|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1-514 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 982.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 1 MVVEFKNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLVINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFK 80
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 81 AAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGKKVNDR 160
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 161 EGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKE 240
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 241 IGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKC 320
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 321 SACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYFVEPT 400
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 401 IFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGY 480
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
490 500 510
....*....|....*....|....*....|....
gi 1231725153 481 HPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:PRK03137 481 HPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-514 |
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: 856.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 5 FKNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLVINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKE 84
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 85 AYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaHGKKVNDREGEH 164
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL-RGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 165 NQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 245 LVDHIDTHFVTFTGSRATGTRIYERSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACS 324
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 325 RAIVHKDVYDEILEKSVKLTKELTLGNTEDN-TYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDST--GYFVEPTI 401
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPeVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAaeGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 402 FSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYH 481
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|...
gi 1231725153 482 PFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:cd07124 480 PFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-514 |
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: 729.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 5 FKNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLVINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKE 84
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 85 AYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGKKVNDREGEH 164
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 165 NQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 245 LVDHIDTHFVTFTGSRATGTRIYERSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACS 324
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 325 RAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYFVEPTIFS 403
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSaDVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 404 GLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPF 483
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500 510
....*....|....*....|....*....|.
gi 1231725153 484 GGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
35-512 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 571.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 35 QDIPLVINGEKIF--KEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRK 112
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 113 AEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARsMMDLAHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGT 191
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAG-EARRLYGETIpSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 192 TLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSA 271
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 272 vvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN 351
Cdd:COG1012 242 ------ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 352 -TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGT-DDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:COG1012 316 pLDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAvVGYHPFGGFKMSGTDAKtGSPDYLLHFLEQK 508
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETK 473
|
....
gi 1231725153 509 VVSE 512
Cdd:COG1012 474 TVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
50-510 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 554.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDE 129
Cdd:pfam00171 7 ETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 130 AVGDAAEGIDFIEYYARSMMDLaHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAED 209
Cdd:pfam00171 86 ARGEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 210 TPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGG 289
Cdd:pfam00171 165 TPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA------QNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 290 KDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFD 368
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDpDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 369 KIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:pfam00171 319 RVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231725153 448 ITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGyHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADG-LPFGGFKQSGF-GREGGPYGLEEYTEVKTV 459
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
20-514 |
4.44e-172 |
|
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: 494.79 E-value: 4.44e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 20 DMFKEELKKVKGQLGQDIPLVINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAE 99
Cdd:cd07083 2 RAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 100 LMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDL-AHGKKVNDREGEHNQYFYKPIGTGVTI 178
Cdd:cd07083 82 LLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLrYPAVEVVPYPGEDNESFYVGLGAGVVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 179 PPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTG 258
Cdd:cd07083 162 SPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 259 SRATGTRIYERSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILE 338
Cdd:cd07083 242 SLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 339 KSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIF 417
Cdd:cd07083 322 RLLKRAERLSVGPpEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 418 GPV--VGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAKT 495
Cdd:cd07083 402 GPVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKT 481
|
490
....*....|....*....
gi 1231725153 496 GSPDYLLHFLEQKVVSEMF 514
Cdd:cd07083 482 GGPHYLRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-510 |
9.34e-161 |
|
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: 463.22 E-value: 9.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 76 EDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGK 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 156 KVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVP 235
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 236 GDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGF 315
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA------ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 316 SGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDST 393
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 394 -GYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrg 472
Cdd:cd07078 315 kGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN-- 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1231725153 473 CTSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07078 393 DYSVGAEPSaPFGGVKQSGI-GREGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-512 |
1.63e-154 |
|
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: 450.49 E-value: 1.63e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 21 MFKEELKKVKGQLGQDIPLvINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAEL 100
Cdd:cd07125 18 ALADALKAFDEKEWEAIPI-INGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 101 MLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPP 180
Cdd:cd07125 97 LEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 181 WNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSR 260
Cdd:cd07125 177 WNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGST 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 261 ATGTRIyeRSAVVHEGQDFLKrVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKS 340
Cdd:cd07125 257 ETAKLI--NRALAERDGPILP-LIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEML 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 341 VKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYFVEPTIFSGLKSKDriMQEEIFGP 419
Cdd:cd07125 334 KGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFD--LTTEVFGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 420 VVGFV--KVNDFDEAIEVANDTDYGLTGAVIT-NNRE--HWIKAVNeydVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAK 494
Cdd:cd07125 412 ILHVIrfKAEDLDEAIEDINATGYGLTLGIHSrDEREieYWRERVE---AGNLYINRNITGAIVGRQPFGGWGLSGTGPK 488
|
490
....*....|....*...
gi 1231725153 495 TGSPDYLLHFLEQKVVSE 512
Cdd:cd07125 489 AGGPNYLLRFGNEKTVSL 506
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-510 |
2.39e-146 |
|
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: 428.30 E-value: 2.39e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKI--FKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07131 3 IGGEWVdsASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVGDAAEGIDFIEYYA---RSMmdlaHGKKVNDREGEHNQY-FYKPIGTGVTIPPWNFPFAIMAGTTLA 194
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAgegRRL----FGETVPSELPNKDAMtRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 195 PVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVH 274
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 275 egqdflKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TE 353
Cdd:cd07131 239 ------KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDgLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 354 DNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGaTLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVgyH-PFGGFKMSGTDAKTGSPDYLLHFLEQ 507
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV--HlPFGGVKKSGNGHREAGTTALDAFTEW 470
|
...
gi 1231725153 508 KVV 510
Cdd:cd07131 471 KAV 473
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
40-494 |
1.30e-144 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 423.58 E-value: 1.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 40 VINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVM 119
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 120 VYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVA 198
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRL-SGETLpSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 199 GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYeRSAVVHegqd 278
Cdd:cd07097 163 GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIA-AAAAAR---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 279 fLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTY 357
Cdd:cd07097 238 -GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDaLDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 358 MGPVINKKQFDKIKNYIEVGKEEG-KLEQGGG--TDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIE 434
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGaKLVYGGErlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 435 VANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRgcTSAVVGYH-PFGGFKMSGTDAK 494
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNL--PTAGVDYHvPFGGRKGSSYGPR 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
40-497 |
1.52e-136 |
|
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: 403.10 E-value: 1.52e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 40 VINGEKIF-KEDTIESINPANTSQlIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07086 2 VIGGEWVGsGGETFTSRNPANGEP-IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVGDAAEGIDfIEYYA----RSMmdlaHGKKVNDREGEHNQY-FYKPIGTGVTIPPWNFPFAIMAGTTL 193
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMID-ICDYAvglsRML----YGLTIPSERPGHRLMeQWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 APVVAGNTVLLKPAEDTPYTAYKLIEILEEA----GLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYER 269
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 270 SAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTL 349
Cdd:cd07086 235 VA------RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 350 GN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGG--TDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:cd07086 309 GDpLDEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231725153 426 VNDFDEAIEVANDTDYGLTGAVIT---NNREHWIKAvNEYDVGNLYLNRGCTSAVVGYhPFGGFKMSGTDAKTGS 497
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTedlREAFRWLGP-KGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGS 461
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-514 |
4.25e-136 |
|
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: 403.51 E-value: 4.25e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSV-QDNVDMFKEELKKVKGqLGQDIPLVINGEKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKE 84
Cdd:cd07123 2 VNEPVLSYAPgSPERAKLQEALAELKS-LTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 85 AYKSWKTWSASDRAELMLRVAAII--RRRKAEIAAVMVYEaGKPWDEAVGDAA-EGIDFIEYYARSMMDLAHGKKVNDRE 161
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLsgKYRYELNAATMLGQ-GKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 162 GEHNQYFYKPI-GTGVTIPPWNFPfAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKE 240
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 241 IGDYLVDHIDTHFVTFTGSRATGTRIYERSAV-VHEGQDFlKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQK 319
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnLDRYRTY-PRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 320 CSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLE--QGGGTDDSTGYF 396
Cdd:cd07123 318 CSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEiiAGGKCDDSVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 397 VEPTIFSGLKSKDRIMQEEIFGPVVGfVKV---NDFDEAIEVANDT-DYGLTGAVITNNRehwiKAVNE------YDVGN 466
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLT-VYVypdSDFEETLELVDTTsPYALTGAIFAQDR----KAIREatdalrNAAGN 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1231725153 467 LYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:cd07123 473 FYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-510 |
1.02e-134 |
|
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: 398.18 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKI--FKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07088 2 INGEFVpsSSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAgTTLAP-VV 197
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIA-RKLAPaLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 198 AGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegq 277
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 278 DFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNT 356
Cdd:cd07088 234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDpFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 357 YMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDST-GYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIE 434
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231725153 435 VANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHpfGGFKMSGT---DAKTGspdyLLHFLEQKVV 510
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHG----LEEYLQTKVV 466
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
55-511 |
8.15e-134 |
|
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: 395.26 E-value: 8.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:cd07103 2 INPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYA----RSmmdlaHGKKVNDREGEHNQYFYK-PIGTGVTIPPWNFPFAiMAGTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07103 81 DYAASFLEWFAeearRI-----YGRTIPSPAPGKRILVIKqPVGVVAAITPWNFPAA-MITRKIAPALAaGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 209 DTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMG 288
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 289 GKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQF 367
Cdd:cd07103 229 GNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNgLDEGTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 368 DKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07103 309 EKVEALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231725153 447 VITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGyhPFGGFKMSGTdAKTGSPDYLLHFLEQKVVS 511
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDAEA--PFGGVKESGL-GREGGKEGLEEYLETKYVS 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-510 |
6.79e-126 |
|
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: 375.36 E-value: 6.79e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV-G 132
Cdd:cd07093 1 NFNPA-TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 133 DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMagtT--LAPVVA-GNTVLLKPAED 209
Cdd:cd07093 80 DIPRAAANFRFFA-DYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLL---TwkIAPALAfGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 210 TPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGG 289
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA------PNLKPVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 290 KDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDN-TYMGPVINKKQFD 368
Cdd:cd07093 230 KNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPdTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 369 KIKNYIEVGKEEG-KLEQGGGTDDS----TGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07093 310 KVLGYVELARAEGaTILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231725153 444 TGAVITNNREHWIKAVNEYDVGNLYLN----RGCTSavvgyhPFGGFKMSGTDAKTGspDYLLHF-LEQKVV 510
Cdd:cd07093 390 AAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDLRT------PFGGVKASGIGREGG--DYSLEFyTELKNV 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
39-490 |
1.50e-125 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 375.01 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEkiFKE----DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYK--SWKTWSASDRAELMLRVAAIIRRRK 112
Cdd:cd07091 6 LFINNE--FVDsvsgKTFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 113 AEIAAVMVYEAGKPWDE-AVGDAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGT 191
Cdd:cd07091 83 DELAALESLDNGKPLEEsAKGDVALSIKCLRYYA-GWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPL-LMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 192 TLAP-VVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERS 270
Cdd:cd07091 161 KLAPaLAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 271 AvvhegQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLG 350
Cdd:cd07091 241 A-----KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 351 NTED-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07091 316 DPFDpDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgcTSAVVGYH-PFGGFKMSG 490
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
6-514 |
3.03e-124 |
|
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: 373.74 E-value: 3.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSVQDNV-DMFKEELKKVKGQLgQDIPLVINGEKIFKED-TIESINPANTSQLIAKASKATTTDVEDAFKAAK 83
Cdd:TIGR01236 1 ANEPVLPFRPGSPErDLLRKSLKELKSSS-LEIPLVIGGEEVYDSNeRIPQVNPHNHQAVLAKATNATEEDAMKAVEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 84 EAYKSWKTWSASDRAELMLRVAAIIR-RRKAEIAAV-MVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaHGKKVNDRE 161
Cdd:TIGR01236 80 DAKKDWSNLPFYDRAAIFLKAADLLSgPYRYEILAAtMLGQSKTVYQAEIDAVAELIDFFRFNVKYAREL-YAQQPISAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 162 GEHNQYFYKPI-GTGVTIPPWNFpFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKE 240
Cdd:TIGR01236 159 GEWNRTEYRPLeGFVYAISPFNF-TAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 241 IGDYLVDHIDTHFVTFTGSRATGTRIYERSAV-VHEGQDFlKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQK 319
Cdd:TIGR01236 238 VSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQnLDRYHNF-PRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 320 CSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGK---EEGKLEQGGGTDDSTGY 395
Cdd:TIGR01236 317 CSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDfRGFMGAVIDEQSFDKIVKYIEDAKkdpEALTILYGGKYDDSQGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 396 FVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND--FDEAIEVA-NDTDYGLTGAVITNNREHWIKAVN--EYDVGNLYLN 470
Cdd:TIGR01236 397 FVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVdSTSQYGLTGAVFAKDRKAILEADKklRFAAGNFYIN 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1231725153 471 RGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:TIGR01236 477 DKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETF 520
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
80-510 |
4.30e-123 |
|
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: 365.01 E-value: 4.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 80 KAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAHGKKVND 159
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 160 REGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPK 239
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 240 EIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQK 319
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAA------ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 320 CSACSRAIVHKDVYDEILEKSVkltkeltlgntedntymgpvinkkqfdkiknyievgkeegkleqgggtddstgyfvep 399
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 400 TIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVG 479
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 1231725153 480 YhPFGGFKMSGTDAKtGSPDYLLHFLEQKVV 510
Cdd:cd06534 337 A-PFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-490 |
5.62e-122 |
|
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: 365.67 E-value: 5.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKI--FKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07138 3 IDGAWVapAGTETIDVINPA-TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVGDAAE-GIDFIEYYARSMMDLAHGKKVND----REgehnqyfykPIGTGVTIPPWNFPFAIMAGTTL 193
Cdd:cd07138 82 ITLEMGAPITLARAAQVGlGIGHLRAAADALKDFEFEERRGNslvvRE---------PIGVCGLITPWNWPLNQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 APVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvv 273
Cdd:cd07138 153 PALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 274 hegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTE 353
Cdd:cd07138 231 ----DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 354 D-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG-GTDD--STGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07138 307 DpATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGpGRPEglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVgyhPFGGFKMSG 490
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA---PFGGYKQSG 445
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
55-511 |
8.38e-120 |
|
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: 359.15 E-value: 8.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYARsmMDLAHgKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTtLAP-VVAGNTVLLKPAEDTPYT 213
Cdd:cd07106 81 GGAVAWLRYTAS--LDLPD-EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWK-IAPaLLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 214 AYKLIEILEEAgLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAI 293
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAA------KTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 294 VVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKN 372
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDgLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 373 YIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNN 451
Cdd:cd07106 309 LVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 452 REHWIKAVNEYDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVS 511
Cdd:cd07106 389 LERAEAVARRLEAGTVWIN---THGALDPDaPFGGHKQSGIGVEFG-IEGLKEYTQTQVIN 445
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-510 |
1.41e-119 |
|
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: 359.17 E-value: 1.41e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:cd07114 1 SINPA-TGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFIEYYArSMMDLAHGKKVNDREGE-HNQYFYKPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPAED 209
Cdd:cd07114 80 AQVRYLAEWYRYYA-GLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLA-KKLAPALAaGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 210 TPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGG 289
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA------ENLAPVTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 290 KDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFD 368
Cdd:cd07114 232 KSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDpETQMGPLATERQLE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 369 KIKNYIEVGKEEG-KLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07114 312 KVERYVARAREEGaRVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 444 TGAVITNN--REHwiKAVNEYDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07114 392 AAGIWTRDlaRAH--RVARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIGRENGI-EAIREYTQTKSV 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
54-490 |
6.52e-119 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 357.31 E-value: 6.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKS-WKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVG 132
Cdd:cd07109 1 VFDPS-TGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 133 DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPfAIMAGTTLAPVVA-GNTVLLKPAEDTP 211
Cdd:cd07109 80 DVEAAARYFEYYG-GAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYP-LQITGRSVAPALAaGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 212 YTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTriyersAVVHEGQDFLKRVIAEMGGKD 291
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGI------AVMRAAAENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 292 AIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIK 371
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 372 NYIEVGKEEGKLEQGGGT----DDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:cd07109 312 GFVARARARGARIVAGGRiaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1231725153 448 ITNN--REHWIkaVNEYDVGNLYLNRGCTSAVVGYhPFGGFKMSG 490
Cdd:cd07109 392 WTRDgdRALRV--ARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
74-490 |
2.81e-118 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 354.91 E-value: 2.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 74 DVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAH 153
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILRE-AAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 154 GKKV-NDREGEHNQYFYKPIGT-GVtIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTPYT-AYKLIEILEEAGLPKG 229
Cdd:cd07104 80 GEILpSDVPGKESMVRRVPLGVvGV-ISPFNFPL-ILAMRSVAPALAlGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 230 VVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIV 309
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDLAVSAAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 310 TSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG 387
Cdd:cd07104 232 FGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDpRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 388 GTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNL 467
Cdd:cd07104 312 TYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
410 420
....*....|....*....|....
gi 1231725153 468 YLNrgCTSAVVGYH-PFGGFKMSG 490
Cdd:cd07104 389 HIN--DQTVNDEPHvPFGGVKASG 410
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
50-507 |
3.11e-117 |
|
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: 353.45 E-value: 3.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWkTWSASDRAE---LMLRVAAIIRRRKAEIAAVMVYEAGKP 126
Cdd:cd07112 2 ETFATINPA-TGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAErkaVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 127 WDEAV-GDAAEGIDFIEYYARSMmDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPfAIMAGTTLAPVVA-GNTVLL 204
Cdd:cd07112 80 ISDALaVDVPSAANTFRWYAEAI-DKVYGEVAPTGPDALALITREPLGVVGAVVPWNFP-LLMAAWKIAPALAaGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 205 KPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSavvheGQDFLKRVI 284
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS-----GQSNLKRVW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 285 AEMGGKDA-IVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVI 362
Cdd:cd07112 233 LECGGKSPnIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 363 NKKQFDKIKNYIEVGKEEG-KLEQGGGTD--DSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDT 439
Cdd:cd07112 313 SEAHFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 440 DYGLTGAVITNN--REH----WIKA----VNEYDVGNLylnrgcTSavvgyhPFGGFKMSGtdaktGSPDYLLHFLEQ 507
Cdd:cd07112 393 VYGLAASVWTSDlsRAHrvarRLRAgtvwVNCFDEGDI------TT------PFGGFKQSG-----NGRDKSLHALDK 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
54-490 |
1.00e-114 |
|
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: 346.73 E-value: 1.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVG- 132
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 133 DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTP 211
Cdd:cd07115 80 DVPRAADTFRYYA-GWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPL-MFAAWKVAPALAaGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 212 YTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKD 291
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA------GNLKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 292 AIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKI 370
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDpKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 371 KNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVIT 449
Cdd:cd07115 312 LDYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1231725153 450 NN--REH-----------WIKAVNEYDVGNlylnrgctsavvgyhPFGGFKMSG 490
Cdd:cd07115 392 RDlgRAHrvaaalkagtvWINTYNRFDPGS---------------PFGGYKQSG 430
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
55-510 |
1.22e-114 |
|
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: 346.54 E-value: 1.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWkTWS--ASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKP------ 126
Cdd:cd07089 2 INPA-TEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWStdAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtara 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 127 --WD---EAVGDAAEGIDFIEYY----ARSMMDLAHGKKVnDREgehnqyfykPIGTGVTIPPWNFPFAIMAGTTLAPVV 197
Cdd:cd07089 80 mqVDgpiGHLRYFADLADSFPWEfdlpVPALRGGPGRRVV-RRE---------PVGVVAAITPWNFPFFLNLAKLAPALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 198 AGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegq 277
Cdd:cd07089 150 AGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 278 DFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NT 356
Cdd:cd07089 224 ATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADpGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 357 YMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDS--TGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAI 433
Cdd:cd07089 304 VMGPLISAAQRDRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAV 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231725153 434 EVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVvgYHPFGGFKMSGTDAKTGsPDYLLHFLEQKVV 510
Cdd:cd07089 384 RIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLGRENG-IEGLEEFLETKSI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
50-510 |
6.77e-114 |
|
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: 344.94 E-value: 6.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAY--KSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKP- 126
Cdd:cd07139 14 ETIDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 127 WDEAVGDAAEGIDFIEYYARSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTtLAP-VVAGNTVLLK 205
Cdd:cd07139 93 SWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALK-IAPaLAAGCTVVLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 206 PAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIA 285
Cdd:cd07139 172 PSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG------ERLARVTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 286 EMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINK 364
Cdd:cd07139 245 ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDpLDPATQIGPLASA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 365 KQFDKIKNYIEVGKEEG-KLEQGGG--TDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:cd07139 325 RQRERVEGYIAKGRAEGaRLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 442 GLTGAVITNNREHWIKAVNEYDVGNLYLNrgctSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07139 405 GLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDAYLETKSI 469
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
52-491 |
3.61e-113 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 342.65 E-value: 3.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 52 IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:cd07149 1 IEVISPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFIEYYARSMMDLaHGKKVN---DREGEHNQYFYK--PIGTGVTIPPWNFPFAIMA---GTTLApvvAGNTVL 203
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRL-AGETIPfdaSPGGEGRIGFTIrePIGVVAAITPFNFPLNLVAhkvGPAIA---AGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 204 LKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqdfLKRV 283
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 284 IAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVI 362
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDpLDEDTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 363 NKKQFDKIKNYIEVGKEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:cd07149 308 SEAEAERIEEWVEEAVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1231725153 442 GLTGAVITNNREHWIKAVNEYDVGNLYLNRGcTSAVVGYHPFGGFKMSGT 491
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMINDS-STFRVDHMPYGGVKESGT 433
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
53-490 |
3.71e-113 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 342.39 E-value: 3.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 53 ESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVG 132
Cdd:cd07150 2 DDLNPA-DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 133 DAAEGIDFIEYyARSMMDLAHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTP 211
Cdd:cd07150 81 ETTFTPELLRA-AAGECRRVRGETLpSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 212 YTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVvhegqdFLKRVIAEMGGKD 291
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR------HLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 292 AIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKI 370
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDpDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 371 KNYIEVGKEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVIT 449
Cdd:cd07150 314 KRQVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1231725153 450 NNREHWIKAVNEYDVGNLYLNrgCTSAVVGYH-PFGGFKMSG 490
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHIN--DPTILDEAHvPFGGVKASG 430
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
35-490 |
6.89e-113 |
|
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: 342.85 E-value: 6.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 35 QDIPLVINGEKIFKED--TIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKT-WSASDRAELMLRVAAIIRRR 111
Cdd:cd07144 6 QPTGLFINNEFVKSSDgeTIKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADLVEKN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 112 KAEIAAVMVYEAGKPWDE-AVGDAAEGIDFIEYYARSMmDLAHGKKVndrEGEHNQYFY---KPIGTGVTIPPWNFPFAi 187
Cdd:cd07144 85 RDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWA-DKIQGKTI---PTSPNKLAYtlhEPYGVCGQIIPWNYPLA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 188 MAGTTLAPVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRI 266
Cdd:cd07144 160 MAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 267 YERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKE 346
Cdd:cd07144 240 MKAAA------QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 347 -LTLGNT-EDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG---GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPV 420
Cdd:cd07144 314 nYKVGSPfDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 421 VGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVvgYHPFGGFKMSG 490
Cdd:cd07144 394 VVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
55-512 |
3.15e-112 |
|
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: 340.10 E-value: 3.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYARSMMDLAHGKKVN---DREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDT 210
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAvplPSEDFKARVRREPVGVVGLITPWNFPL-LMAAWKVAPALAaGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegQDfLKRVIAEMGGK 290
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-----QD-IKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 291 DAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT-EDNTYMGPVINKKQFDK 369
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 370 IKNYIEVGKEEG-KLEQGGGTDD--STGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231725153 447 VITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGsPDYLLHFLEQKVVSE 512
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIGRELG-EWGLDNYLEVKQITR 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
51-510 |
4.42e-112 |
|
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: 340.86 E-value: 4.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 51 TIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYK---SWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPW 127
Cdd:cd07141 23 TFPTINPA-TGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 128 DEA-VGDAAEGIDFIEYYArSMMDLAHGKKVnDREGEHNQYF-YKPIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLL 204
Cdd:cd07141 102 SKSyLVDLPGAIKVLRYYA-GWADKIHGKTI-PMDGDFFTYTrHEPVGVCGQIIPWNFPL-LMAAWKLAPALAcGNTVVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 205 KPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSavvheGQDFLKRVI 284
Cdd:cd07141 179 KPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA-----GKSNLKRVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 285 AEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT-EDNTYMGPVIN 363
Cdd:cd07141 254 LELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPfDPKTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 364 KKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:cd07141 334 EEQFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 443 LTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07141 414 LAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGE-YGLQEYTEVKTV 478
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
41-508 |
1.10e-110 |
|
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: 336.98 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKI--FKEDTIESINPANTSqLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAEIA 116
Cdd:cd07119 2 IDGEWVeaASGKTRDIINPANGE-VIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 117 AVMVYEAGKPWDEAVGDAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTLAP- 195
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYA-GLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPL-LQAAWKLAPa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 196 VVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhe 275
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 276 gqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED- 354
Cdd:cd07119 235 --GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 355 NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDF 429
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGaRLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 430 DEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRgctsavvgYH------PFGGFKMSGTDAKTGsPDYLLH 503
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--------YHpyfaeaPWGGYKQSGIGRELG-PTGLEE 463
|
....*
gi 1231725153 504 FLEQK 508
Cdd:cd07119 464 YQETK 468
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
55-490 |
1.61e-110 |
|
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: 335.81 E-value: 1.61e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:cd07090 2 IEPA-TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYArsmmDLAHgkkvnDREGEHNQ-----YFY---KPIGTGVTIPPWNFPFAImAGTTLAPVVA-GNTVLLK 205
Cdd:cd07090 81 DSSADCLEYYA----GLAP-----TLSGEHVPlpggsFAYtrrEPLGVCAGIGAWNYPIQI-ASWKSAPALAcGNAMVYK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 206 PAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIA 285
Cdd:cd07090 151 PSPFTPLTALLLAEILTEAGLPDGVFNVVQGG-GETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 286 EMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDN-TYMGPVINK 364
Cdd:cd07090 224 ELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEdTQMGALISE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 365 KQFDKIKNYIEVGKEEG-KLEQGGGTDDST-----GYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:cd07090 304 EHLEKVLGYIESAKQEGaKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRAND 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1231725153 439 TDYGLTGAVITNN--REHwiKAVNEYDVGNLYLNR-GCTSAVVgyhPFGGFKMSG 490
Cdd:cd07090 384 TTYGLAAGVFTRDlqRAH--RVIAQLQAGTCWINTyNISPVEV---PFGGYKQSG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
55-511 |
5.31e-110 |
|
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: 334.71 E-value: 5.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPW-DEAVGD 133
Cdd:cd07108 2 INPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 134 AAEGIDFIEYYArsmmDLAHGKKVNDREGEHNQYFY---KPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:cd07108 81 AAVLADLFRYFG----GLAGELKGETLPFGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGK 290
Cdd:cd07108 157 PLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA------DRLIPVSLELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 291 DAIVVDENVDTDLAAEAIVTSA-FGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDN-TYMGPVINKKQFD 368
Cdd:cd07108 230 SPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEaTDIGAIISEKQFA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 369 KIKNYIEVGKE--EGKLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:cd07108 310 KVCGYIDLGLStsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 443 LTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAV-VGYhpfGGFKMSGTdAKTGSPDYLL-HFLEQKVVS 511
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPgQSY---GGFKQSGL-GREASLEGMLeHFTQKKTVN 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
54-510 |
7.97e-109 |
|
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: 331.65 E-value: 7.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGD 133
Cdd:cd07107 1 VINPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 134 AAEGIDFIEYYARSMMDLaHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYT 213
Cdd:cd07107 80 VMVAAALLDYFAGLVTEL-KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 214 AYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIyERSAVvhegqDFLKRVIAEMGGKDAI 293
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAI-MRAAA-----EGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 294 VVDENVDTDLAAEAIVTSA-FGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIK 371
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDpTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 372 NYIEVGKEEG-KLEQGGGTDD----STGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07107 312 HYIDSAKREGaRLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 447 VITNNREHWIKAVNEYDVGNLYLNRgctsavVGYH----PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWING------SSRHflgaPFGGVKNSGIGREECL-EELLSYTQEKNV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
55-491 |
2.02e-108 |
|
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: 330.44 E-value: 2.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGD- 133
Cdd:cd07092 2 VDPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 134 AAEGIDFIEYYA---RSMmdlaHGKKVNDREGEHNQYFYK-PIGTGVTIPPWNFPFAiMAGTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07092 81 LPGAVDNFRFFAgaaRTL----EGPAAGEYLPGHTSMIRRePIGVVAQIAPWNYPLM-MAAWKIAPALAaGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 209 DTPYTAYKLIEILEEaGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMG 288
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA------DTLKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 289 GKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQF 367
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDeDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 368 DKIKNYIEVGKEEGKLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:cd07092 309 ERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1231725153 448 ITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGT 491
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-511 |
3.68e-108 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 345.65 E-value: 3.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLvINGEKifkeDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEA 85
Cdd:PRK11904 523 KNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPI-INGEG----EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 86 YKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYA---RSMMdlAHGKKVNDREG 162
Cdd:PRK11904 598 FPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAaqaRRLF--GAPEKLPGPTG 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 163 EHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIG 242
Cdd:PRK11904 676 ESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVG 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 243 DYLVDHIDTHFVTFTGSRATGTRIyERSAVVHEGQdfLKRVIAEMGGKDAIVVD-----ENVDTDlaaeaIVTSAFGFSG 317
Cdd:PRK11904 756 AALTADPRIAGVAFTGSTETARII-NRTLAARDGP--IVPLIAETGGQNAMIVDstalpEQVVDD-----VVTSAFRSAG 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 318 QKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDST--G 394
Cdd:PRK11904 828 QRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTenG 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 395 YFVEPTIFSgLKSKDRImQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAV---ITNNREHWIKAVNeydVGNLYL 469
Cdd:PRK11904 908 HFVAPTAFE-IDSISQL-EREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIhsrIEETADRIADRVR---VGNVYV 982
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1231725153 470 NRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVS 511
Cdd:PRK11904 983 NRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
49-490 |
2.72e-106 |
|
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: 325.41 E-value: 2.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 49 EDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKP-- 126
Cdd:cd07151 9 ERTIDVLNPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTri 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 127 -----WDEAVGDAAEgidfieyyARSMMDLAHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNFPFAiMAGTTLAPVVA-G 199
Cdd:cd07151 88 kanieWGAAMAITRE--------AATFPLRMEGRILpSDVPGKENRVYREPLGVVGVISPWNFPLH-LSMRSVAPALAlG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 200 NTVLLKPAEDTPYTAYKLI-EILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqD 278
Cdd:cd07151 159 NAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG------R 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 279 FLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTY 357
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDpSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 358 MGPVINKKQFDKIKNYIEVGKEEGKLEQGGGtdDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAN 437
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG--EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1231725153 438 DTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCT--SAVVgyhPFGGFKMSG 490
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVndEPHV---PFGGEKNSG 442
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-511 |
3.02e-106 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 342.69 E-value: 3.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLvINGEKIfKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEA 85
Cdd:COG4230 528 RNSAGLDLSDEAVLAALSAALAAAAEKQWQAAPL-IAGEAA-SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAA 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 86 YKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMmdlahgkkvndREGEHN 165
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQA-----------RRLFAA 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 166 QYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYL 245
Cdd:COG4230 675 PTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAAL 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 246 VDHIDTHFVTFTGSRATGTRIyERSAVVHEGQDflkrV--IAEMGGKDAIVVD-----ENVDTDlaaeaIVTSAFGFSGQ 318
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLI-NRTLAARDGPI----VplIAETGGQNAMIVDssalpEQVVDD-----VLASAFDSAGQ 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 319 KCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKL--EQGGGTDDSTGY 395
Cdd:COG4230 825 RCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADlSTDVGPVIDAEARANLEAHIERMRAEGRLvhQLPLPEECANGT 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 396 FVEPTIFSgLKSKDRImQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGC 473
Cdd:COG4230 905 FVAPTLIE-IDSISDL-EREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNI 982
|
490 500 510
....*....|....*....|....*....|....*...
gi 1231725153 474 TSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVS 511
Cdd:COG4230 983 IGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVT 1020
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
37-489 |
3.11e-102 |
|
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: 315.23 E-value: 3.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 37 IPLVINGEKIFKEDT--IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:cd07085 1 LKLFINGEWVESKTTewLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAHGKKVNDREGEHNQYFYK-PIGTGVTIPPWNFPFAI-MAGTT 192
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIpLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 193 LApVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAv 272
Cdd:cd07085 159 MA-IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGG-KEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 vhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN- 351
Cdd:cd07085 236 -----ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 352 TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG------GTDDstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFV 424
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGrgvkvpGYEN--GNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231725153 425 KVNDFDEAIEVANDTDYGlTGAVI-TNNREHWIKAVNEYDVGNLYLNRGCtsAV-VGYHPFGGFKMS 489
Cdd:cd07085 389 RVDTLDEAIAIINANPYG-NGAAIfTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGS 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
39-490 |
4.29e-102 |
|
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: 315.05 E-value: 4.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKI--FKEDTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIA 116
Cdd:cd07559 3 NFINGEWVapSKGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 117 AVMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTLAP 195
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFA-GVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPL-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 196 VVA-GNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvh 274
Cdd:cd07559 160 ALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 275 egqDFLKRVIAEMGGKDA-I----VVDENVDTDLAAEAIVTsAFGF-SGQKCSACSRAIVHKDVYDEILEKSVKLTKELT 348
Cdd:cd07559 236 ---ENLIPVTLELGGKSPnIffddAMDADDDFDDKAEEGQL-GFAFnQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 349 LGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGG----TDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVG 422
Cdd:cd07559 312 VGNPLDpETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 423 FVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
31-510 |
4.56e-102 |
|
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: 314.85 E-value: 4.56e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 31 GQLGQDIPLVINGE--KIFKEDTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYK-SW-KTWSASDRAELMLRVAA 106
Cdd:cd07143 1 GKYEQPTGLFINGEfvDSVHGGTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 107 IIRRRKAEIAAVMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPF 185
Cdd:cd07143 80 LMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYG-GWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 186 aIMAGTTLAPVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGT 264
Cdd:cd07143 159 -LMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 265 RIYERSAvvhegQDFLKRVIAEMGGKDAIVVDENVDTDlaaEAIVTSAFGF---SGQKCSACSRAIVHKDVYDEILEKSV 341
Cdd:cd07143 238 KVMEAAA-----KSNLKKVTLELGGKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 342 KLTKELTLGNT-EDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGP 419
Cdd:cd07143 310 EKAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 420 VVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpd 499
Cdd:cd07143 390 VVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIGRELGE-- 465
|
490
....*....|..
gi 1231725153 500 YLLH-FLEQKVV 510
Cdd:cd07143 466 YALEnYTQIKAV 477
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
50-490 |
2.04e-101 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 313.36 E-value: 2.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDE 129
Cdd:PRK13252 22 ETFEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 130 A-VGDAAEGIDFIEYYArsmmDLA---HGKKVNDREGehnQYFY---KPIGTGVTIPPWNFPFAImAGTTLAP-VVAGNT 201
Cdd:PRK13252 101 TsVVDIVTGADVLEYYA----GLApalEGEQIPLRGG---SFVYtrrEPLGVCAGIGAWNYPIQI-ACWKSAPaLAAGNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 202 VLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVhegqdfLK 281
Cdd:PRK13252 173 MIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS------LK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 282 RVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGP 360
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDpATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 361 VINKKQFDKIKNYIEVGKEEG-KLEQGGG--TDDS--TGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEV 435
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGaRLLCGGErlTEGGfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIAR 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 436 ANDTDYGLTGAVITN--NREHwiKAVNEYDVGNLYLNR-GCTSAVVgyhPFGGFKMSG 490
Cdd:PRK13252 406 ANDTEYGLAAGVFTAdlSRAH--RVIHQLEAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
50-510 |
2.45e-100 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 311.24 E-value: 2.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDE 129
Cdd:PLN02278 40 KTFPVYNPA-TGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 130 AVGDAAEGIDFIEYYA----RSMMDLAHGKKVNDREGEHNQyfykPIGTGVTIPPWNFPFAIM---AGTTLApvvAGNTV 202
Cdd:PLN02278 119 AIGEVAYGASFLEYFAeeakRVYGDIIPSPFPDRRLLVLKQ----PVGVVGAITPWNFPLAMItrkVGPALA---AGCTV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKR 282
Cdd:PLN02278 192 VVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATVKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPV 361
Cdd:PLN02278 266 VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDgFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 362 INKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 441 YGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGyhPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:PLN02278 426 AGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGL-GREGSKYGIDEYLEIKYV 492
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
55-510 |
8.73e-100 |
|
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: 308.11 E-value: 8.73e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVG 132
Cdd:cd07118 2 RSPA-HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 133 DAAEGIDFIEYYARSMMDLaHGKKVND----------REgehnqyfykPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTV 202
Cdd:cd07118 81 EIEGAADLWRYAASLARTL-HGDSYNNlgddmlglvlRE---------PIGVVGIITPWNFPFLILSQKLPFALAAGCTV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKR 282
Cdd:cd07118 151 VVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA------RNLKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT-EDNTYMGPV 361
Cdd:cd07118 225 VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 362 INKKQFDKIKNYIEVGKEEG-KLEQGGGTDDS-TGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDT 439
Cdd:cd07118 305 INEAQLAKITDYVDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDT 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231725153 440 DYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgctSAVVGYH--PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07118 385 VYGLSAGVWSKDIDTALTVARRIRAGTVWVN----TFLDGSPelPFGGFKQSGIGRELGR-YGVEEYTELKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-490 |
1.45e-99 |
|
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: 308.35 E-value: 1.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGE-KIFKEDTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSW-KTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07082 6 INGEwKESSGKTIEVYSPID-GEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaHGKKVNDREGEHNQ----YFYK-PIGTGVTIPPWNFPFAImAGTTL 193
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGDSLPGDWFPGTKgkiaQVRRePLGVVLAIGPFNYPLNL-TVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 AP-VVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAV 272
Cdd:cd07082 163 IPaLIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 vhegqdflKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT 352
Cdd:cd07082 243 --------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 353 EDN-TYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTgyFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07082 315 WDNgVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCtSAVVGYHPFGGFKMSG 490
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC-QRGPDHFPFLGRKDSG 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
39-490 |
3.50e-98 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 304.52 E-value: 3.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKIFKEDTIESI-NPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAA 117
Cdd:PRK13473 5 LLINGELVAGEGEKQPVyNPA-TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 118 VMVYEAGKPWDEAVGD----AAEGIDFIEYYARSMmdlaHGKKVNDREGEHNQYFYK-PIGTGVTIPPWNFPFaIMAGTT 192
Cdd:PRK13473 84 LESLNCGKPLHLALNDeipaIVDVFRFFAGAARCL----EGKAAGEYLEGHTSMIRRdPVGVVASIAPWNYPL-MMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 193 LAPVVA-GNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSA 271
Cdd:PRK13473 159 LAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 272 vvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN 351
Cdd:PRK13473 238 ------DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 352 TED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLE--QGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:PRK13473 312 PDDeDTELGPLISAAHRDRVAGFVERAKALGHIRvvTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNN--REHWIKAVNEYdvgnlylnrGCTSavVGYH-------PFGGFKMSG 490
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDvgRAHRVSARLQY---------GCTW--VNTHfmlvsemPHGGQKQSG 451
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
39-510 |
5.79e-98 |
|
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: 304.42 E-value: 5.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKI--FKEDTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYK--SWKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:cd07142 6 LFINGQFVdaASGKTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWDEA-VGDAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTL 193
Cdd:cd07142 85 LAALETWDNGKPYEQArYAEVPLAARLFRYYA-GWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPL-LMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 APVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAv 272
Cdd:cd07142 163 GPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 vhegQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT 352
Cdd:cd07142 242 ----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 353 EDNTY-MGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07142 318 FRKGVeQGPQVDKEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGI-YALNNYLQVKAV 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
39-512 |
1.25e-97 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 304.35 E-value: 1.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKI--FKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAY-----KSWKTWSASDRAELMLRVAAIIRRR 111
Cdd:PLN02467 10 LFIGGEWRepVLGKRIPVVNPA-TEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 112 KAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmDLAHGKKVNDREG------EHNQYFYK-PIGTGVTIPPWNFP 184
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYA----DLAEALDAKQKAPvslpmeTFKGYVLKePLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 185 FaIMAGTTLAPVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATG 263
Cdd:PLN02467 165 L-LMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 264 TRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKL 343
Cdd:PLN02467 244 RKIMTAAA------QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 344 TKELTLGNT-EDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGT---DDSTGYFVEPTIFSGLKSKDRIMQEEIFGP 419
Cdd:PLN02467 318 AKNIKISDPlEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpeHLKKGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 420 VVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGsPD 499
Cdd:PLN02467 398 VLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELG-EW 474
|
490
....*....|...
gi 1231725153 500 YLLHFLEQKVVSE 512
Cdd:PLN02467 475 GLENYLSVKQVTK 487
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
52-511 |
3.47e-97 |
|
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: 301.57 E-value: 3.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 52 IESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA- 130
Cdd:cd07145 1 IEVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 131 --VGDAAEGIDFIEYYARSMmdlaHGKKVNDREGEHNQYFY-----KPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTV 202
Cdd:cd07145 80 veVERTIRLFKLAAEEAKVL----RGETIPVDAYEYNERRIaftvrEPIGVVGAITPFNFPANLFA-HKIAPAIAvGNSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVhegqdfLKR 282
Cdd:cd07145 155 VVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPV 361
Cdd:cd07145 229 VALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDeSTDLGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 362 INKKQFDKIKNYIEVGKEEG-KLEQGGGTDDstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:cd07145 309 ISPEAVERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 441 YGLTGAVITNNREHWIKAVNEYDVGNLYLNrGCTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVVS 511
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI-GREGVRYTMLEMTEEKTIV 455
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-512 |
1.71e-96 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 316.81 E-value: 1.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLVINGEKifKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEA 85
Cdd:PRK11905 525 RNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGGDV--DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 86 YKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmdlAHGKKVNDREGEhn 165
Cdd:PRK11905 603 FPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYA------AQARRLLNGPGH-- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 166 qyfyKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYL 245
Cdd:PRK11905 675 ----KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 246 VDHIDTHFVTFTGSRATGTRIyERSAVVHEGQDFLkrVIAEMGGKDAIVVD-----ENVDTDlaaeaIVTSAFGFSGQKC 320
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLI-QRTLAKRSGPPVP--LIAETGGQNAMIVDssalpEQVVAD-----VIASAFDSAGQRC 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 321 SA----CsraiVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEGKL--EQGGGTDDST 393
Cdd:PRK11905 823 SAlrvlC----LQEDVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETEK 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 394 GYFVEPTIF--SGLkskdRIMQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITnnR-----EHWIKAVNeydV 464
Cdd:PRK11905 899 GTFVAPTLIeiDSI----SDLEREVFGPVLHVVrfKADELDRVIDDINATGYGLTFGLHS--RidetiAHVTSRIR---A 969
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1231725153 465 GNLYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSE 512
Cdd:PRK11905 970 GNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPI 1017
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-510 |
2.45e-96 |
|
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: 300.13 E-value: 2.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKIFKEDT--IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKS-WKTWSASDRAELMLRVAAIIRRRKAEIAA 117
Cdd:cd07113 4 IDGRPVAGQSEkrLDITNPA-TEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 118 VMVYEAGKPWDEAVG-DAAEGIDFIEYYARSMMDLAhGKKVN----DREGEHNQYFY--KPIGTGVTIPPWNFPFAIMAG 190
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKIN-GETLApsipSMQGERYTAFTrrEPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 191 TTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIyERS 270
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK-GAVGAQLISHPDVAKVSFTGSVATGKKI-GRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 271 AVVHegqdfLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLG 350
Cdd:cd07113 240 AASD-----LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 351 N-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07113 315 SpMDESVMFGPLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGC--TSAVvgyhPFGGFKMSGTDAKTGSpDYLLHFLE 506
Cdd:cd07113 395 EEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS-AFIDDYTE 469
|
....
gi 1231725153 507 QKVV 510
Cdd:cd07113 470 LKSV 473
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
75-490 |
1.47e-95 |
|
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: 296.29 E-value: 1.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 75 VEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmdlAHG 154
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYA------ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 155 KKVN-----DREGEHNQYFYKPIGTGVTIPPWNFPF---AIMAGTTLApvvAGNTVLLKPAEDTPYTAYKLIEILEEAGL 226
Cdd:cd07100 75 EAFLadepiETDAGKAYVRYEPLGVVLGIMPWNFPFwqvFRFAAPNLM---AGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 227 PKGVVNFVPGDPKEIgDYLVDHIDTHFVTFTGSRATGtriyerSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAE 306
Cdd:cd07100 152 PEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAG------RAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 307 AIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLE 384
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDpMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 385 QGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDV 464
Cdd:cd07100 305 LGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEA 384
|
410 420
....*....|....*....|....*.
gi 1231725153 465 GNLYLNRGCTSAVvgYHPFGGFKMSG 490
Cdd:cd07100 385 GMVFINGMVKSDP--RLPFGGVKRSG 408
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
39-495 |
2.68e-92 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 289.35 E-value: 2.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKIFKE--DTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIA 116
Cdd:cd07117 3 LFINGEWVKGSsgETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 117 AVMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTLAP 195
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFA-GVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPF-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 196 VVA-GNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvh 274
Cdd:cd07117 160 ALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 275 egqdflKRVIA---EMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN 351
Cdd:cd07117 236 ------KKLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 352 T-EDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:cd07117 310 PlDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 426 VNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKT 495
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIGRET 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-498 |
4.84e-92 |
|
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: 287.65 E-value: 4.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 62 QLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFI 141
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 142 eYYARSMMDLAHGKKVNDREGEHNQYFYKPIGT-GVtIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTPYTAYKLI- 218
Cdd:cd07152 82 -HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVvGV-ISPFNFPL-ILAMRSVAPALAlGNAVVLKPDPRTPVSGGVVIa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 219 EILEEAGLPKGVVNFVPGDPkEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDEN 298
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAG------RHLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 299 VDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVG 377
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDpATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 378 KEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWI 456
Cdd:cd07152 312 VAAGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1231725153 457 KAVNEYDVGNLYLNRGcTSAVVGYHPFGGFKMSGTDAKTGSP 498
Cdd:cd07152 389 ALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
101-501 |
1.11e-91 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 285.86 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 101 MLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEY---YARSMmdlaHGKKV-NDREGEHNQYFYKPIGTGV 176
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYmaeWARRY----EGEIIqSDRPGENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 177 TIPPWNFPFAIMAgTTLAP-VVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVT 255
Cdd:PRK10090 77 GILPWNFPFFLIA-RKMAPaLLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 256 FTGSRATGTRIYERSAvvhegQDFLKrVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDE 335
Cdd:PRK10090 156 MTGSVSAGEKIMAAAA-----KNITK-VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 336 ILEKSVKLTKELTLGNT--EDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIM 412
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPaeRNDIAMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 413 QEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHpfGGFKMS--- 489
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgig 387
|
410
....*....|..
gi 1231725153 490 GTDAKTGSPDYL 501
Cdd:PRK10090 388 GADGKHGLHEYL 399
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-512 |
2.69e-90 |
|
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: 283.82 E-value: 2.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 60 TSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGK----PWDEaVGDAA 135
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEE-VLDVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 136 EGIdfiEYYARSMMDLAHGKKvndREG-----EHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:cd07101 84 IVA---RYYARRAERLLKPRR---RRGaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDthFVTFTGSRATGTRIYERSAvvhegqdflKRVI---AEM 287
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAG---------RRLIgcsLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 288 GGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTY-MGPVINKKQ 366
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPdMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 367 FDKIKNYIEVGKEEGKLEQGGGTD--DSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLT 444
Cdd:cd07101 307 LDRVTAHVDDAVAKGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231725153 445 GAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVSE 512
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
55-510 |
4.74e-90 |
|
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: 282.96 E-value: 4.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:cd07099 1 RNPA-TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYARSMMDLAHGKKVNDREGEHNQYF---YKPIG-TGVtIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKAtveYRPYGvVGV-ISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDH-IDthFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGG 289
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDAgVD--KVAFTGSVATGRKVMAAAA------ERLIPVVLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 290 KDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTE-DNTYMGPVINKKQFD 368
Cdd:cd07099 230 KDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDiGDADIGPMTTARQLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 369 KIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:cd07099 310 IVRRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231725153 448 ITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGG-GRRHGAEGLREFCRPKAI 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
39-510 |
9.11e-90 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 284.78 E-value: 9.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKI--FKEDTIESINPaNTSQLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:PLN02466 60 LLINGQFVdaASGKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTL 193
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYA-GWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPL-LMFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 APVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAv 272
Cdd:PLN02466 217 GPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 vhegQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT 352
Cdd:PLN02466 296 ----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 353 -EDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:PLN02466 372 fKKGVEQGPQIDSEQFEKILRYIKSGVESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpdYLLH-FLEQKV 509
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKGI--YSLNnYLQVKA 527
|
.
gi 1231725153 510 V 510
Cdd:PLN02466 528 V 528
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
52-510 |
8.65e-89 |
|
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: 279.70 E-value: 8.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 52 IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:cd07094 1 LDVHNPY-DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFI--------EYYARSM-MDLAHGKKvnDREGEHNQyfyKPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNT 201
Cdd:cd07094 80 VEVDRAIDTLrlaaeeaeRIRGEEIpLDATQGSD--NRLAWTIR---EPVGVVLAITPFNFPLNLVA-HKLAPAIAtGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 202 VLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqdfLK 281
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 282 RVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGP 360
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDpLDEDTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 361 VINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTgyfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDT 439
Cdd:cd07094 306 LISEEAAERVERWVEEAVEAGaRLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANST 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231725153 440 DYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGcTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07094 383 DYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGV-GREGVPYAMEEMTEEKTV 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
39-510 |
1.09e-87 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 278.24 E-value: 1.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKI--FKEDTIESINPaNTSQLIAKASKATTTDVEDAFKAAKEAYK--SWKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:PLN02766 23 LFINGEFVdaASGKTFETRDP-RTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWdeAVGDAAE---GIDFIEYYARSMmDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFP---FAIM 188
Cdd:PLN02766 102 LAALDTIDAGKLF--ALGKAVDipaAAGLLRYYAGAA-DKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPstmFFMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 189 AGTTLApvvAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYE 268
Cdd:PLN02766 179 VAPALA---AGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 269 RSAVVHegqdfLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELT 348
Cdd:PLN02766 256 AAATSN-----LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 349 LGNTED-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKV 426
Cdd:PLN02766 331 VGDPFDpRARQGPQVDKQQFEKILSYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 427 NDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFLE 506
Cdd:PLN02766 411 KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFGRDQGM-DALDKYLQ 487
|
....
gi 1231725153 507 QKVV 510
Cdd:PLN02766 488 VKSV 491
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-506 |
1.93e-87 |
|
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: 277.95 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 6 KNEPGYDFSVQDNVDMFKEELKKVKGQLGQDIPLVinGEKIFKEDTIESI-NPANTSQLIAKASKATTTDVEDAFKAAKE 84
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKTWQAAPII--GHSYKADGEAQPVtNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 85 AYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmdlahgKKVNDREGeh 164
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYA---------KQVRDVLG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 165 nQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:TIGR01238 155 -EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 245 LVDHIDTHFVTFTGSRATGTRIYERSAVVHEGQDFLkrvIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACS 324
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 325 RAIVHKDVYDEILEKSVKLTKELTLGNT-EDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDST----GYFVEP 399
Cdd:TIGR01238 311 VLCVQEDVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRacqhGTFVAP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 400 TIFSgLKSKDRiMQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAV 477
Cdd:TIGR01238 391 TLFE-LDDIAE-LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAV 468
|
490 500
....*....|....*....|....*....
gi 1231725153 478 VGYHPFGGFKMSGTDAKTGSPDYLLHFLE 506
Cdd:TIGR01238 469 VGVQPFGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
50-513 |
5.13e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 277.14 E-value: 5.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGK---- 125
Cdd:PRK09407 32 PTREVTAPF-TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKarrh 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 126 PWDEaVGDAAEGIDfieYYARSMMDLAHGKK------VNDREGEHnqyfYKPIGT-GVtIPPWNFPFAIMAGTTLAPVVA 198
Cdd:PRK09407 111 AFEE-VLDVALTAR---YYARRAPKLLAPRRragalpVLTKTTEL----RQPKGVvGV-ISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 199 GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDthFVTFTGSRATGTRIYERSAvvhegqd 278
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAG------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 279 flKRVI---AEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDN 355
Cdd:PRK09407 253 --RRLIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 356 TY-MGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTG-YFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEA 432
Cdd:PRK09407 331 SAdMGSLISEAQLETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 433 IEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVS 511
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGRRHG-AEGLLKYTESQTIA 489
|
..
gi 1231725153 512 EM 513
Cdd:PRK09407 490 TQ 491
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
55-483 |
6.98e-87 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 274.89 E-value: 6.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPwdeaVGDA 134
Cdd:cd07102 1 ISPI-DGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP----IAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYARSMMDLAHGKKVNDREGE----HNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:cd07102 76 GGEIRGMLERARYMISIAEEALADIRVPEkdgfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIyERSAvvhegQDFLKRVIAEMGGK 290
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAI-QRAA-----AGRFIKVGLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 291 DAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDK 369
Cdd:cd07102 229 DPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDpLDPSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 370 IKNYIEVGKEEG-KLEQGGGT---DDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:cd07102 309 VRAQIADAIAKGaRALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1231725153 446 AVITNNREHWIKAVNEYDVGNLYLNR------------------GCTSAVVGYHPF 483
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNRcdyldpalawtgvkdsgrGVTLSRLGYDQL 444
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
74-490 |
1.04e-85 |
|
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: 270.99 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 74 DVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYArSMMDLAH 153
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-SLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 154 GKKVN-DREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVN 232
Cdd:cd07105 80 GGSIPsDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 233 FVPGDPK---EIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIV 309
Cdd:cd07105 160 VVTHSPEdapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA------KHLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 310 TSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGntedNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGG 388
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVDDALSKGaKLVVGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 389 TDDS-TGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNL 467
Cdd:cd07105 310 ADESpSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420
....*....|....*....|....*.
gi 1231725153 468 YLNrGCT---SAVVgyhPFGGFKMSG 490
Cdd:cd07105 390 HIN-GMTvhdEPTL---PHGGVKSSG 411
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
39-511 |
4.10e-85 |
|
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: 271.29 E-value: 4.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKIFKED--TIESINPANTSqLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:cd07140 8 LFINGEFVDAEGgkTYNTINPTDGS-VICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWDEAVGD-AAEGIDFIEYYArSMMDLAHGKK--VNDREGEHNQYFYK--PIGTGVTIPPWNFPFAIMA 189
Cdd:cd07140 87 LATIESLDSGAVYTLALKThVGMSIQTFRYFA-GWCDKIQGKTipINQARPNRNLTLTKrePIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 190 GTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYER 269
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 270 SAVVHegqdfLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTL 349
Cdd:cd07140 246 CAVSN-----LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 350 GNTED-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVN 427
Cdd:cd07140 321 GDPLDrSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 428 --DFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGyhPFGGFKMSGTDAKTGSpDYLLHFL 505
Cdd:cd07140 401 dgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLGE-EALNEYL 477
|
....*.
gi 1231725153 506 EQKVVS 511
Cdd:cd07140 478 KTKTVT 483
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
40-493 |
2.85e-84 |
|
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: 268.69 E-value: 2.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 40 VINGEKIFKEDTIESINPANTSQlIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVM 119
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEP-IARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 120 VYEAGKPWDEAVGDAAEGIDFIEY---YARSMmdlaHGKKVN-DREGEHNQYFYKPIGTGVTIPPWNFPFAIMA-GTTLA 194
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFavgLSRQL----YGLTIPsERPGHRMMEQWNPLGVVGVITAFNFPVAVWGwNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 195 pVVAGNTVLLKPAEDTPYTA---YKLI-EILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGtriyerS 270
Cdd:cd07130 157 -LVCGNVVVWKPSPTTPLTAiavTKIVaRVLEKNGLPGAIASLVCGG-ADVGEALVKDPRVPLVSFTGSTAVG------R 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 271 AVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLG 350
Cdd:cd07130 229 QVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 351 N-TEDNTYMGPVINKKQFDKIKNYIEVGKEE-GKLEQGGGTDDSTGYFVEPTIFSGLkSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07130 309 DpLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDT 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231725153 429 FDEAIEVANDTDYGLTGAVITNN---REHWIKAVNEyDVGNLYLNRGCTSAVVGyHPFGGFKM------SGTDA 493
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDlrnAFRWLGPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKEtgggreSGSDA 459
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
73-496 |
9.25e-84 |
|
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: 266.53 E-value: 9.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 73 TDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA---VGDAAEGIDFIEYYARSM- 148
Cdd:cd07146 18 GTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTryeVGRAADVLRFAAAEALRDd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 149 -----MDLAHGKK----VNDREgehnqyfykPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPAEDTPYTAYKLI 218
Cdd:cd07146 98 gesfsCDLTANGKarkiFTLRE---------PLGVVLAITPFNHPLNQVA-HKIAPAIAaNNRIVLKPSEKTPLSAIYLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 219 EILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqdfLKRVIAEMGGKDAIVVDEN 298
Cdd:cd07146 168 DLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 299 VDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVG 377
Cdd:cd07146 240 ADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDpMDPATDMGTVIDEEAAIQIENRVEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 378 KEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWI 456
Cdd:cd07146 320 IAQGaRVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1231725153 457 KAVNEYDVGNLYLNRGctsavVGYH----PFGGFKMSGTDAKTG 496
Cdd:cd07146 397 RLVERLDVGTVNVNEV-----PGFRselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
52-490 |
5.27e-82 |
|
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: 262.18 E-value: 5.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 52 IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:cd07147 1 LEVTNPY-TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFIEYYAR-------SMMDLAHGKKVNDREGEHNQYfykPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVL 203
Cdd:cd07147 80 GEVARAIDTFRIAAEeatriygEVLPLDISARGEGRQGLVRRF---PIGPVSAITPFNFPLNLVA-HKVAPAIAaGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 204 LKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGdPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSavvheGQdflKRV 283
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARA-----GK---KKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 284 IAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVI 362
Cdd:cd07147 227 VLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDpKDDATDVGPMI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 363 NKKQFDKIKNYIEVGKEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:cd07147 307 SESEAERVEGWVNEAVDAGaKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1231725153 442 GLTGAVITNNREHWIKAVNEYDVGNLYLNRgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSG 431
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-508 |
1.02e-81 |
|
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: 262.33 E-value: 1.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGE--KIFKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07111 26 INGKwvKPENRKSFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAV-GDAAEGIDFIEYYA--RSMMDLA-HGkkvndregehnqyfYKPIGTGVTIPPWNFPFAIMAgTTLA 194
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHAgwAQLLDTElAG--------------WKPVGVVGQIVPWNFPLLMLA-WKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 195 PVVA-GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPkEIGDYLVDHIDTHFVTFTGSRATGTRIyeRSAVV 273
Cdd:cd07111 170 PALAmGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRAL--RRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 274 HEGqdflKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTE 353
Cdd:cd07111 247 GTG----KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 354 D-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDE 431
Cdd:cd07111 323 DkAIDMGAIVDPAQLKRIRELVEEGRAEGaDVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231725153 432 AIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQK 508
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGF-GREGGKEGLYEYLRPS 476
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
55-505 |
2.86e-81 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 275.70 E-value: 2.86e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 55 INPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:PRK11809 664 INPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEV 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYA---RSMMDlahgkkvNDRegehnqyfYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTP 211
Cdd:PRK11809 744 REAVDFLRYYAgqvRDDFD-------NDT--------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 212 YTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVHEGQDFLKRVIAEMGGKD 291
Cdd:PRK11809 809 LIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPLIAETGGQN 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 292 AIVVD-----ENVDTDlaaeaIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTED-NTYMGPVINKK 365
Cdd:PRK11809 889 AMIVDssaltEQVVAD-----VLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDAE 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 366 QFDKIKNYIEVGKEEG----KLEQGGGTDDSTGYFVEPTIFSgLKSKDRiMQEEIFGPVVGFVKV--NDFDEAIEVANDT 439
Cdd:PRK11809 964 AKANIERHIQAMRAKGrpvfQAARENSEDWQSGTFVPPTLIE-LDSFDE-LKREVFGPVLHVVRYnrNQLDELIEQINAS 1041
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231725153 440 DYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFL 505
Cdd:PRK11809 1042 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLL 1107
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-508 |
3.17e-80 |
|
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: 257.66 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYK--SWKTwSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:cd07120 1 SIDPA-TGEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFIEYYA---RSMmdlaHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPA 207
Cdd:cd07120 79 FEISGAISELRYYAglaRTE----AGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLV-RSLAPALAaGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 208 EDTPYTAYKLIEILEEA-GLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqDFLKRVIAE 286
Cdd:cd07120 154 GQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA------PTLKRLGLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 287 MGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTY-MGPVINKK 365
Cdd:cd07120 228 LGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASdMGPLIDRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 366 QFDKIKNYIEVGKEEGK--LEQGGGTDD--STGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:cd07120 308 NVDRVDRMVERAIAAGAevVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 442 GLTGAVITNNREHWIKAVNEYDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQK 508
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWIN---DWNKLFAEaEEGGYRQSGL-GRLHGVAALEDFIEYK 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
41-490 |
2.98e-79 |
|
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: 255.84 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKI--FKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAV 118
Cdd:cd07116 5 IGGEWVapVKGEYFDNITPV-TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 119 MVYEAGKPWDEAVG-DAAEGIDFIEYYARSMMdlAHGKKVNDREGEHNQY-FYKPIGTGVTIPPWNFPFaIMAGTTLAPV 196
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCIR--AQEGSISEIDENTVAYhFHEPLGVVGQIIPWNFPL-LMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 197 VA-GNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhe 275
Cdd:cd07116 161 LAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 276 gqDFLKRVIAEMGGKD-----AIVVDENVD-TDLAAEAIVTSAFGfSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTL 349
Cdd:cd07116 236 --ENIIPVTLELGGKSpniffADVMDADDAfFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 350 GNTED-NTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGG-----GTDDSTGYFVEPTIFSGlkSKDRIMQEEIFGPVVG 422
Cdd:cd07116 313 GNPLDtETMIGAQASLEQLEKILSYIDIGKEEGaEVLTGGernelGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 423 FVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07116 391 VTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
74-490 |
2.48e-78 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 251.81 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 74 DVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAh 153
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 154 GKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNF 233
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 234 VPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAF 313
Cdd:cd07095 160 VQGG-RETGEALAAHEGIDGLLFTGSAATGLLLHRQFA-----GRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 314 GFSGQKCSACSRAIVHKD-VYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKnyievgKEEGKLEQGGGTD- 390
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGApDAEPPFMGPLIIAAAAARYL------LAQQDLLALGGEPl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 391 ------DSTGYFVEPTIFSGLKSKDRiMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDV 464
Cdd:cd07095 308 lamerlVAGTAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420
....*....|....*....|....*.
gi 1231725153 465 GNLYLNRGCTSAvVGYHPFGGFKMSG 490
Cdd:cd07095 387 GIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
39-490 |
5.56e-76 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 247.56 E-value: 5.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGEKIF-KEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAA 117
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPV-SGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 118 VMVYEAGKPWDEAVGDAAEGIDFIE-----YYARSmmdlahGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTT 192
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAisiqaYHERT------GEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 193 LAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAv 272
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGG-RETGKALAAHPDIDGLLFTGSANTGYLLHRQFA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 vheGQDflKRVIA-EMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVY-DEILEKSVKLTKELTLG 350
Cdd:PRK09457 234 ---GQP--EKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 351 --NTEDNTYMGPVINKKQFDKI----KNYIEVG----KEEGKLEQGGGtddstgyFVEPTIFSGLKSKDRImQEEIFGPV 420
Cdd:PRK09457 309 rwDAEPQPFMGAVISEQAAQGLvaaqAQLLALGgkslLEMTQLQAGTG-------LLTPGIIDVTGVAELP-DEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 421 VGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAvVGYHPFGGFKMSG 490
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-507 |
8.13e-71 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 234.02 E-value: 8.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 39 LVINGE--KIFKEDTIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKS--WKTWSASDRAELMLRVAAIIRRRKAE 114
Cdd:PRK09847 22 LFINGEytAAAENETFETVDPV-TQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 115 IAAVMVYEAGKPWDEAVGDAAEG-IDFIEYYARSMmDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFaIMAGTTL 193
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGaARAIRWYAEAI-DKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL-LLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 194 AP-VVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIyersaV 272
Cdd:PRK09847 179 GPaLAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL-----L 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 273 VHEGQDFLKRVIAEMGGKDA-IVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN 351
Cdd:PRK09847 254 KDAGDSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 352 TED-NTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:PRK09847 334 PLDpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 431 EAIEVANDTDYGLTGAVITNN--REH----WIKA----VNEYDVGNLYLnrgctsavvgyhPFGGFKMSGTdaktgSPDY 500
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDlsRAHrmsrRLKAgsvfVNNYNDGDMTV------------PFGGYKQSGN-----GRDK 475
|
....*..
gi 1231725153 501 LLHFLEQ 507
Cdd:PRK09847 476 SLHALEK 482
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
50-501 |
1.69e-70 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 232.87 E-value: 1.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 50 DTIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDE 129
Cdd:PRK11241 26 EVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 130 AVGDAAEGIDFIEYYA----RSMMDLAHGKKVNDREGEHNQyfykPIGTGVTIPPWNFPFAIM---AGTTLApvvAGNTV 202
Cdd:PRK11241 105 AKGEISYAASFIEWFAeegkRIYGDTIPGHQADKRLIVIKQ----PIGVTAAITPWNFPAAMItrkAGPALA---AGCTM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegQDfLKR 282
Cdd:PRK11241 178 VLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA-----KD-IKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPV 361
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDgLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 362 INKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231725153 441 YGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGyhPFGGFKMSG---TDAKTGSPDYL 501
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-490 |
7.89e-67 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 222.69 E-value: 7.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 52 IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV 131
Cdd:PRK09406 3 IATINPA-TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 132 GDAAEGIDFIEYYARSMMDL-----AHGKKVndreGEHNQYF-YKPIGTGVTIPPWNFP------FAimagttlAP-VVA 198
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALladepADAAAV----GASRAYVrYQPLGVVLAVMPWNFPlwqvvrFA-------APaLMA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 199 GNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVpgdpkEIGDYLVDHI--DTHFV--TFTGSRATGtriyerSAVVH 274
Cdd:PRK09406 151 GNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSGAVEAIlrDPRVAaaTLTGSEPAG------RAVAA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 275 EGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TE 353
Cdd:PRK09406 220 IAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDpTD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 354 DNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEA 432
Cdd:PRK09406 300 PDTDVGPLATEQGRDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 433 IEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNrGCTSAVVGYhPFGGFKMSG 490
Cdd:PRK09406 380 IEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSG 435
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
51-490 |
4.76e-65 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 218.86 E-value: 4.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 51 TIESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA 130
Cdd:PLN00412 32 SVAITNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 131 VGDAAEGIDFIEYYARS-MMDLAHGKKVNDRE---GEHNQYFYK---PIGTGVTIPPWNFPFAiMAGTTLAP-VVAGNTV 202
Cdd:PLN00412 111 VTEVVRSGDLISYTAEEgVRILGEGKFLVSDSfpgNERNKYCLTskiPLGVVLAIPPFNYPVN-LAVSKIAPaLIAGNAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRaTGTRIYERSAVVhegqdflkR 282
Cdd:PLN00412 190 VLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAISKKAGMV--------P 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVI 362
Cdd:PLN00412 261 LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 363 NKKQFDKIKNYIEVGKEEG-KLEQGGGTDdstGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:PLN00412 341 SESSANFIEGLVMDAKEKGaTFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNF 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1231725153 442 GLTGAVITNNREHWIKAVNEYDVGNLYLN----RGctsavVGYHPFGGFKMSG 490
Cdd:PLN00412 418 GLQGCVFTRDINKAILISDAMETGTVQINsapaRG-----PDHFPFQGLKDSG 465
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
56-512 |
6.63e-65 |
|
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: 217.55 E-value: 6.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 56 NPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPW-DEAVGD- 133
Cdd:cd07098 2 DPA-TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMvDASLGEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 134 --AAEGIDFIeyyarsmmdLAHGKKV---NDREGEHNQYF------YKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTV 202
Cdd:cd07098 81 lvTCEKIRWT---------LKHGEKAlrpESRPGGLLMFYkrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 203 LLKPAEDTPYTAYKLIEILEEA----GLPKGVVNFVPGDPkEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhegqD 278
Cdd:cd07098 152 VVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAA------E 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 279 FLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTY- 357
Cdd:cd07098 225 SLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVd 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 358 MGPVINKKQFDKIKNYIEVGKEEG-KLEQGG----GTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEA 432
Cdd:cd07098 305 VGAMISPARFDRLEELVADAVEKGaRLLAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 433 IEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDaKTGSPDYLLHFLEQKVVSE 512
Cdd:cd07098 385 VEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTE 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
54-490 |
9.08e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 206.64 E-value: 9.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 54 SINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGD 133
Cdd:PRK13968 11 SVNPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 134 AAEGIDFIEYYARsmmdlaHGKKVNDREG---EHNQYF--YKPIGTGVTIPPWNFP-FAIMAGTtlAPVV-AGNTVLLKP 206
Cdd:PRK13968 90 VAKSANLCDWYAE------HGPAMLKAEPtlvENQQAVieYRPLGTILAIMPWNFPlWQVMRGA--VPILlAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 207 AEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVD-HIDThfVTFTGSRATGTRIYERSAVVhegqdfLKRVIA 285
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDsRIAA--VTVTGSVRAGAAIGAQAGAA------LKKCVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 286 EMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINK 364
Cdd:PRK13968 234 ELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDpRDEENALGPMARF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 365 KQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:PRK13968 314 DLRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1231725153 444 TGAVITNNREHWIKAVNEYDVGNLYLNRGCTS-AVVGyhpFGGFKMSG 490
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFINGYCASdARVA---FGGVKKSG 438
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
76-490 |
1.84e-58 |
|
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: 199.67 E-value: 1.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 76 EDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA----VGDAAEGIDFIEYYARSMMDL 151
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 152 AHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYTAyKLIEILEEAGLP 227
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQ----LALAPLIgaiaAGNTVVLKPSELAPATS-ALLAKLIPKYFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 228 KGVVNFVPGDPKEIGDYL---VDHIdthFvtFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLA 304
Cdd:cd07087 156 PEAVAVVEGGVEVATALLaepFDHI---F--FTGSPAVGKIVMEAAA------KHLTPVTLELGGKSPCIVDKDANLEVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 305 AEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIevgkEEGKLE 384
Cdd:cd07087 225 ARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLL----DDGKVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 385 QGGGTDDSTGYfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDV 464
Cdd:cd07087 301 IGGQVDKEERY-IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420
....*....|....*....|....*.
gi 1231725153 465 GNLYLNRGCTSAVVGYHPFGGFKMSG 490
Cdd:cd07087 380 GGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
27-470 |
8.44e-58 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 202.28 E-value: 8.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 27 KKVKGQLGQDIPLVINGEKIFKEDT--IESINPAnTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRV 104
Cdd:PLN02419 104 QSTQPQMPPRVPNLIGGSFVESQSSsfIDVINPA-TQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 105 AAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNF 183
Cdd:PLN02419 183 QELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH-ACGMATLQMGEYLpNVSNGVDTYSIREPLGVCAGICPFNF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 184 PFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIgDYLVDHIDTHFVTFTGSRATG 263
Cdd:PLN02419 262 PAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 264 TRIYERSAVvhEGqdflKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVY---DEILEKS 340
Cdd:PLN02419 341 MHIYARAAA--KG----KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 341 VKLtkELTLGnTEDNTYMGPVINKKQFDKIKNYIEVGKEEG-KLEQGGGTDDSTGY----FVEPTIFSGLKSKDRIMQEE 415
Cdd:PLN02419 415 KAL--KVTCG-SEPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1231725153 416 IFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLN 470
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
171-496 |
3.10e-55 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 191.28 E-value: 3.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 171 PIGTGVTIPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIG---D 243
Cdd:cd07135 108 PLGVVLIIGPWNYPVL----LALSPLVgaiaAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTallE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 244 YLVDHIdthFvtFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSAC 323
Cdd:cd07135 183 QKFDKI---F--YTGSGRVGRIIAEAAA------KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 324 SRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIEVGKeeGKLEQGGGTDDSTgYFVEPTIFS 403
Cdd:cd07135 252 DYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--GKVVIGGEMDEAT-RFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 404 GLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNR---EHWIKAVNEYD--VGNLYLNRGCTSAvv 478
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKseiDHILTRTRSGGvvINDTLIHVGVDNA-- 406
|
330
....*....|....*...
gi 1231725153 479 gyhPFGGFKMSGTDAKTG 496
Cdd:cd07135 407 ---PFGGVGDSGYGAYHG 421
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
51-497 |
2.14e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 188.12 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 51 TIESINPANtSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA 130
Cdd:PLN02315 35 LVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 131 VGDAAEGIDFIEYYARSMMDLAHGKKVNDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:PLN02315 114 IGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAY---KLI-EILEEAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYErsavvHEGQDFLKRVIaE 286
Cdd:PLN02315 194 PLITIamtKLVaEVLEKNNLPGAIFTSFCGG-AEIGEAIAKDTRIPLVSFTGSSKVGLMVQQ-----TVNARFGKCLL-E 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 287 MGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT-EDNTYMGPVINKK 365
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPlEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 366 QFDKIKNYIEVGKEEG-KLEQGGGTDDSTGYFVEPTIFSGLKSKDrIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLT 444
Cdd:PLN02315 347 SKKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTIVEISPDAD-VVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLS 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1231725153 445 GAVITNNRE---HWIKAVNEyDVGNLYLNRGCTSAVVGyHPFGGFKMSGTDAKTGS 497
Cdd:PLN02315 426 SSIFTRNPEtifKWIGPLGS-DCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
78-490 |
2.00e-52 |
|
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: 183.58 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 78 AFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPwdeavgdAAEgIDFIEYYArSMMDLAHGKKV 157
Cdd:cd07134 3 VFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP-------AAE-VDLTEILP-VLSEINHAIKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 158 NDR-------------EGEHNQYFYKPIGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYTAYKLIEI 220
Cdd:cd07134 74 LKKwmkpkrvrtplllFGTKSKIRYEPKGVCLIISPWNYPF----NLAFGPLVsaiaAGNTAILKPSELTPHTSAVIAKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 221 LEEAGLPKGVVNFVpGDPkEIGDYL----VDHIdthFvtFTGSRATGtRIYERSAVVHegqdfLKRVIAEMGGKDAIVVD 296
Cdd:cd07134 150 IREAFDEDEVAVFE-GDA-EVAQALlelpFDHI---F--FTGSPAVG-KIVMAAAAKH-----LASVTLELGGKSPTIVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 297 ENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELtLGNTE---DNTYMGPVINKKQFDKIKNY 373
Cdd:cd07134 217 ETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKF-YGKDAarkASPDLARIVNDRHFDRLKGL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 374 IEVGKEEG-KLEQGGGTDDSTGYfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNR 452
Cdd:cd07134 296 LDDAVAKGaKVEFGGQFDAAQRY-IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDK 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 1231725153 453 EHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSG 490
Cdd:cd07134 375 ANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
166-490 |
2.88e-52 |
|
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: 183.47 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 166 QYFYKPIGTGVTIPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEI 241
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQL----ALAPLIgaiaAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 242 GDYL---VDHIdthFvtFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQ 318
Cdd:cd07136 170 QELLdqkFDYI---F--FTGSVRVGKIVMEAAA------KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 319 KCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIevgkEEGKLEQGGGTDDSTGYfVE 398
Cdd:cd07136 239 TCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLL----DNGKIVFGGNTDRETLY-IE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 399 PTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNlylnrGCTSAVV 478
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGG-----GCINDTI 388
|
330
....*....|....*...
gi 1231725153 479 gYH------PFGGFKMSG 490
Cdd:cd07136 389 -MHlanpylPFGGVGNSG 405
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
72-490 |
9.58e-52 |
|
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: 182.62 E-value: 9.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 72 TTDVEDAFKAAKEAYKSWKT---W-SASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAEGIDFIEYYARS 147
Cdd:cd07148 17 TVDWAAIDKALDTAHALFLDrnnWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 148 MMDLAhGKKV-----NDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILE 222
Cdd:cd07148 97 LGQLG-GREIpmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 223 EAGLPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAvvhEGqdflKRVIAEMGGKDAIVVDENVDTD 302
Cdd:cd07148 176 EAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA---PG----TRCALEHGGAAPVIVDRSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 303 LAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEG 381
Cdd:cd07148 248 AMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDpTDPDTEVGPLIRPREVDRVEEWVNEAVAAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 382 -KLEQGGGTDDSTGYfvEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVN 460
Cdd:cd07148 328 aRLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVR 405
|
410 420 430
....*....|....*....|....*....|
gi 1231725153 461 EYDVGNLYLNRGcTSAVVGYHPFGGFKMSG 490
Cdd:cd07148 406 RLDATAVMVNDH-TAFRVDWMPFAGRRQSG 434
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-493 |
1.86e-47 |
|
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: 170.48 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 76 EDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAV--------GDAAEGIDFI------ 141
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLpewmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 142 EYYARSMMDLAHGkkvndregehnQYFYK-PIGTGVTIPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYTAyK 216
Cdd:cd07132 81 EPVKKNLATLLDD-----------VYIYKePLGVVLIIGAWNYPLQL----TLVPLVgaiaAGNCVVIKPSEVSPATA-K 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 217 LIEILeeagLPK-------GVVNfvpGDPKEIGDYL---VDHIdthFvtFTGSRATGTRIYERSAVvhegqdFLKRVIAE 286
Cdd:cd07132 145 LLAEL----IPKyldkecyPVVL---GGVEETTELLkqrFDYI---F--YTGSTSVGKIVMQAAAK------HLTPVTLE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 287 MGGKDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQ 366
Cdd:cd07132 207 LGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 367 FDKIKNYIEvgkeEGKLEQGGGTDDSTGYfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07132 287 FQRLKKLLS----GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALY 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1231725153 447 VITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDA 493
Cdd:cd07132 362 VFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGA 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
68-490 |
7.69e-42 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 156.34 E-value: 7.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 68 SKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEA-VGDAAEGIDFIEYyar 146
Cdd:PTZ00381 2 EPDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkMTEVLLTVAEIEH--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 147 smmDLAHGKKVNDRE--------GEHNQYF-YKPIGTGVTIPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYT 213
Cdd:PTZ00381 79 ---LLKHLDEYLKPEkvdtvgvfGPGKSYIiPEPLGVVLVIGAWNYPLN----LTLIPLAgaiaAGNTVVLKPSELSPHT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 214 AyKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFvtFTGSRATGTRIYERSAvvhegqDFLKRVIAEMGGKDAI 293
Cdd:PTZ00381 152 S-KLMAKLLTKYLDPSYVRVIEGGVEVTTELLKEPFDHIF--FTGSPRVGKLVMQAAA------ENLTPCTLELGGKSPV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 294 VVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNY 373
Cdd:PTZ00381 223 IVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 374 IEVGKeeGKLEQGGGTDDSTGYfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNRE 453
Cdd:PTZ00381 303 IKDHG--GKVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKR 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 1231725153 454 HWIKAVNEYDVGNLYLNRgCTSAVVGYH-PFGGFKMSG 490
Cdd:PTZ00381 380 HKELVLENTSSGAVVIND-CVFHLLNPNlPFGGVGNSG 416
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
75-499 |
1.74e-36 |
|
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: 140.45 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 75 VEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAvGDAAEGIDFIEYYArsmmDLAHG 154
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARA----FVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 155 KKVNDREGEHNQYFYKP------IGTGVT--IPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAG- 225
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQqshgyrWPYGPVlvIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 226 LPKGVVNFVPGDpKEIGDYLVDHIDTHFVTFTGSRATGTRIYersAVVHEGqdflkRVIAEMGGKDAIVVDENVDT-DLA 304
Cdd:cd07084 156 LPPEDVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLA---LDAKQA-----RIYLELAGFNWKVLGPDAQAvDYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 305 AEAIVTSAFGFSGQKCSACSRAIVHKdvyDEILEKSVKLTKELTLGNTEDNTYMGPVInkkQFDKIKNYIEVGKEEG--- 381
Cdd:cd07084 227 AWQCVQDMTACSGQKCTAQSMLFVPE---NWSKTPLVEKLKALLARRKLEDLLLGPVQ---TFTTLAMIAHMENLLGsvl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 382 ----KLEQGGGTDDSTGYFVEPTIFSGLKSKDR---IMQEEIFGPVVGFVKVNDFDEA--IEVANDTDYGLTGAVITNNR 452
Cdd:cd07084 301 lfsgKELKNHSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDP 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1231725153 453 EHWIKAVNEYDV-GNLY-LNRGCTSAVVGYHPFGGFKMSGTDAKTGSPD 499
Cdd:cd07084 381 IFLQELIGNLWVaGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
166-496 |
3.22e-35 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 136.77 E-value: 3.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 166 QYFYKPIGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEi 241
Cdd:cd07137 96 EIVSEPLGVVLVISAWNFPF----LLSLEPVIgaiaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPE- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 242 GDYLVDH-IDTHFvtFTGSRATGtRIYERSAVVHegqdfLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGF-SGQK 319
Cdd:cd07137 170 TTALLEQkWDKIF--FTGSPRVG-RIIMAAAAKH-----LTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 320 CSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGGGTDDSTGYfVEP 399
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLY-IEP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 400 TIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVG 479
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
330
....*....|....*..
gi 1231725153 480 YHPFGGFKMSGTDAKTG 496
Cdd:cd07137 401 TLPFGGVGESGFGAYHG 417
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
76-438 |
7.84e-35 |
|
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: 135.69 E-value: 7.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 76 EDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGkpwdeavGDAAEGIDFIEYYArSMMDLAHGK 155
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFG-------HRSRHETLLAEILP-SIAGIKHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 156 -------KVNDRE------GEHNQYFYKPIG-TGVtIPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYTAYKL 217
Cdd:cd07133 73 khlkkwmKPSRRHvgllflPAKAEVEYQPLGvVGI-IVPWNYPLYL----ALGPLIaalaAGNRVMIKPSEFTPRTSALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 218 IEILEEAGLPKgVVNFVPGDPkEIGDYLV----DHIdthfvTFTGSRATGtRIYERSAVVHegqdfLKRVIAEMGGKDAI 293
Cdd:cd07133 148 AELLAEYFDED-EVAVVTGGA-DVAAAFSslpfDHL-----LFTGSTAVG-RHVMRAAAEN-----LTPVTLELGGKSPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 294 VVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKEL--TLGNTEDNTymgPVINKKQFDKIK 371
Cdd:cd07133 215 IIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPDYT---SIINERHYARLQ 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 372 NYIEVGKEEG-KLEQ--GGGTDDSTGYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:cd07133 292 GLLEDARAKGaRVIElnPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINA 361
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
48-454 |
5.32e-33 |
|
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: 131.62 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 48 KEDTIESINPAnTSQLIAKASkATTTDVEDAFKAAKE-AYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKP 126
Cdd:cd07128 13 TGDGRTLHDAV-TGEVVARVS-SEGLDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAATGATR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 127 WDEAVgDAAEGIDFIEYYA---RSMMDLAH----GKKVN-DREGEH-NQYFYKPI-GTGVTIPPWNFPFAIMAGTtLAP- 195
Cdd:cd07128 91 RDSWI-DIDGGIGTLFAYAslgRRELPNAHflveGDVEPlSKDGTFvGQHILTPRrGVAVHINAFNFPVWGMLEK-FAPa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 196 VVAGNTVLLKPAEDTPYTAYKLIEILEEAG-LPKGVVNFVPGDPkeiGDyLVDHIDTH-FVTFTGSRATGTRIYERSAVV 273
Cdd:cd07128 169 LLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSV---GD-LLDHLGEQdVVAFTGSAATAAKLRAHPNIV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 274 HEGqdflKRVIAEMG-------GKDAIVVDENVD---TDLAAEAIVTSafgfsGQKCSACSRAIVHKDVYDEILEKSVKL 343
Cdd:cd07128 245 ARS----IRFNAEADslnaailGPDATPGTPEFDlfvKEVAREMTVKA-----GQKCTAIRRAFVPEARVDAVIEALKAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 344 TKELTLGN-TEDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQGG-------GTDDSTGYFVEPTIF--SGLKSKDRIMQ 413
Cdd:cd07128 316 LAKVVVGDpRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrfevvGADAEKGAFFPPTLLlcDDPDAATAVHD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1231725153 414 EEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREH 454
Cdd:cd07128 396 VEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAF 436
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
75-490 |
4.00e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 125.99 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 75 VEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDAAeGI--DFIEYYARSMMDLA 152
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEV-GVltKSANLALSNLKKWM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 153 HGKKVNDREG---EHNQYFYKPIGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYTAYKLIEILeEAG 225
Cdd:PLN02203 87 APKKAKLPLVafpATAEVVPEPLGVVLIFSSWNFPI----GLSLEPLIgaiaAGNAVVLKPSELAPATSAFLAANI-PKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 226 LPKGVVNFVPGDPkEIGDYLVDH-IDTHFvtFTGSRATGtRIYERSAVVHegqdfLKRVIAEMGGKDAIVVD---ENVDT 301
Cdd:PLN02203 162 LDSKAVKVIEGGP-AVGEQLLQHkWDKIF--FTGSPRVG-RIIMTAAAKH-----LTPVALELGGKCPCIVDslsSSRDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 302 DLAAEAIVTSAFGF-SGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIEVGKEE 380
Cdd:PLN02203 233 KVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 381 GKLEQGGGTDDSTgYFVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVN 460
Cdd:PLN02203 313 ASIVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILS 391
|
410 420 430
....*....|....*....|....*....|....
gi 1231725153 461 EYDVGNLYLNrgctSAVVGYH----PFGGFKMSG 490
Cdd:PLN02203 392 ETSSGSVTFN----DAIIQYAcdslPFGGVGESG 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
56-454 |
1.20e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.26 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 56 NPANTSQLiAKASkATTTDVEDAFKAAKE-AYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGDA 134
Cdd:PRK11903 25 DPVTGEEL-VRVS-ATGLDLAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 135 AEGIDFIEYYARSmmdlahGKKVNDR----EGE----------HNQYFYKPI-GTGVTIPPWNFPFAIMAGTTLAPVVAG 199
Cdd:PRK11903 103 DGGIFTLGYYAKL------GAALGDArllrDGEavqlgkdpafQGQHVLVPTrGVALFINAFNFPAWGLWEKAAPALLAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 200 NTVLLKPAEDTPYTAYKLIEILEEAG-LPKGVVNFVPGDPKEigdyLVDHIDT-HFVTFTGSRATGTRIYERSAVVHEGQ 277
Cdd:PRK11903 177 VPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAG----LLDHLQPfDVVSFTGSAETAAVLRSHPAVVQRSV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 278 dflkRVIAEMGGKDAIVV--DENVDT---DLAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEILEKSVKLTKELTLGNT 352
Cdd:PRK11903 253 ----RVNVEADSLNSALLgpDAAPGSeafDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 353 EDNTY-MGPVINKKQFDKIKNYIEVGKEEGKLEQGGGT------DDSTGYFVEPTIF--SGLKSKDRIMQEEIFGPVVGF 423
Cdd:PRK11903 329 RNDGVrMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdaDPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATL 408
|
410 420 430
....*....|....*....|....*....|.
gi 1231725153 424 VKVNDFDEAIEVANDTDYGLTGAVITNNREH 454
Cdd:PRK11903 409 LPYRDAAHALALARRGQGSLVASVYSDDAAF 439
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
170-496 |
2.82e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 108.59 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 170 KPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEEAgLPKGVVNFVPGDPKEIGDYLVDHI 249
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 250 DTHFvtFTGSRATGtRIYERSAVVHegqdfLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFGF-SGQKCSACSRAIV 328
Cdd:PLN02174 190 DKIF--YTGSSKIG-RVIMAAAAKH-----LTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 329 HKDVYDEILEKSVKLTKELTLGNTEDNTYMGPVINKKQFDKIKNYIEVGKEEGKLEQgGGTDDSTGYFVEPTIFSGLKSK 408
Cdd:PLN02174 262 TKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVY-GGEKDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 409 DRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEYDVGNLYLNRGCTSAVVGYHPFGGFKM 488
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....*...
gi 1231725153 489 SGTDAKTG 496
Cdd:PLN02174 421 SGMGAYHG 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
41-484 |
3.29e-21 |
|
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: 96.41 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 41 INGEKIFK--EDTIESINPantsqLIAKASKATTTDVEDAFKAAkEAYKSWktwsasdrAELMLRVAAIIRRRKAE--IA 116
Cdd:cd07126 20 LNGDKFISvpDTDEDEINE-----FVDSLRQCPKSGLHNPLKNP-ERYLLY--------GDVSHRVAHELRKPEVEdfFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 117 AVMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMD-LAHGKKV-NDREGEHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLA 194
Cdd:cd07126 86 RLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRfLARSFNVpGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 195 PVVAGNTVLLKPAEDTPYTAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDhIDTHFVTFTGSratgTRIYERSAVVH 274
Cdd:cd07126 166 ALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGS----SKVAERLALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 275 EGqdflkRVIAEMGGKDAIVVDENV-DTDLAAEAIVTSAFGFSGQKCSACSRAIVHKD-VYDEILEKSVKLTKELTLgnt 352
Cdd:cd07126 241 HG-----KVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 353 EDNTyMGPVI---NKKQFDKIKNYIEVgkEEGKLEQGG-----GTDDSTGYFVEPT-IFSGLKSKD-----RIMQEEIFG 418
Cdd:cd07126 313 EDLT-IGPVLtwtTERILDHVDKLLAI--PGAKVLFGGkpltnHSIPSIYGAYEPTaVFVPLEEIAieenfELVTTEVFG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 419 P--VVGFVKVNDFDEAIEVANDTDYGLTGAVITNNrEHWIKAVNEYDV-GNLYLN-RGCTSAVVGYHPFG 484
Cdd:cd07126 390 PfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSND-IRFLQEVLANTVnGTTYAGiRARTTGAPQNHWFG 458
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
75-454 |
6.60e-19 |
|
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: 89.14 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 75 VEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEAGKP--------------------------WD 128
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPearlqgelgrttgqlrlfadlvregsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 129 EAVGDAAegidfieyyarsMMDLAHGKKVNDREGehnqyfYKPIGTGVTIPPWNFPFA--IMAGTTLAPVVAGNTVLLKP 206
Cdd:cd07129 81 DARIDPA------------DPDRQPLPRPDLRRM------LVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 207 AEDTPYTA---YKLI-EILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSRATGTRIYERSAVVHEGqdflKR 282
Cdd:cd07129 143 HPAHPGTSelvARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP----IP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 283 VIAEMGGKDAIVVDEN---VDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKdvyDEILEKSVKLTKElTLGNTEDNTYMG 359
Cdd:cd07129 219 FYAELGSVNPVFILPGalaERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPA---GPAGDAFIAALAE-ALAAAPAQTMLT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 360 PVInkkqfdkIKNYiEVGKEE-----GKLEQGGGTDDSTGYFVEPTIF----SGLkSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07129 295 PGI-------AEAY-RQGVEAlaaapGVRVLAGGAAAEGGNQAAPTLFkvdaAAF-LADPALQEEVFGPASLVVRYDDAA 365
|
410 420
....*....|....*....|....
gi 1231725153 431 EAIEVANDTDYGLTGAVITNNREH 454
Cdd:cd07129 366 ELLAVAEALEGQLTATIHGEEDDL 389
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
73-436 |
1.18e-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: 82.53 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 73 TDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIA-AVMvYEAGKPWDEAV---GDAAE--GIDFIEYYAR 146
Cdd:cd07127 84 CDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAhAVM-HTTGQAFMMAFqagGPHAQdrGLEAVAYAWR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 147 SMMDLAHGKKVNDREGEHNQYF----YKPIGTGV-------TIPPWN-FPfaimagTTLAPVVAGNTVLLKPAEDT---- 210
Cdd:cd07127 163 EMSRIPPTAEWEKPQGKHDPLAmektFTVVPRGValvigcsTFPTWNgYP------GLFASLATGNPVIVKPHPAAilpl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 211 PYTAYKLIEILEEAGLPKGVVNFVPGDPKE-IGDYLVDHIDTHFVTFTGSRATGTRIYErsavvHEGQdflKRVIAEMGG 289
Cdd:cd07127 237 AITVQVAREVLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWLEA-----NARQ---AQVYTEKAG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 290 KDAIVVDENVDTDLAAEAIVTSAFGFSGQKCSACSRAIVHKD---------VYDEILEKSVKLTKELTLGNTEDNTYMGP 360
Cdd:cd07127 309 VNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGLLADPARAAALLGA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 361 VINKKQFDKIknyievgkeeGKLEQGGGT-DDSTGY----FVE-----PTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07127 389 IQSPDTLARI----------AEARQLGEVlLASEAVahpeFPDarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTD 458
|
....*.
gi 1231725153 431 EAIEVA 436
Cdd:cd07127 459 HSIELA 464
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
73-463 |
4.76e-13 |
|
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: 71.11 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 73 TDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEA--GKPWD-----EAVGDAAEGIDFIEYYA 145
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETgmGRVEDkiaknHLAAEKTPGTEDLTTTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 146 RSmmdlahgkkvndreGEH--NQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYTAYKLIEILEE 223
Cdd:cd07121 84 WS--------------GDNglTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 224 A----GLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSratgtriyerSAVVHEGQDFLKRVIAEMGGKDAIVVDENV 299
Cdd:cd07121 150 AiaeaGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGG----------PAVVKAALSSGKKAIGAGAGNPPVVVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 300 DTDLAAEAIVTSAfGFSGQ-KCSACSRAIVHKDVYDEILEKSVK-------------LTKELTLgntednTYMGPVINKK 365
Cdd:cd07121 220 DIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADYLIAAMQRngayvlndeqaeqLLEVVLL------TNKGATPNKK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 366 QfdkiknyieVGKEEGK-LEQGGGTDDStgyfVEPTIFSGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL- 443
Cdd:cd07121 293 W---------VGKDASKiLKAAGIEVPA----DIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNr 359
|
410 420
....*....|....*....|.
gi 1231725153 444 -TGAVITNNREHWIKAVNEYD 463
Cdd:cd07121 360 hTAIIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
75-436 |
3.38e-11 |
|
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: 65.36 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 75 VEDAFKAAKEAYKSWKTWSASDRAELM--LRVAAIIRRRKAEIAAVMVYEAGKPWDEAVGD--AAEGIdfieyYARSMMD 150
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFraAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNhfAAEYI-----YNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 151 LAHGKKVNDREGeHNQYFYKPIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKP---AEDTPYTAYKLI-EILEEAGL 226
Cdd:cd07081 76 KTCGVLTGDENG-GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 227 PKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSratgtriyerSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAE 306
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATGG----------PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 307 AIVTSAFGFSGQKCSACSRAIVHKDVYDEILEK-----SVKLTKeltlgntEDNTYMGPVINKkqfDKIKNYIEVGKEEG 381
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLfegqgAYKLTA-------EELQQVQPVILK---NGDVNRDIVGQDAY 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1231725153 382 KLEQGGG---TDDSTGYFVEPTIFsglkSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07081 295 KIAAAAGlkvPQETRILIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
44-436 |
3.47e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 65.31 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 44 EKIFKEDTIESINPANTSQLIAKASKATTTDVEDAFKAAKEAYKSWKTWSASDRAELMLRVAAIIRRRKAEIAAVMVYEA 123
Cdd:PRK15398 7 EQVVKAVLAEMLSSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 124 G---------KpwDEAVGDAAEGIDFIEYYARSmmdlahgkkvndreGEHNQ--YFYKPIGTGVTIPPWNFPFAIMAGTT 192
Cdd:PRK15398 87 GmgrvedkiaK--NVAAAEKTPGVEDLTTEALT--------------GDNGLtlIEYAPFGVIGAVTPSTNPTETIINNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 193 LAPVVAGNTVLLKPAEDTPYTAYKLIEILEEA----GLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSratgtriye 268
Cdd:PRK15398 151 ISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGG--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 269 rSAVVHEGQDFLKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAfGFSGQ-KCSACSRAIVHKDVYDEILEKSVK----- 342
Cdd:PRK15398 222 -PAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIAEKEVIVVDSVADELMRLMEKngavl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 343 LTKELTLGNTEDNTYMGPVINKKQfdkiknyieVGKEEGK-LEQGGGTDDSTgyfvEPTIFSGLKSKDRIMQEEIFGPVV 421
Cdd:PRK15398 300 LTAEQAEKLQKVVLKNGGTVNKKW---------VGKDAAKiLEAAGINVPKD----TRLLIVETDANHPFVVTELMMPVL 366
|
410
....*....|....*
gi 1231725153 422 GFVKVNDFDEAIEVA 436
Cdd:PRK15398 367 PVVRVKDVDEAIALA 381
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
171-388 |
2.25e-09 |
|
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: 59.16 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 171 PIGTGVTIPPWNFPFAIMAGTTLApVVAGNTVLLKPAEDTPYTAYKLIEILEEA---GLPKGVVNFVPGDPKEIGDYLVD 247
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 248 HIDTHFVTFTGSRATGTRIYERSAVvhegqdflKRVIAEMGGKDAIVVDENVDTDLAAEAIVTSAFgFSGQKCSACSRAI 327
Cdd:cd07077 179 HPKIDLIVATGGRDAVDAAVKHSPH--------IPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLY 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231725153 328 VHKDVYDEILEK--------------SVKLTKELTLGNTED--NTYMGPVInkKQFDKIKNYIEVGKEEGKLEQGGG 388
Cdd:cd07077 250 VVDDVLDPLYEEfklklvveglkvpqETKPLSKETTPSFDDeaLESMTPLE--CQFRVLDVISAVENAWMIIESGGG 324
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
213-454 |
4.66e-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: 52.11 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 213 TAYKLIEILEEAGLPKGVVNFVPGDPKEIGDYLVDHIDTHFVTFTGSratgtriyerSAVVHEgqdflkrviAEMGGKDA 292
Cdd:cd07122 141 AAKIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG----------PGMVKA---------AYSSGKPA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 293 I---------VVDENVDTDLAAEAIVTS-AFGFsGQKCSACSRAIVHKDVYDEILEksvkltkELtlgnTEDNTYmgpVI 362
Cdd:cd07122 202 IgvgpgnvpaYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRA-------EL----KRRGAY---FL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231725153 363 NKKQFDKIKNYIE----------VGKEEGKLEQGGG--TDDSTGYFVEPtiFSGLKSKDRIMQEEIFgPVVGFVKVNDFD 430
Cdd:cd07122 267 NEEEKEKLEKALFddggtlnpdiVGKSAQKIAELAGieVPEDTKVLVAE--ETGVGPEEPLSREKLS-PVLAFYRAEDFE 343
|
250 260
....*....|....*....|....*...
gi 1231725153 431 EAIEVAND-TDYGLTG--AVI-TNNREH 454
Cdd:cd07122 344 EALEKARElLEYGGAGhtAVIhSNDEEV 371
|
|
| |
