|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1-515 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 1049.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 1 MVVAYKHEPFTDFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQ 80
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 81 VADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESR 160
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 161 PIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSE 240
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 241 VGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNPGQIWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKC 320
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 321 SACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDiNMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKGWFIQP 400
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 401 TIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVG 480
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500 510
....*....|....*....|....*....|....*
gi 1926909037 481 YQPFGGFNMSGTDSKAGGPDYLALHMQAKTTSETL 515
Cdd:PRK03137 480 YHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-513 |
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: 875.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 5 YKHEPFTDFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADA 84
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 85 TFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKdGMPVESRPIEY 164
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLR-GFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 165 NRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDY 244
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 245 LVDHPRTRFVSFTGSRDVGIRIYERAAKVNPGQIWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACS 324
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 325 RAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDD--SKGWFIQPTI 402
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLElaAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 403 VADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQ 482
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|.
gi 1926909037 483 PFGGFNMSGTDSKAGGPDYLALHMQAKTTSE 513
Cdd:cd07124 480 PFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-513 |
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: 839.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 5 YKHEPFTDFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADA 84
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 85 TFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRPIEY 164
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 165 NRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDY 244
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 245 LVDHPRTRFVSFTGSRDVGIRIYERAAKVNPGQIWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACS 324
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 325 RAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKGWFIQPTIVA 404
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 405 DVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPF 484
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500
....*....|....*....|....*....
gi 1926909037 485 GGFNMSGTDSKAGGPDYLALHMQAKTTSE 513
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVTE 509
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
35-515 |
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: 556.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 35 QDYPLIIGGEKIT--TEDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRK 112
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 113 HEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMT 192
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 193 TAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAK 272
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 273 vnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNP 352
Cdd:COG1012 243 ------NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 353 DAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEG-DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDF 430
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 431 DHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAiVGYQPFGGFNMSGTDSKaGGPDYLALHMQAKT 510
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
....*
gi 1926909037 511 TSETL 515
Cdd:COG1012 475 VTIRL 479
|
|
| 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: 545.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 50 DKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNE 129
Cdd:pfam00171 7 ETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 130 ADADTAEAIDFMEYYGRQMLKLkDGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAST 209
Cdd:pfam00171 86 ARGEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 210 TPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGG 289
Cdd:pfam00171 165 TPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 290 KDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFD 369
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 370 KVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAV 448
Cdd:pfam00171 319 RVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926909037 449 VSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYqPFGGFNMSGTdSKAGGPDYLALHMQAKT 510
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGF-GREGGPYGLEEYTEVKT 458
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
21-514 |
2.96e-179 |
|
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: 512.89 E-value: 2.96e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 21 AFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADI 100
Cdd:cd07083 3 AMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 101 LFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMP-VESRPIEYNRFSYIPLGVGVIIS 179
Cdd:cd07083 83 LLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGLGAGVVIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 180 PWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGS 259
Cdd:cd07083 163 PWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 260 RDVGIRIYERAAKVNPGQIWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNR 339
Cdd:cd07083 243 LETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 340 AVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFG 419
Cdd:cd07083 323 LLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 420 PV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAG 497
Cdd:cd07083 403 PVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
490
....*....|....*..
gi 1926909037 498 GPDYLALHMQAKTTSET 514
Cdd:cd07083 483 GPHYLRRFLEMKAVAER 499
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-510 |
6.50e-160 |
|
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: 461.29 E-value: 6.50e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 76 EKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGM 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 156 PVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVP 235
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 236 GNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGF 315
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE------NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 316 SGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDS- 393
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 394 KGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRG 473
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1926909037 474 CTGAiVGYQPFGGFNMSGTdSKAGGPDYLALHMQAKT 510
Cdd:cd07078 395 SVGA-EPSAPFGGVKQSGI-GREGGPYGLEEYTEPKT 429
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-513 |
8.39e-157 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 456.66 E-value: 8.39e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 16 EANKLAFEEGLKKVESYLGQDYPLIIGGEkITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPE 95
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIINGEE-TETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 96 MRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRPIEYNRFSYIPLGVG 175
Cdd:cd07125 92 ERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 176 VIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVS 255
Cdd:cd07125 172 VCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 256 FTGSRDVGIRIYE-RAAKVNPgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYD 334
Cdd:cd07125 252 FTGSTETAKLINRaLAERDGP----ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 335 HVLNRAVELTKELTVGNPdaKDIN--MGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKGWFIQPTIVADVAEDarL 412
Cdd:cd07125 328 RFIEMLKGAMASLKVGDP--WDLStdVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIF--D 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 413 MKEEIFGPV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMS 490
Cdd:cd07125 404 LTTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLS 483
|
490 500
....*....|....*....|...
gi 1926909037 491 GTDSKAGGPDYLALHMQAKTTSE 513
Cdd:cd07125 484 GTGPKAGGPNYLLRFGNEKTVSL 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
37-510 |
3.99e-147 |
|
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: 430.13 E-value: 3.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFS 116
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 117 AILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRP---IEYNRfsyIPLGVGVIISPWNFPFAIMAGMTT 193
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPgveVETTR---EPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 194 AALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKV 273
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 274 npgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPD 353
Cdd:cd07097 238 ------GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 354 AKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGE---GDDsKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKD 429
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGErlkRPD-EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 430 FDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGaiVGYQ-PFGGFNMSGTDSKAGGPDYLALHMQA 508
Cdd:cd07097 391 YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALEFYTTI 468
|
..
gi 1926909037 509 KT 510
Cdd:cd07097 469 KT 470
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-499 |
1.59e-140 |
|
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: 413.67 E-value: 1.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 41 IGGEKI--TTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAI 118
Cdd:cd07131 3 IGGEWVdsASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 119 LVKEAGKPWNEADADTAEAIDFMEYY---GRQMLklkdGMPVESRPIEYNRFSY-IPLGVGVIISPWNFPFAIMAGMTTA 194
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAageGRRLF----GETVPSELPNKDAMTRrQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 195 ALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVN 274
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 275 pgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDA 354
Cdd:cd07131 239 ------KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 355 KDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGG-----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKD 429
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGgerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 430 FDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVgYQPFGGFNMSGTDSKAGGP 499
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGT 461
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-502 |
8.49e-128 |
|
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: 382.32 E-value: 8.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 6 KHEPFTDF---SVEANKLafEEGLKKVESyLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVA 82
Cdd:cd07123 2 VNEPVLSYapgSPERAKL--QEALAELKS-LTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 83 DATFQTWRKSKPEMRADILFRAAAIVR-RRKHEFSAILVKEAGKPWNEADADTA-EAIDFMEYYGRQMLKLKDGMPVESR 160
Cdd:cd07123 79 LEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 161 PIEYNRFSYIPL-GVGVIISPWNFPfAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGS 239
Cdd:cd07123 159 AGVWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 240 EVGDYLVDHPRTRFVSFTGSRDVGIRIYERAA------KVNPgqiwlkRVIAEMGGKDTMVVDKEADLELAAKSIVASAF 313
Cdd:cd07123 238 VVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryRTYP------RIVGETGGKNFHLVHPSADVDSLVTATVRGAF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 314 GFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKE--EGKIVSGGEGD 391
Cdd:cd07123 312 EYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGKCD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 392 DSKGWFIQPTIVADVAEDARLMKEEIFGPVVAF--CKAKDFDHALAIANNT-EYGLTGAVVSNNRDHIEKAREDFH--VG 466
Cdd:cd07123 392 DSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAG 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 1926909037 467 NLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYL 502
Cdd:cd07123 472 NFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNL 507
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
39-491 |
5.40e-127 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 378.86 E-value: 5.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGE--KITTEDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:cd07091 6 LFINNEfvDSVSGKTFPTINPAT-EEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNE-ADADTAEAIDFMEYYGrqmlKLKDGMPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAG 190
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYA----GWADKIQGKTIPIDGNFLAYTrrePIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 191 MTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERA 270
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 271 AKVNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVG 350
Cdd:cd07091 241 AKSN-----LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 351 NPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKD 429
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 430 FDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgcTGAIVGYQ-PFGGFNMSG 491
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
52-491 |
2.11e-126 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 377.29 E-value: 2.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 52 IVSVNPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07086 15 FTSRNPANGEPIA-RVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYY---GRQMlklkDG--MPVEsRPieyNRFSY---IPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVL 203
Cdd:cd07086 94 GEVQEMIDICDYAvglSRML----YGltIPSE-RP---GHRLMeqwNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 204 LKPASTTPVVAAK----FMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiw 279
Cdd:cd07086 166 WKPSETTPLTAIAvtkiLAEVLEKNGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 280 lKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINM 359
Cdd:cd07086 240 -GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 360 GPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEG--DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAI 436
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1926909037 437 ANNTEYGLTGAVVSNNRDHIEKAREDF--HVGNLYFNRGCTGAIVGyQPFGGFNMSG 491
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
55-491 |
2.26e-126 |
|
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: 376.39 E-value: 2.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADT 134
Cdd:cd07103 2 INPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLkDGMPVESrPIEYNRFSYI--PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPV 212
Cdd:cd07103 81 DYAASFLEWFAEEARRI-YGRTIPS-PAPGKRILVIkqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 213 VAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDT 292
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT------VKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 293 MVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVM 372
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 373 SYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSN 451
Cdd:cd07103 313 ALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1926909037 452 NRDHIEKAREDFHVGNLYFNRGCTGAIVgyQPFGGFNMSG 491
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESG 430
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
12-512 |
2.10e-125 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 393.92 E-value: 2.10e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 12 DFSVEANKLAFEEGLKKVESYLGQDYPlIIGGEKITTEDKIVsVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRK 91
Cdd:COG4230 534 DLSDEAVLAALSAALAAAAEKQWQAAP-LIAGEAASGEARPV-RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 92 SKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQmlklkdgmpveSRPIEYNRFSYIP 171
Cdd:COG4230 612 TPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQ-----------ARRLFAAPTVLRG 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 172 LGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRT 251
Cdd:COG4230 681 RGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRI 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 252 RFVSFTGSRDVGIRIYERAAKVNPGQIWLkrvIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACsRAV-IHE 330
Cdd:COG4230 761 AGVAFTGSTETARLINRTLAARDGPIVPL---IAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSAL-RVLcVQE 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 331 DVYDHVLNRAVELTKELTVGNPD--AKDInmGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDS--KGWFIQPTI--VA 404
Cdd:COG4230 837 DIADRVLEMLKGAMAELRVGDPAdlSTDV--GPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcaNGTFVAPTLieID 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 405 DVAEdarlMKEEIFGP---VVAFcKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGY 481
Cdd:COG4230 915 SISD----LEREVFGPvlhVVRY-KADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGV 989
|
490 500 510
....*....|....*....|....*....|.
gi 1926909037 482 QPFGGFNMSGTDSKAGGPDYLALHMQAKTTS 512
Cdd:COG4230 990 QPFGGEGLSGTGPKAGGPHYLLRFATERTVT 1020
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
82-510 |
1.07e-120 |
|
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: 358.85 E-value: 1.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 82 ADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRP 161
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 162 IEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEV 241
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 242 GDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCS 321
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAEN------LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 322 ACSRAVIHEDVYDHVLNRAVeltkeltvgnpdakdinmgpvndqaafdkvmsyvaigkeegkivsggegddskgwfiqpT 401
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV-----------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 402 IVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAiVGY 481
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPE 336
|
410 420
....*....|....*....|....*....
gi 1926909037 482 QPFGGFNMSGTdSKAGGPDYLALHMQAKT 510
Cdd:cd06534 337 APFGGVKNSGI-GREGGPYGLEEYTRTKT 364
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-512 |
2.29e-120 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 378.00 E-value: 2.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 12 DFSVEANKLAFEEGLKKVESYLGQDYPLIIGgekitTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRK 91
Cdd:PRK11904 529 NLNDRSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSR 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 92 SKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYY---GRQMLklkdGMPVESR-PI-EYNR 166
Cdd:PRK11904 604 TPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYaaqARRLF----GAPEKLPgPTgESNE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 167 FSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLV 246
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALT 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 247 DHPRTRFVSFTGSRDVGIRI----YERAAKVNPgqiwlkrVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSA 322
Cdd:PRK11904 760 ADPRIAGVAFTGSTETARIInrtlAARDGPIVP-------LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 323 CSRAVIHEDVYDHVLnravELTK----ELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDS--KGW 396
Cdd:PRK11904 833 LRVLFVQEDIADRVI----EMLKgamaELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGteNGH 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 397 FIQPTIVAdvAEDARLMKEEIFGPV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGC 474
Cdd:PRK11904 909 FVAPTAFE--IDSISQLEREVFGPIlhVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQ 986
|
490 500 510
....*....|....*....|....*....|....*...
gi 1926909037 475 TGAIVGYQPFGGFNMSGTDSKAGGPDYLALHMQAKTTS 512
Cdd:PRK11904 987 IGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-506 |
4.70e-119 |
|
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: 358.12 E-value: 4.70e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 41 IGGEKITTEDK--IVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAI 118
Cdd:cd07088 2 INGEFVPSSSGetIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 119 LVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVS 198
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 199 GNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvNpgqi 278
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 279 wLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDIN 358
Cdd:cd07088 236 -ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 359 MGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDS-KGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAI 436
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 437 ANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQpfGGFNMSGT---DSKAGGPDYLALHM 506
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHGLEEYLQTKV 465
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
12-502 |
3.11e-117 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 373.05 E-value: 3.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 12 DFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEkiTTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRK 91
Cdd:PRK11905 531 DLSDEATLAALDEALNAFAAKTWHAAPLLAGGD--VDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 92 SKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGMPVEsrpieynrfsyiP 171
Cdd:PRK11905 609 TPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHK------------P 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 172 LGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRT 251
Cdd:PRK11905 677 LGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRI 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 252 RFVSFTGSRDVGIRIYERAAKVNPGQIWLkrvIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHED 331
Cdd:PRK11905 757 AGVMFTGSTEVARLIQRTLAKRSGPPVPL---IAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQED 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 332 VYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIV--SGGEGDDSKGWFIQPTI--VADVA 407
Cdd:PRK11905 834 VADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhqLPLPAETEKGTFVAPTLieIDSIS 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 408 EdarlMKEEIFGPV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFG 485
Cdd:PRK11905 914 D----LEREVFGPVlhVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFG 989
|
490
....*....|....*..
gi 1926909037 486 GFNMSGTDSKAGGPDYL 502
Cdd:PRK11905 990 GEGLSGTGPKAGGPLYL 1006
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
62-492 |
1.89e-115 |
|
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: 348.43 E-value: 1.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFM 141
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 142 EYYGRQMLKLK-DGMPVESRPIEYNRFSY---IPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKF 217
Cdd:cd07149 90 RLSAEEAKRLAgETIPFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 218 MEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAkvnpgqiwLKRVIAEMGGKDTMVVDK 297
Cdd:cd07149 170 AELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 298 EADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAI 377
Cdd:cd07149 242 DADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 378 GKEEG-KIVSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHI 456
Cdd:cd07149 322 AVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1926909037 457 EKAREDFHVGNLYFNRGCTgAIVGYQPFGGFNMSGT 492
Cdd:cd07149 399 LKAARELEVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-511 |
2.34e-115 |
|
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: 348.40 E-value: 2.34e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADA- 132
Cdd:cd07093 1 NFNPATGEVL-AKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGrQMLKLKDGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPV 212
Cdd:cd07093 80 DIPRAAANFRFFA-DYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 213 VAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDT 292
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 293 MVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVM 372
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 373 SYVAIGKEEG-KIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGA 447
Cdd:cd07093 313 GYVELARAEGaTILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 448 VVSNNRDHIEKAREDFHVG----NLYFNRGCTgaivgyQPFGGFNMSGTdSKAGGPDYLALHMQAKTT 511
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGtvwvNCWLVRDLR------TPFGGVKASGI-GREGGDYSLEFYTELKNV 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-511 |
5.14e-115 |
|
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: 347.62 E-value: 5.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYYGRQMLKLKDG-MPVESRPIeynrFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAvIPVDKGDY----LNFTrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEM 287
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYVAIGKEEG-KIVSGGE----GDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEY 442
Cdd:cd07114 310 LEKVERYVARAREEGaRVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEY 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 443 GLTGAVVSNNRDHIEKAREDFHVGNLYFNrgcTGAIVGYQ-PFGGFNMSGTDsKAGGPDYLALHMQAKTT 511
Cdd:cd07114 390 GLAAGIWTRDLARAHRVARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIG-RENGIEAIREYTQTKSV 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-491 |
1.13e-114 |
|
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: 346.80 E-value: 1.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 41 IGGEKI--TTEDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAI 118
Cdd:cd07138 3 IDGAWVapAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 119 LVKEAGKPWNEADADTAE-AIDFMEYYgrqmLKLKDGMPVESRpIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALV 197
Cdd:cd07138 82 ITLEMGAPITLARAAQVGlGIGHLRAA----ADALKDFEFEER-RGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 198 SGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgq 277
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 278 iwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDI 357
Cdd:cd07138 233 --VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 358 NMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEG---DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHA 433
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGPGrpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 434 LAIANNTEYGLTGAVVSNNRDHIEK-AREdFHVGNLYFNrgctGAIVGYQ-PFGGFNMSG 491
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAvARR-LRAGQVHIN----GAAFNPGaPFGGYKQSG 445
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
54-491 |
2.53e-113 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 343.06 E-value: 2.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQT-WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADA 132
Cdd:cd07109 1 VFDPST-GEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGRQMLKLkDGmpvESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAST 209
Cdd:cd07109 80 DVEAAARYFEYYGGAADKL-HG---ETIPLGPGYFVYTvrePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 210 TPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAK-VNPgqiwlkrVIAEMG 288
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEnVVP-------VTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 289 GKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGnPDAKDINMGPVNDQAAF 368
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 369 DKVMSYVAIGKEEG-KIVSGG---EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL 444
Cdd:cd07109 308 DRVEGFVARARARGaRIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 445 TGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYqPFGGFNMSG 491
Cdd:cd07109 388 VAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
75-499 |
1.06e-110 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 335.27 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 75 AEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMeyygRQMLklkdG 154
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL----REAA----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 155 MPVESR----PIEYN-RFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAA-KFMEVLEEAG 225
Cdd:cd07104 74 LPRRPEgeilPSDVPgKESMVrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIFEEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 226 LPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAA 305
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDADLDLAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 306 KSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KI 384
Cdd:cd07104 228 SAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 385 VSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFH 464
Cdd:cd07104 308 LTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLE 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 1926909037 465 VGNLYFNRGCT--GAIVgyqPFGGFNMSGTdSKAGGP 499
Cdd:cd07104 385 TGMVHINDQTVndEPHV---PFGGVKASGG-GRFGGP 417
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
55-491 |
1.21e-110 |
|
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: 335.65 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADT 134
Cdd:cd07106 2 INPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLK-----DGMPVESRpieynrfsYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAST 209
Cdd:cd07106 81 GGAVAWLRYTASLDLPDEvieddDTRRVELR--------RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 210 TPVVAAKFMEVLEEAgLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGG 289
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 290 KDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFD 369
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 370 KVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAV 448
Cdd:cd07106 305 KVKELVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1926909037 449 VSNNRDHIEKAREDFHVGNLYFNRgcTGAIVGYQPFGGFNMSG 491
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSG 425
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-491 |
4.75e-110 |
|
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: 334.68 E-value: 4.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 56 NPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTA 135
Cdd:cd07150 5 NPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 136 EAIDFMEYYGRQMLKLKDgmpvESRPIEYN-RFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07150 84 FTPELLRAAAGECRRVRG----ETLPSDSPgTVSMSvrrPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKD 291
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRH------LKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 292 TMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKV 371
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 372 MSYVAIGKEEG-KIVSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVS 450
Cdd:cd07150 314 KRQVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1926909037 451 NNRDHIEKAREDFHVGNLYFNrGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHIN-DPTILDEAHVPFGGVKASG 430
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
55-491 |
8.28e-109 |
|
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: 331.62 E-value: 8.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADT 134
Cdd:cd07110 2 INPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLKDGMPvESRPIEYNRFS----YIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTT 210
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAE-RAVPLPSEDFKarvrREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 211 PVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGK 290
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 291 DTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDK 370
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 371 VMSYVAIGKEEG-KIVSGGE--GDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGA 447
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1926909037 448 VVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
54-497 |
4.28e-108 |
|
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: 329.72 E-value: 4.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADAD 133
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 134 TAEAIDFMEYYGRQMLKLK-DGMPVESRPIEYNRfsYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPV 212
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKgETIPVGGRNLHYTL--REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 213 VAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDT 292
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG------IKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 293 MVVDKEADLELAAKSIVASA-FGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKV 371
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 372 MSYVAIGKEEG-KIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07107 311 MHYIDSAKREGaRLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 447 AVVSNNRDHIEKAREDFHVGNLYFNRGCT---GAivgyqPFGGFNMSGTDSKAG 497
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRhflGA-----PFGGVKNSGIGREEC 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
54-491 |
9.97e-108 |
|
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: 328.63 E-value: 9.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPAnKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA-DA 132
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGRQMLKLK-DGMPVESRPIEYNRFSyiPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEgEVIPVRGPFLNYTVRE--PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYeRAAKVNpgqiwLKRVIAEMGGKD 291
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIM-QGAAGN-----LKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 292 TMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKV 371
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 372 MSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVS 450
Cdd:cd07115 312 LDYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1926909037 451 NNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
55-502 |
7.94e-107 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 346.58 E-value: 7.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANKEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADT 134
Cdd:PRK11809 664 INPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEV 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMlklkdgmpvesRPiEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVA 214
Cdd:PRK11809 744 REAVDFLRYYAGQV-----------RD-DFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 215 AKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGiRIYER--AAKVNP-GQ-IWLkrvIAEMGGK 290
Cdd:PRK11809 812 AQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRnlAGRLDPqGRpIPL---IAETGGQ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 291 DTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDK 370
Cdd:PRK11809 888 NAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKAN 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 371 VMSYVAIGKEEGKIVSGGEGDDSKGW----FIQPTIV--ADVAEdarlMKEEIFGPV---VAFcKAKDFDHALAIANNTE 441
Cdd:PRK11809 968 IERHIQAMRAKGRPVFQAARENSEDWqsgtFVPPTLIelDSFDE----LKREVFGPVlhvVRY-NRNQLDELIEQINASG 1042
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926909037 442 YGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYL 502
Cdd:PRK11809 1043 YGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1103
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
55-510 |
1.77e-106 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 325.74 E-value: 1.77e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKS-KPEMRADILFRAAAIVRRRKHEFSAILVKEAGKP-WNEADA 132
Cdd:cd07089 2 INPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGRQMLK--LKDGMPVESRPIEYNR--FSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAS 208
Cdd:cd07089 81 QVDGPIGHLRYFADLADSfpWEFDLPVPALRGGPGRrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 209 TTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMG 288
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 289 GKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAF 368
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 369 DKVMSYVAIGKEEG-KIVSGGEGDDS--KGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLT 445
Cdd:cd07089 315 DRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926909037 446 GAVVSNNRDH-IEKAREdFHVGNLYFNRGCTGAIvgYQPFGGFNMSGTdSKAGGPDYLALHMQAKT 510
Cdd:cd07089 395 GGVWSADVDRaYRVARR-IRTGSVGINGGGGYGP--DAPFGGYKQSGL-GRENGIEGLEEFLETKS 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
52-492 |
9.58e-105 |
|
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: 321.22 E-value: 9.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 52 IVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07145 1 IEVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYYGRQMLKLKDG-MPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGEtIPVDAYEYNERRIAFTvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEM 287
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYVAIGKEEG-KIVSGGEGDDskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07145 314 VERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1926909037 447 AVVSNNRDHIEKAREDFHVGNLYFNrGCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
55-491 |
1.03e-104 |
|
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: 321.95 E-value: 1.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADA 132
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGRQMLKLKDGMpVESRPieyNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAST 209
Cdd:cd07119 97 DIDDVANCFRYYAGLATKETGEV-YDVPP---HVISRTvrePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 210 TPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGG 289
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 290 KDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFD 369
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 370 KVMSYVAIGKEEG-KIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL 444
Cdd:cd07119 327 KVLSYIQLGKEEGaRLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1926909037 445 TGAVVSNNRDHIEK-ARE---------DFHVgnlYFNRGctgaivgyqPFGGFNMSG 491
Cdd:cd07119 407 AGAVWTKDIARANRvARRlragtvwinDYHP---YFAEA---------PWGGYKQSG 451
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
12-502 |
1.48e-103 |
|
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: 319.55 E-value: 1.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 12 DFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVsVNPANKEELVGRVSKASRELAEKAMQVADATFQTWRK 91
Cdd:TIGR01238 14 DLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPV-TNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 92 SKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMlklKDGMPvesrpieynRFSYIP 171
Cdd:TIGR01238 93 TPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQV---RDVLG---------EFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 172 LGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRT 251
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 252 RFVSFTGSRDVGIRIYERAAKVNPGQIWLkrvIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHED 331
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 332 VYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKGW----FIQPTIVA--D 405
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACqhgtFVAPTLFEldD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 406 VAEdarlMKEEIFGPV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQP 483
Cdd:TIGR01238 398 IAE----LSEEVFGPVlhVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
490
....*....|....*....
gi 1926909037 484 FGGFNMSGTDSKAGGPDYL 502
Cdd:TIGR01238 474 FGGQGLSGTGPKAGGPHYL 492
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
39-491 |
2.42e-103 |
|
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: 318.20 E-value: 2.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGEKITTED--KIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQT-WRKSKPEMRADILFRAAAIVRRRKHEF 115
Cdd:cd07144 10 LFINNEFVKSSDgeTIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 116 SAILVKEAGKPWNE-ADADTAEAIDFMEYYGrqmlKLKDGMPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGM 191
Cdd:cd07144 89 AAIEALDSGKPYHSnALGDLDEIIAVIRYYA----GWADKIQGKTIPTSPNKLAYTlhePYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 192 TTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGiRIYERAA 271
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG-RLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 272 KVNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKE-LTVG 350
Cdd:cd07144 244 AQN-----LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 351 NPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEG---DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCK 426
Cdd:cd07144 319 SPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 427 AKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNR---GCTGAivgyqPFGGFNMSG 491
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsndSDVGV-----PFGGFKMSG 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-510 |
2.45e-103 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 317.92 E-value: 2.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 38 PLIIGGEKI--TTEDKIVSVNPANKEeLVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEF 115
Cdd:cd07085 2 KLFINGEWVesKTTEWLDVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 116 SAILVKEAGKPWNEADADTAEAIDFMEYY-GRQMLKLKDGMPVESRPIEyNRFSYIPLGVGVIISPWNFPFAIMAGMTTA 194
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFAcSIPHLLKGEYLENVARGID-TYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 195 ALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVN 274
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 275 pgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDA 354
Cdd:cd07085 239 ------KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 355 KDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDD----SKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKD 429
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 430 FDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGctgaI---VGYQPFGGFNmsgtDSKAG-----GPDY 501
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVP----IpvpLAFFSFGGWK----GSFFGdlhfyGKDG 464
|
....*....
gi 1926909037 502 LALHMQAKT 510
Cdd:cd07085 465 VRFYTQTKT 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-511 |
5.39e-103 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 316.85 E-value: 5.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQ--TWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA- 130
Cdd:cd07112 6 TINPAT-GRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 131 DADTAEAIDFMEYYGRQMLKLKDgmpvESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYG----EVAPTGPDALALItrePLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwLKRVIAEM 287
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSN-----LKRVWLEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVV-DKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQA 366
Cdd:cd07112 236 GGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 367 AFDKVMSYVAIGKEEG-KIVSGGEGD--DSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYG 443
Cdd:cd07112 316 HFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 444 LTGAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGtdskaGGPDyLALH-----MQAKTT 511
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG-----NGRD-KSLHaldkyTELKTT 460
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
39-510 |
5.67e-103 |
|
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: 316.82 E-value: 5.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGEKIT--TEDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQ--TWRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:cd07139 1 LFIGGRWVApsGSETIDVVSPAT-EEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKP-WNEADADTAEAIDFMEYYgrqmLKLKDGMPVESR----PIEYNRFSYIPLGVGVIISPWNFPFAIMA 189
Cdd:cd07139 80 LARLWTAENGMPiSWSRRAQGPGPAALLRYY----AALARDFPFEERrpgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 190 GMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYER 269
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 270 AAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTV 349
Cdd:cd07139 235 CGER------LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 350 GNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEG--DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCK 426
Cdd:cd07139 309 GDPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 427 AKDFDHALAIANNTEYGLTGAVVSNNRDH-IEKAREdFHVGNLYFNrgctGAIVGYQ-PFGGFNMSGTdSKAGGPDYLAL 504
Cdd:cd07139 389 YDDEDDAVRIANDSDYGLSGSVWTADVERgLAVARR-IRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDA 462
|
....*.
gi 1926909037 505 HMQAKT 510
Cdd:cd07139 463 YLETKS 468
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
75-491 |
6.02e-101 |
|
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: 310.16 E-value: 6.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 75 AEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYY---GRQMLKL 151
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYaenAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 152 KdgmPVESRPIEynrfSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPA 228
Cdd:cd07100 81 E---PIETDAGK----AYVryePLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 229 GVVNFVPGNGSEVgDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSI 308
Cdd:cd07100 154 GVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKN------LKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 309 VASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSG 387
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 388 GEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGN 467
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420
....*....|....*....|....*..
gi 1926909037 468 LYFNrgctgAIVGYQ---PFGGFNMSG 491
Cdd:cd07100 387 VFIN-----GMVKSDprlPFGGVKRSG 408
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
37-491 |
1.39e-100 |
|
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: 311.04 E-value: 1.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKITTEDKIVSV-NPANKEeLVGRVSKASRELAEKAMQVADATFQTWRKSKP-EMRADILFRAAAIVRRRKHE 114
Cdd:cd07082 2 FKYLINGEWKESSGKTIEVySPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLkDGMPVESRPIEYNR-----FSYIPLGVGVIISPWNFPFAIMA 189
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGDSLPGDWFPGTKgkiaqVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 190 GMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYER 269
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 270 AAKvnpgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTV 349
Cdd:cd07082 240 HPM--------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 350 GNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDdsKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAK 428
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 429 DFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIvGYQPFGGFNMSG 491
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
56-511 |
1.45e-100 |
|
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: 310.39 E-value: 1.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 56 NPANKEeLVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTA 135
Cdd:cd07090 3 EPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 136 EAIDFMEYYGrqmlKLKDGMPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPV 212
Cdd:cd07090 82 SSADCLEYYA----GLAPTLSGEHVPLPGGSFAYTrrePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 213 VAAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDT 292
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG------IKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 293 MVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVM 372
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 373 SYVAIGKEEG-KIVSGGEGDDSK-----GWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07090 311 GYIESAKQEGaKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 447 AVVSNN--RDHIEKARedFHVGNLYFNR-GCTGAIVgyqPFGGFNMSGTdSKAGGPDYLALHMQAKTT 511
Cdd:cd07090 391 GVFTRDlqRAHRVIAQ--LQAGTCWINTyNISPVEV---PFGGYKQSGF-GRENGTAALEHYTQLKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
55-492 |
5.77e-100 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 309.66 E-value: 5.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQ---TWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA- 130
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 131 DADTAEAIDFMEYYGrqmlKLKDGMPVESRPIEYNRFSYI---PLGV-GVIIsPWNFPFAIMAGMTTAALVSGNTVLLKP 206
Cdd:cd07141 106 LVDLPGAIKVLRYYA----GWADKIHGKTIPMDGDFFTYTrhePVGVcGQII-PWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 207 ASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwLKRVIAE 286
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSN-----LKRVTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 287 MGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQA 366
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 367 AFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLT 445
Cdd:cd07141 336 QFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLA 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 446 GAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07141 416 AAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
55-492 |
8.03e-99 |
|
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: 305.41 E-value: 8.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNE-ADAD 133
Cdd:cd07092 2 VDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 134 TAEAIDFMEYYG---RQMLKLKDGmpvesrpiEY--NRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLK 205
Cdd:cd07092 81 LPGAVDNFRFFAgaaRTLEGPAAG--------EYlpGHTSMIrrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 206 PASTTPVVAAKFMEVLEEaGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIA 285
Cdd:cd07092 153 PSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT------LKRVHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 286 EMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQ 365
Cdd:cd07092 226 ELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 366 AAFDKVMSYVAIGKEEGKIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLT 445
Cdd:cd07092 306 AQRERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 446 GAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGT 492
Cdd:cd07092 386 SSVWTRDVGRAMRLSARLDFGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
47-455 |
4.52e-98 |
|
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: 304.23 E-value: 4.52e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 47 TTEDKIVSVNPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKP 126
Cdd:cd07151 7 TSERTIDVLNPYTGETLA-EIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 127 -------WNEADADTAEAIDF---MEyyGRQMLKLKDGmpvesrpiEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAAL 196
Cdd:cd07151 86 rikanieWGAAMAITREAATFplrME--GRILPSDVPG--------KENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 197 VSGNTVLLKPASTTPVVAAK-FMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnp 275
Cdd:cd07151 156 ALGNAVVLKPASDTPITGGLlLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRH-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 276 gqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAK 355
Cdd:cd07151 234 ----LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 356 DINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHAL 434
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420
....*....|....*....|.
gi 1926909037 435 AIANNTEYGLTGAVVSNNRDH 455
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLER 407
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
37-491 |
8.55e-98 |
|
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: 303.88 E-value: 8.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKITTEDK--IVSVNPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:cd07559 1 YDNFINGEWVAPSKGeyFDNYNPVNGKVLC-EIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEA-DADTAEAIDFMEYYGRQMLKLKDGMPVesrpIEYNRFSYI---PLGV-GVIIsPWNFPFaIMA 189
Cdd:cd07559 80 LAVAETLDNGKPIRETlAADIPLAIDHFRYFAGVIRAQEGSLSE----IDEDTLSYHfhePLGVvGQII-PWNFPL-LMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 190 GMTTA-ALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYE 268
Cdd:cd07559 154 AWKLApALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 269 RAAKVnpgqiwLKRVIAEMGGKDTM-----VVDKEADLELAAKSIVAsAFGF-SGQKCSACSRAVIHEDVYDHVLNRAVE 342
Cdd:cd07559 233 YAAEN------LIPVTLELGGKSPNiffddAMDADDDFDDKAEEGQL-GFAFnQGEVCTCPSRALVQESIYDEFIERAVE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 343 LTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGE----GDDSKGWFIQPTIVADVAEDARLMKEEI 417
Cdd:cd07559 306 RFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 418 FGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07559 386 FGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
27-491 |
1.34e-97 |
|
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: 303.68 E-value: 1.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 27 KKVESYLGqdypLIIGGEKITTEDK--IVSVNPANkEELVGRVSKASRELAEKAMQVADATFQT-WRKS-KPEMRADILF 102
Cdd:cd07143 1 GKYEQPTG----LFINGEFVDSVHGgtVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 103 RAAAIVRRRKHEFSAILVKEAGKPWNEADA-DTAEAIDFMEYYGRQMLKLKdGMPVESRPieyNRFSYI---PLGVGVII 178
Cdd:cd07143 76 KLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIH-GQVIETDI---KKLTYTrhePIGVCGQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 179 SPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTG 258
Cdd:cd07143 152 IPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 259 SRDVGIRIYERAAKVNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLN 338
Cdd:cd07143 232 STLVGRKVMEAAAKSN-----LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 339 RAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEI 417
Cdd:cd07143 307 RFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 418 FGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07143 387 FGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
56-491 |
7.57e-97 |
|
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: 300.82 E-value: 7.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 56 NPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPW-NEADADT 134
Cdd:cd07108 3 NPATGQVI-GEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLKDgmpvESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07108 82 AVLADLFRYFGGLAGELKG----ETLPFGPDVLTYTvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKD 291
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR------LIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 292 TMVVDKEADLELAAKSIVASA-FGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDK 370
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 371 VMSYVAIGKE--EGKIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL 444
Cdd:cd07108 311 VCGYIDLGLStsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 445 TGAVVSNNRDHIEKAREDFHVGNLYFNRGctGAIVGYQPFGGFNMSG 491
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
62-491 |
2.80e-95 |
|
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: 296.65 E-value: 2.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFM 141
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 142 --------EYYGRQMlKLKDGMPVESRPIEYNRFsyiPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVV 213
Cdd:cd07094 90 rlaaeeaeRIRGEEI-PLDATQGSDNRLAWTIRE---PVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 214 AAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvnpgqiwlKRVIAEMGGKDTM 293
Cdd:cd07094 166 ALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 294 VVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMS 373
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 374 YVAIGKEEG-KIVSGGEGDDSkgwFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNN 452
Cdd:cd07094 318 WVEEAVEAGaRLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 1926909037 453 RDHIEKAREDFHVGNLYFNRGcTGAIVGYQPFGGFNMSG 491
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
63-491 |
7.54e-94 |
|
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: 292.70 E-value: 7.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 63 LVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDF 140
Cdd:cd07118 9 VVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 141 MEY---YGRQML-----KLKDGM-PVESRPieynrfsyiPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07118 89 WRYaasLARTLHgdsynNLGDDMlGLVLRE---------PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKD 291
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARN------LKKVSLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 292 TMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKV 371
Cdd:cd07118 234 PQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 372 MSYVAIGKEEG-KIVSGGEGDDS-KGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVV 449
Cdd:cd07118 314 TDYVDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1926909037 450 SNNRDHIEKAREDFHVGNLYFNRGCTGAIvgYQPFGGFNMSG 491
Cdd:cd07118 394 SKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
37-491 |
1.01e-93 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 293.71 E-value: 1.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKI--TTEDKIVSVNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:PRK13252 7 QSLYIDGAYVeaTSGETFEVINPATGEVL-ATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEAD-ADTAEAIDFMEYYGrqmlKLKDGMPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAG 190
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYA----GLAPALEGEQIPLRGGSFVYTrrePLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 191 MTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGsEVGDYLVDHPRTRFVSFTGSRDVGIRIYERA 270
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 271 AKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVG 350
Cdd:PRK13252 241 AAS------LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 351 NPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFC 425
Cdd:PRK13252 315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGerltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926909037 426 KAKDFDHALAIANNTEYGLTGAVVSN--NRDHIEKARedFHVGNLYFNR-GCTGAIVgyqPFGGFNMSG 491
Cdd:PRK13252 395 TFDDEDEVIARANDTEYGLAAGVFTAdlSRAHRVIHQ--LEAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-499 |
1.06e-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: 289.58 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIdfm 141
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 142 eyygrQMLKLKDGMPVESR----PIEYNRFSY---IPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVA 214
Cdd:cd07152 79 -----GELHEAAGLPTQPQgeilPSAPGRLSLarrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 215 -AKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDTM 293
Cdd:cd07152 154 gVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRH------LKKVSLELGGKNAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 294 VVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMS 373
Cdd:cd07152 227 IVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 374 YVAIGKEEG-KIVSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNN 452
Cdd:cd07152 307 IVDDSVAAGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRD 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 453 RDHIEKAREDFHVGNLYFNRGcTGAIVGYQPFGGFNMSGTDSKAGGP 499
Cdd:cd07152 384 VGRAMALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
101-505 |
1.35e-92 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 288.17 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 101 LFRAAAIVRRRKHEFSAILVKEAGKPWNEADAD---TAEAIDFMEYYGRQMlklkDGMPVES-RPIEyNRFSY-IPLGVG 175
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEvafTADYIDYMAEWARRY----EGEIIQSdRPGE-NILLFkRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 176 VIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVS 255
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 256 FTGSRDVGIRIYERAAKvNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDH 335
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAK-N-----ITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 336 VLNRAVELTKELTVGNP-DAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLM 413
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 414 KEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQpfGGFNMS--- 490
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgig 387
|
410
....*....|....*
gi 1926909037 491 GTDSKAGGPDYLALH 505
Cdd:PRK10090 388 GADGKHGLHEYLQTQ 402
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
54-509 |
3.54e-92 |
|
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: 289.39 E-value: 3.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQ--TWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07142 23 TIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 -ADTAEAIDFMEYYGRQMLKLKdGMPVesrPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:cd07142 102 yAEVPLAARLFRYYAGWADKIH-GMTL---PADGPHHVYTlhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwLKRVIAEM 287
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN-----LKPVTLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:cd07142 253 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07142 333 FEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAA 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 447 AVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTdSKAGGPDYLALHMQAK 509
Cdd:cd07142 413 GVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGI-GREKGIYALNNYLQVK 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
41-505 |
9.48e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 288.90 E-value: 9.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 41 IGGEKITTED--KIVSVNPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAI 118
Cdd:PLN02278 29 IGGKWTDAYDgkTFPVYNPATGEVIA-NVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 119 LVKEAGKPWNEADADTAEAIDFMEYY-----------------GRQMLKLKDgmpvesrpieynrfsyiPLGVGVIISPW 181
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFaeeakrvygdiipspfpDRRLLVLKQ-----------------PVGVVGAITPW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 182 NFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRD 261
Cdd:PLN02278 171 NFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 262 VGIRIYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAV 341
Cdd:PLN02278 251 VGKKLMAGAAAT------VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 342 ELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYV--AIGKeEGKIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFG 419
Cdd:PLN02278 325 KAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVqdAVSK-GAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 420 PVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGyqPFGGFNMSGT---DSKA 496
Cdd:PLN02278 404 PVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLgreGSKY 481
|
....*....
gi 1926909037 497 GGPDYLALH 505
Cdd:PLN02278 482 GIDEYLEIK 490
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
55-491 |
1.35e-91 |
|
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: 286.81 E-value: 1.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADT 134
Cdd:cd07099 1 RNPAT-GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLKDGMPVESRPIEYN---RFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEAGLPAGVVNFVPGNGsEVGDYLVDHpRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKD 291
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER------LIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 292 TMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKV 371
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 372 MSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVS 450
Cdd:cd07099 312 RRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1926909037 451 NNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
36-491 |
4.10e-89 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 281.41 E-value: 4.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 36 DYPLIIGGEKITTEDKIVSV-NPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVyNPATGEVLA-EIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEADAD----TAEAIDFMEYYGRQMLKLKDGmpvesrpiEY--NRFSYI---PLGVGVIISPWNFPF 185
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDeipaIVDVFRFFAGAARCLEGKAAG--------EYleGHTSMIrrdPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 186 AIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIR 265
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 266 IYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTK 345
Cdd:PRK13473 232 VLSAAADS------VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 346 ELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG--KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVA 423
Cdd:PRK13473 306 TLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926909037 424 FCKAKDFDHALAIANNTEYGLTGAVVSNN--RDHIEKAREDFhvgnlyfnrGCT-----GAIVGYQPFGGFNMSG 491
Cdd:PRK13473 386 VTPFDDEDQAVRWANDSDYGLASSVWTRDvgRAHRVSARLQY---------GCTwvnthFMLVSEMPHGGQKQSG 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-448 |
8.36e-89 |
|
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: 280.00 E-value: 8.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANKEELvGRVSKASRELAEKAMQVADATFQ--TWRkSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07120 1 SIDPATGEVI-GTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYYGrQMLKLKDGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTP 211
Cdd:cd07120 79 FEISGAISELRYYA-GLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 212 VVAAKFMEVLEEA-GLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGK 290
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT------LKRLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 291 DTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDK 370
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 371 VMSYV--AIGKEEGKIVSGGEGDD--SKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07120 312 VDRMVerAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
..
gi 1926909037 447 AV 448
Cdd:cd07120 392 SV 393
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
62-491 |
3.13e-88 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 278.36 E-value: 3.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFM 141
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 142 EYYGRQMLKLkDG--MPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAK 216
Cdd:cd07147 90 RIAAEEATRI-YGevLPLDISARGEGRQGLVrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 217 FMEVLEEAGLPAGVVNFVPGNgSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvnpgqiwlKRVIAEMGGKDTMVVD 296
Cdd:cd07147 169 LGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--------KKVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 297 KEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVA 376
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 377 IGKEEG-KIVSGGEGDDSkgwFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDH 455
Cdd:cd07147 320 EAVDAGaKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1926909037 456 IEKAREDFHVGNLYFN-----RgctgaiVGYQPFGGFNMSG 491
Cdd:cd07147 397 ALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSG 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
37-491 |
4.61e-88 |
|
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: 278.57 E-value: 4.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKITTE--DKIVSVNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:cd07117 1 YGLFINGEWVKGSsgETIDSYNPANGETL-SEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEA-DADTAEAIDFMEYYGRQMLKLKDgmpvESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAG 190
Cdd:cd07117 80 LAMVETLDNGKPIRETrAVDIPLAADHFRYFAGVIRAEEG----SANMIDEDTLSIVlrePIGVVGQIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 191 MTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERA 270
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 271 AKvnpgqiwlkRVIA---EMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKEL 347
Cdd:cd07117 235 AK---------KLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 348 TVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGG----EGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVV 422
Cdd:cd07117 306 KVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926909037 423 AFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07117 386 TVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
39-491 |
1.91e-87 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 277.77 E-value: 1.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGEKITTEDK--IVSVNPANkEELVGRVSKASRELAEKAMQVADATF-----QTWRKSKPEMRADILFRAAAIVRRR 111
Cdd:PLN02467 10 LFIGGEWREPVLGkrIPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 112 KHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQM--LKLKDGMPVeSRPIEYNRfSYI---PLGVGVIISPWNFPFa 186
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAeaLDAKQKAPV-SLPMETFK-GYVlkePLGVVGLITPWNYPL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 187 IMAGMTTA-ALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIR 265
Cdd:PLN02467 166 LMATWKVApALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 266 IYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTK 345
Cdd:PLN02467 246 IMTAAAQM------VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 346 ELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGE--GDDSKGWFIQPTIVADVAEDARLMKEEIFGPVV 422
Cdd:PLN02467 320 NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGaTILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926909037 423 AFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-491 |
1.60e-83 |
|
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: 265.29 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 78 AMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKP-WN---EADADTAE-AIDFMEYYGRQMLKLK 152
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWEaqtEVAAMAGKiDISIKAYHERTGERAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 153 DGMPVESRpieynrFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVN 232
Cdd:cd07095 85 PMAQGRAV------LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 233 FVPGNGsEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvNPGQIwlkrvIA-EMGGKDTMVVDKEADLELAAKSIVAS 311
Cdd:cd07095 159 LVQGGR-ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAG-RPGKI-----LAlEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 312 AFGFSGQKCSACSRAVIHED-VYDHVLNRAVELTKELTVGNPDAKDINMGP-VNDQAAFDKVMSYVAIGKEEGKIVSGGE 389
Cdd:cd07095 232 AFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPlIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 390 GDDSKGWFIQPTIVaDVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLY 469
Cdd:cd07095 312 RLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|..
gi 1926909037 470 FNRGCTGAiVGYQPFGGFNMSG 491
Cdd:cd07095 391 WNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
62-497 |
2.89e-83 |
|
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: 265.38 E-value: 2.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADAtfqtwRKSK--PEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAID 139
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAAS-----YRSTltRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 140 FMEYYGRQMLKLkDG--MPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVA 214
Cdd:cd07146 85 VLRFAAAEALRD-DGesFSCDLTANGKARKIFTlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 215 AKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAkvnpgqiwLKRVIAEMGGKDTMV 294
Cdd:cd07146 164 IYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 295 VDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSY 374
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 375 VAIGKEEG-KIVSGGEGDdskGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNR 453
Cdd:cd07146 316 VEEAIAQGaRVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1926909037 454 DHIEKAREDFHVGNLYFNRGctgaiVGYQ----PFGGFNMSGTDSKAG 497
Cdd:cd07146 393 DTIKRLVERLDVGTVNVNEV-----PGFRselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
37-491 |
6.76e-82 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 262.82 E-value: 6.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 37 YPLIIGGEKITTED--KIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRK 112
Cdd:cd07140 6 HQLFINGEFVDAEGgkTYNTINPTD-GSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 113 HEFSAILVKEAGKPWNEA-DADTAEAIDFMEYYGRQMLKLK-DGMPV-ESRP---IEYNRFSyiPLGVGVIISPWNFPFA 186
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQgKTIPInQARPnrnLTLTKRE--PIGVCGIVIPWNYPLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 187 IMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRI 266
Cdd:cd07140 163 MLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 267 YERAAKVNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKE 346
Cdd:cd07140 243 MKSCAVSN-----LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 347 LTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFC 425
Cdd:cd07140 318 MKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 426 KAK--DFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRgctgaivgYQ------PFGGFNMSG 491
Cdd:cd07140 398 KFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--------YNktdvaaPFGGFKQSG 463
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
42-458 |
7.88e-82 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 262.14 E-value: 7.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 42 GGEKITTEDKIVSVNPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVK 121
Cdd:cd07130 4 DGEWGGGGGVVTSISPANGEPIA-RVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 122 EAGKPWNEADADTAEAIDFMEY---YGRQMlklkDG--MPVEsRP----IEynrfSYIPLGVGVIISPWNFPFAIMAGMT 192
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFavgLSRQL----YGltIPSE-RPghrmME----QWNPLGVVGVITAFNFPVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 193 TAALVSGNTVLLKPASTTPVVAAK----FMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGS----RDVGI 264
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGStavgRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 265 RIYERaakvnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELT 344
Cdd:cd07130 233 AVAAR----------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 345 KELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEE-GKIVSGGEGDDSKGWFIQPTIVaDVAEDARLMKEEIFGPVVA 423
Cdd:cd07130 303 KQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILY 381
|
410 420 430
....*....|....*....|....*....|....*
gi 1926909037 424 FCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEK 458
Cdd:cd07130 382 VLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
75-452 |
9.74e-82 |
|
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: 260.59 E-value: 9.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 75 AEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAID-FMEYYGRQMLKLKD 153
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGmLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 154 GMPVEsrpiEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGV 230
Cdd:cd07105 82 SIPSD----KPGTLAMVvkePVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 231 VNFV---PGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKS 307
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAANA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 308 IVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAkdinmGPVNDQAAFDKVMSYV--AIGKEeGKIV 385
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVddALSKG-AKLV 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 386 SGGEGDDSK-GWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNN 452
Cdd:cd07105 306 VGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRD 373
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
49-492 |
1.22e-81 |
|
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: 261.99 E-value: 1.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 49 EDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQT-WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPW 127
Cdd:cd07113 14 EKRLDITNPAT-EQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 128 NEADA-DTAEAIDFMEYYGRQMLKLKDGMPVESRPI----EYNRFSYI-PLGVGVIISPWNFPFAIMAGMTTAALVSGNT 201
Cdd:cd07113 93 HLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSmqgeRYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 202 VLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGsEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLK 281
Cdd:cd07113 173 IVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASD------LT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 282 RVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGP 361
Cdd:cd07113 246 RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 362 VNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNT 440
Cdd:cd07113 326 LANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDT 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1926909037 441 EYGLTGAVVSNNRDHIEKAREDFHVGNLYFN-RGCTGAIVgyqPFGGFNMSGT 492
Cdd:cd07113 406 PFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGI 455
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
55-484 |
1.73e-81 |
|
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: 260.64 E-value: 1.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWneadADT 134
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPI----AQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 135 AEAIDFMEYYGRQMLKLKDGMPVESRPIEYNRF-SYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTT 210
Cdd:cd07102 76 GGEIRGMLERARYMISIAEEALADIRVPEKDGFeRYIrrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 211 PVVAAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIyERAAKVNpgqiwLKRVIAEMGGK 290
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAI-QRAAAGR-----FIKVGLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 291 DTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDK 370
Cdd:cd07102 229 DPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 371 VMSYVAIGKEEGKIVSGGEG----DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTG 446
Cdd:cd07102 309 VRAQIADAIAKGARALIDGAlfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1926909037 447 AVVSNNRDHIEKAREDFHVGNLYFNR------------------GCTGAIVGYQPF 484
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNRcdyldpalawtgvkdsgrGVTLSRLGYDQL 444
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
57-491 |
3.69e-81 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 259.93 E-value: 3.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 57 PANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAE 136
Cdd:cd07101 3 PFTGEPL-GELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 137 AIDFMEYYGRQMLKL------KDGMPVESRPIEYnrfsYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTT 210
Cdd:cd07101 82 VAIVARYYARRAERLlkprrrRGAIPVLTRTTVN----RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 211 PVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHprTRFVSFTGSRDVGIRIYERAAkvnpgqiwlKRVI---AEM 287
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG---------RRLIgcsLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYVAIGKEEGKIV-SGGEGDDSKG-WFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLT 445
Cdd:cd07101 307 LDRVTAHVDDAVAKGATVlAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 446 GAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQ-PFGGFNMSG 491
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSG 433
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
62-510 |
1.34e-80 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 260.14 E-value: 1.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQ--TWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADA-DTAEAI 138
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 139 DFMEYYGRQMLKLKDGMPVESRPIeynrFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAA 215
Cdd:PLN02766 127 GLLRYYAGAADKIHGETLKMSRQL----QGYTlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 216 KFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwLKRVIAEMGGKDTMVV 295
Cdd:PLN02766 203 FYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN-----LKQVSLELGGKSPLLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 296 DKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYV 375
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 376 AIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRD 454
Cdd:PLN02766 358 EHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLD 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1926909037 455 HIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTdSKAGGPDYLALHMQAKT 510
Cdd:PLN02766 438 VANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGF-GRDQGMDALDKYLQVKS 490
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
54-502 |
2.47e-80 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 258.48 E-value: 2.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 54 SVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA-DA 132
Cdd:cd07111 41 TINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 133 DTAEAIDFMEYYGRQMLKLKDGMPvesrpieynrfSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPV 212
Cdd:cd07111 120 DIPLVARHFYHHAGWAQLLDTELA-----------GWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 213 VAAKFMEVLEEAGLPAGVVNFVPGNGSeVGDYLVDHPRTRFVSFTGSRDVGiRIYERAAKvnpGqiWLKRVIAEMGGKDT 292
Cdd:cd07111 189 TALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVG-RALRRATA---G--TGKKLSLELGGKSP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 293 MVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVM 372
Cdd:cd07111 262 FIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 373 SYVAIGKEEGKIVSGGEGD-DSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSN 451
Cdd:cd07111 342 ELVEEGRAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSE 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1926909037 452 NRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTdSKAGGPDYL 502
Cdd:cd07111 422 NLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGF-GREGGKEGL 469
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
61-497 |
7.19e-79 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 256.66 E-value: 7.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 61 EELVGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNE-ADADTAEA 137
Cdd:PLN02466 83 GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKAELPMF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 138 IDFMEYYGRQMLKLKdGMPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKF 217
Cdd:PLN02466 163 ARLFRYYAGWADKIH-GLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 218 MEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwLKRVIAEMGGKDTMVVDK 297
Cdd:PLN02466 242 AKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN-----LKPVTLELGGKSPFIVCE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 298 EADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAI 377
Cdd:PLN02466 317 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 378 GKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHI 456
Cdd:PLN02466 397 GVESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTA 476
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1926909037 457 EKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSGTDSKAG 497
Cdd:PLN02466 477 NTLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKG 515
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
62-491 |
3.72e-76 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 249.02 E-value: 3.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 62 ELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKpwNEADA-----DTAE 136
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK--ARRHAfeevlDVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 137 AidfMEYYGRQMLKL------KDGMPVESRPIEYnrfsYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTT 210
Cdd:PRK09407 121 T---ARYYARRAPKLlaprrrAGALPVLTKTTEL----RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 211 PVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHprTRFVSFTGSRDVGIRIYERAAkvnpgqiwlKRVI---AEM 287
Cdd:PRK09407 194 PLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG---------RRLIgfsLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYVAIGKEEG-KIVSGGEGDDSKG-WFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLT 445
Cdd:PRK09407 343 LETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1926909037 446 GAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQ-PFGGFNMSG 491
Cdd:PRK09407 423 ASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSG 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
50-502 |
1.32e-75 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 246.36 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 50 DKIVSVNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNE 129
Cdd:PRK11241 26 EVIDVTNPANGDKL-GSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 130 ADADTAEAIDFMEYYGRQMLKL-KDGMP---VESRPIEYNRfsyiPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLK 205
Cdd:PRK11241 105 AKGEISYAASFIEWFAEEGKRIyGDTIPghqADKRLIVIKQ----PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 206 PASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIA 285
Cdd:PRK11241 181 PASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD------IKKVSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 286 EMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQ 365
Cdd:PRK11241 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 366 AAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL 444
Cdd:PRK11241 335 KAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926909037 445 TGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGyqPFGGFNMSG---TDSKAGGPDYL 502
Cdd:PRK11241 415 AAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
66-491 |
7.03e-73 |
|
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: 239.28 E-value: 7.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 66 RVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA-DADTAEAIDFMEYY 144
Cdd:cd07116 31 EVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAADIPLAIDHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 145 GRQMLKLKDGMP-VESRPIEYNrfSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEE 223
Cdd:cd07116 111 AGCIRAQEGSISeIDENTVAYH--FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 224 AgLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGK-------DTMVVD 296
Cdd:cd07116 189 L-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN------IIPVTLELGGKspniffaDVMDAD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 297 kEADLELAAKSIVASAFGfSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVA 376
Cdd:cd07116 262 -DAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYID 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 377 IGKEEG-KIVSGGE----GDDSKGWFIQPTIVADvAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSN 451
Cdd:cd07116 340 IGKEEGaEVLTGGErnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTR 418
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1926909037 452 NRDHIEKAREDFHVGNLYFNrgCTGAIVGYQPFGGFNMSG 491
Cdd:cd07116 419 DGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-491 |
1.17e-70 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 232.71 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 52 IVSVNPANKEeLVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:PRK09406 3 IATINPATGE-TVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYYGRQMLKLKDGMPVESRPIEYNR--FSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPAST 209
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEPADAAAVGASRayVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 210 TPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDhPRTRFVSFTGSRDVGiriyeRAAKVNPGQIwLKRVIAEMGG 289
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRD-PRVAAATLTGSEPAG-----RAVAAIAGDE-IKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 290 KDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFD 369
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 370 KVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAV 448
Cdd:PRK09406 315 EVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1926909037 449 VSNNRDHIEKAREDFHVGNLYFNrgctGAIVGYQ--PFGGFNMSG 491
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSG 435
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
39-491 |
2.29e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 232.54 E-value: 2.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGEKIT-TEDKIVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSA 117
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 118 ILVKEAGKP-W---NEADADTAE-AIDFMEYY---GRQMLKLKDGMPVesrpieynrFSYIPLGVGVIISPWNFPFAIMA 189
Cdd:PRK09457 82 VIARETGKPlWeaaTEVTAMINKiAISIQAYHertGEKRSEMADGAAV---------LRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 190 GMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYER 269
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 270 AAKvNPGQIwlkrVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVY-DHVLNRAVELTKELT 348
Cdd:PRK09457 232 FAG-QPEKI----LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 349 VGNPDAKDIN-MGPVNDQAAFDKVMS----YVAIGKE---EGKIVSGGEGddskgwFIQPTIVaDVAEDARLMKEEIFGP 420
Cdd:PRK09457 307 VGRWDAEPQPfMGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG------LLTPGII-DVTGVAELPDEEYFGP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926909037 421 VVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAiVGYQPFGGFNMSG 491
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
56-512 |
9.61e-67 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 222.83 E-value: 9.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 56 NPANKEeLVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTA 135
Cdd:TIGR01722 22 NPATNE-VTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 136 EAIDFMEYY-GRQMLKLKDGMPVESRPIEYnrFSY-IPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVV 213
Cdd:TIGR01722 101 RGLEVVEHAcGVNSLLKGETSTQVATRVDV--YSIrQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 214 AAKFMEVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNpgqiwlKRVIAEMGGKDTM 293
Cdd:TIGR01722 179 AVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG------KRVQALGGAKNHM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 294 VVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVyDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMS 373
Cdd:TIGR01722 252 VVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVAS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 374 YVAIGKEEG-KIVSGGEGDDSKGW----FIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAV 448
Cdd:TIGR01722 331 LIAGGAAEGaEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAI 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926909037 449 VSNNRDHIEKAREDFHVGNLYFNRGCTgAIVGYQPFGGFNMS-GTDSKAGGPDYLALHMQAKTTS 512
Cdd:TIGR01722 411 FTRDGAAARRFQHEIEVGQVGVNVPIP-VPLPYFSFTGWKDSfFGDHHIYGKQGTHFYTRGKTVT 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
46-491 |
3.48e-66 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 220.89 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 46 ITTEDKIVSVNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGK 125
Cdd:PRK13968 3 ITPATHAISVNPATGEQL-SVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 126 PWNEADADTAEAIDFMEYY---GRQMLKlkdgmpVESRPIEYNR--FSYIPLGVGVIISPWNFP-FAIMAGmTTAALVSG 199
Cdd:PRK13968 82 PINQARAEVAKSANLCDWYaehGPAMLK------AEPTLVENQQavIEYRPLGTILAIMPWNFPlWQVMRG-AVPILLAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 200 NTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDhPRTRFVSFTGSRDVGIRIYERAAKVnpgqiw 279
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 280 LKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINM 359
Cdd:PRK13968 228 LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 360 GPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIAN 438
Cdd:PRK13968 308 GPMARFDLRDELHHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 439 NTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGC-TGAIVGyqpFGGFNMSG 491
Cdd:PRK13968 388 DSEFGLSATIFTTDETQARQMAARLECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
55-502 |
1.22e-62 |
|
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: 211.77 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANKEELvGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADAD- 133
Cdd:cd07098 1 YDPATGQHL-GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 134 ---TAEAIDFMEYYGRQMLKlkdgmPvESRPIEYN------RFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLL 204
Cdd:cd07098 80 ilvTCEKIRWTLKHGEKALR-----P-ESRPGGLLmfykraRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 205 KPASTTPVVAAKFMEVLEEA----GLPAGVVNFVPGNGsEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVnpgqiwL 280
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES------L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 281 KRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMG 360
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 361 PVNDQAAFDKVMSYVAIGKEEG-KIVSGGE----GDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALA 435
Cdd:cd07098 307 AMISPARFDRLEELVADAVEKGaRLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926909037 436 IANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDsKAGGPDYL 502
Cdd:cd07098 387 IANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGL 452
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
34-459 |
2.40e-62 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 211.92 E-value: 2.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 34 GQDYPLIIGGE-KITTEDKIVSV-NPANKEELVgRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRR 111
Cdd:PLN00412 13 GDVYKYYADGEwRTSSSGKSVAItNPSTRKTQY-KVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 112 KHEFSAILVKEAGKPWNEADADTAEAIDFMEY--------YGRQMLKLKDGMPVESRPiEYNRFSYIPLGVGVIISPWNF 183
Cdd:PLN00412 92 KAPIAECLVKEIAKPAKDAVTEVVRSGDLISYtaeegvriLGEGKFLVSDSFPGNERN-KYCLTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 184 PFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSrDVG 263
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 264 IRIYERAAKVnPGQIwlkrviaEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVEL 343
Cdd:PLN00412 250 IAISKKAGMV-PLQM-------ELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 344 TKELTVGNPDaKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSggEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVA 423
Cdd:PLN00412 322 VAKLTVGPPE-DDCDITPVVSESSANFIEGLVMDAKEKGATFC--QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLP 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1926909037 424 FCKAKDFDHALAIANNTEYGLTGAVVSnnRDhIEKA 459
Cdd:PLN00412 399 VIRINSVEEGIHHCNASNFGLQGCVFT--RD-INKA 431
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-491 |
6.84e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 210.52 E-value: 6.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 39 LIIGGE--KITTEDKIVSVNPANKEELvGRVSKASRELAEKAMQVADATFQT--WRKSKPEMRADILFRAAAIVRRRKHE 114
Cdd:PRK09847 22 LFINGEytAAAENETFETVDPVTQAPL-AKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 115 FSAILVKEAGKPWNEA-DADTAEAIDFMEYYGRQMLKLKDgmpvESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAG 190
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYG----EVATTSSHELAMIvrePVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 191 MTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERA 270
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 271 AKVNPGQIWLkrviaEMGGKDTMVVDKEA-DLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTV 349
Cdd:PRK09847 257 GDSNMKRVWL-----EAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 350 GNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEgddSKGW--FIQPTIVADVAEDARLMKEEIFGPVVAFCKA 427
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGR---NAGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 428 KDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVgyQPFGGFNMSG 491
Cdd:PRK09847 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG 470
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
55-508 |
4.71e-60 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 204.57 E-value: 4.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANKEeLVGRVSKASRELAEKAMQVADATFQT---WrkSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:cd07148 4 VNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEYYGRQMLKLK-DGMPVESRPIEYNRFSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGgREIPMGLTPASAGRIAFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFMEVLEEAGLPAGVVNFVPgNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIyerAAKVNPGQiwlkRVIAEM 287
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWML---RSKLAPGT----RCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 288 GGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAA 367
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 368 FDKVMSYV--AIGKeEGKIVSGGE--GDDSkgwfIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYG 443
Cdd:cd07148 313 VDRVEEWVneAVAA-GARLLCGGKrlSDTT----YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926909037 444 LTGAVVSNNRDHIEKAREDFHVGNLYFNRGcTGAIVGYQPFGGFNMSGTDSkaGGPDYLALHMQA 508
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYGT--GGIPYTMHDMTQ 449
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
52-497 |
7.87e-58 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 200.06 E-value: 7.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 52 IVSVNPANKEElVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD 131
Cdd:PLN02315 36 VSSVNPANNQP-IAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 132 ADTAEAIDFMEY---YGRQMlklkDGMPVES-RPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPA 207
Cdd:PLN02315 115 GEVQEIIDMCDFavgLSRQL----NGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 208 STTPVVAAKFM----EVLEEAGLPAGVVNFVPGnGSEVGDYLVDHPRTRFVSFTGSRDVGIrIYERAAKVNPGQIWLkrv 283
Cdd:PLN02315 191 PTTPLITIAMTklvaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGL-MVQQTVNARFGKCLL--- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 284 iaEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVN 363
Cdd:PLN02315 266 --ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 364 ---DQAAFDKVMSyvAIGKEEGKIVSGGEGDDSKGWFIQPTIVaDVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNT 440
Cdd:PLN02315 344 tpeSKKNFEKGIE--IIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSV 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1926909037 441 EYGLTGAVVSNNRDHIEK--AREDFHVGNLYFNRGCTGAIVGyQPFGGFNMSGTDSKAG 497
Cdd:PLN02315 421 PQGLSSSIFTRNPETIFKwiGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
38-471 |
2.37e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 198.43 E-value: 2.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 38 PLIIGGEKITTEDK--IVSVNPANkEELVGRVSKASRELAEKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEF 115
Cdd:PLN02419 115 PNLIGGSFVESQSSsfIDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 116 SAILVKEAGKPWNEADADTAEAIDFMEYY-GRQMLKLKDGMPVESRPIEYNRFSYiPLGVGVIISPWNFPFAIMAGMTTA 194
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHAcGMATLQMGEYLPNVSNGVDTYSIRE-PLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 195 ALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVgDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVN 274
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 275 pgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVlNRAVELTKELTVGNPDA 354
Cdd:PLN02419 352 ------KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWE-DKLVERAKALKVTCGSE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 355 KDINMGPVNDQAAFDKVMSYVAIGKEEGK---------IVSGGEgddsKGWFIQPTIVADVAEDARLMKEEIFGPVVAFC 425
Cdd:PLN02419 425 PDADLGPVISKQAKERICRLIQSGVDDGAkllldgrdiVVPGYE----KGNFIGPTILSGVTPDMECYKEEIFGPVLVCM 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1926909037 426 KAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFN 471
Cdd:PLN02419 501 QANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
84-491 |
2.50e-54 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 188.50 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 84 ATFQTwRKSKP-EMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD----ADTAEAIDFMEYYGRQMLKLKD-GMPV 157
Cdd:cd07087 9 ETFLT-GKTRSlEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVVLGEIDHALKHLKKWMKPRRvSVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 158 ESRPIEynrfSYI---PLGVGVIISPWNFPF----AIMAGmttaALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGV 230
Cdd:cd07087 88 LLQPAK----AYVipePLGVVLIIGPWNYPLqlalAPLIG----AIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 231 VNFVPGnGSEVGDYLVDHPrtrF--VSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSI 308
Cdd:cd07087 159 VAVVEG-GVEVATALLAEP---FdhIFFTGSPAVGKIVMEAAAK------HLTPVTLELGGKSPCIVDKDANLEVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 309 VASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDiNMGPVNDQAAFDKVMSYVaigkEEGKIVSGG 388
Cdd:cd07087 229 AWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLL----DDGKVVIGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 389 EGDDSKGwFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNL 468
Cdd:cd07087 304 QVDKEER-YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
410 420
....*....|....*....|...
gi 1926909037 469 YFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07087 383 CVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
170-492 |
7.33e-53 |
|
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: 185.12 E-value: 7.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 170 IPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGdYLVDHp 249
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT-ALLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 250 RTRFVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIH 329
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAK------HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 330 EDVYDHVLNRAVELTKELTVGNPDAKDiNMGPVNDQAAFDKVMSYvaIGKEEGKIVSGGEGDDSKGwFIQPTIVADVAED 409
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSL--LDTTKGKVVIGGEMDEATR-FIPPTIVSDVSWD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 410 ARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNR-----GCTGAivgyqPF 484
Cdd:cd07135 334 DSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtlihvGVDNA-----PF 408
|
....*...
gi 1926909037 485 GGFNMSGT 492
Cdd:cd07135 409 GGVGDSGY 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
168-491 |
8.00e-50 |
|
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: 176.93 E-value: 8.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 168 SYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGnGSEVGDY 244
Cdd:cd07136 94 SYIyyePYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 245 LVDhprTRF--VSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSA 322
Cdd:cd07136 172 LLD---QKFdyIFFTGSVRVGKIVMEAAAK------HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 323 CSRAVIHEDVYDHVLNRAVELTKEL----TVGNPDAKDInmgpVNDQAaFDKVMSYVaigkEEGKIVSGGEGDDsKGWFI 398
Cdd:cd07136 243 PDYVLVHESVKEKFIKELKEEIKKFygedPLESPDYGRI----INEKH-FDRLAGLL----DNGKIVFGGNTDR-ETLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 399 QPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAredfhVGNLYFNRGCTG-A 477
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKV-----LENLSFGGGCINdT 387
|
330
....*....|....*...
gi 1926909037 478 IV----GYQPFGGFNMSG 491
Cdd:cd07136 388 IMhlanPYLPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
84-491 |
2.49e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 174.06 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 84 ATFQTwRKSKP-EMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEAD-ADT----AEAIDFMEYYGRQMLKLKDGMPV 157
Cdd:PTZ00381 18 ESFLT-GKTRPlEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVlltvAEIEHLLKHLDEYLKPEKVDTVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 158 ESRPIEynrfSYI---PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFV 234
Cdd:PTZ00381 97 VFGPGK----SYIipePLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 235 PGnGSEVGDYLVDHPRTrFVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFG 314
Cdd:PTZ00381 172 EG-GVEVTTELLKEPFD-HIFFTGSPRVGKLVMQAAAE------NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 315 FSGQKCSACSRAVIHEDVYDHVLNRAVELTKELtVGNPDAKDINMGPVNDQAAFDKVMSYvaIGKEEGKIVSGGEGDDSK 394
Cdd:PTZ00381 244 NAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAEL--IKDHGGKVVYGGEVDIEN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 395 GWfIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGC 474
Cdd:PTZ00381 321 KY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCV 399
|
410
....*....|....*..
gi 1926909037 475 TGAIVGYQPFGGFNMSG 491
Cdd:PTZ00381 400 FHLLNPNLPFGGVGNSG 416
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
84-491 |
6.76e-46 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 166.25 E-value: 6.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 84 ATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPwnEADADTAEAIDFMEYYGRQMLKLKDGM-PVESR-P 161
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP--AAEVDLTEILPVLSEINHAIKHLKKWMkPKRVRtP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 162 IEY----NRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVpgN 237
Cdd:cd07134 87 LLLfgtkSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE--G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 238 GSEVGDYLVDHPrtrF--VSFTGSRDVGIRIYERAAKVnpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGF 315
Cdd:cd07134 165 DAEVAQALLELP---FdhIFFTGSPAVGKIVMAAAAKH------LASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 316 SGQKCSACSRAVIHEDVYDHVLNRAV-ELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEG-KIVSGGEGDDS 393
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEHLKaEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGaKVEFGGQFDAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 394 KGwFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrg 473
Cdd:cd07134 316 QR-YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-- 392
|
410 420
....*....|....*....|..
gi 1926909037 474 ctGAIVGYQ----PFGGFNMSG 491
Cdd:cd07134 393 --DVVLHFLnpnlPFGGVNNSG 412
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
76-504 |
1.16e-42 |
|
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: 157.40 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 76 EKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA-----DADTAEAIDFMEYYGRqmlk 150
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicgDQVQLRARAFVIYSYR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 151 LKDGmPVESRPIEYN---RFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAG-L 226
Cdd:cd07084 78 IPHE-PGNHLGQGLKqqsHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 227 PAGVVNFVPGNGsEVGDYLVDHPRTRFVSFTGSRDVGiriyeRAAKVNPGQIwlkRVIAEMGGKDTMVVDKEAD-LELAA 305
Cdd:cd07084 157 PPEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVA-----EKLALDAKQA---RIYLELAGFNWKVLGPDAQaVDYVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 306 KSIVASAFGFSGQKCSACSRAVIHEdvyDHVLNRAVELTKELTVGNPDaKDINMGPVndqaAFDKVMSYVAIGKEEGKIV 385
Cdd:cd07084 228 WQCVQDMTACSGQKCTAQSMLFVPE---NWSKTPLVEKLKALLARRKL-EDLLLGPV----QTFTTLAMIAHMENLLGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 386 SGGEGDDSKGWFIQPTIVADVA--------EDAR---LMKEEIFGPV--VAFCKAKDFDHALAIANNTEYGLTGAVVSNN 452
Cdd:cd07084 300 LLFSGKELKNHSIPSIYGACVAsalfvpidEILKtyeLVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSND 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 453 RDHIEKAREDFHV-GNLYF-NRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYLAL 504
Cdd:cd07084 380 PIFLQELIGNLWVaGRTYAiLRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
171-491 |
6.91e-40 |
|
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: 149.68 E-value: 6.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 171 PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPaSTTPVVAAKFMEVLeeagLPA-------GVVNfvpgNGSEVGD 243
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKP-SEVSPATAKLLAEL----IPKyldkecyPVVL----GGVEETT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 244 YLVDHpRTRFVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSAC 323
Cdd:cd07132 171 ELLKQ-RFDYIFYTGSTSVGKIVMQAAAK------HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 324 SRAVIHEDVYDHVLNRAVELTKELtVGNPDAKDINMGP-VNDQAaFDKVMSYVaigkEEGKIVSGGEGDDSKGwFIQPTI 402
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRiINDRH-FQRLKKLL----SGGKVAIGGQTDEKER-YIAPTV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 403 VADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQ 482
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSL 396
|
....*....
gi 1926909037 483 PFGGFNMSG 491
Cdd:cd07132 397 PFGGVGNSG 405
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
84-497 |
6.36e-39 |
|
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: 147.17 E-value: 6.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 84 ATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADAD-----TAEAIDFMEYYGRQMLKLKDGMPVE 158
Cdd:cd07137 10 ETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDevsvlVSSCKLAIKELKKWMAPEKVKTPLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 159 SRPIEYNRFSYiPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVvAAKFMEVLEEAGLPAGVVNFVPGnG 238
Cdd:cd07137 90 TFPAKAEIVSE-PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPA-TSALLAKLIPEYLDTKAIKVIEG-G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 239 SEVGDYLVDHPRTRfVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGF-SG 317
Cdd:cd07137 167 VPETTALLEQKWDK-IFFTGSPRVGRIIMAAAAK------HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 318 QKCSACSRAVIHEDvYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEGDDSKgWF 397
Cdd:cd07137 240 QACIAPDYVLVEES-FAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKN-LY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 398 IQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGA 477
Cdd:cd07137 318 IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQY 397
|
410 420
....*....|....*....|
gi 1926909037 478 IVGYQPFGGFNMSGTDSKAG 497
Cdd:cd07137 398 AIDTLPFGGVGESGFGAYHG 417
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
95-491 |
4.02e-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: 136.46 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 95 EMRADILFRAAAIVRRRKHEFSAILVKEAGkpwNEADADTA--------EAIDfmeyYGRQmlKLKDGMPVESRPIE--- 163
Cdd:cd07133 20 EERRDRLDRLKALLLDNQDALAEAISADFG---HRSRHETLlaeilpsiAGIK----HARK--HLKKWMKPSRRHVGllf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 164 ---YNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGnGSE 240
Cdd:cd07133 91 lpaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 241 VG--------DYLVdhprtrfvsFTGSRDVGiRIYERAAKVNpgqiwLKRVIAEMGGKDTMVVDKEADLELAAKSIVASA 312
Cdd:cd07133 169 VAaafsslpfDHLL---------FTGSTAVG-RHVMRAAAEN-----LTPVTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 313 FGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKEL---TVGNPDAKDInmgpVNDqAAFDKVMSYVAIGKEEG-KIVSGG 388
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYTSI----INE-RHYARLQGLLEDARAKGaRVIELN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 389 EG--DDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVG 466
Cdd:cd07133 309 PAgeDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSG 388
|
410 420
....*....|....*....|....*
gi 1926909037 467 NLYFNRGCTGAIVGYQPFGGFNMSG 491
Cdd:cd07133 389 GVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
55-456 |
7.37e-33 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 131.37 E-value: 7.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 55 VNPANKEELVgRVSKASRELAEkAMQVA-DATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADAD 133
Cdd:PRK11903 24 FDPVTGEELV-RVSATGLDLAA-AFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 134 TAEAIDFMEYYGRQMLKL------KDGMPVE--SRPIEYNRFSYIPL-GVGVIISPWNFPFAIMAGMTTAALVSGNTVLL 204
Cdd:PRK11903 102 IDGGIFTLGYYAKLGAALgdarllRDGEAVQlgKDPAFQGQHVLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 205 KPASTTPVVAAKFMEVLEEAG-LPAGVVNFVPGNGSEvgdyLVDHPRT-RFVSFTGSRDVGIRIYERAAKVNPGQiwlkR 282
Cdd:PRK11903 182 KPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAG----LLDHLQPfDVVSFTGSAETAAVLRSHPAVVQRSV----R 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 283 VIAEMGGKDTMVVDKEAD-----LELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVGNPDAKDI 357
Cdd:PRK11903 254 VNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 358 NMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEG------DDSKGWFIQPTI-VADVAEDARLMKE-EIFGPVVAFCKAKD 429
Cdd:PRK11903 334 RMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdaDPAVAACVGPTLlGASDPDAATAVHDvEVFGPVATLLPYRD 413
|
410 420
....*....|....*....|....*..
gi 1926909037 430 FDHALAIANNTEYGLTGAVVSNNRDHI 456
Cdd:PRK11903 414 AAHALALARRGQGSLVASVYSDDAAFL 440
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
41-458 |
7.90e-29 |
|
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: 119.68 E-value: 7.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 41 IGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEkAMQVADA---------TFQTwrkskpemRADILFRAAAIVRRR 111
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAA-AVAYAREkggpalralTFHE--------RAAMLKALAKYLMER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 112 KHEFSAILVKEAGkpwNEADA--DTAEAIDFMEYY---GRQMLK----LKDGMPVE-SRPieyNRFS----YIPL-GVGV 176
Cdd:cd07128 76 KEDLYALSAATGA---TRRDSwiDIDGGIGTLFAYaslGRRELPnahfLVEGDVEPlSKD---GTFVgqhiLTPRrGVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 177 IISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAG-LPAGVVNFVPGNgseVGDyLVDHPRTR-FV 254
Cdd:cd07128 150 HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGD-LLDHLGEQdVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 255 SFTGSRDVGIRIyeraaKVNPGQIWLK-RVIAEMG-------GKDtmVVDKEADLELAAKSIVASAFGFSGQKCSACSRA 326
Cdd:cd07128 226 AFTGSAATAAKL-----RAHPNIVARSiRFNAEADslnaailGPD--ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 327 VIHEDVYDHVLNRAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGG------EGDDS-KGWFIQ 399
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrfevVGADAeKGAFFP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926909037 400 PTI-VADVAEDARLMKE-EIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEK 458
Cdd:cd07128 379 PTLlLCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
171-491 |
1.56e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 118.29 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 171 PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLeEAGLPAGVVNFVPGnGSEVGDYLVDHPR 250
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 251 TRfVSFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVD---KEADLELAAKSIVASAFGF-SGQKCSACSRA 326
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAAK------HLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 327 VIHEDVYDHVLNRAVELTKELTVGNPDAKDiNMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGeGDDSKGWFIQPTIVADV 406
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGG-SIDEKKLFIEPTILLNP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 407 AEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNrgctGAIVGYQ---- 482
Cdd:PLN02203 337 PLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN----DAIIQYAcdsl 412
|
....*....
gi 1926909037 483 PFGGFNMSG 491
Cdd:PLN02203 413 PFGGVGESG 421
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
171-497 |
1.83e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 115.14 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 171 PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAgLPAGVVNFVPGNGSEVGDYLVDHPR 250
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 251 TRFvsFTGSRDVGIRIYERAAKvnpgqiWLKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGF-SGQKCSACSRAVIH 329
Cdd:PLN02174 191 KIF--YTGSSKIGRVIMAAAAK------HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 330 EDVYDHVLNrAVELTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGEgDDSKGWFIQPTIVADVAED 409
Cdd:PLN02174 263 KEYAPKVID-AMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 410 ARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVVSNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNM 489
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....*...
gi 1926909037 490 SGTDSKAG 497
Cdd:PLN02174 421 SGMGAYHG 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
76-481 |
1.39e-25 |
|
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: 109.17 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 76 EKAMQVADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKP--------------------------WNE 129
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPearlqgelgrttgqlrlfadlvregsWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 130 ADADTAEAidfmeyyGRQMLklkdgmpveSRP-IeynRFSYIPLGVGVIISPWNFPFA--IMAGMTTAALVSGNTVLLK- 205
Cdd:cd07129 82 ARIDPADP-------DRQPL---------PRPdL---RRMLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 206 ----PAsTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKVNPGqiwlK 281
Cdd:cd07129 143 hpahPG-TSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP----I 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 282 RVIAEMGGKDTMVVDKEA---DLELAAKSIVASAFGFSGQKCSACSRAVIHEDV-YDHVLNRAVELTKE------LTVGn 351
Cdd:cd07129 218 PFYAELGSVNPVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAapaqtmLTPG- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 352 pdakdInmgpvndQAAFDKvmSYVAIGKEEGKIVSGGEGDDSKGWFIQPTIVADVAEDAR---LMKEEIFGPVVAFCKAK 428
Cdd:cd07129 297 -----I-------AEAYRQ--GVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRYD 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 429 DFDHALAIANNTEYGLTGAVVSNNRDHiEKARE-----DFHVGNLYFNRGCTGAIVGY 481
Cdd:cd07129 363 DAAELLAVAEALEGQLTATIHGEEDDL-ALAREllpvlERKAGRLLFNGWPTGVEVCP 419
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
166-452 |
3.60e-24 |
|
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: 105.66 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 166 RFSYIPLGvgvIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYL 245
Cdd:cd07126 140 RWPYGPVA---IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 246 VD-HPRTrfVSFTGSRdvgiRIYERAAKVNPGQIWLkrviaEMGGKDTMVVDKE-ADLELAAKSIVASAFGFSGQKCSAC 323
Cdd:cd07126 217 LEaNPRM--TLFTGSS----KVAERLALELHGKVKL-----EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 324 SRAVIHED-VYDHVLNRAVELTKELTVgnpdaKDINMGPV---NDQAAFDKVMSYVAIGKEE----GKIVSGGEGDDSKG 395
Cdd:cd07126 286 SILFAHENwVQAGILDKLKALAEQRKL-----EDLTIGPVltwTTERILDHVDKLLAIPGAKvlfgGKPLTNHSIPSIYG 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926909037 396 wFIQPTIV------ADVAEDARLMKEEIFGP--VVAFCKAKDFDHALAIANNTEYGLTGAVVSNN 452
Cdd:cd07126 361 -AYEPTAVfvpleeIAIEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
82-461 |
4.21e-17 |
|
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: 84.07 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 82 ADATFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEA-DADTAEAID----FMEYYGRQMLKLkdgmP 156
Cdd:cd07127 93 ARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfQAGGPHAQDrgleAVAYAWREMSRI----P 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 157 VESR---------PIEYN-RFSYIPLGVGVIISPWNFP-FAIMAGMTtAALVSGNTVLLKP--ASTTPV--VAAKFMEVL 221
Cdd:cd07127 169 PTAEwekpqgkhdPLAMEkTFTVVPRGVALVIGCSTFPtWNGYPGLF-ASLATGNPVIVKPhpAAILPLaiTVQVAREVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 222 EEAGLPAGVVNFVPGN-GSEVGDYLVDHPRTRFVSFTGSRDVGIRIYERAAKvnpgqiwlKRVIAEMGGKDTMVVDKEAD 300
Cdd:cd07127 248 AEAGFDPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--------AQVYTEKAGVNTVVVDSTDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 301 LELAAKSIVASAFGFSGQKCSACSRAVIHED---------VYDHVlnrAVELTKELT--VGNPDAKDINMGPVNDQAAFD 369
Cdd:cd07127 320 LKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEV---AADLAAAIDglLADPARAAALLGAIQSPDTLA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 370 KVMSYVAIGK--EEGKIVSGGEGDDSKgwFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNT--EYG-L 444
Cdd:cd07127 397 RIAEARQLGEvlLASEAVAHPEFPDAR--VRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaM 474
|
410
....*....|....*..
gi 1926909037 445 TGAVVSNNRDHIEKARE 461
Cdd:cd07127 475 TVGVYSTDPEVVERVQE 491
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
171-377 |
4.08e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 64.94 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 171 PLGVGVIISPWNFPfaiMAGMTTA--ALVSGNTVLLKPASTTPVvAAKFMEVLEEAGLPAG----VVNFVPGNGSEVGDY 244
Cdd:cd07077 100 PIGVTMHILPSTNP---LSGITSAlrGIATRNQCIFRPHPSAPF-TNRALALLFQAADAAHgpkiLVLYVPHPSDELAEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 245 LVDHPRTRFVSFTGSRDVgiriYERAAKVNPGqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFgFSGQKCSACS 324
Cdd:cd07077 176 LLSHPKIDLIVATGGRDA----VDAAVKHSPH----IPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQ 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926909037 325 RAVIHEDVYDHVLNR-----AVE----------LTKELTVGNPDAKDINMGPVNDQAAFDKVMSYVAI 377
Cdd:cd07077 247 NLYVVDDVLDPLYEEfklklVVEglkvpqetkpLSKETTPSFDDEALESMTPLECQFRVLDVISAVEN 314
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
195-458 |
4.13e-10 |
|
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: 61.74 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 195 ALVSGNTVLLKP---ASTTPVVAAKFM-EVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFVSFTGSRDVgiriyERA 270
Cdd:cd07122 119 ALKTRNAIIFSPhprAKKCSIEAAKIMrEAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGM-----VKA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 271 AK--------VNPGQIwlkrviaemggkdTMVVDKEADLELAAKSIVAS-AFGFsGQKCSACSRAVIHEDVYDHVLnrav 341
Cdd:cd07122 194 AYssgkpaigVGPGNV-------------PAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVR---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 342 eltkeltvgnpdakdinmgpvndqAAFDKVMSYVAIGKEEGKIVSGGEGDDSKgwfIQPTIVA------------DVAED 409
Cdd:cd07122 256 ------------------------AELKRRGAYFLNEEEKEKLEKALFDDGGT---LNPDIVGksaqkiaelagiEVPED 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926909037 410 ARLM--------KEEIF-----GPVVAFCKAKDFDHALAIAN-NTEY---GLTGAVVSNNRDHIEK 458
Cdd:cd07122 309 TKVLvaeetgvgPEEPLsreklSPVLAFYRAEDFEEALEKAReLLEYggaGHTAVIHSNDEEVIEE 374
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
169-459 |
2.53e-09 |
|
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: 59.17 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 169 YIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEA----GLPAGVVNFVPGNGSEVGDY 244
Cdd:cd07121 95 YAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 245 LVDHPRTRFVSFTGSRDVGiriyeRAAkVNPGqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAfGFSGQKCSACS 324
Cdd:cd07121 175 LMAHPDINLLVVTGGPAVV-----KAA-LSSG----KKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNLPCIAE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 325 RAVIHED-VYDHVL-----NRAVELTKEltvgNPDAKDINMGPVNDQAAFDKvmSYVaiGKEEGKIVS--GGEGDDSKgw 396
Cdd:cd07121 244 KEVIAVDsVADYLIaamqrNGAYVLNDE----QAEQLLEVVLLTNKGATPNK--KWV--GKDASKILKaaGIEVPADI-- 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926909037 397 fiqPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL--TGAVVSNNRDHIEKA 459
Cdd:cd07121 314 ---RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKM 375
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
167-459 |
2.62e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.06 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 167 FSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKP----ASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVG 242
Cdd:PRK15398 125 IEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETA 204
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 243 DYLVDHPRTRFVSFTGsrdvGIRIYERAAKVNpgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAfGFSGQKCSA 322
Cdd:PRK15398 205 QRLMKHPGIALLVVTG----GPAVVKAAMKSG------KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNLPCI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 323 CSRAVIHED-VYDHVLNR-----AVELTKELTVGNPDAKDINMGPVNDqaafdkvmSYVaiGKEEGKIVS--GGEGDDSK 394
Cdd:PRK15398 274 AEKEVIVVDsVADELMRLmekngAVLLTAEQAEKLQKVVLKNGGTVNK--------KWV--GKDAAKILEaaGINVPKDT 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926909037 395 gwfiqPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGL--TGAVVSNNRDHIEKA 459
Cdd:PRK15398 344 -----RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKM 405
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
171-458 |
7.20e-08 |
|
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: 54.58 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 171 PLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKP---ASTTPVVAAKFM-EVLEEAGLPAGVVNFVPGNGSEVGDYLV 246
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 247 DHPRTRFVSFTGsrdvGIRIYERAAKVNpgqiwlKRVIAEMGGKDTMVVDKEADLELAAKSIVASAFGFSGQKCSACSRA 326
Cdd:cd07081 175 KFPGIGLLLATG----GPAVVKAAYSSG------KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926909037 327 VIHEDVYDHVLNR-----AVELTKEltvgnpdakdiNMGPVNDQAAFDKVMSYVAIGKEEGKIVSGGE---GDDSKGWFI 398
Cdd:cd07081 245 IVVDSVYDEVMRLfegqgAYKLTAE-----------ELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGlkvPQETRILIG 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926909037 399 QPTIVADVAEDArlmkEEIFGPVVAFCKAKDFDHALAIA----NNTEYGLTGAVVSNNRDHIEK 458
Cdd:cd07081 314 EVTSLAEHEPFA----HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIEN 373
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