------------------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2J40_B 381 nEGQLVLGGKRLEGEGYFIAPTVFTEVPPKARiaqeEIFGPVLSVIRVKDFAEALEVANDT----PYGLTGGVYSRKREH 456
Cdd:cd07077 263 -KLKLVVEGLKVPQETKPLSKETTPSFDDEAL----ESMTPLECQFRVLDVISAVENAWMIiesgGGPHTRCVYTHKINK 337
|
..
2J40_B 457 LE 458
Cdd:cd07077 338 VD 339
|
|
| |
