|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
40-561 |
0e+00 |
|
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: 916.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 40 VNEQPLDYAKGSPERAKLTQALEKLKGElPVQVPIQISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALK 119
Cdd:cd07123 2 VNEPVLSYAPGSPERAKLQEALAELKSL-TVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 120 AKPAWEAMPFEDRAAIFLRAAELVTGKYRADIVAATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQQPRVQAEG 199
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 200 TWGKLEYRPLEGFVYAVAPFNFTALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVT 279
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 280 NTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVGqgIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKC 359
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLD--RYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 360 SANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKDEGYYV 439
Cdd:cd07123 319 SAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 440 HPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDWESTLDLVNTTSPYALTGSIFATDVAATRQAQTALKHAAGMLYINTK 519
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDK 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 115384268 520 CTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTIKEEF 561
Cdd:cd07123 479 PTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
41-572 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 675.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 41 NEQPLDYAKGSPERAKLTQALEKLKGElPVQVPIQISGSTVATHGSR-KQENPSRHREIVAEYATAGPEQVNAAVEAALK 119
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSS-SLEIPLVIGGEEVYDSNERiPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 120 AKPAWEAMPFEDRAAIFLRAAELVTGKYRADIVAATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQQPrVQAEG 199
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQP-ISAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 200 TWGKLEYRPLEGFVYAVAPFNFTALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVT 279
Cdd:TIGR01236 160 EWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 280 NTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVGQgiYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKC 359
Cdd:TIGR01236 240 DQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDR--YHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 360 SANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPE-LELVAGGHASKDEGYY 438
Cdd:TIGR01236 318 SAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTILYGGKYDDSQGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 439 VHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDWESTLDLVNTTSPYALTGSIFATDVAATRQAQTALKHAAGMLYINT 518
Cdd:TIGR01236 398 VEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYIND 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 115384268 519 KCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTIKEEFTELDRVEYPSN 572
Cdd:TIGR01236 478 KCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYM 531
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
71-561 |
7.93e-139 |
|
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: 411.44 E-value: 7.93e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 71 QVPIQISGSTVATHGSRKQE--NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYR 148
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDviNPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE-ERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 149 ADIVAATMLGQGKNIWQAEIDAPaETADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL 228
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 229 -VGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKI 307
Cdd:COG1012 161 kLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 308 GAGVgqgiynsyPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLT 387
Cdd:COG1012 241 AENL--------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 388 VGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDpELELVAGGHASKDE-GYYVHPTVYRTTNPRHDLMQRELFGPILTVY 466
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 467 VYpdHDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAvVGQHPFGGSRDSGTNDKTGTMA 546
Cdd:COG1012 392 PF--DDEEEAIALANDT-EYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGREG 465
|
490
....*....|....*
gi 115384268 547 hLQRFVSVQTIKEEF 561
Cdd:COG1012 466 -LEEYTETKTVTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-561 |
1.18e-133 |
|
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: 398.88 E-value: 1.18e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 54 RAKLTQALEKLKGELPVQVPIQISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRA 133
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 134 AIFLRAAELVTGKYRADIVAATMLGqGKNiWQAEIDAPAETADFFRCYVQECWSLYGQQPRVQA-EGTWGKLEYRPLeGF 212
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKN-WVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 213 VYAVAPFNFT-ALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAAL 291
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 292 SFIGSTQVFKGLQKKIGAGVGQgiYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESA 371
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPG--QTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 372 WPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSdpELELVAGGHASKDEGYYVHPTVYRTTNPRH 451
Cdd:cd07083 316 YEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 452 DLMQRELFGPILTVYVYPDHDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALkhAAGMLYINTKCTGAVVGQHPFG 531
Cdd:cd07083 394 RIAQEEIFGPVLSVIRYKDDDFAEALEVANST-PYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFG 470
|
490 500 510
....*....|....*....|....*....|
gi 115384268 532 GSRDSGTNDKTGTMAHLQRFVSVQTIKEEF 561
Cdd:cd07083 471 GFKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
39-561 |
2.14e-124 |
|
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: 375.41 E-value: 2.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 39 FVNEQPLDYAKGSpERAKLTQALEKLKGELPVQVPIQISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAAL 118
Cdd:cd07124 1 FRNEPFTDFADEE-NRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 119 KAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLYGQqPRVQAE 198
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADADV-AEAIDFLEYYAREMLRLRGF-PVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 199 GTWGKLEYRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEV 277
Cdd:cd07124 157 GEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 278 VTNTLLQRPEFAALSFIGSTQVfkGLQKKIGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQ 357
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREV--GLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 358 KCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKDEGY 437
Cdd:cd07124 314 KCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 438 YVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYIN 517
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLAVIKA--KDFDEALEIANDT-EYGLTGGVFSRSPEHLERARREFE--VGNLYAN 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 115384268 518 TKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTIKEEF 561
Cdd:cd07124 469 RKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
91-557 |
4.38e-113 |
|
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: 344.51 E-value: 4.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDA 170
Cdd:pfam00171 13 NPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE-ERKDELAELETLENGKPLAEARGEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 171 PaETADFFRCYVQECWSLYGQqPRVQAEGTWGKLEYRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPSDSALH 249
Cdd:pfam00171 91 D-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPL-GVVGAITPWNFpLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 250 ASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVVGETGGK 329
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAV--G--RHIAEAAAQNL----KRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 330 NWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDR 409
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 410 LAEVLHAARSDpELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNTTsPYALT 489
Cdd:pfam00171 320 VLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRF--KDEEEAIEIANDT-EYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115384268 490 GSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVGqHPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:pfam00171 396 AGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGREGGPYG-LEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
39-561 |
3.14e-102 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 318.42 E-value: 3.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 39 FVNEQPLDYAKgsPE-RAKLTQALEKLKGELPVQVPIQISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAA 117
Cdd:PRK03137 5 YKHEPFTDFSV--EEnVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 118 LKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLYGQQPRVQA 197
Cdd:PRK03137 83 LEAFETWKKWSPEDRARILLRAAAIIRRR-KHEFSAWLVKEAGKPWAEADADT-AEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 198 EGTWGKLEYRPLeGFVYAVAPFNFTA--LGATLVGPAAlLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDA 275
Cdd:PRK03137 161 PGEHNRYFYIPL-GVGVVISPWNFPFaiMAGMTLAAIV-AGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 276 EVVTNTLLQRPEFAALSFIGSTQVfkGLQKKIGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQ 355
Cdd:PRK03137 239 SEVGDYLVDHPKTRFITFTGSREV--GLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 356 GQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEyNHFVNAVIHERAYDRLAEVLHAARSdpELELVAGGHASKDE 435
Cdd:PRK03137 317 GQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKE--EGRLVLGGEGDDSK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 436 GYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPdhDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLY 515
Cdd:PRK03137 394 GYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK--DFDHALEIANNT-EYGLTGAVISNNREHLEKARREFH--VGNLY 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 115384268 516 INTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTIKEEF 561
Cdd:PRK03137 469 FNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
111-557 |
1.35e-100 |
|
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: 311.45 E-value: 1.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 111 NAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLYG 190
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEV-ARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 191 QQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQ 269
Cdd:cd07078 79 EVIPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 270 FLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVGqgiynsypRVVGETGGKNWGLVHPSANIKNAVLNTIR 349
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLK--------RVTLELGGKSPLIVFDDADLDAAVKGAVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 350 AAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDpELELVAGG 429
Cdd:cd07078 230 GAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAE-GAKLLCGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 430 HASKDE-GYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNTTsPYALTGSIFATDVAATRQAQTALK 508
Cdd:cd07078 309 KRLEGGkGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDT-EYGLAAGVFTRDLERALRVAERLE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 115384268 509 haAGMLYINTKCTGAVVGQhPFGGSRDSGTNdKTGTMAHLQRFVSVQTI 557
Cdd:cd07078 386 --AGTVWINDYSVGAEPSA-PFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
41-561 |
1.25e-93 |
|
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: 296.01 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 41 NEQPLDYAKgSPERAKLTQALEKLKGELPVQVPIQISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKA 120
Cdd:TIGR01237 3 HEPFTDFAD-EENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 121 KPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLYGQQPRVQAEGT 200
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAEV-AEAIDFMEYYARQMIELAKGKPVNSREGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 201 WGKLEYRPLeGFVYAVAPFNFtaLGATLVGPAA---LLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEV 277
Cdd:TIGR01237 160 TNQYVYTPT-GVTVVISPWNF--PFAIMVGMTVapiVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 278 VTNTLLQRPEFAALSFIGSTQVfkGLQKKIGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQ 357
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREV--GTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 358 KCSANSRLYVAESAWPEF-KRLLQAQLSKlTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSdpELELVAGGHASKDEG 436
Cdd:TIGR01237 315 KCSAGSRAVVHEKVYDEVvERFVEITESL-KVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKA--EGRLVSGGCGDDSKG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 437 YYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDhdWESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYI 516
Cdd:TIGR01237 392 YFIGPTIFADVDRKARLAQEEIFGPVVAFIRASD--FDEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYF 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 115384268 517 NTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTIKEEF 561
Cdd:TIGR01237 467 NRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
52-557 |
2.00e-81 |
|
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: 264.44 E-value: 2.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 52 PERAKLTQALEKLKGELPVQVPIQISGSTvaTHGSRKQ-ENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFE 130
Cdd:cd07125 14 VPLEALADALKAFDEKEWEAIPIINGEET--ETGEGAPvIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 131 DRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAeIDAPAETADFFRCYVQEcwsLYGQQPRVQAEGTWG---KLEYR 207
Cdd:cd07125 92 ERAEILEKAADLLE-ANRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQ---ARELFSDPELPGPTGelnGLELH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 208 PLeGFVYAVAPFNF---TALGATLvgpAALL-GNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLL 283
Cdd:cd07125 167 GR-GVFVCISPWNFplaIFTGQIA---AALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 284 QRPEFAALSFIGSTQVFKGLQKKIgAGVGQGIYnsypRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANS 363
Cdd:cd07125 243 AHPRIDGVIFTGSTETAKLINRAL-AERDGPIL----PLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 364 RLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEvlHAARSDPELELVAGGHASKDEGYYVHPTV 443
Cdd:cd07125 318 LLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRA--HTELMRGEAWLIAPAPLDDGNGYFVAPGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 444 YRTTNPrhDLMQRELFGPILTVYVYPDHDWESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGA 523
Cdd:cd07125 396 IEIVGI--FDLTTEVFGPILHVIRFKAEDLDEAIEDINATG-YGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGA 470
|
490 500 510
....*....|....*....|....*....|....
gi 115384268 524 VVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTI 557
Cdd:cd07125 471 IVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTV 504
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
115-557 |
1.71e-76 |
|
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: 246.76 E-value: 1.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 115 EAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLYGQQPR 194
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGEV-ARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 195 VQAEGTWGKLEYRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPG 273
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 274 DAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVGqgiynsypRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFE 353
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLK--------PVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 354 YQGQKCSANSRLYVAESAWPEFKRLLQaqlskltvgpvdeynhfvnaviheraydrlaevlhaarsdpelelvagghask 433
Cdd:cd06534 230 NAGQICTAASRLLVHESIYDEFVEKLV----------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 434 degyyvhpTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGM 513
Cdd:cd06534 257 --------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGT 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 115384268 514 LYINTKCTGAVVGQhPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd06534 324 VYINDSSIGVGPEA-PFGGVKNSGIGREGGPYG-LEEYTRTKTV 365
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
76-557 |
4.49e-72 |
|
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: 238.30 E-value: 4.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAAT 155
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDEL--EARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 156 M-LGQGKNIwqaeIDAPAET---ADFFRCYVQECWSLYGQ-----QPRVQAEGTwgkleYRPLeGFVYAVAPFNF-TALG 225
Cdd:cd07097 83 LtREEGKTL----PEARGEVtraGQIFRYYAGEALRLSGEtlpstRPGVEVETT-----REPL-GVVGLITPWNFpIAIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 226 ATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqk 305
Cdd:cd07097 153 AWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAV------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 306 kiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSK 385
Cdd:cd07097 227 --GRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 386 LTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDpELELVAGGHA--SKDEGYYVHPTVYRTTNPRHDLMQRELFGPIL 463
Cdd:cd07097 305 LKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSE-GAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 464 TVYVYpdHDWESTLDLVNTTsPYALTGSIFATDvaatrqaqtaLKHA--------AGMLYINTKCTGavVGQH-PFGGSR 534
Cdd:cd07097 384 AVIRV--RDYDEALAIANDT-EFGLSAGIVTTS----------LKHAthfkrrveAGVVMVNLPTAG--VDYHvPFGGRK 448
|
490 500
....*....|....*....|...
gi 115384268 535 DSGTNDKTGTMAHLQRFVSVQTI 557
Cdd:cd07097 449 GSSYGPREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
91-557 |
7.16e-68 |
|
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: 227.62 E-value: 7.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATMLGQ-GKNIWQAEID 169
Cdd:cd07131 20 NPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELL--KKRKEELARLVTREmGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 170 apaetadffrcyVQECWSL----YGQQPRVQAEGTWGKLE-------YRPLeGFVYAVAPFNF-TALGATLVGPAALLGN 237
Cdd:cd07131 98 ------------VQEAIDMaqyaAGEGRRLFGETVPSELPnkdamtrRQPI-GVVALITPWNFpVAIPSWKIFPALVCGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 238 VVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYN 317
Cdd:cd07131 165 TVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEV--------GERIGETCAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 318 SYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNh 396
Cdd:cd07131 237 PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGdGLDEET- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 397 FVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKD---EGYYVHPTVYRTTNPRHDLMQRELFGPIltVYVYPDHDW 473
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyeKGYFVEPTVFTDVTPDMRIAQEEIFGPV--VALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 474 ESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVgQHPFGGSRDSGTNDKTGTMAHLQRFVS 553
Cdd:cd07131 394 EEAIEIANDT-EYGLSSAIYTEDVNKAFRARRDLE--AGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTE 469
|
....
gi 115384268 554 VQTI 557
Cdd:cd07131 470 WKAV 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
97-538 |
3.20e-64 |
|
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: 217.22 E-value: 3.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATMLGQ-GKNIWQA--EIDAPAE 173
Cdd:cd07145 10 EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELI--ERRKEELAKLLTIEvGKPIKQSrvEVERTIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 174 TadfFRCYVQECWSLYGQQPRVQA-EGTWGKLEY---RPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSAL 248
Cdd:cd07145 88 L---FKLAAEEAKVLRGETIPVDAyEYNERRIAFtvrEPI-GVVGAITPFNFPAnLFAHKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 249 HASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKiGAGVGQgiynsypRVVGETGG 328
Cdd:cd07145 164 LTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGK-------KVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 329 KNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHERAY 407
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGdPLDE-STDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 408 DRLAEVLHAARSDPElELVAGGhaSKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTvyVYPDHDWESTLDLVNTTsPYA 487
Cdd:cd07145 315 ERMENLVNDAVEKGG-KILYGG--KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLP--IAKVKDDEEAVEIANST-EYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 115384268 488 LTGSIFATDVAATRQAQTALKhaAGMLYINtKCTGAVVGQHPFGGSRDSGT 538
Cdd:cd07145 389 LQASVFTNDINRALKVARELE--AGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
90-557 |
6.78e-64 |
|
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: 216.15 E-value: 6.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAE-I 168
Cdd:cd07115 2 LNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARrL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 169 DAPAeTADFFRCYVQECWSLYGQQPRVQAegtwGKLEYRPLE--GFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKPSD 245
Cdd:cd07115 80 DVPR-AADTFRYYAGWADKIEGEVIPVRG----PFLNYTVREpvGVVGAIVPWNFPlMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 246 SALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGE 325
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAV--------GRKIMQGAAGNLKRVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 326 TGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHE 404
Cdd:cd07115 227 LGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGdPLDPKTQ-MGPLVSQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 405 RAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNTTS 484
Cdd:cd07115 306 AQFDRVLDYVDVGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115384268 485 pYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07115 383 -YGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSGFGREMGREA-LDEYTEVKSV 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
95-538 |
8.11e-64 |
|
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: 215.92 E-value: 8.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 95 HREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATM-LGQGKNIWQA--EIDAP 171
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIaLEAGKPIKDArkEVDRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 172 AETadfFRCYVQECWSLYGQQ-PRVQAEGTWGKLEY---RPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDS 246
Cdd:cd07149 86 IET---LRLSAEEAKRLAGETiPFDASPGGEGRIGFtirEPI-GVVAAITPFNFPLnLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGagvgqgiynsYPRVVGET 326
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG----------LKKVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHER 405
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGdPLDE-DTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 AYDRLAE-----VLHAARsdpeleLVAGGhasKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLV 480
Cdd:cd07149 311 EAERIEEwveeaVEGGAR------LLTGG---KRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115384268 481 NtTSPYALTGSIFatdvaaTRQAQTALKHA----AGMLYINTKCTgAVVGQHPFGGSRDSGT 538
Cdd:cd07149 380 N-DSPYGLQAGVF------TNDLQKALKAAreleVGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
110-537 |
5.00e-61 |
|
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: 208.15 E-value: 5.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 110 VNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDApAETADFFRCYVQECWSLY 189
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE-ERRDEIADWLIRESGSTRPKAAFEV-GAAIAILREAAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 190 GQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPS-DSALHASWLLHRILLEAGLPKDV 267
Cdd:cd07104 80 GEILPSDVPGKESMVRRVPL-GVVGVISPFNFpLILAMRSVAPALALGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 268 IQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVVGETGGKNWGLVHPSANIKNAVLNT 347
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAV--G--RHIGELAGRHL----KKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 348 IRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHERAYDRLAEVLHAARSDpELELV 426
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGdPRDPDTV-IGPLINERQVDRVHAIVEDAVAA-GARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 427 AGGHAskdEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNTTsPYALTGSIFATDVaaTRQAQTA 506
Cdd:cd07104 309 TGGTY---EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPF--DDDEEAVELANDT-EYGLSAAVFTRDL--ERAMAFA 380
|
410 420 430
....*....|....*....|....*....|...
gi 115384268 507 LKHAAGMLYIN--TKCTGAVVgqhPFGGSRDSG 537
Cdd:cd07104 381 ERLETGMVHINdqTVNDEPHV---PFGGVKASG 410
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
90-537 |
2.29e-60 |
|
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: 206.90 E-value: 2.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHrEIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGkyRADIVAATM-LGQGKNIWQA-- 166
Cdd:cd07103 2 INPATG-EVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRE--RAEDLARLLtLEQGKPLAEArg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 167 EIDApaeTADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSD 245
Cdd:cd07103 79 EVDY---AASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPV-GVVAAITPWNFPAAMITRkIAPALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 246 ----SALHaswlLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVgqgiynsyPR 321
Cdd:cd07103 155 etplSALA----LAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV--------KR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 322 VVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGP-VDEYNHfVNA 400
Cdd:cd07103 223 VSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNgLDEGTD-MGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 401 VIHERAYDRLAEVLHAARSDpELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLV 480
Cdd:cd07103 302 LINERAVEKVEALVEDAVAK-GAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPF--DTEDEVIARA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 115384268 481 NTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkcTGAVVGQH-PFGGSRDSG 537
Cdd:cd07103 379 NDT-PYGLAAYVFTRDLARAWRVAEALE--AGMVGIN---TGLISDAEaPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
91-537 |
1.80e-59 |
|
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: 205.10 E-value: 1.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHREIVAEYaTAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgkyRADIVAatmLGQ------GKNIW 164
Cdd:cd07086 19 NPANGEPIARVF-PASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL----RKKKEA---LGRlvslemGKILP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 165 QAE------IDapaeTADFFrcyVQECWSLYGQ-----QPRVQAEGTWgkleyRPLeGFVYAVAPFNF-TALGATLVGPA 232
Cdd:cd07086 91 EGLgevqemID----ICDYA---VGLSRMLYGLtipseRPGHRLMEQW-----NPL-GVVGVITAFNFpVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 233 ALLGNVVIWKPSDSALHASWLLHRILLEA----GLPKDVIQFLPGDAEVvTNTLLQRPEFAALSFIGSTQVfkglqkkiG 308
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEV--------G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 309 AGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTV 388
Cdd:cd07086 229 RRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 389 G-PVDEYNhFVNAVIHERAYDRLAEVLHAARSDpELELVAGGHAS--KDEGYYVHPTVYRTTNPRHDLMQRELFGPILtv 465
Cdd:cd07086 309 GdPLDEGT-LVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPIL-- 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115384268 466 YVYPDHDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKHAAGMLYINTKCTGAVVGQhPFGGSRDSG 537
Cdd:cd07086 385 YVIKFDSLEEAIAINNDV-PQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGG-AFGGEKETG 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
97-564 |
2.60e-59 |
|
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: 204.10 E-value: 2.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATMLGQGKNIWQAEIDAPAETAD 176
Cdd:cd07150 10 SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM--ERRADDLIDLLIDEGGSTYGKAWFETTFTPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGAT-LVGPAALLGNVVIWKPSDSALHASWLLH 255
Cdd:cd07150 88 LLRAAAGECRRVRGETLPSDSPGTVSMSVRRPL-GVVAGITPFNYPLILATkKVAFALAAGNTVVLKPSEETPVIGLKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 256 RILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiynSYPRVVGETGGKNWGLVH 335
Cdd:cd07150 167 EIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR--------HLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 336 PSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLH 415
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 416 AARSDPElELVAGGHAskdEGYYVHPTVYRTTNPRHDLMQRELFGPIltVYVYPDHDWESTLDLVNTTSpYALTGSIFAT 495
Cdd:cd07150 319 DAVAKGA-KLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPV--TSVIPAKDAEEALELANDTE-YGLSAAILTN 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115384268 496 DVaaTRQAQTALKHAAGMLYIN--TKCTGAVVgqhPFGGSRDSGTNdKTGTMAHLqrfvsvqtikEEFTEL 564
Cdd:cd07150 392 DL--QRAFKLAERLESGMVHINdpTILDEAHV---PFGGVKASGFG-REGGEWSM----------EEFTEL 446
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
91-538 |
1.94e-58 |
|
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: 201.64 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQA---E 167
Cdd:cd07093 3 NPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE-ARADELALLESLDTGKPITLArtrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDAPAETADFFRCYV-QECWSLYGQQPrvqaeGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSD 245
Cdd:cd07093 81 IPRAAANFRFFADYIlQLDGESYPQDG-----GALNYVLRQPV-GVAGLITPWNLPLMLLTWkIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 246 SALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTqvfkGLQKKIGAGVGQGIynsyPRVVGE 325
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGET----ATGRTIMRAAAPNL----KPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 326 TGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHE 404
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGdPLDP-DTEVGPLISK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 405 RAYDRLAEVLHAARSDpELELVAGGHASK----DEGYYVHPTVYrtTNPRHD--LMQRELFGPILTvyVYPDHDWESTLD 478
Cdd:cd07093 306 EHLEKVLGYVELARAE-GATILTGGGRPElpdlEGGYFVEPTVI--TGLDNDsrVAQEEIFGPVVT--VIPFDDEEEAIE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 479 LVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKC-----TgavvgqhPFGGSRDSGT 538
Cdd:cd07093 381 LANDT-PYGLAAYVWTRDLGRAHRVARRLE--AGTVWVNCWLvrdlrT-------PFGGVKASGI 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
95-567 |
7.57e-57 |
|
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: 197.56 E-value: 7.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 95 HREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQA--EIDA 170
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 171 paeTADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATLVGPAAL-LGNVVIWKPSDSALH 249
Cdd:cd07118 85 ---AADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPI-GVVGIITPWNFPFLILSQKLPFALaAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 250 ASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVgqgiynsyPRVVGETGGK 329
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNL--------KKVSLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 330 NWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHERAYD 408
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGdPLDPETK-VGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 409 RLAEVLHAARSDPELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTsPYAL 488
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD--EAIALANDT-VYGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 489 TGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVvgQHPFGGSRDSGTNDKTGTMAhlqrfvsvqtiKEEFTELDRV 567
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSGIGRELGRYG-----------VEEYTELKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
91-537 |
1.13e-56 |
|
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: 197.41 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHrEIVAEYATAGPEQVNAAVEAALKA-KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATML--GQGKNIWQAE 167
Cdd:cd07082 22 SPIDG-EVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEEVANLLMWeiGKTLKDALKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDApaeTADFFRCYVQECWSLYGQQ-PRVQAEGTWGKL-EYR--PLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWK 242
Cdd:cd07082 100 VDR---TIDYIRDTIEELKRLDGDSlPGDWFPGTKGKIaQVRrePL-GVVLAIGPFNYPLnLTVSKLIPALIMGNTVVFK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 243 PSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLqKKIGAGVgqgiynsypRV 322
Cdd:cd07082 176 PATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-KKQHPMK---------RL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 323 VGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVI 402
Cdd:cd07082 246 VLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 403 HERAYDRLAEVL-----HAARsdpeleLVAGGHasKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTL 477
Cdd:cd07082 326 DPKSADFVEGLIddavaKGAT------VLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV--NDIEEAI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 478 DLVNtTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCtgavvgQH-----PFGGSRDSG 537
Cdd:cd07082 396 ELAN-KSNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
76-553 |
1.19e-56 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 205.87 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELvtgkYRAD---IV 152
Cdd:PRK11905 558 LLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL----MEAHmpeLF 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 153 AATMLGQGKNIWQAeIDAPAETADFFRCYVQecwslygqqprvQAEGTWGKLEYRPLeGFVYAVAPFNFTAlgATLVG-- 230
Cdd:PRK11905 634 ALAVREAGKTLANA-IAEVREAVDFLRYYAA------------QARRLLNGPGHKPL-GPVVCISPWNFPL--AIFTGqi 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 231 PAALL-GNVVIWKPSDS----ALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQK 305
Cdd:PRK11905 698 AAALVaGNTVLAKPAEQtpliAARAVRLLH----EAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 306 KIGAGVGQGIynsyPrVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSK 385
Cdd:PRK11905 774 TLAKRSGPPV----P-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDE 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 386 LTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPEL--ELVAGGHASKdeGYYVHPTVYRTTNPRHdlMQRELFGPIL 463
Cdd:PRK11905 849 LRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVL 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 464 TVYVYPDHDWESTLDLVNTTSpYALTGSIFatdvaaTR---QAQTALKHA-AGMLYINTKCTGAVVGQHPFGGSRDSGTN 539
Cdd:PRK11905 925 HVVRFKADELDRVIDDINATG-YGLTFGLH------SRideTIAHVTSRIrAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
490
....*....|....
gi 115384268 540 DKTGTMAHLQRFVS 553
Cdd:PRK11905 998 PKAGGPLYLGRLVR 1011
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
51-557 |
3.63e-56 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 204.28 E-value: 3.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 51 SPERAKLTQALEKLKGELPVQVPIqISGstvathGSRKQE--NPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMP 128
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPI-ING------EGEARPvvSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTP 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 129 FEDRAAIFLRAAELVTgKYRADIVAATMLGQGKnIWQAEIDAPAETADFFRCYVQECWSLYGQqpRVQAEGTWGKLEYRP 208
Cdd:PRK11904 606 VEERAAILERAADLLE-ANRAELIALCVREAGK-TLQDAIAEVREAVDFCRYYAAQARRLFGA--PEKLPGPTGESNELR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 209 LEG---FVyAVAPFNFTAlgATLVGP--AALL-GNVVIWKPSDS----ALHASWLLHrillEAGLPKDVIQFLPGDAEVV 278
Cdd:PRK11904 682 LHGrgvFV-CISPWNFPL--AIFLGQvaAALAaGNTVIAKPAEQtpliAAEAVKLLH----EAGIPKDVLQLLPGDGATV 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 279 TNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVGQGIYnsyprVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQK 358
Cdd:PRK11904 755 GAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVP-----LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQR 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 359 CSANSRLYVAESAWPEFKRLLQAQLSKLTVGpvDEYNHF--VNAVIHERAYDRLAEvlHAARSDPELELVAGGHASKD-- 434
Cdd:PRK11904 830 CSALRVLFVQEDIADRVIEMLKGAMAELKVG--DPRLLStdVGPVIDAEAKANLDA--HIERMKREARLLAQLPLPAGte 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 435 EGYYVHPTVYRTTNPrhDLMQRELFGPILTVYVYPDHDWESTLDLVNTTSpYALTGSI------FATDVAATRQaqtalk 508
Cdd:PRK11904 906 NGHFVAPTAFEIDSI--SQLEREVFGPILHVIRYKASDLDKVIDAINATG-YGLTLGIhsrieeTADRIADRVR------ 976
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 115384268 509 haAGMLYINTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTI 557
Cdd:PRK11904 977 --VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
109-564 |
9.54e-56 |
|
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: 193.95 E-value: 9.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 109 QVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDAPAeTADFFRCYVQECWSL 188
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLE-SRRDEFIEAMMEETGATAAWAGFNVDL-AAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 189 YGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDV 267
Cdd:cd07105 79 IGGSIPSDKPGTLAMVVKEPV-GVVLGIAPWNAPvILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 268 IQFL---PGDAEVVTNTLLQRPEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVVGETGGKNWGLVHPSANIKNAV 344
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRV--G--RIIAETAAKHL----KPVLLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 345 LNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDeynhfVNAVIHERAYDRLAEVLHAARSDPElE 424
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKGA-K 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 425 LVAGGHASK-DEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNTTSpYALTGSIFATDVAatRQA 503
Cdd:cd07105 304 LVVGGLADEsPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSE-YGLSAAVFTRDLA--RAL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115384268 504 QTALKHAAGMLYINtkctGAVVG---QHPFGGSRDSGTNdktgtmahlqRFVSVQTIkEEFTEL 564
Cdd:cd07105 379 AVAKRIESGAVHIN----GMTVHdepTLPHGGVKSSGYG----------RFNGKWGI-DEFTET 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
82-537 |
1.02e-55 |
|
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: 194.79 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 82 ATHGSRKQENPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGK 161
Cdd:cd07088 10 SSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR-ENADELAKLIVEEQGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 162 NIWQAEIDApAETADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVI 240
Cdd:cd07088 88 TLSLARVEV-EFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPI-GVVAGILPWNFPfFLIARKLAPALVTGNTIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 241 WKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTqvfkGLQKKIGAGVGQGIynsyP 320
Cdd:cd07088 166 IKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGST----EAGQKIMEAAAENI----T 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 321 RVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVN 399
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGdPFDA-ATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 400 AVIHERAYDRLAEVLHAARSDPElELVAGGH-ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLD 478
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGA-TLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 479 LVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVGQHpfGGSRDSG 537
Cdd:cd07088 394 LANDSE-YGLTSYIYTENLNTAMRATNELE--FGETYINRENFEAMQGFH--AGWKKSG 447
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
90-567 |
1.64e-55 |
|
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: 194.12 E-value: 1.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGkyRADIVAATM-LGQGKNI-WQAE 167
Cdd:cd07108 2 INPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLaLETGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDApAETADFFRCYVQECWSLYGQQ-PrvQAEGTwgkLEY---RPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWK 242
Cdd:cd07108 79 PEA-AVLADLFRYFGGLAGELKGETlP--FGPDV---LTYtvrEPL-GVVGAILPWNAPLMLAALkIAPALVAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 243 PSDSALHASWLLHRILLEAgLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTqvfkglqkkigaGVGQGIYNSY-PR 321
Cdd:cd07108 152 AAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGST------------EVGKIIYRAAaDR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 322 VVG---ETGGKNWGLVHPSANIKNAVLNTIRAA-FEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNH 396
Cdd:cd07108 219 LIPvslELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGdPLDEATD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 397 fVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKD----EGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHD 472
Cdd:cd07108 299 -IGAIISEKQFAKVCGYIDLGLSTSGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDED 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 473 weSTLDLVNtTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINtKCTGAVVGQhPFGGSRDSGtndktgtmahLQRFV 552
Cdd:cd07108 378 --EVIAMAN-DSHYGLAAYVWTRDLGRALRAAHALE--AGWVQVN-QGGGQQPGQ-SYGGFKQSG----------LGREA 440
|
490
....*....|....*
gi 115384268 553 SVQTIKEEFTELDRV 567
Cdd:cd07108 441 SLEGMLEHFTQKKTV 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
90-537 |
2.90e-55 |
|
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: 193.13 E-value: 2.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtGKYRADIVAATMLGQGKNIWQA--E 167
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAI-EANAEELARLLTLEQGKPLAEAqfE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDApaeTADFFRCYVQecwslYGQQPRVQAEGTWGKLE--YRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPS 244
Cdd:cd07106 80 VGG---AVAWLRYTAS-----LDLPDEVIEDDDTRRVElrRKPL-GVVAAIVPWNFPLLLAAWkIAPALLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 DSALHASWLLHRILLEAgLPKDVIQFLPGDAEVvtNTLLQR-PEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVV 323
Cdd:cd07106 151 PFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL--GPALTShPDIRKISFTGSTAT--G--KKVMASAAKTL----KRVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 324 GETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIH 403
Cdd:cd07106 220 LELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 404 ERAYDRLAEVLHAARSDpELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTT 483
Cdd:cd07106 300 KMQYDKVKELVEDAKAK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED--EVIARANDS 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 115384268 484 sPYALTGSIFATDVAatRQAQTALKHAAGMLYINTKctGAVVGQHPFGGSRDSG 537
Cdd:cd07106 377 -EYGLGASVWSSDLE--RAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
91-546 |
2.53e-54 |
|
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: 190.84 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTGkyRADIVAAT-MLGQGKNI---- 163
Cdd:cd07114 3 NPA-TGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEA--NAEELAELeTRDNGKLIretr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 164 WQAeidapAETADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWK 242
Cdd:cd07114 80 AQV-----RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPL-GVVAAITPWNSPlLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 243 PSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQGIynsyPRV 322
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTET----GRHIARAAAENL----APV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 323 VGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAV 401
Cdd:cd07114 226 TLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGdPLDPETQ-MGPL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 402 IHERAYDRLAEVLHAARSDpELELVAGG----HASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTL 477
Cdd:cd07114 305 ATERQLEKVERYVARAREE-GARVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE--EAI 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115384268 478 DLVNTTsPYALTGSIFATDVA-ATRQAQtALKhaAGMLYINT-KCTGAVVgqhPFGGSRDSGTNDKTGTMA 546
Cdd:cd07114 382 ALANDS-EYGLAAGIWTRDLArAHRVAR-AIE--AGTVWVNTyRALSPSS---PFGGFKDSGIGRENGIEA 445
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
76-555 |
3.46e-54 |
|
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: 191.66 E-value: 3.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAAT 155
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 156 MLGQGKNIWQAeIDAPAETADFFRCYVQecwslygqqprvQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAAL 234
Cdd:TIGR01238 121 VREAGKTIHNA-IAEVREAVDFCRYYAK------------QVRDVLGEFSVESR-GVFVCISPWNFPlAIFTGQISAALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 235 LGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIgagvGQG 314
Cdd:TIGR01238 187 AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTL----AQR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 315 IYNSYPrVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEY 394
Cdd:TIGR01238 263 EDAPVP-LIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 395 NHFVNAVIHERAYDRLAEVLHAARSDPE--LELVAGGHASKDEGYYVHPTVYRTTNprHDLMQRELFGPILTVYVYPDHD 472
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQKkiAQLTLDDSRACQHGTFVAPTLFELDD--IAELSEEVFGPVLHVVRYKARE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 473 WESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFV 552
Cdd:TIGR01238 420 LDQIVDQINQTG-YGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLT 496
|
...
gi 115384268 553 SVQ 555
Cdd:TIGR01238 497 QVQ 499
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
97-563 |
1.78e-53 |
|
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: 188.27 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDApAETAD 176
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE-EHADEIADWIVRESGSIRPKAGFEV-GAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFrcyvQECWSLyGQQPRVQ----AEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKPS-DSALHA 250
Cdd:cd07152 80 EL----HEAAGL-PTQPQGEilpsAPGRLSLARRVPL-GVVGVISPFNFPlILAMRSVAPALALGNAVVLKPDpRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 251 SWLLHRILLEAGLPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQGIynsyPRVVGETGGKN 330
Cdd:cd07152 154 GVVIARLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAV----GRKVGEAAGRHL----KKVSLELGGKN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 331 WGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHERAYDR 409
Cdd:cd07152 225 ALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGdPATGQVA-LGPLINARQLDR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 410 LAEVLHAARsDPELELVAGGHAskdEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpDHDwESTLDLVNTTsPYALT 489
Cdd:cd07152 304 VHAIVDDSV-AAGARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVF-DSD-EEAVALANDT-EYGLS 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115384268 490 GSIFATDVAatRQAQTALKHAAGMLYINTKcTGAVVGQHPFGGSRDSGTNDKTGTMAHLqrfvsvqtikEEFTE 563
Cdd:cd07152 377 AGIISRDVG--RAMALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGPANW----------EEFTQ 437
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
91-564 |
1.43e-52 |
|
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: 186.36 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDA 170
Cdd:cd07151 16 NPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRESGSTRIKANIEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 171 PA------ETADF-FRCYVQECWSLY-GQQPRVqaegtwgkleYRPLEGFVYAVAPFNFT-ALGATLVGPAALLGNVVIW 241
Cdd:cd07151 94 GAamaitrEAATFpLRMEGRILPSDVpGKENRV----------YREPLGVVGVISPWNFPlHLSMRSVAPALALGNAVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 242 KP-SDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYP 320
Cdd:cd07151 164 KPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPV--------GRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 321 RVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVN 399
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGdPSDPDTV-VG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 400 AVIHERAYDRLAEVLHAARSDpELELVAGGHAskdEGYYVHPTVYRTTNPRHDLMQRELFGPIltVYVYPDHDWESTLDL 479
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEE-GATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPV--APIIKADDEEEALEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 480 VNTTsPYALTGSIFATDVaaTRQAQTALKHAAGMLYINTKctgaVVGQHP---FGGSRDSGtndktgtmahLQRFvSVQT 556
Cdd:cd07151 389 ANDT-EYGLSGAVFTSDL--ERGVQFARRIDAGMTHINDQ----PVNDEPhvpFGGEKNSG----------LGRF-NGEW 450
|
....*...
gi 115384268 557 IKEEFTEL 564
Cdd:cd07151 451 ALEEFTTD 458
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
97-537 |
1.73e-52 |
|
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: 185.88 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQA-EIDAPaE 173
Cdd:cd07112 13 RVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE-AHRDELALLETLDMGKPISDAlAVDVP-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 174 TADFFRCYVQECWSLYGQQPRVqAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSD----SAL 248
Cdd:cd07112 91 AANTFRWYAEAIDKVYGEVAPT-GPDALALITREPL-GVVGAVVPWNFPLLMAAWkIAPALAAGNSVVLKPAEqsplTAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 249 haswLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiyNSYPRVVGETGG 328
Cdd:cd07112 169 ----RLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQ-------SNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 329 KNWGLVHPSA-NIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHERA 406
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGdPLDP-ATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 407 YDRLAEVLHAARSDpELELVAGGHASKDE--GYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTs 484
Cdd:cd07112 317 FDKVLGYIESGKAE-GARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE--EAVALANDS- 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 115384268 485 PYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSG 537
Cdd:cd07112 393 VYGLAASVWTSDLSRAHRVARRLR--AGTVWVN--CFDEGDITTPFGGFKQSG 441
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
90-537 |
4.05e-52 |
|
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: 184.75 E-value: 4.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHREIvAEYATAGPEQVNAAVEAALKAKPAWE-AMPFEDRAAIFLRAAELVTGkyRADIVAATM-LGQGKNIWQAE 167
Cdd:cd07109 2 FDPSTGEVF-ARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIRE--HADELARLEsLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDAPAeTADFFRCYVQECWSLYGQQ-PrvQAEGTWGKLEYRPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSD 245
Cdd:cd07109 79 ADVEA-AARYFEYYGGAADKLHGETiP--LGPGYFVYTVREPH-GVTGHIIPWNYPLqITGRSVAPALAAGNAVVVKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 246 SALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGE 325
Cdd:cd07109 155 DAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET--------GIAVMRAAAENVVPVTLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 326 TGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEyNHFVNAVIHER 405
Cdd:cd07109 227 LGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 AYDRLAEVLHAARSDpELELVAGGHASKD---EGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNT 482
Cdd:cd07109 306 QLDRVEGFVARARAR-GARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 483 TSpYALTGSIFATDVAatRQAQTALKHAAGMLYINTKCTGAVVgQHPFGGSRDSG 537
Cdd:cd07109 383 TD-YGLVAGVWTRDGD--RALRVARRLRAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
76-536 |
4.42e-52 |
|
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: 185.03 E-value: 4.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQE--NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVA 153
Cdd:cd07085 5 INGEWVESKTTEWLDvyNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE-ENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 154 ATMLGQGKNIWQAEidapaetADFFR--------CYVQECwsLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALG 225
Cdd:cd07085 83 LITLEHGKTLADAR-------GDVLRglevvefaCSIPHL--LKGEYLENVARGIDTYSYRQPL-GVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 226 ATLVGPAAL-LGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVtNTLLQRPEFAALSFIGSTQVfkglq 304
Cdd:cd07085 153 PLWMFPMAIaCGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPV----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 305 kkigagvGQGIY----NSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQ 380
Cdd:cd07085 227 -------GEYIYeraaANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 381 AQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPElELVAGG----HASKDEGYYVHPTVYRTTNPRHDLMQR 456
Cdd:cd07085 300 ERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGA-KLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 457 ELFGPILTVyVYPDhDWESTLDLVNtTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkctgaV-----VGQHPFG 531
Cdd:cd07085 379 EIFGPVLSI-VRVD-TLDEAIAIIN-ANPYGNGAAIFTRSGAAARKFQREVD--AGMVGIN------VpipvpLAFFSFG 447
|
....*
gi 115384268 532 GSRDS 536
Cdd:cd07085 448 GWKGS 452
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-557 |
4.83e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 192.46 E-value: 4.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 53 ERAKLTQALEKLKGELPVQVPIqISGSTVATHgSRKQENPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDR 132
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAAPL-IAGEAASGE-ARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 133 AAIFLRAAELVTgKYRADIVAATMLGQGKNIW--QAEIdapAETADFFRCYVQecwslygqqprvQAEGTWGK-LEYRPL 209
Cdd:COG4230 618 AAILERAADLLE-AHRAELMALLVREAGKTLPdaIAEV---REAVDFCRYYAA------------QARRLFAApTVLRGR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 210 eGFVYAVAPFNFtALgATLVGP--AALL-GNVVIWKPSDS----ALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTL 282
Cdd:COG4230 682 -GVFVCISPWNF-PL-AIFTGQvaAALAaGNTVLAKPAEQtpliAARAVRLLH----EAGVPADVLQLLPGDGETVGAAL 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 283 LQRPEFAALSFIGSTQVFKGLQKKIGAGVGQGIynsyPrVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSAN 362
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLINRTLAARDGPIV----P-LIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSAL 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 363 SRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEvlHAARSDPELELVAGGHASKD--EGYYVH 440
Cdd:COG4230 830 RVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEA--HIERMRAEGRLVHQLPLPEEcaNGTFVA 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 441 PTVYRTTNPRHdlMQRELFGPILTVYVYPDHDWESTLDLVNTTSpYALTGSI------FATDVaaTRQAQtalkhaAGML 514
Cdd:COG4230 908 PTLIEIDSISD--LEREVFGPVLHVVRYKADELDKVIDAINATG-YGLTLGVhsrideTIDRV--AARAR------VGNV 976
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 115384268 515 YINTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVSVQTI 557
Cdd:COG4230 977 YVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
97-559 |
1.82e-51 |
|
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: 182.89 E-value: 1.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAeIDAPAETAD 176
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHA-FEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFRCYVQECWSLYGQQPRVQAEGTWGKLE--YRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKP-SDSALHASW 252
Cdd:cd07101 85 VARYYARRAERLLKPRRRRGAIPVLTRTTvnRRPK-GVVGVISPWNYPlTLAVSDAIPALLAGNAVVLKPdSQTALTALW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 253 LlHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFaaLSFIGSTQVfkglQKKIGAGVGQgiynsypRVVG---ETGGK 329
Cdd:cd07101 164 A-VELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTAT----GRVVAERAGR-------RLIGcslELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 330 NWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDR 409
Cdd:cd07101 230 NPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 410 LAEVLHAARSDPElELVAGGHASKDEGYYVH-PTVYRTTNPRHDLMQRELFGPIltVYVYPDHDWESTLDLVNTTsPYAL 488
Cdd:cd07101 310 VTAHVDDAVAKGA-TVLAGGRARPDLGPYFYePTVLTGVTEDMELFAEETFGPV--VSIYRVADDDEAIELANDT-DYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115384268 489 TGSIFATDVAatRQAQTALKHAAGMLYIN---TKCTGAVvgQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTIKE 559
Cdd:cd07101 386 NASVWTRDGA--RGRRIAARLRAGTVNVNegyAAAWASI--DAPMGGMKDSGLGRRHGAEG-LLKYTETQTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
97-557 |
9.88e-51 |
|
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: 180.96 E-value: 9.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEIDAPAeTAD 176
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVDIDS-SAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFRCYVQECWSLYGQQprVQ-AEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSDSALHASWLL 254
Cdd:cd07090 86 CLEYYAGLAPTLSGEH--VPlPGGSFAYTRREPL-GVCAGIGAWNYPIQIASWkSAPALACGNAMVYKPSPFTPLTALLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 255 HRILLEAGLPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQGIynsyPRVVGETGGKNWGLV 334
Cdd:cd07090 163 AEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPT----GKKVMSAAAKGI----KHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 335 HPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHFvNAVIHERAYDRLAEV 413
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGdPLDEDTQM-GALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 414 LHAARSDPElELVAGGHASKDE-----GYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNTTsPYAL 488
Cdd:cd07090 313 IESAKQEGA-KVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTE--EEVIRRANDT-TYGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 489 TGSIFATDVAatRQAQTALKHAAGMLYINTKCTGAVvgQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07090 389 AAGVFTRDLQ--RAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFGRENGTAA-LEHYTQLKTV 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
91-537 |
3.86e-50 |
|
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: 179.47 E-value: 3.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAiFLRA-AELVTGKyRADIVAATMLGQGKNIWQAEID 169
Cdd:cd07110 3 NPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAK-YLRAiAEGVRER-REELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 170 ApAETADFFRCYVQECWSLYGQQPR---VQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSD 245
Cdd:cd07110 80 V-DDVAGCFEYYADLAEQLDAKAERavpLPSEDFKARVRREPV-GVVGLITPWNFPLLMAAWkVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 246 SALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGE 325
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTAT--------GSQVMQAAAQDIKPVSLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 326 TGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHER 405
Cdd:cd07110 230 LGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 AYDRLAEVLHAARSDpELELVAGGH--ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNtT 483
Cdd:cd07110 310 QYEKVLSFIARGKEE-GARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED--EAIALAN-D 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 115384268 484 SPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSG 537
Cdd:cd07110 386 SEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
109-537 |
8.39e-50 |
|
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: 177.85 E-value: 8.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 109 QVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATM-LGQGKNIW--QAEIDAPAETADFfrcyvqec 185
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELL--KANKEELARLIsRETGKPLWeaQTEVAAMAGKIDI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 186 wSLYGQQPRV---QAEGTWGK--LEYRPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSALHASWLLHRILL 259
Cdd:cd07095 71 -SIKAYHERTgerATPMAQGRavLRHRPH-GVMAVFGPFNFPGhLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 260 EAGLPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGagvGQgiynsyPRVV--GETGGKNWGLVHPS 337
Cdd:cd07095 149 EAGLPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFA---GR------PGKIlaLEMGGNNPLVVWDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 338 ANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAW-PEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERA---YDRLAEV 413
Cdd:cd07095 219 ADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAaarYLLAQQD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 414 LHAARSDPELELvaggHASKDEGYYVHPTVYRTTNPRhDLMQRELFGPILTVYVYpdHDWESTLDLVNTTsPYALTGSIF 493
Cdd:cd07095 299 LLALGGEPLLAM----ERLVAGTAFLSPGIIDVTDAA-DVPDEEIFGPLLQVYRY--DDFDEAIALANAT-RFGLSAGLL 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 115384268 494 ATDVAATRQAQTALKhaAGMLYINTKCTGAvVGQHPFGGSRDSG 537
Cdd:cd07095 371 SDDEALFERFLARIR--AGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
96-537 |
2.55e-49 |
|
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: 177.24 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 96 REIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATM-LGQGKNIWQAEIDApAET 174
Cdd:cd07094 9 GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLL--KKRAEEFAKIIaCEGGKPIKDARVEV-DRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 175 ADFFRCYVQECWSLYGQ------QPRVQAEGTWGKLEyrPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSA 247
Cdd:cd07094 86 IDTLRLAAEEAERIRGEeipldaTQGSDNRLAWTIRE--PV-GVVLAITPFNFPLnLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 248 LHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGagvgqgiynsYPRVVGETG 327
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG----------GKRIALELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 328 GKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHERA 406
Cdd:cd07094 233 GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGdPLDE-DTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 407 YDRLAEVLHAARSDPElELVAGGhasKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNTTsPY 486
Cdd:cd07094 312 AERVERWVEEAVEAGA-RLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRIANST-DY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 487 ALTGSIFATDVAAtrqaqtALKHAAGMlyintKCTGAVVGQH--------PFGGSRDSG 537
Cdd:cd07094 385 GLQAGIFTRDLNV------AFKAAEKL-----EVGGVMVNDSsafrtdwmPFGGVKESG 432
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
76-538 |
4.88e-49 |
|
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: 176.86 E-value: 4.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQE--NPSRhREIVAEYATAGPEQVNAAVEAALKA-KPAWEAMPFEDRAAIFLRAAELVTgKYRADIV 152
Cdd:cd07113 4 IDGRPVAGQSEKRLDitNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 153 AATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQQ-----PRVQAEgTWGKLEYRPLEGFVYAVAPFNFTAL-GA 226
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsiPSMQGE-RYTAFTRREPVGVVAGIVPWNFSVMiAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 227 TLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVvTNTLLQRPEFAALSFIGSTQVfkglqkk 306
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVAT------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 307 iGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKL 386
Cdd:cd07113 233 -GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 387 TVG-PVDEYNHFvNAVIHERAYDRLAEVLHAARSDpELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTV 465
Cdd:cd07113 312 QVGsPMDESVMF-GPLANQPHFDKVCSYLDDARAE-GDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSF 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115384268 466 YVYPDHdwESTLDLVNTTsPYALTGSIFATDVA-ATRQAQtalKHAAGMLYIN--TKCTGAVvgqhPFGGSRDSGT 538
Cdd:cd07113 390 VPYEDE--EELIQLINDT-PFGLTASVWTNNLSkALRYIP---RIEAGTVWVNmhTFLDPAV----PFGGMKQSGI 455
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
97-557 |
7.19e-49 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 177.38 E-value: 7.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQA--EIDAPAET 174
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVL-ENREELLDLVQLETGKARRHAfeEVLDVALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 175 AdffRCYVQECWSLYGQQPRVQAEGTWGKL-EYRPLEGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKP-SDSALHAS 251
Cdd:PRK09407 122 A---RYYARRAPKLLAPRRRAGALPVLTKTtELRQPKGVVGVISPWNYPlTLAVSDAIPALLAGNAVVLKPdSQTPLTAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 252 WLlHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFaaLSFIGSTqvfkGLQKKIGAGVGQgiynsypRVVG---ETGG 328
Cdd:PRK09407 199 AA-VELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGST----ATGRVLAEQAGR-------RLIGfslELGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 329 KNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYD 408
Cdd:PRK09407 265 KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 409 RLAEVLHAARSDPElELVAGGHASKDEG-YYVHPTVYRTTNPRHDLMQRELFGPIltVYVYPDHDWESTLDLVNTTsPYA 487
Cdd:PRK09407 345 TVSAHVDDAVAKGA-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPV--VSVYPVADVDEAVERANDT-PYG 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115384268 488 LTGSIFATDVAATRQAQTALKhaAGMLYIN---TKCTGAVvgQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIR--AGTVNVNegyAAAWGSV--DAPMGGMKDSGLGRRHGAEG-LLKYTESQTI 488
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
97-537 |
1.68e-48 |
|
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: 174.74 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDApAETAD 176
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE-ERFEELAETIVLEAGKPIKDARGEV-ARAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFRCYVQECWSLYGQQPRV----QAEGTWGKLEYRPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSALHAS 251
Cdd:cd07147 88 TFRIAAEEATRIYGEVLPLdisaRGEGRQGLVRRFPI-GPVSAITPFNFPLnLVAHKVAPAIAAGCPFVLKPASRTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 252 WLLHRILLEAGLPKDVIQFLPGDAEVvTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiynsyPRVVGETGGKNW 331
Cdd:cd07147 167 LILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGK----------KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 332 GLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHERAYDRL 410
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGdPKDD-ATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 411 AEVLHAARsDPELELVAGGhasKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNtTSPYALTG 490
Cdd:cd07147 315 EGWVNEAV-DAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAVN-DSKFGLQA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 491 SIFATDVaatRQAQTALKHaagmlyinTKCTGAVVG--------QHPFGGSRDSG 537
Cdd:cd07147 388 GVFTRDL---EKALRAWDE--------LEVGGVVINdvptfrvdHMPYGGVKDSG 431
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
76-557 |
3.73e-48 |
|
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: 174.23 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQE--NPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVA 153
Cdd:cd07138 3 IDGAWVAPAGTETIDviNPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYE-ARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 154 ATMLGQGKNIWQAE---IDAPAETADFFRcyvqecwSLYGQQPRVQAEGTwGKLEYRPLeGFVYAVAPFNFTALGATL-V 229
Cdd:cd07138 81 AITLEMGAPITLARaaqVGLGIGHLRAAA-------DALKDFEFEERRGN-SLVVREPI-GVCGLITPWNWPLNQIVLkV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 230 GPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkGlqKKIGA 309
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA--G--KRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 310 GVGQGIynsyPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG 389
Cdd:cd07138 228 AAADTV----KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 390 -PVDEYNHfVNAVIHERAYDRLAEVLHAARsDPELELVAGGH---ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTV 465
Cdd:cd07138 304 dPRDPATT-LGPLASAAQFDRVQGYIQKGI-EEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 466 YVYPDHDweSTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkcTGAVVGQHPFGGSRDSGtNDKTGTM 545
Cdd:cd07138 382 IPYDDED--EAIAIANDT-PYGLAGYVWSADPERARAVARRLR--AGQVHIN---GAAFNPGAPFGGYKQSG-NGREWGR 452
|
490
....*....|..
gi 115384268 546 AHLQRFVSVQTI 557
Cdd:cd07138 453 YGLEEFLEVKSI 464
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
76-537 |
4.04e-48 |
|
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: 174.52 E-value: 4.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQE--NPSRHREIVAEYAtAGPEQVNAAVEAALKA-KPAWEAMPFEDRAAIFLRAAELVTgKYRADIV 152
Cdd:cd07144 12 INNEFVKSSDGETIKtvNPSTGEVIASVYA-AGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVE-KNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 153 AATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQQprvqAEGTWGKLEY---RPLeGFVYAVAPFNFT-ALGATL 228
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKT----IPTSPNKLAYtlhEPY-GVCGQIIPWNYPlAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 229 VGPAALLGNVVIWKPSD----SALHaswlLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQ 304
Cdd:cd07144 165 LAPALAAGNTVVIKPAEntplSLLY----FANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 305 KKIGagvgqgiyNSYPRVVGETGGKNWGLVHPSANIKNAVlNTIRAAFEY-QGQKCSANSRLYVAESAWPEFKRLLQA-- 381
Cdd:cd07144 241 KAAA--------QNLKAVTLECGGKSPALVFEDADLDQAV-KWAAAGIMYnSGQNCTATSRIYVQESIYDKFVEKFVEhv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 382 -QLSKLTvGPVDEyNHFVNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDE---GYYVHPTVYRTTNPRHDLMQRE 457
Cdd:cd07144 312 kQNYKVG-SPFDD-DTVVGPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 458 LFGPILTVYVYPDHDweSTLDLVNTTsPYALTGSIFATDVaaTRQAQTALKHAAGMLYINTKCTGAVvgQHPFGGSRDSG 537
Cdd:cd07144 389 IFGPVVVISKFKTYE--EAIKKANDT-TYGLAAAVFTKDI--RRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
97-557 |
5.75e-48 |
|
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: 173.58 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWE-AMPFEDRAAIFLRAAELVTGK---YRADIVA----ATMLGQGKNIWQ--A 166
Cdd:cd07089 8 EVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARkeeLRALLVAevgaPVMTARAMQVDGpiG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 167 EIDAPAETADFFRcyvqecWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFT-ALGATLVGPAALLGNVVIWKPS- 244
Cdd:cd07089 88 HLRYFADLADSFP------WEFDLPVPALRGGPGRRVVRREPV-GVVAAITPWNFPfFLNLAKLAPALAAGNTVVLKPAp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 DSALHAsWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVVG 324
Cdd:cd07089 161 DTPLSA-LLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAV--G--RRIMAQAAATL----KRVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 325 ETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIH 403
Cdd:cd07089 232 ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGdPADPGTV-MGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 404 ERAYDRLAEVLHAARSDpELELVAGGH--ASKDEGYYVHPTVYrtTNPRHD--LMQRELFGPILTVYVYPDHDweSTLDL 479
Cdd:cd07089 311 AAQRDRVEGYIARGRDE-GARLVTGGGrpAGLDKGFYVEPTLF--ADVDNDmrIAQEEIFGPVLVVIPYDDDD--EAVRI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 480 VNtTSPYALTGSIFATDVAatRQAQTALKHAAGMLYINtkctGAVVGQH--PFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07089 386 AN-DSDYGLSGGVWSADVD--RAYRVARRIRTGSVGIN----GGGGYGPdaPFGGYKQSGLGRENGIEG-LEEFLETKSI 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
90-538 |
1.40e-47 |
|
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: 172.56 E-value: 1.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHREIvAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATMLGQGKNIWQAEID 169
Cdd:cd07107 2 INPATGQVL-ARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRL--REHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 170 APAETADFFRCYVQECWSLYGQQPRVQAEGtWGKLEYRPLeGFVYAVAPFNFTALGATLVGPAALL-GNVVIWKPSDSAL 248
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPY-GVVARIVAFNHPLMFAAAKIAAPLAaGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 249 HASWLLHRILLEAgLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTqvfkGLQKKIGAGVGQGIynsyPRVVGETGG 328
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSV----PTGRAIMRAAAEGI----KHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 329 KNWGLVHPSANIKNAVLNTIRAA-FEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAY 407
Cdd:cd07107 228 KNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 408 DRLAEVLHAARSDPElELVAGGHASKDE----GYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTT 483
Cdd:cd07107 308 DRVMHYIDSAKREGA-RLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQANGV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 484 sPYALTGSIFATDVaaTRQAQTALKHAAGMLYINTkctgavVGQH----PFGGSRDSGT 538
Cdd:cd07107 385 -EYGLTAAIWTNDI--SQAHRTARRVEAGYVWING------SSRHflgaPFGGVKNSGI 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
97-537 |
2.32e-47 |
|
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: 171.64 E-value: 2.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGK--NIWQAEIDAPAET 174
Cdd:cd07099 7 EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAETGKprADAGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 175 ADFFRCYVQEcwsLYGQQPRVQAEGTWGK---LEYRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPSDSALHA 250
Cdd:cd07099 86 IDWAARNAPR---VLAPRKVPTGLLMPNKkatVEYRPY-GVVGVISPWNYpLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 251 SWLLHRILLEAGLPKDVIQFLPGDAEvvTNTLLQRPEFAALSFIGSTqvfkGLQKKIGAGVGQgiyNSYPrVVGETGGKN 330
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGA--TGAALIDAGVDKVAFTGSV----ATGRKVMAAAAE---RLIP-VVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 331 WGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHER----- 405
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqldiv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 ------AYDRLAEVLhaarsdpelelvAGGHASKDEGYYVHPTVYrtTNPRHD--LMQRELFGPILTVYVYPDHDweSTL 477
Cdd:cd07099 312 rrhvddAVAKGAKAL------------TGGARSNGGGPFYEPTVL--TDVPHDmdVMREETFGPVLPVMPVADED--EAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 478 DLVNtTSPYALTGSIFATDVAatRQAQTALKHAAGMLYINTKCTGAVVGQHPFGGSRDSG 537
Cdd:cd07099 376 ALAN-DSRYGLSASVFSRDLA--RAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
91-553 |
1.17e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 176.32 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKYRadivaaTMLG-----QGKNIWQ 165
Cdd:PRK11809 665 NPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQ------TLMGllvreAGKTFSN 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 166 AeIDAPAETADFFRCYVqecwslygqqprVQAEGTWGKLEYRPLeGFVYAVAPFNFTAlgATLVG--PAALL-GNVVIWK 242
Cdd:PRK11809 739 A-IAEVREAVDFLRYYA------------GQVRDDFDNDTHRPL-GPVVCISPWNFPL--AIFTGqvAAALAaGNSVLAK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 243 PSD-SALHASWLLhRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVG-QGiyNSYP 320
Cdd:PRK11809 803 PAEqTPLIAAQAV-RILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQG--RPIP 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 321 rVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNA 400
Cdd:PRK11809 880 -LIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGP 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 401 VIHERAYDRLAEVLHAARSD--PELELVAGGHASKDEGYYVHPTVYRTTNprHDLMQRELFGPILTVYVYPDHDWESTLD 478
Cdd:PRK11809 959 VIDAEAKANIERHIQAMRAKgrPVFQAARENSEDWQSGTFVPPTLIELDS--FDELKREVFGPVLHVVRYNRNQLDELIE 1036
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 479 LVNTTSpYALTGSIFaTDVAATRQAQTALKHaAGMLYINTKCTGAVVGQHPFGGSRDSGTNDKTGTMAHLQRFVS 553
Cdd:PRK11809 1037 QINASG-YGLTLGVH-TRIDETIAQVTGSAH-VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLA 1108
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
96-537 |
1.35e-46 |
|
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: 169.73 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 96 REIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyrADIVAATMLGQ-GKNIWQA--EIDAPA 172
Cdd:cd07102 6 GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAAN--TDEIAEELTWQmGRPIAQAggEIRGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 173 ETADFFRCYVQECWSlygQQPRVQAEGTWGKLEYRPLeGFVYAVAPFN---FTALGAtlVGPAALLGNVVIWKPSDSALH 249
Cdd:cd07102 84 ERARYMISIAEEALA---DIRVPEKDGFERYIRREPL-GVVLIIAPWNypyLTAVNA--VIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 250 ASWLLHRILLEAGLPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGagvgqgiynsyPRVVG---ET 326
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAA-----------GRFIKvglEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHFvNAVIHER 405
Cdd:cd07102 226 GGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGdPLDPSTTL-GPVVSAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 AYDRLAEVLHAARSDPELELVAGGHASKDE--GYYVHPTVYRTTNPRHDLMQRELFGPILTVY-VYPDhdwESTLDLVNt 482
Cdd:cd07102 305 AADFVRAQIADAIAKGARALIDGALFPEDKagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMkVKSD---AEAIALMN- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 483 TSPYALTGSIFATDVAATRQAQTALkhAAGMLYINtkCTGAVVGQHPFGGSRDSG 537
Cdd:cd07102 381 DSEYGLTASVWTKDIARAEALGEQL--ETGTVFMN--RCDYLDPALAWTGVKDSG 431
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
66-557 |
4.21e-46 |
|
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: 168.86 E-value: 4.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 66 GELPVQVPIQISGSTV-ATHGSRKQ-ENPSrHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAE 141
Cdd:cd07143 1 GKYEQPTGLFINGEFVdSVHGGTVKvYNPS-TGKLITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 142 LVtgKYRADIVAAT-MLGQGKNI-WQAEIDApAETADFFRCYVQECWSLYGQQPRVQAEgtwgKLEYRPLE--GFVYAVA 217
Cdd:cd07143 80 LM--ERNLDYLASIeALDNGKTFgTAKRVDV-QASADTFRYYGGWADKIHGQVIETDIK----KLTYTRHEpiGVCGQII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 218 PFNFTALG-ATLVGPAALLGNVVIWKPSD----SALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALS 292
Cdd:cd07143 153 PWNFPLLMcAWKIAPALAAGNTIVLKPSEltplSALYMTKLIP----EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 293 FIGSTQVfkglqkkiGAGVGQGIYNS-YPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESA 371
Cdd:cd07143 229 FTGSTLV--------GRKVMEAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 372 WPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRH 451
Cdd:cd07143 301 YDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVTEDM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 452 DLMQRELFGPILTVYVYPDHdwESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFG 531
Cdd:cd07143 380 KIVKEEIFGPVVAVIKFKTE--EEAIKRANDST-YGLAAAVFTNNINNAIRVANALK--AGTVWVN--CYNLLHHQVPFG 452
|
490 500
....*....|....*....|....*.
gi 115384268 532 GSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07143 453 GYKQSGIGRELGEYA-LENYTQIKAV 477
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
90-558 |
1.38e-45 |
|
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: 167.39 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHrEIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQ-A 166
Cdd:cd07091 24 INPATE-EVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIE-RDRDELAALESLDNGKPLEEsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 167 EIDAPaETADFFRCYVQECWSLYGQQPRVQAEG-TWGKLEyrPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPS 244
Cdd:cd07091 102 KGDVA-LSIKCLRYYAGWADKIQGKTIPIDGNFlAYTRRE--PI-GVCGQIIPWNFPLLMLAWkLAPALAAGNTVVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 D----SALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiyNSYP 320
Cdd:cd07091 178 EqtplSALYLAELIK----EAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK-------SNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 321 RVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVN 399
Cdd:cd07091 247 KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGdPFDP-DTFQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 400 AVIHERAYDRLAEVLHAARSDpELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDL 479
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED--EVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115384268 480 VNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTIK 558
Cdd:cd07091 403 ANDTE-YGLAAGVFTKDINKALRVSRALK--AGTVWVN--TYNVFDAAVPFGGFKQSGFGRELGEEG-LEEYTQVKAVT 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
76-537 |
4.98e-45 |
|
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: 165.83 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQENPSRH-REIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTGKyRADIV 152
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPAtEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEAR-ADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 153 AATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGP 231
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPV-GVVAAIVPWNAPLFLAALkIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 232 AALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEV----VTNtllqrPEFAALSFIGSTQVfkGlqKKI 307
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVgeylVRH-----PGVDKVSFTGSTAA--G--RRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 308 GAGVGQGIynsyPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLT 387
Cdd:cd07139 232 AAVCGERL----ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 388 VG-PVDEYNhFVNAVIHERAYDRLAEVLHAARSDpELELVAGGH--ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILT 464
Cdd:cd07139 308 VGdPLDPAT-QIGPLASARQRERVEGYIAKGRAE-GARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 465 VYVYPDHDwestlDLVNTT--SPYALTGSIFATDVAAtrqaqtALKHA----AGMLYINtkctGAVVGQH-PFGGSRDSG 537
Cdd:cd07139 386 VIPYDDED-----DAVRIAndSDYGLSGSVWTADVER------GLAVArrirTGTVGVN----GFRLDFGaPFGGFKQSG 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
90-538 |
1.40e-44 |
|
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: 164.04 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHREIvAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQAEID 169
Cdd:cd07092 2 VDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEEN-AEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 170 APAETADFFRCYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSDSAL 248
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWkIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 249 HASWLLHRILLEaGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGETGG 328
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRT--------GKKVARAAADTLKRVHLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 329 KNWGLVHPSANIkNAVLNTIR-AAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAY 407
Cdd:cd07092 230 KAPVIVFDDADL-DAAVAGIAtAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 408 DRLAEVLHAARSDpeLELVAGGHASKDEGYYVHPTVyrTTNPRHD--LMQRELFGPILTVYVYPDHDweSTLDLVNTTsP 485
Cdd:cd07092 309 ERVAGFVERAPAH--ARVLTGGRRAEGPGYFYEPTV--VAGVAQDdeIVQEEIFGPVVTVQPFDDED--EAIELANDV-E 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 115384268 486 YALTGSIFATDVAATRQAQTALKhaAGMLYINTKctGAVVGQHPFGGSRDSGT 538
Cdd:cd07092 382 YGLASSVWTRDVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
91-537 |
6.00e-44 |
|
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: 162.87 E-value: 6.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVtgkyRADIVAATML---GQGKNIWQ 165
Cdd:cd07119 19 NPA-NGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKI----REDAEELARLetlNTGKTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 166 AEIDApAETADFFRCYVQECWSLYGQQPRVqAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPS 244
Cdd:cd07119 94 SEIDI-DDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPV-GVCGLITPWNYPLLQAAWkLAPALAAGNTVVIKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 D----SALHaswlLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYP 320
Cdd:cd07119 171 EvtplTTIA----LFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT--------GRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 321 RVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNA 400
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 401 VIHERAYDRLAEVLHAARSDpELELVAGGHASKD----EGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwEST 476
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEE-GARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--EEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115384268 477 LDLVNTTsPYALTGSIFATDVAATRQAQTALKHaaGMLYINtkCTGAVVGQHPFGGSRDSG 537
Cdd:cd07119 396 IRLANDT-PYGLAGAVWTKDIARANRVARRLRA--GTVWIN--DYHPYFAEAPWGGYKQSG 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
76-537 |
3.18e-43 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 160.85 E-value: 3.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQ-ENPSRHrEIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGkyRADIVAA 154
Cdd:PRK13473 7 INGELVAGEGEKQPvYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEE--NADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 155 T-MLGQGKNIWQA---EIDAPAETADFF----RCyvqecwsLYGqqprvQAEGtwgklEY---------RPLEGFVYAVA 217
Cdd:PRK13473 84 LeSLNCGKPLHLAlndEIPAIVDVFRFFagaaRC-------LEG-----KAAG-----EYleghtsmirRDPVGVVASIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 218 PFNFTAL-GATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAgLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGS 296
Cdd:PRK13473 147 PWNYPLMmAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 297 TQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIkNAVLNTIRAAFEYQ-GQKCSANSRLYVAESAWPEF 375
Cdd:PRK13473 226 IAT--------GKHVLSAAADSVKRTHLELGGKAPVIVFDDADL-DAVVEGIRTFGYYNaGQDCTAACRIYAQRGIYDDL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 376 KRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQ 455
Cdd:PRK13473 297 VAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 456 RELFGPILTVYVYPDHDweSTLDLVNtTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTgaVVGQHPFGGSRD 535
Cdd:PRK13473 377 REVFGPVVSVTPFDDED--QAVRWAN-DSDYGLASSVWTRDVGRAHRVSARLQ--YGCTWVNTHFM--LVSEMPHGGQKQ 449
|
..
gi 115384268 536 SG 537
Cdd:PRK13473 450 SG 451
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
76-537 |
1.51e-42 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 159.35 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSRKQE-NPSRHrEIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAA 154
Cdd:PRK09457 5 INGDWIAGQGEAFESrNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL--EENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 155 tMLGQ--GKNIWQAEIDAPAETADF---FRCYVQECwslyGQQPRVQAEGTWGkLEYRPLeGFVYAVAPFNFTA-LGATL 228
Cdd:PRK09457 82 -VIARetGKPLWEAATEVTAMINKIaisIQAYHERT----GEKRSEMADGAAV-LRHRPH-GVVAVFGPYNFPGhLPNGH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 229 VGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGST-------QVFK 301
Cdd:PRK09457 155 IVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRE-TGKALAAHPDIDGLLFTGSAntgyllhRQFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 302 GLQKKIGAgvgqgiynsyprvvGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPE--FKRLL 379
Cdd:PRK09457 234 GQPEKILA--------------LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDafLARLV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 380 QAqLSKLTVGPVDEYNH-FVNAVIHERAYDRLAE-----VLHAARSDPELELVAGGHAskdegyYVHPTVYRTTNPRhDL 453
Cdd:PRK09457 300 AV-AKRLTVGRWDAEPQpFMGAVISEQAAQGLVAaqaqlLALGGKSLLEMTQLQAGTG------LLTPGIIDVTGVA-EL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 454 MQRELFGPILTVYVYPDHDweSTLDLVNTTSpYALTGSIFATDVAatrQAQTALKHA-AGMLYINTKCTGAvVGQHPFGG 532
Cdd:PRK09457 372 PDEEYFGPLLQVVRYDDFD--EAIRLANNTR-FGLSAGLLSDDRE---DYDQFLLEIrAGIVNWNKPLTGA-SSAAPFGG 444
|
....*
gi 115384268 533 SRDSG 537
Cdd:PRK09457 445 VGASG 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
101-537 |
2.17e-42 |
|
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: 158.23 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 101 EYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAiFLRAAELVTGKYRADIVAATMLGQGKNIWQA---EIDAPAETADf 177
Cdd:cd07098 11 SVPADTPEDVDEAIAAARAAQREWAKTSFAERRK-VLRSLLKYILENQEEICRVACRDTGKTMVDAslgEILVTCEKIR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 178 frcyvqecWSL-YGQ---QPRVQAEGTW-----GKLEYRPLeGFVYAVAPFNF---TALGATLvgpAALL-GNVVIWKPS 244
Cdd:cd07098 89 --------WTLkHGEkalRPESRPGGLLmfykrARVEYEPL-GVVGAIVSWNYpfhNLLGPII---AALFaGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 DsalHASW-------LLHRILLEAGLPKDVIQFLPGDAEVvTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQgiyn 317
Cdd:cd07098 157 E---QVAWssgfflsIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPV----GKKVMAAAAE---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 318 SYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHF 397
Cdd:cd07098 225 SLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 398 VNAVIHERAYDRLAEVLhAARSDPELELVAGG----HASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdw 473
Cdd:cd07098 305 VGAMISPARFDRLEELV-ADAVEKGARLLAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD-- 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115384268 474 ESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVGQHPFGGSRDSG 537
Cdd:cd07098 382 EEAVEIANST-EYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSG 442
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
110-557 |
3.74e-41 |
|
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: 154.16 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 110 VNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAATM-LGQGKNIWQA--EIDapaETADFFRCYVQECW 186
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLL--RERKDELARLItLEMGKPIAEAraEVE---KCAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 187 SLYGQQPrVQAEGTWGKLEYRPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPK 265
Cdd:cd07100 76 AFLADEP-IETDAGKAYVRYEPL-GVVLGIMPWNFPFwQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 266 DVIQFLPGDAEVVtNTLLQRPEFAALSFIGSTQVfkGlqKKIGAGVGQGIynsyPRVVGETGGKNWGLVHPSANIKNAVL 345
Cdd:cd07100 154 GVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERA--G--RAVAAEAGKNL----KKSVLELGGSDPFIVLDDADLDKAVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 346 NTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEynhfvNAVIHERAYDRLAEVLHA-------- 416
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGdPMDE-----DTDLGPLARKDLRDELHEqveeavaa 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 417 -ARsdpeleLVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDwEStLDLVNtTSPYALTGSIFAT 495
Cdd:cd07100 300 gAT------LLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE-EA-IALAN-DSPFGLGGSVFTT 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 496 DVAatRQAQTALKHAAGMLYINTkctgaVVGQH---PFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07100 371 DLE--RAERVARRLEAGMVFING-----MVKSDprlPFGGVKRSGYGRELGRFG-IREFVNIKTV 427
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
76-537 |
4.41e-41 |
|
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: 154.86 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHGSR--KQENPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKYRADIVA 153
Cdd:cd07111 26 INGKWVKPENRKsfPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 154 ATMLGqGKNIWQA-EIDAPAETADFFRcyvqecwslYGQQPRVQAEGTWGkleYRPLeGFVYAVAPFNFTALGATL-VGP 231
Cdd:cd07111 105 ESLDN-GKPIRESrDCDIPLVARHFYH---------HAGWAQLLDTELAG---WKPV-GVVGQIVPWNFPLLMLAWkICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 232 AALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNtLLQRPEFAALSFIGSTQVFKGLQKKIgAGV 311
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSA-LANHPGVDKVAFTGSTEVGRALRRAT-AGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 312 GqgiynsyPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-P 390
Cdd:cd07111 249 G-------KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGdP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 391 VDEyNHFVNAVIHERAYDRLAEVLHAARSDPELELVAGGHASKDeGYYVHPTVYRTTNPRHDLMQRELFGPILTvyVYPD 470
Cdd:cd07111 322 LDK-AIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115384268 471 HDWESTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSG 537
Cdd:cd07111 398 RTAKEAVALANNT-PYGLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESG 459
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
97-557 |
5.56e-41 |
|
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: 154.05 E-value: 5.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAmpfEDRAAIFLRAAELVTGKYRAdivAATMLGQ--GKNIWQA--EIDapa 172
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAASYRSTLTR---YQRSAILNKAAALLEARREE---FARLITLesGLCLKDTryEVG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 173 ETADFFRCYVQECWSLYGQQPRVQAEGTWG-KLEY---RPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKPSDSA 247
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESFSCDLTANGKaRKIFtlrEPL-GVVLAITPFNHPLnQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 248 LHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGqgiynsYPRVVGETG 327
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAV----GKAIAATAG------YKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 328 GKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNhFVNAVIHERA 406
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGdPMDPAT-DMGTVIDEEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 407 YDRLAEVLHAARSDPELELVAGGHaskdEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTSpY 486
Cdd:cd07146 309 AIQIENRVEEAIAQGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLD--EAIAISNSTA-Y 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 487 ALTGSIFATDVAatrqaqtALKHAAGMLYINTKCTGAVVG----QHPFGGSRDSGTNDKTGTMAHLQRFVSVQTI 557
Cdd:cd07146 382 GLSSGVCTNDLD-------TIKRLVERLDVGTVNVNEVPGfrseLSPFGGVKDSGLGGKEGVREAMKEMTNVKTY 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
77-557 |
3.23e-40 |
|
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: 152.65 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 77 SGSTVAThgsrkqENPsRHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAA 154
Cdd:cd07142 17 SGKTFPT------IDP-RNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLE-KHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 155 TMLGQGKNIWQAEI-DAPAeTADFFRCYVQECWSLYGQQprVQAEGTW-GKLEYRPLeGFVYAVAPFNFTAL-GATLVGP 231
Cdd:cd07142 89 ETWDNGKPYEQARYaEVPL-AARLFRYYAGWADKIHGMT--LPADGPHhVYTLHEPI-GVVGQIIPWNFPLLmFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 232 AALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGV 311
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEV----GKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 312 GQGiyNSYPrVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGpv 391
Cdd:cd07142 241 AKS--NLKP-VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 392 DEYNHFVN---AVIHERAYDRLAEVLHAARSDPelELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVY 468
Cdd:cd07142 316 DPFRKGVEqgpQVDKEQFEKILSYIEHGKEEGA--TLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 469 pdhdweSTLDLV---NTTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTM 545
Cdd:cd07142 394 ------KTVDEVikrANNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKGIY 463
|
490
....*....|..
gi 115384268 546 AhLQRFVSVQTI 557
Cdd:cd07142 464 A-LNNYLQVKAV 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
91-557 |
2.31e-38 |
|
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: 147.22 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSrHREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyrADIVAAT-MLGQGKNIWQAE-I 168
Cdd:cd07117 22 NPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDEN--KELLAMVeTLDNGKPIRETRaV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 169 DAPAeTADFFRcYVQECWSLYGQQPRVQAEGTWGKLEYRPLeGFVYAVAPFNFTAL-GATLVGPAALLGNVVIWKPSDSA 247
Cdd:cd07117 99 DIPL-AADHFR-YFAGVIRAEEGSANMIDEDTLSIVLREPI-GVVGQIIPWNFPFLmAAWKLAPALAAGNTVVIKPSSTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 248 LHASWLLHRILLEAgLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkGLQKKIGAGvgqgiYNSYPRVVgETG 327
Cdd:cd07117 176 SLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEV--GRDVAIAAA-----KKLIPATL-ELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 328 GKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHERA 406
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGnPLDP-DTQMGAQVNKDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 407 YDRLAEVLHAARSDpELELVAGGH----ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNt 482
Cdd:cd07117 326 LDKILSYVDIAKEE-GAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED--EVIDMAN- 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 483 TSPYALTGSIFATDVaaTRQAQTALKHAAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTI 557
Cdd:cd07117 402 DSEYGLGGGVFTKDI--NRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIGRETHKSM-LDAYTQMKNI 471
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
97-538 |
1.03e-37 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 145.99 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDApAETAD 176
Cdd:PLN02278 51 EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII-ANKEDLAQLMTLEQGKPLKEAIGEV-AYGAS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 177 FFRCYVQECWSLYGQ-QPRVQAEGTWGKLEyRPLeGFVYAVAPFNF-TALGATLVGPAALLGNVVIWKPSDSALHASWLL 254
Cdd:PLN02278 129 FLEYFAEEAKRVYGDiIPSPFPDRRLLVLK-QPV-GVVGAITPWNFpLAMITRKVGPALAAGCTVVVKPSELTPLTALAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 255 HRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVgqgiynsyPRVVGETGGKNWGLV 334
Cdd:PLN02278 207 AELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV--------KRVSLELGGNAPFIV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 335 HPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVL 414
Cdd:PLN02278 279 FDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 415 HAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNTTSpYALTGSIFA 494
Cdd:PLN02278 359 QDAVSKGA-KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFT 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 115384268 495 TDVAATRQAQTALKHaaGMLYINTKCTGAVVGqhPFGGSRDSGT 538
Cdd:PLN02278 435 RDLQRAWRVSEALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
97-546 |
2.21e-37 |
|
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: 144.41 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKYRADIVAATMlGQGKNIWQA-EIDAPAeTA 175
Cdd:cd07559 27 KVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL-DNGKPIRETlAADIPL-AI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 176 DFFRcYVQECWslygqqpRVQaEGTWGKLE--------YRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSdS 246
Cdd:cd07559 105 DHFR-YFAGVI-------RAQ-EGSLSEIDedtlsyhfHEPL-GVVGQIIPWNFPLLMAAWkLAPALAAGNTVVLKPA-S 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGET 326
Cdd:cd07559 174 QTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTV--------GRLIMQYAAENLIPVTLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKnwglvhpSANI-----KNAVLNTIRAAFE-------YQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDE 393
Cdd:cd07559 246 GGK-------SPNIffddaMDADDDFDDKAEEgqlgfafNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGnPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 394 yNHFVNAVIHERAYDRLAEVLHAARSDpELELVAGGHASK----DEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYP 469
Cdd:cd07559 319 -ETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGERLTlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 470 DHDweSTLDLVNTTsPYALTGSIFatdvaaTRQAQTALKHA----AGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTM 545
Cdd:cd07559 397 DEE--EAIAIANDT-EYGLGGGVW------TRDINRALRVArgiqTGRVWVN--CYHQYPAHAPFGGYKKSGIGRETHKM 465
|
.
gi 115384268 546 A 546
Cdd:cd07559 466 M 466
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-543 |
1.49e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 140.33 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 6 LSQSTRAVALHTSSRRVGGPTLSRYLSLWQPPKFVNEQPLDyakgSPERAKLTQALekLKGELPVQVpiqiSGSTVATHG 85
Cdd:PLN02466 10 LSRSLSASSSALLRSRGRNGGRGRGIRRFSTAAAAVEEPIT----PPVQVSYTQLL--INGQFVDAA----SGKTFPTLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 86 SRKQEnpsrhreIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNI 163
Cdd:PLN02466 80 PRTGE-------VIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 164 WQ-AEIDAPAeTADFFRCYVQECWSLYGQQprVQAEGTWG-KLEYRPLeGFVYAVAPFNFTALG-ATLVGPAALLGNVVI 240
Cdd:PLN02466 152 EQsAKAELPM-FARLFRYYAGWADKIHGLT--VPADGPHHvQTLHEPI-GVAGQIIPWNFPLLMfAWKVGPALACGNTIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 241 WKPSD----SALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFK---GLQKKigagvgq 313
Cdd:PLN02466 228 LKTAEqtplSALYAAKLLH----EAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKivlELAAK------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 314 giYNSYPrVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGpvde 393
Cdd:PLN02466 297 --SNLKP-VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVG---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 394 yNHFVNAVIHERAYD--RLAEVLHAARSDPE--LELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYP 469
Cdd:PLN02466 370 -DPFKKGVEQGPQIDseQFEKILRYIKSGVEsgATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115384268 470 DHDweSTLDLVNTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTG 543
Cdd:PLN02466 449 DLD--EVIRRANNT-RYGLAAGVFTQNLDTANTLSRALR--VGTVWVN--CFDVFDAAIPFGGYKMSGIGREKG 515
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
97-555 |
2.12e-35 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 138.86 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVtgKYRADIVAAT-MLGQGKNIWQAEIDAPAETA 175
Cdd:PRK13252 33 EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL--RERNDELAALeTLDTGKPIQETSVVDIVTGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 176 DFFRCYVQECWSLYGQQPRVQaEGTWGKLEYRPLeGFVYAVAPFNF---TAL--GAtlvgPAALLGNVVIWKPSD----S 246
Cdd:PRK13252 111 DVLEYYAGLAPALEGEQIPLR-GGSFVYTRREPL-GVCAGIGAWNYpiqIACwkSA----PALAAGNAMIFKPSEvtplT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHaswlLHRILLEAGLPKDVIQFLPGDAEVVTnTLLQRPEFAALSFIGSTqvfkGLQKKIGAGVGQGIynsyPRVVGET 326
Cdd:PRK13252 185 ALK----LAEIYTEAGLPDGVFNVVQGDGRVGA-WLTEHPDIAKVSFTGGV----PTGKKVMAAAAASL----KEVTMEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHFvNAVIHER 405
Cdd:PRK13252 252 GGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGdPMDPATNF-GPLVSFA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 406 AYDRLAEVLHAARSDPElELVAGGHA----SKDEGYYVHPTVYrtTNPRHD--LMQRELFGPILTVYVYPDHDweSTLDL 479
Cdd:PRK13252 331 HRDKVLGYIEKGKAEGA-RLLCGGERltegGFANGAFVAPTVF--TDCTDDmtIVREEIFGPVMSVLTFDDED--EVIAR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115384268 480 VNTTsPYALTGSIFATDVaaTRQAQTALKHAAGMLYINTkcTGAVVGQHPFGGSRDSGTNDKTG--TMAHLQRFVSVQ 555
Cdd:PRK13252 406 ANDT-EYGLAAGVFTADL--SRAHRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIGRENGiaTLEHYTQIKSVQ 478
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
76-557 |
2.22e-35 |
|
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: 139.02 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVATHgsrkqeNPSRHrEIVAEYATAGPEQVNAAVEAALKA---KPAWEAMPFEDRAAIFLRAAELVTgKYRADIV 152
Cdd:cd07141 19 VSGKTFPTI------NPATG-EKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIE-RDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 153 AATMLGQGKNIW-QAEIDAPaETADFFRCYVQECWSLYGQQprVQAEG---TWGKLEyrPLeGFVYAVAPFNFTALGATL 228
Cdd:cd07141 91 SLETLDNGKPFSkSYLVDLP-GAIKVLRYYAGWADKIHGKT--IPMDGdffTYTRHE--PV-GVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 229 -VGPAALLGNVVIWKPSD----SALHASWLLHrillEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGL 303
Cdd:cd07141 165 kLAPALACGNTVVLKPAEqtplTALYLASLIK----EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 304 QKKIGAgvgqgiyNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQL 383
Cdd:cd07141 241 QQAAGK-------SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 384 SKLTVG-PVDEYNHFvNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPI 462
Cdd:cd07141 314 KKRVVGnPFDPKTEQ-GPQIDEEQFKKILELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 463 LTVYVYpdhdweSTLDLV----NTTsPYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGT 538
Cdd:cd07141 392 QQIFKF------KTIDEVieraNNT-TYGLAAAVFTKDIDKAITFSNALR--AGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
490
....*....|....*....
gi 115384268 539 NDKTGTMAhLQRFVSVQTI 557
Cdd:cd07141 461 GRELGEYG-LQEYTEVKTV 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
97-537 |
6.05e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 137.18 E-value: 6.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyrADIVAATM-LGQGKNIWQAEIDApAETA 175
Cdd:PRK09406 12 ETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAE--ADQVAALMtLEMGKTLASAKAEA-LKCA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 176 DFFRCYVQECWSLYGQQP----RVQAEGTWGKleYRPLeGFVYAVAPFNFTALGAT-LVGPAALLGNVVIWKPSD----S 246
Cdd:PRK09406 89 KGFRYYAEHAEALLADEPadaaAVGASRAYVR--YQPL-GVVLAVMPWNFPLWQVVrFAAPALMAGNVGLLKHASnvpqT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRilleAGLPKDVIQ-FLPGDAEVvtNTLLQRPEFAALSFIGStqvfkglqKKIGAGVGQGIYNSYPRVVGE 325
Cdd:PRK09406 166 ALYLADLFRR----AGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGS--------EPAGRAVAAIAGDEIKKTVLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 326 TGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHE 404
Cdd:PRK09406 232 LGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGdPTDPDTD-VGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 405 RAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTs 484
Cdd:PRK09406 311 QGRDEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADID--EAIEIANAT- 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 485 PYALTGSIFATDVAATRQAQTALKhaAGMLYINtkctGAVVG--QHPFGGSRDSG 537
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLE--AGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
91-537 |
7.66e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 137.35 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHrEIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQA--EI 168
Cdd:PRK11241 32 NPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMM-EHQDDLARLMTLEQGKPLAEAkgEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 169 dapAETADFFRCYVQECWSLYGQQ-PRVQAEGTWGKLEyRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSDS 246
Cdd:PRK11241 110 ---SYAASFIEWFAEEGKRIYGDTiPGHQADKRLIVIK-QPI-GVTAAITPWNFPAAMITRkAGPALAAGCTMVLKPASQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVgqgiynsyPRVVGET 326
Cdd:PRK11241 185 TPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI--------KKVSLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERA 406
Cdd:PRK11241 257 GGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 407 YDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTSpY 486
Cdd:PRK11241 337 VAKVEEHIADALEKGA-RVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA--DVIAQANDTE-F 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 115384268 487 ALTGSIFATDVAATRQAQTALKHaaGMLYINTKCTGAVVGqhPFGGSRDSG 537
Cdd:PRK11241 413 GLAAYFYARDLSRVFRVGEALEY--GIVGINTGIISNEVA--PFGGIKASG 459
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
97-537 |
1.35e-33 |
|
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: 133.49 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIF------LRA-----AELVT---GKYRADivaatmlGQGKn 162
Cdd:cd07130 23 EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVrqigdaLRKkkealGKLVSlemGKILPE-------GLGE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 163 iWQAEIDapaeTADFfrcYVQECWSLYGQ-----QPRVQAEGTWgkleyRPLeGFVYAVAPFNFT----ALGATLvgpAA 233
Cdd:cd07130 95 -VQEMID----ICDF---AVGLSRQLYGLtipseRPGHRMMEQW-----NPL-GVVGVITAFNFPvavwGWNAAI---AL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 234 LLGNVVIWKPSDS----ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVtNTLLQRPEFAALSFIGSTQVfkglqkkiGA 309
Cdd:cd07130 158 VCGNVVVWKPSPTtpltAIAVTKIVARVLEKNGLPGAIASLVCGGADVG-EALVKDPRVPLVSFTGSTAV--------GR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 310 GVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG 389
Cdd:cd07130 229 QVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 390 -PVDEYNHfVNAVIHERAYDRLAEVLHAARSDpELELVAGGHASKDEGYYVHPTVyrTTNPRHD-LMQRELFGPILtvYV 467
Cdd:cd07130 309 dPLDDGTL-VGPLHTKAAVDNYLAAIEEAKSQ-GGTVLFGGKVIDGPGNYVEPTI--VEGLSDApIVKEETFAPIL--YV 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 468 YPDHDWESTLDLvNTTSPYALTGSIFATDVAATRQAQTALKHAAGMLYINTKCTGAVVGQhPFGGSRDSG 537
Cdd:cd07130 383 LKFDTLEEAIAW-NNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGG-AFGGEKETG 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
148-537 |
1.02e-32 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 129.86 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 148 RADIVAATMLG-QGKNIWQAEIDApAETADFFRcYVQEcWSLYGQQPRVQAEgtwgkleyRPLE---------GFVYAVA 217
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEV-AFTADYID-YMAE-WARRYEGEIIQSD--------RPGEnillfkralGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 218 PFNFTA-LGATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGS 296
Cdd:PRK10090 80 PWNFPFfLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 297 TQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFK 376
Cdd:PRK10090 160 VSA--------GEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 377 RLLQAQLSKLTVG-PVDEYNHFVNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQ 455
Cdd:PRK10090 232 NRLGEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 456 RELFGPILTVYVYPDHDweSTLDLVNtTSPYALTGSIFATDVAATRQAQTALKHaaGMLYINTKCTGAVVGQHpfGGSRD 535
Cdd:PRK10090 311 EETFGPVLPVVAFDTLE--EAIAMAN-DSDYGLTSSIYTQNLNVAMKAIKGLKF--GETYINRENFEAMQGFH--AGWRK 383
|
..
gi 115384268 536 SG 537
Cdd:PRK10090 384 SG 385
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
97-557 |
1.34e-32 |
|
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: 130.54 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKA--KPAW------EAMPFEDRAAIFLRAAELVtgkyrADIVAatmLGQGKNIWQA-- 166
Cdd:cd07120 8 EVIGTYADGGVAEAEAAIAAARRAfdETDWahdprlRARVLLELADAFEANAERL-----ARLLA---LENGKILGEArf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 167 EIDAPAETAdffRCYVQECWSLYGQQPRVQAeGTWGKLEYRPLeGFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKP-S 244
Cdd:cd07120 80 EISGAISEL---RYYAGLARTEAGRMIEPEP-GSFSLVLREPM-GVAGIIVPWNSPVvLLVRSLAPALAAGCTVVVKPaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 DSALHASWLLhRILLEA-GLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQGIynsyPRVV 323
Cdd:cd07120 155 QTAQINAAII-RILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT----GRAIMAAAAPTL----KRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 324 GETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIH 403
Cdd:cd07120 226 LELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 404 ERAYDRLAEVLHAARSDPELELVAGGHASKD--EGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVN 481
Cdd:cd07120 306 RANVDRVDRMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALAN 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115384268 482 TTSpYALTGSIFATDVA-ATRQAQtALKhaAGMLYINTKctGAVVGQHPFGGSRDSGTNDKTGtMAHLQRFVSVQTI 557
Cdd:cd07120 384 DTD-YGLAASVWTRDLArAMRVAR-AIR--AGTVWINDW--NKLFAEAEEGGYRQSGLGRLHG-VAALEDFIEYKHI 453
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
51-517 |
1.87e-32 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 131.79 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 51 SPERAKLTQaleklkgeLPVQVPIQISGSTVATHGSRKQE--NPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMP 128
Cdd:PLN02419 101 SPEQSTQPQ--------MPPRVPNLIGGSFVESQSSSFIDviNPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 129 FEDRAAIFLRAAELVtgKYRADIVAATMLG-QGKNIWQAEidapaetADFFR---CYVQECWSLYGQQPRVQAEGTWGKL 204
Cdd:PLN02419 172 ITTRQRVMLKFQELI--RKNMDKLAMNITTeQGKTLKDSH-------GDIFRgleVVEHACGMATLQMGEYLPNVSNGVD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 205 EY---RPLeGFVYAVAPFNFTALGATLVGPAALL-GNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVtN 280
Cdd:PLN02419 243 TYsirEPL-GVCAGICPFNFPAMIPLWMFPVAVTcGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-N 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 281 TLLQRPEFAALSFIGSTQVFKGLQKKiGAGVGQgiynsypRVVGETGGKNWGLVHPSANIkNAVLNTIRAA-FEYQGQKC 359
Cdd:PLN02419 321 AICDDEDIRAVSFVGSNTAGMHIYAR-AAAKGK-------RIQSNMGAKNHGLVLPDANI-DATLNALLAAgFGAAGQRC 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 360 SA-NSRLYVAESAWPEFKRLLQAQLSKLTVGpvDEYNHFVNAVIHERAYDRLAEVLHAARSDPELELVAGGH---ASKDE 435
Cdd:PLN02419 392 MAlSTVVFVGDAKSWEDKLVERAKALKVTCG--SEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvPGYEK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 436 GYYVHPTVYRTTNPRHDLMQRELFGPILTvyVYPDHDWESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLY 515
Cdd:PLN02419 470 GNFIGPTILSGVTPDMECYKEEIFGPVLV--CMQANSFDEAISIINKNK-YGNGAAIFTSSGAAARKFQMDIE--AGQIG 544
|
..
gi 115384268 516 IN 517
Cdd:PLN02419 545 IN 546
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
91-573 |
7.09e-32 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 129.08 E-value: 7.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 91 NPSRHrEIVAEYATAGPEQVNAAVEAALKA-----KPAWEAMPFEDRAAiFLRAAELVTGKYRADIVAATMLGQGKNIWQ 165
Cdd:PLN02467 29 NPATE-ETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAK-YLRAIAAKITERKSELAKLETLDCGKPLDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 166 AEIDAPaETADFFRCYVQECWSLYGQQP---RVQAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIW 241
Cdd:PLN02467 107 AAWDMD-DVAGCFEYYADLAEALDAKQKapvSLPMETFKGYVLKEPL-GVVGLITPWNYPLLMATWkVAPALAAGCTAVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 242 KPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglQKKIGAGVGQGIYnsyPr 321
Cdd:PLN02467 185 KPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT----GRKIMTAAAQMVK---P- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 322 VVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAV 401
Cdd:PLN02467 257 VSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 402 IHERAYDRLAEVLHAARSDpELELVAGGHASKD--EGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDL 479
Cdd:PLN02467 337 VSEGQYEKVLKFISTAKSE-GATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED--EAIEL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 480 VNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGTMAhLQRFVSVQTIke 559
Cdd:PLN02467 414 ANDSH-YGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSGFGRELGEWG-LENYLSVKQV-- 485
|
490
....*....|....
gi 115384268 560 efteldrVEYPSNE 573
Cdd:PLN02467 486 -------TKYISDE 492
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
70-561 |
9.86e-32 |
|
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: 128.38 E-value: 9.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 70 VQVPIQ--ISGSTVATHGSRKQE--NPSrHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELV 143
Cdd:cd07140 2 LKMPHQlfINGEFVDAEGGKTYNtiNPT-DGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 144 TgKYRADIVAATMLGQGKNIWQAEIDAPAETADFFRCYVQECWSLYGQ-----QPRVQAEGTWGKLEyrPLeGFVYAVAP 218
Cdd:cd07140 81 E-EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKtipinQARPNRNLTLTKRE--PI-GVCGIVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 219 FNFTALGATLVGPAALL-GNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGST 297
Cdd:cd07140 157 WNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 298 QVFKGLQKKIGAgvgqgiyNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKR 377
Cdd:cd07140 237 PIGKHIMKSCAV-------SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 378 LLQAQLSKLTVG-PVD-EYNHfvNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQ 455
Cdd:cd07140 310 RVVEEVKKMKIGdPLDrSTDH--GPQNHKAHLDKLVEYCERGVKEGA-TLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 456 RELFGPILTVYVYPDHDWESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVGqhPFGGSRD 535
Cdd:cd07140 387 EESFGPIMIISKFDDGDVDGVLQRANDTE-YGLASGVFTKDINKALYVSDKLE--AGTVFVNTYNKTDVAA--PFGGFKQ 461
|
490 500
....*....|....*....|....*.
gi 115384268 536 SGTNDKTGTMAhLQRFVSVQTIKEEF 561
Cdd:cd07140 462 SGFGKDLGEEA-LNEYLKTKTVTIEY 486
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
90-557 |
6.00e-31 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 126.16 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 90 ENPSRHREIvAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAE 167
Cdd:PRK09847 40 VDPVTQAPL-AKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLME-AHAEELALLETLDTGKPIRHSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 168 IDAPAETADFFRCYVQECWSLYGQQPRVqAEGTWGKLEYRPLeGFVYAVAPFNFTALGATL-VGPAALLGNVVIWKPSDS 246
Cdd:PRK09847 118 RDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPV-GVIAAIVPWNFPLLLTCWkLGPALAAGNSVILKPSEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiyNSYPRVVGET 326
Cdd:PRK09847 196 SPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD-------SNMKRVWLEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSA-NIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEyNHFVNAVIHE 404
Cdd:PRK09847 269 GGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGhPLDP-ATTMGTLIDC 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 405 RAYDRLAEVLHAARSDPELEL--VAGGHASkdegyYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLDLVNt 482
Cdd:PRK09847 348 AHADSVHSFIREGESKGQLLLdgRNAGLAA-----AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAN- 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115384268 483 TSPYALTGSIFATDVAATRQAQTALKhaAGMLYINTKCTGAVVgqHPFGGSRDSGtNDKTGTMAHLQRFVSVQTI 557
Cdd:PRK09847 420 DSQYGLGAAVWTRDLSRAHRMSRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
76-557 |
2.67e-30 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 124.55 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 76 ISGSTVAThgsrkqENPsRHREIVAEYATAGPEQVNAAVEAALKA--KPAWEAMPFEDRAAIFLRAAELVTgKYRADIVA 153
Cdd:PLN02766 33 ASGKTFET------RDP-RTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE-EHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 154 ATMLGQGKNIWQAE-IDAPAeTADFFRCYVQECWSLYGQQPRVQAEgTWGKLEYRPLeGFVYAVAPFNF-TALGATLVGP 231
Cdd:PLN02766 105 LDTIDAGKLFALGKaVDIPA-AAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPI-GVVGHIIPWNFpSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 232 AALLGNVVIWKPSD-SALHASWLLHrILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVfkglqkkiGAG 310
Cdd:PLN02766 182 ALAAGCTMVVKPAEqTPLSALFYAH-LAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEV--------GRK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 311 VGQGIYNSYPRVVG-ETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG 389
Cdd:PLN02766 253 IMQAAATSNLKQVSlELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 390 -PVDEYNHfVNAVIHERAYDR-LAEVLHAARSDPELelVAGGHASKDEGYYVHPTVYrtTNPRHDLM--QRELFGPILTV 465
Cdd:PLN02766 333 dPFDPRAR-QGPQVDKQQFEKiLSYIEHGKREGATL--LTGGKPCGDKGYYIEPTIF--TDVTEDMKiaQDEIFGPVMSL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 466 YVYpdHDWESTLDLVNTTSpYALTGSIFATDVAATRQAQTALKhaAGMLYINtkCTGAVVGQHPFGGSRDSGTNDKTGtM 545
Cdd:PLN02766 408 MKF--KTVEEAIKKANNTK-YGLAAGIVTKDLDVANTVSRSIR--AGTIWVN--CYFAFDPDCPFGGYKMSGFGRDQG-M 479
|
490
....*....|..
gi 115384268 546 AHLQRFVSVQTI 557
Cdd:PLN02766 480 DALDKYLQVKSV 491
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
193-537 |
3.32e-30 |
|
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: 123.02 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 193 PRVQAEGTwGKLEYRPLeGFVYAVAPFNF---TALgATLVGP-AAllGNVVIWKPSDSALHASWLLHRiLLEAGLPKDVI 268
Cdd:cd07087 86 PLLLQPAK-AYVIPEPL-GVVLIIGPWNYplqLAL-APLIGAiAA--GNTVVLKPSELAPATSALLAK-LIPKYFDPEAV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 269 QFLPGDAEVVTNtLLQRPeFAALSFIGSTQVfkGlqKKIGAGVGQgiyNSYPrVVGETGGKNWGLVHPSANIKNAVLNTI 348
Cdd:cd07087 160 AVVEGGVEVATA-LLAEP-FDHIFFTGSPAV--G--KIVMEAAAK---HLTP-VTLELGGKSPCIVDKDANLEVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 349 RAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLtVGPVDEYNHFVNAVIHERAYDRLAEVLHAARsdpeleLVAG 428
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGK------VVIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 429 GHASKDEgYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNTTsPYALTGSIFATDvaatRQAQTALK 508
Cdd:cd07087 303 GQVDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLD--EAIEFINSR-PKPLALYLFSED----KAVQERVL 374
|
330 340 350
....*....|....*....|....*....|.
gi 115384268 509 H--AAGMLYINTKCTGAVVGQHPFGGSRDSG 537
Cdd:cd07087 375 AetSSGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
97-557 |
9.66e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 119.20 E-value: 9.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 97 EIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRA--------AIFLRAAELvtgkyrADIVAATMlgqGKNIWQAEI 168
Cdd:PRK13968 18 EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAqklrdigkALRARSEEM------AQMITREM---GKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 169 DApAETADFFRCYVQECWSLYGQQPRVqAEGTWGKLEYRPLeGFVYAVAPFNFtALGATLVG--PAALLGNVVIWKPSDS 246
Cdd:PRK13968 89 EV-AKSANLCDWYAEHGPAMLKAEPTL-VENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGavPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 247 ALHASWLLHRILLEAGLPKDVIQFLPGDAEVVTNTLlQRPEFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGET 326
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRA--------GAAIGAQAGAALKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 327 GGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHF-------V 398
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGdPRDEENALgpmarfdL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 399 NAVIHERAYDRLAEvlhAARsdpeleLVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHdwESTLD 478
Cdd:PRK13968 316 RDELHHQVEATLAE---GAR------LLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDA--EHALE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 479 LVNtTSPYALTGSIFATDvaATRQAQTALKHAAGMLYINTKCtgAVVGQHPFGGSRDSGTNDKtgtMAH--LQRFVSVQT 556
Cdd:PRK13968 385 LAN-DSEFGLSATIFTTD--ETQARQMAARLECGGVFINGYC--ASDARVAFGGVKKSGFGRE---LSHfgLHEFCNIQT 456
|
.
gi 115384268 557 I 557
Cdd:PRK13968 457 V 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
96-547 |
1.07e-28 |
|
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: 119.06 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 96 REIVAEYATAGPEQVNAAVEAA---LKAKPAWeaMPFEDRAAIFLRAAELVTGkyRADIVAATMLGQGKNIWqaeIDAPA 172
Cdd:cd07148 9 LKPIGEVPTVDWAAIDKALDTAhalFLDRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGGKPL---VDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 173 ETA---DFFRCYVQECWSLYGQQ-PRVQAEGTWGKLEYRPLE--GFVYAVAPFNFTA-LGATLVGPAALLGNVVIWKP-S 244
Cdd:cd07148 82 EVTraiDGVELAADELGQLGGREiPMGLTPASAGRIAFTTREpiGVVVAISAFNHPLnLIVHQVAPAIAAGCPVIVKPaL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 245 DSALHASWLLhRILLEAGLPKDVIQFLPGDAEVvTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVgqgiynsypRVVG 324
Cdd:cd07148 162 ATPLSCLAFV-DLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT---------RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 325 ETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIH 403
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGdPTDPDTE-VGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 404 ERAYDRLAEVLHAARsDPELELVAGGHASKDEGYyvHPTVyrTTNPRHD--LMQRELFGPILTVYVYPDHDweSTLDLVN 481
Cdd:cd07148 310 PREVDRVEEWVNEAV-AAGARLLCGGKRLSDTTY--APTV--LLDPPRDakVSTQEIFGPVVCVYSYDDLD--EAIAQAN 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115384268 482 TTsPYALTGSIFATDVAATRQAQTALKHAAGMlyINTKcTGAVVGQHPFGGSRDSGTNdkTGTMAH 547
Cdd:cd07148 383 SL-PVAFQAAVFTKDLDVALKAVRRLDATAVM--VNDH-TAFRVDWMPFAGRRQSGYG--TGGIPY 442
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
110-555 |
4.70e-27 |
|
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: 113.87 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 110 VNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTGKyRADIVAATMLGQGKNIWQA-EIDAPAET-------ADFFRCY 181
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAeNICGDQVQlrarafvIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 182 VQECWSLyGQQPRVQAEGtwgkleYRPLEGFVYAVAPFNFTALGATLVGPAALL-GNVVIWKPSDSALHASWLLHRILLE 260
Cdd:cd07084 80 HEPGNHL-GQGLKQQSHG------YRWPYGPVLVIGAFNFPLWIPLLQLAGALAmGNPVIVKPHTAVSIVMQIMVRLLHY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 261 AG-LPKDVIQFLPGDAEvVTNTLLQRPEFAALSFIGStqvfkglqkkigAGVGQGIYN--SYPRVVGETGGKNWGLVHPS 337
Cdd:cd07084 153 AGlLPPEDVTLINGDGK-TMQALLLHPNPKMVLFTGS------------SRVAEKLALdaKQARIYLELAGFNWKVLGPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 338 ANIKNAVL-NTIRAAFEYQGQKCSANSRLYVAES-----AWPEFKRLLQAQ-LSKLTVGPVDEYNhfVNAVIHERAYDRL 410
Cdd:cd07084 220 AQAVDYVAwQCVQDMTACSGQKCTAQSMLFVPENwsktpLVEKLKALLARRkLEDLLLGPVQTFT--TLAMIAHMENLLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 411 AEVLHAARSDPELElvagghASKDEGYYVHPTVYRTTNP---RHDLMQRELFGPILTVYVYPDhDWESTLDLVNTTSPYA 487
Cdd:cd07084 298 SVLLFSGKELKNHS------IPSIYGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKK-DQLALVLELLERMHGS 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115384268 488 LTGSIFATDVAATRQAQTALKHAAGMLYINTKCTGAVVGQHPFGGSRDSGTNDKTGT---MAHLQRFVSVQ 555
Cdd:cd07084 371 LTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGpeaIKLVWRCHAEQ 441
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
199-537 |
5.96e-27 |
|
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: 113.48 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 199 GTWGKLEYRPlEGFVYAVAPFNF---TALGATLVGPAAllGNVVIWKPSDSALHASWLLHRILLEAGLPKDVIQFlPGDA 275
Cdd:cd07134 91 GTKSKIRYEP-KGVCLIISPWNYpfnLAFGPLVSAIAA--GNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVF-EGDA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 276 EVVTNtLLQRPeFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQ 355
Cdd:cd07134 167 EVAQA-LLELP-FDHIFFTGSPAV--------GKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 356 GQKCSANSRLYVAESAWPEFKRLLQAQLSKL-----TVGPVDEYNHFVNavihERAYDRLAEVLHAARSDPElELVAGGh 430
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygkdaARKASPDLARIVN----DRHFDRLKGLLDDAVAKGA-KVEFGG- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 431 ASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNtTSPYALTGSIFATDVAATRQ--AQTalk 508
Cdd:cd07134 311 QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLD--EVIEYIN-AKPKPLALYVFSKDKANVNKvlART--- 384
|
330 340
....*....|....*....|....*....
gi 115384268 509 hAAGMLYINTKCTGAVVGQHPFGGSRDSG 537
Cdd:cd07134 385 -SSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
191-537 |
1.41e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 113.20 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 191 QQPRVQAEGTwGKLEYRPLeGFVYAVAPFNFTALgaTLVGPAA---LLGNVVIWKPSDSALHASWLLHRiLLEAGLPKDV 267
Cdd:PTZ00381 93 DTVGVFGPGK-SYIIPEPL-GVVLVIGAWNYPLN--LTLIPLAgaiAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 268 IQFLPGDAEVVTNTLLQRpeFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNT 347
Cdd:PTZ00381 168 VRVIEGGVEVTTELLKEP--FDHIFFTGSPRV--------GKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 348 IRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLtVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDpeleLVA 427
Cdd:PTZ00381 238 AWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK----VVY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 428 GGHASKDEgYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNtTSPYALTGSIFATDvaatRQAQTAL 507
Cdd:PTZ00381 313 GGEVDIEN-KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENID--EVLEFIN-SRPKPLALYYFGED----KRHKELV 384
|
330 340 350
....*....|....*....|....*....|...
gi 115384268 508 KH--AAGMLYINtKCTGAVVGQH-PFGGSRDSG 537
Cdd:PTZ00381 385 LEntSSGAVVIN-DCVFHLLNPNlPFGGVGNSG 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
203-538 |
3.15e-24 |
|
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: 105.38 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 203 KLEYRPLeGFVYAVAPFNFTALgaTLVGP--AALL-GNVVIWKPSDSALHASWLLHRILLEAgLPKDVIQFLPGDAEVVT 279
Cdd:cd07135 103 RIRKEPL-GVVLIIGPWNYPVL--LALSPlvGAIAaGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 280 NTLLQRpeFAALSFIGSTQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKC 359
Cdd:cd07135 179 ALLEQK--FDKIFYTGSGRV--------GRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQIC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 360 SANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNaVIHERAYDRLAEVLHAARSDpeleLVAGGHASKDEgYYV 439
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTR-IVNPRHFNRLKSLLDTTKGK----VVIGGEMDEAT-RFI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 440 HPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNtTSPYALTGSIFATDVAATRQAQTalkhaagmlyiNTK 519
Cdd:cd07135 323 PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLD--EAIKVIN-SRDTPLALYIFTDDKSEIDHILT-----------RTR 388
|
330 340
....*....|....*....|....*...
gi 115384268 520 CTGAVVG---QH------PFGGSRDSGT 538
Cdd:cd07135 389 SGGVVINdtlIHvgvdnaPFGGVGDSGY 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
77-537 |
1.33e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 104.45 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 77 SGSTVAThgsrkqENPSRhREIVAEYATAGPEQVNAAVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATM 156
Cdd:PLN00412 29 SGKSVAI------TNPST-RKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILK-EHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 157 lgqgKNIWQAEIDAPAE---TADFFRcYVQEcwslygQQPRVQAEGTW---------GKLEY-----RPLeGFVYAVAPF 219
Cdd:PLN00412 101 ----KEIAKPAKDAVTEvvrSGDLIS-YTAE------EGVRILGEGKFlvsdsfpgnERNKYcltskIPL-GVVLAIPPF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 220 NFTA-LGATLVGPAALLGNVVIWKPSD----SALHASWLLHRilleAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFI 294
Cdd:PLN00412 169 NYPVnLAVSKIAPALIAGNAVVLKPPTqgavAALHMVHCFHL----AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 295 G-STQVfkGLQKKIGAGVGQGiynsyprvvgETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWP 373
Cdd:PLN00412 245 GgDTGI--AISKKAGMVPLQM----------ELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 374 EFKRLLQAQLSKLTVGPVDEyNHFVNAVIHERAYDRLAEVLHAARSDPelelvAGGHAS-KDEGYYVHPTVYRTTNPRHD 452
Cdd:PLN00412 313 ALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKG-----ATFCQEwKREGNLIWPLLLDNVRPDMR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 453 LMQRELFGPILTVYVYpdHDWESTLDLVNtTSPYALTGSIFATDVAATRQAQTALKhaAGMLYINTkcTGAVVGQH-PFG 531
Cdd:PLN00412 387 IAWEEPFGPVLPVIRI--NSVEEGIHHCN-ASNFGLQGCVFTRDINKAILISDAME--TGTVQINS--APARGPDHfPFQ 459
|
....*.
gi 115384268 532 GSRDSG 537
Cdd:PLN00412 460 GLKDSG 465
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
202-468 |
1.16e-21 |
|
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: 97.96 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 202 GKLEYRPLeGFVYAVAPFN--FTALGATLVGP-AAllGNVVIWKPSDSALHASWLLHRILLEAgLPKDVIQFLPGDAEVV 278
Cdd:cd07136 94 SYIYYEPY-GVVLIIAPWNypFQLALAPLIGAiAA--GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 279 TNTLLQRpeFAALSFIGSTQVfkglqkkigagvGQGIYNSYPR----VVGETGGKNWGLVHPSANIKNAV--------LN 346
Cdd:cd07136 170 QELLDQK--FDYIFFTGSVRV------------GKIVMEAAAKhltpVTLELGGKSPCIVDEDANLKLAAkrivwgkfLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 347 TiraafeyqGQKCSANSRLYVAESAWPEFKRLLQAQLSKL-TVGPVD--EYNHFVNavihERAYDRLAEVLhaarsDPEl 423
Cdd:cd07136 236 A--------GQTCVAPDYVLVHESVKEKFIKELKEEIKKFyGEDPLEspDYGRIIN----EKHFDRLAGLL-----DNG- 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 115384268 424 ELVAGGHASKDEgYYVHPTVYRTTNPRHDLMQRELFGPILTVYVY 468
Cdd:cd07136 298 KIVFGGNTDRET-LYIEPTILDNVTWDDPVMQEEIFGPILPVLTY 341
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
203-537 |
1.97e-18 |
|
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: 87.93 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 203 KLEYRPLeGFVYAVAPFNF----------TALGAtlvgpaallGNVVIWKPSDSALHASWLLHRiLLEAGLPKDVIQFLP 272
Cdd:cd07133 96 EVEYQPL-GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAE-LLAEYFDEDEVAVVT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 273 GDAEVVtntllqrPEFAALSF-----IGSTQVfkGlqKKIGAGVGQgiyNSYPrVVGETGGKNWGLVHPSANIKNAVLNT 347
Cdd:cd07133 165 GGADVA-------AAFSSLPFdhllfTGSTAV--G--RHVMRAAAE---NLTP-VTLELGGKSPAIIAPDADLAKAAERI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 348 IRAAFEYQGQKCSANSRLYVAESAWPEFKRLLQAQLSKLtvgpvdeYNHFVN-----AVIHERAYDRLAEVLHAARSD-P 421
Cdd:cd07133 230 AFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-------YPTLADnpdytSIINERHYARLQGLLEDARAKgA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 422 ELELVAGGHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYPDHDweSTLDLVNT-TSPYALTgsIFATDvaaT 500
Cdd:cd07133 303 RVIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLD--EAIDYINArPRPLALY--YFGED---K 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 115384268 501 RQAQTALKH-AAGMLYINTkcTGAVVGQH--PFGGSRDSG 537
Cdd:cd07133 376 AEQDRVLRRtHSGGVTIND--TLLHVAQDdlPFGGVGASG 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
206-544 |
5.28e-15 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 77.57 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 206 YRPLeGFVYAVAPFNF--TALG--ATLvgpAALLGNVVIWKPSDS----ALHASWLLHRILLEAGLPKDVIQFLPGDAEV 277
Cdd:PLN02315 152 WNPL-GIVGVITAFNFpcAVLGwnACI---ALVCGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLPGAIFTSFCGGAEI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 278 vTNTLLQRPEFAALSFIGSTqvfkglqkKIGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQ 357
Cdd:PLN02315 228 -GEAIAKDTRIPLVSFTGSS--------KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 358 KCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHFVNAVIHERAYDRLAEVLHAARSDPElELVAGGHASKDEGY 437
Cdd:PLN02315 299 RCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGG-KILTGGSAIESEGN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 438 YVHPTVYRTTnPRHDLMQRELFGPILtvYVYPDHDWESTLDLvNTTSPYALTGSIFatdvaaTRQAQTALK----HAA-- 511
Cdd:PLN02315 378 FVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIEI-NNSVPQGLSSSIF------TRNPETIFKwigpLGSdc 447
|
330 340 350
....*....|....*....|....*....|...
gi 115384268 512 GMLYINTKCTGAVVGQhPFGGSRDSGTNDKTGT 544
Cdd:PLN02315 448 GIVNVNIPTNGAEIGG-AFGGEKATGGGREAGS 479
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
201-538 |
5.80e-13 |
|
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: 70.90 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 201 WGKLEYRPLeGFVYAVAPFNFTALGAT--LVGPAALlGNVVIWKPSDSALHASWLLHRiLLEAGLPKDVIQFLPGDAEVV 278
Cdd:cd07137 94 KAEIVSEPL-GVVLVISAWNFPFLLSLepVIGAIAA-GNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 279 TNTLLQRpeFAALSFIGSTqvfkglqkKIGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEY-QGQ 357
Cdd:cd07137 171 TALLEQK--WDKIFFTGSP--------RVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 358 KCSANSRLYVAESAWPEFKRLLQAQLSKLtVGPVDEYNHFVNAVIHERAYDRLAEVLhaarSDPELE--LVAGGhaSKDE 435
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLL----DDPSVAdkIVHGG--ERDE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 436 -GYYVHPTVyrTTNPRHD--LMQRELFGPILTVYVYpdHDWESTLDLVNtTSPYALTGSIFATDVAATRQ--AQTalkhA 510
Cdd:cd07137 314 kNLYIEPTI--LLDPPLDssIMTEEIFGPLLPIITV--KKIEESIEIIN-SRPKPLAAYVFTKNKELKRRivAET----S 384
|
330 340
....*....|....*....|....*...
gi 115384268 511 AGMLYINTKCTGAVVGQHPFGGSRDSGT 538
Cdd:cd07137 385 SGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
218-463 |
4.67e-11 |
|
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: 64.94 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 218 PFNFTAlgATLVGP-AAllGNVVIWKPSDSALHASWLLHRiLLEAGLPKDVIQFLPGDAEVVTNTLLQRpeFAALSFIGS 296
Cdd:cd07132 113 PLQLTL--VPLVGAiAA--GNCVVIKPSEVSPATAKLLAE-LIPKYLDKECYPVVLGGVEETTELLKQR--FDYIFYTGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 297 TQVfkglqkkiGAGVGQGIYNSYPRVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYVAESAWPEFK 376
Cdd:cd07132 186 TSV--------GKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 377 RLLQAQLSKLTVGPVDEYNHFvNAVIHERAYDRLAEVLhaarsdPELELVAGGHASKDEgYYVHPTVYRTTNPRHDLMQR 456
Cdd:cd07132 258 EALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKLL------SGGKVAIGGQTDEKE-RYIAPTVLTDVKPSDPVMQE 329
|
....*..
gi 115384268 457 ELFGPIL 463
Cdd:cd07132 330 EIFGPIL 336
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
206-535 |
4.76e-11 |
|
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: 65.21 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 206 YRPLEGFVYAVAPFNF-------TALGATLVGPAALLgnvviwkPSDSALhaSWLLH---RILLEAGLPKDVIQFLPGDA 275
Cdd:cd07126 139 YRWPYGPVAIITPFNFpleipalQLMGALFMGNKPLL-------KVDSKV--SVVMEqflRLLHLCGMPATDVDLIHSDG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 276 EVVtNTLLQRPEFAALSFIGSTQVFKGLQKKIGAgvgqgiynsypRVVGETGGKNWGLVHPS-ANIKNAVLNTIRAAFEY 354
Cdd:cd07126 210 PTM-NKILLEANPRMTLFTGSSKVAERLALELHG-----------KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYAC 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 355 QGQKCSANSRLYVAESaW------PEFKRLL-QAQLSKLTVGPVDEYNhfvNAVIHERAyDRLAEVlhaarsdPELELVA 427
Cdd:cd07126 278 SGQKCSAQSILFAHEN-WvqagilDKLKALAeQRKLEDLTIGPVLTWT---TERILDHV-DKLLAI-------PGAKVLF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 428 GGHASKDEGyyvHPTVYRTTNP--------------RHDLMQRELFGPILTVYVYPDHDWESTLDLVNTTsPYALTGSIF 493
Cdd:cd07126 346 GGKPLTNHS---IPSIYGAYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQLPLVLEALERM-HAHLTAAVV 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 115384268 494 ATDVaatRQAQTALKHAA-GMLY--INTKCTGAvVGQHPFGGSRD 535
Cdd:cd07126 422 SNDI---RFLQEVLANTVnGTTYagIRARTTGA-PQNHWFGPAGD 462
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
208-529 |
1.19e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 63.96 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 208 PLEGFVYAVAPFNFTALG-ATLVGPAALLGNVVIWKPsdsALHASWLLHR---ILLEAG-LPKDVIQFLPGDAevvTNTL 282
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGlWEKAAPALLAGVPVIVKP---ATATAWLTQRmvkDVVAAGiLPAGALSVVCGSS---AGLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 283 LQRPEFAALSFIGSTQ---VFKGLQKKIGAGVgqgiynsypRVVGETGGKNWGLVHPSAN---------IKNAVLN-TIR 349
Cdd:PRK11903 221 DHLQPFDVVSFTGSAEtaaVLRSHPAVVQRSV---------RVNVEADSLNSALLGPDAApgseafdlfVKEVVREmTVK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 350 AafeyqGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNHfVNAVIHERAYDRLAEVLHAARSDPELELVAG 428
Cdd:PRK11903 292 S-----GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGnPRNDGVR-MGPLVSRAQLAAVRAGLAALRAQAEVLFDGG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 429 GHASKDE----GYYVHPTVYRTTNPR-----HDlmqRELFGPILTVYVYpdHDWESTLDLVNTTSPyALTGSIFATDVAA 499
Cdd:PRK11903 366 GFALVDAdpavAACVGPTLLGASDPDaatavHD---VEVFGPVATLLPY--RDAAHALALARRGQG-SLVASVYSDDAAF 439
|
330 340 350
....*....|....*....|....*....|
gi 115384268 500 TRQAQTALKHAAGMLYIntkCTGAVVGQHP 529
Cdd:PRK11903 440 LAAAALELADSHGRVHV---ISPDVAALHT 466
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
208-472 |
2.89e-09 |
|
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: 59.59 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 208 PLEGFVYAVAPFNFTALG-ATLVGPAALLGNVVIWKPSDSALHASWLLHRILLEAG-LPKDVIQFLPGDaevVTNTLLQR 285
Cdd:cd07128 143 PRRGVAVHINAFNFPVWGmLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDLLDHL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 286 PEFAALSFIGSTQVfkGLQKKIGAG-VGQGIynsypRVVGETGGKNWGLVHPSAN---------IKNAVLN-TIRAafey 354
Cdd:cd07128 220 GEQDVVAFTGSAAT--AAKLRAHPNiVARSI-----RFNAEADSLNAAILGPDATpgtpefdlfVKEVAREmTVKA---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 355 qGQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVG-PVDEYNH---FVNAVIHERAYDRLAEVLHAA---RSDPELELVA 427
Cdd:cd07128 289 -GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGdPRLEGVRmgpLVSREQREDVRAAVATLLAEAevvFGGPDRFEVV 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 115384268 428 GGHASKdeGYYVHPTVYRTTNPR-----HDLmqrELFGPILTVYVYPDHD 472
Cdd:cd07128 368 GADAEK--GAFFPPTLLLCDDPDaatavHDV---EAFGPVATLMPYDSLA 412
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
96-524 |
4.80e-06 |
|
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: 49.40 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 96 REIVAEYATAGPEQVnaaVEAALKAKPAWEAMPFEDRAAIFLRAAELVTgKYRADIVAATMLGQGKNIWQAEIDAPAETA 175
Cdd:cd07127 75 VELGVTYPQCDPDAL---LAAARAAMPGWRDAGARARAGVCLEILQRLN-ARSFEMAHAVMHTTGQAFMMAFQAGGPHAQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 176 DffrCYVQECWSLYGQQPRVQAEGTW----GKLEYRPLE----------GFVYAVAPF----NFTALGATLVgpaalLGN 237
Cdd:cd07127 151 D---RGLEAVAYAWREMSRIPPTAEWekpqGKHDPLAMEktftvvprgvALVIGCSTFptwnGYPGLFASLA-----TGN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 238 VVIWKPSDSALHASWLLHRI----LLEAGLPKDVIQFLPGDAEV-VTNTLLQRPEFAALSFIGSTQVFKGLQKKIGAGVg 312
Cdd:cd07127 223 PVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 313 qgiynsyprVVGETGGKNWGLVHPSANIKNAVLNTIRAAFEYQGQKCSANSRLYV---------AESAWPEFKRLLQAQL 383
Cdd:cd07127 302 ---------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 384 SKLTVGPvDEYNHFVNAVIHERAYDRLAEVLHAARSDPELELVAggHASKDEGYYVHPTVYRTTNPRHDLMQRELFGPIL 463
Cdd:cd07127 373 DGLLADP-ARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVA--HPEFPDARVRTPLLLKLDASDEAAYAEERFGPIA 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115384268 464 TVYVYPDHDWESTLDLVNTTSPYALTGSIFATDVAATRQAQTALKHAAGMLYINTkcTGAV 524
Cdd:cd07127 450 FVVATDSTDHSIELARESVREHGAMTVGVYSTDPEVVERVQEAALDAGVALSINL--TGGV 508
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
110-552 |
9.69e-06 |
|
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: 48.31 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 110 VNAAVEAALKAKPAWEAMPFEDRAAiFLRA-AELVTGKyRADIVAATM----LGQGKNiwQAEIdapAETADFFRCYVQE 184
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAA-FLEAiADEIEAL-GDELVARAHaetgLPEARL--QGEL---GRTTGQLRLFADL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 185 CWSLYGQQPRVQAEGTWGKLEYRP----LEGFVYAVAPF---NF-----TALGATLVGPAAllGNVVIWK-----PSDSA 247
Cdd:cd07129 74 VREGSWLDARIDPADPDRQPLPRPdlrrMLVPLGPVAVFgasNFplafsVAGGDTASALAA--GCPVVVKahpahPGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 248 LHASwLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEFAALSFIGSTQVFKGLqKKIGAGVGQGIynsyPrVVGETG 327
Cdd:cd07129 152 LVAR-AIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRAL-FDAAAARPEPI----P-FYAELG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 328 GKNWGLVHPSANIKNAvlNTIRAAFEY-----QGQKCSANSRLYVAESAWPE-FKRLLQAQLSKLTVGPVdeynhfVNAV 401
Cdd:cd07129 225 SVNPVFILPGALAERG--EAIAQGFVGsltlgAGQFCTNPGLVLVPAGPAGDaFIAALAEALAAAPAQTM------LTPG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 402 IHERAYDRLAEVLhaarSDPELELVAGGHASkDEGYYVHPTVYRT---TNPRHDLMQRELFGPILTVYVYPDHDwesTLD 478
Cdd:cd07129 297 IAEAYRQGVEALA----AAPGVRVLAGGAAA-EGGNQAAPTLFKVdaaAFLADPALQEEVFGPASLVVRYDDAA---ELL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 479 LVNTTSPYALTGSIFAT--DVAATRQAQTALKHAAGMLYINTKCTGAVVG---QH--PFGGSRDSGTndkT--GTMAhLQ 549
Cdd:cd07129 369 AVAEALEGQLTATIHGEedDLALARELLPVLERKAGRLLFNGWPTGVEVCpamVHggPYPATTDPRF---TsvGTAA-IE 444
|
...
gi 115384268 550 RFV 552
Cdd:cd07129 445 RFL 447
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
202-537 |
4.49e-05 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 46.26 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 202 GKLEYRPLeGFVYAVAPFNFtALGATL--VGPAALLGNVVIWKPSDSALHASWLLHRILlEAGLPKDVIQFLPGDAEVVT 279
Cdd:PLN02203 102 AEVVPEPL-GVVLIFSSWNF-PIGLSLepLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPAVGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 280 NTLLQRpeFAALSFIGSTqvfkglqkKIGAGVGQGIYNSYPRVVGETGGKNWGLVH---PSANIKNAVLNTIRAAFEY-Q 355
Cdd:PLN02203 179 QLLQHK--WDKIFFTGSP--------RVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 356 GQKCSANSRLYVAESAWPEFKRLLQAQLSKLTVGPVDEYNHfVNAVIHERAYDRLAEVLhaarSDPELE--LVAGGHASK 433
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLL----KDPRVAasIVHGGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115384268 434 DEgYYVHPTVYRTTNPRHDLMQRELFGPILTVYVYpdHDWESTLDLVNtTSPYALTGSIFATDVAATRQAQTalKHAAGM 513
Cdd:PLN02203 324 KK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSIAFIN-SKPKPLAIYAFTNNEKLKRRILS--ETSSGS 397
|
330 340
....*....|....*....|....
gi 115384268 514 LYINTKCTGAVVGQHPFGGSRDSG 537
Cdd:PLN02203 398 VTFNDAIIQYACDSLPFGGVGESG 421
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
232-288 |
1.77e-03 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 40.88 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115384268 232 AALL----GNVVIWKPSDSALH-----ASwLLHRILLEAGLPKDVIQFLPGDAEVVTNTLLQRPEF 288
Cdd:cd07079 127 AAALclksGNAVILRGGSEALHsnralVE-IIQEALEEAGLPEDAVQLIPDTDREAVQELLKLDDY 191
|
|
| |
