|
Name |
Accession |
Description |
Interval |
E-value |
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
11-541 |
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: 956.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 11 ANEPVHDYAPKSPERTRLRTELASLADHPIDLPHVIGGRHRMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMS 90
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 91 AKSDWAALPFDERAAVFLRAADLLAGPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGPGE 170
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLDGFVYAITPFNFTSIAGNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD 250
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAV 330
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 331 SRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKG-AAAVTVAVGGEYDDSEGYFVRP 409
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKdPEALTILYGGKYDDSQGYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLSDDPTDESFVIEYFGPLLSVHVYPDERYEQILDVIDTGSRYALTGAVIADDRQAVLTALDRLRFAAGNFYVNDKPT 489
Cdd:TIGR01236 401 TVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489997281 490 GAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSARSIKETFVAATDHIYPHMA 541
Cdd:TIGR01236 481 GAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-530 |
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: 894.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 10 PANEPVHDYAPKSPERTRLRTELASLADHPIDLPHVIGGRhRMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAM 89
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGK-EVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 90 SAKSDWAALPFDERAAVFLRAADLLAGPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGP- 168
Cdd:cd07123 80 EARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEWNRIDYRPLDGFVYAITPFNFTSIAGNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAV 248
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCS 328
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDDSEGYFVR 408
Cdd:cd07123 320 AASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 409 PTVLLSDDPTDESFVIEYFGPLLSVHVYPDERYEQILDVIDTGSRYALTGAVIADDRQAVLTALDRLRFAAGNFYVNDKP 488
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489997281 489 TGAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSARSIKETFV 530
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFV 521
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-529 |
1.09e-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: 397.72 E-value: 1.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 43 PHVIGGRhRMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPWREKI 122
Cdd:cd07083 20 PLVIGGE-WVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 123 AAATMLGqSKSVYQaEIDAVCELIDFWRFNVAFARQILEQQPI--SGPGEWNRIDYRPLdGFVYAITPFNFT-SIAGNLP 199
Cdd:cd07083 99 ATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GAGVVISPWNFPvAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 200 TAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGT 279
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 280 NIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDI 359
Cdd:cd07083 256 LAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 360 TDLSNYGGALIDQRAFVKNVDAIERAKGAAavTVAVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDE 439
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEG--QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 440 RYEQILDVIDTgSRYALTGAVIADDRQAVLTALDrlRFAAGNFYVNDKPTGAVVGRQPFGGARGSGTNDKAGSPLNLLRW 519
Cdd:cd07083 414 DFAEALEVANS-TPYGLTGGVYSRKREHLEEARR--EFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRF 490
|
490
....*....|
gi 489997281 520 TSARSIKETF 529
Cdd:cd07083 491 LEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-529 |
7.95e-125 |
|
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: 374.46 E-value: 7.95e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 41 DLPHVIGGRHRMG-DGERIDVVQPHrHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGpWR 119
Cdd:COG1012 5 EYPLFIGGEWVAAaSGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE-RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 120 EKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQIL-EQQPISGPGEWNRIDYRPLdGFVYAITPFNFTSIAGNL 198
Cdd:COG1012 83 EELAALLTLETGKPLAEARGE-VDRAADFLRYYAGEARRLYgETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 199 PTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWV 277
Cdd:COG1012 161 KLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 278 GTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYG 357
Cdd:COG1012 241 AENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 358 DITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEY-DDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVY 436
Cdd:COG1012 315 DPLDPGTDMGPLISEAQLERVLAYIEDAVAEGA-ELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 437 PDEryEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPTGAvVGRQPFGGARGSGTNDKAGsPLNL 516
Cdd:COG1012 394 DDE--EEAIALAN-DTEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGREGG-REGL 466
|
490
....*....|...
gi 489997281 517 LRWTSARSIKETF 529
Cdd:COG1012 467 EEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-529 |
5.34e-107 |
|
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: 329.57 E-value: 5.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 12 NEPVHDYAPKSpERTRLRTELASLADH-PIDLPHVIGGRHRMGDgERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMS 90
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVREElGREYPLVIGGKEVRTE-EKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 91 AKSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFnvaFARQILEQQP---ISG 167
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADAD-VAEAIDFLEY---YAREMLRLRGfpvEMV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 168 PGEWNRIDYRPLdGFVYAITPFNF-TSIAGNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:cd07124 156 PGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07124 235 EVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDDSEGYF 406
Cdd:cd07124 315 CSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 407 VRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDerYEQILDvIDTGSRYALTGAVIADDRQAVLTAldRLRFAAGNFYVND 486
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALE-IANDTEYGLTGGVFSRSPEHLERA--RREFEVGNLYANR 469
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489997281 487 KPTGAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSARSIKETF 529
Cdd:cd07124 470 KITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
95-512 |
8.58e-93 |
|
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: 291.36 E-value: 8.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQILEQQPISGPGEWNRI 174
Cdd:pfam00171 45 WRKTPAAERAAILRKAADLLEER-KDELAELETLENGKPLAEARGE-VDRAIDVLRYYAGLARRLDGETLPSDPGRLAYT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 175 DYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVAL 253
Cdd:pfam00171 123 RREPL-GVVGAITPWNFPLLLPAWKIAPALAaGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 254 ADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRA 333
Cdd:pfam00171 202 EHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 334 FIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPTVLl 413
Cdd:pfam00171 276 LVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGA-KLLTGGEAGLDNGYFVEPTVL- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 414 sDDPTDESFVI--EYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPTGA 491
Cdd:pfam00171 354 -ANVTPDMRIAqeEIFGPVLSVIRFKDE--EEAIE-IANDTEYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGD 427
|
410 420
....*....|....*....|.
gi 489997281 492 VVGRqPFGGARGSGTNDKAGS 512
Cdd:pfam00171 428 ADGL-PFGGFKQSGFGREGGP 447
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
41-529 |
1.95e-90 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 286.83 E-value: 1.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 41 DLPHVIGGRHRMGDgERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPWRE 120
Cdd:PRK03137 36 DYPLIIGGERITTE-DKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 121 kiAAATMlgqsksVYQA-----EIDA-VCELIDFWRFnvaFARQILE----QQPISGPGEWNRIDYRPLdGFVYAITPFN 190
Cdd:PRK03137 115 --FSAWL------VKEAgkpwaEADAdTAEAIDFLEY---YARQMLKladgKPVESRPGEHNRYFYIPL-GVGVVISPWN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 191 F-TSIAGNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTAt 269
Cdd:PRK03137 183 FpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSRE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 270 fghlwqwVGTNI---------GRYHsYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVW 340
Cdd:PRK03137 262 -------VGLRIyeraakvqpGQIW-LKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 341 QRMGDELLAKAAELRYGDITDlSNYGGALIDQRAFVKNVDAIERAKGAAAVTvaVGGEYDDSEGYFVRPTVLLSDDPTDE 420
Cdd:PRK03137 334 DEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGRLV--LGGEGDDSKGYFIQPTIFADVDPKAR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 421 SFVIEYFGPLLSVHVYPDerYEQILDvIDTGSRYALTGAVIADDRQAVLTAldRLRFAAGNFYVNDKPTGAVVGRQPFGG 500
Cdd:PRK03137 411 IMQEEIFGPVVAFIKAKD--FDHALE-IANNTEYGLTGAVISNNREHLEKA--RREFHVGNLYFNRGCTGAIVGYHPFGG 485
|
490 500
....*....|....*....|....*....
gi 489997281 501 ARGSGTNDKAGSPLNLLRWTSARSIKETF 529
Cdd:PRK03137 486 FNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
94-525 |
2.62e-88 |
|
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: 278.71 E-value: 2.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKsVYQAEIDAVCELIDFWRFNVAFARQILEQQPISG-PGEWN 172
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEER-REELAALETLETGK-PIEEALGEVARAADTFRYYAGLARRLHGEVIPSPdPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDV 251
Cdd:cd07078 91 IVRREPL-GVVGAITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTATFGHLWQWVGTNIGRyhsyprLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVS 331
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAENLKR------VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 332 RAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDDSEGYFVRPTV 411
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 412 LlsDDPTDESFVI--EYFGPLLSVHVYPDEryEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPT 489
Cdd:cd07078 324 L--TDVDPDMPIAqeEIFGPVLPVIPFKDE--EEAIELAN-DTEYGLAAGVFTRDLERALRVAERLE--AGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 489997281 490 GAVVGrQPFGGARGSGTNdKAGSPLNLLRWTSARSI 525
Cdd:cd07078 397 GAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
41-529 |
1.72e-80 |
|
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: 260.95 E-value: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 41 DLPHVIGGRhRMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPwRE 120
Cdd:TIGR01237 32 TYPLVINGE-RVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRR-RH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 121 KIAAATMLGQSKSVYQAEIDaVCELIDFWRFnvaFARQILE---QQPI-SGPGEWNRIDYRPLdGFVYAITPFNFT-SIA 195
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEADAE-VAEAIDFMEY---YARQMIElakGKPVnSREGETNQYVYTPT-GVTVVISPWNFPfAIM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 196 GNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTAtfghlwq 275
Cdd:TIGR01237 185 VGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSRE------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 276 wVGTNI---------GRYHsYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDE 346
Cdd:TIGR01237 258 -VGTRIferaakvqpGQKH-LKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 347 LLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKgaAAVTVAVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEY 426
Cdd:TIGR01237 336 FVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGK--AEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 427 FGPLLSVHVYPDerYEQILDVIDtGSRYALTGAVIADDRQAVLTAldRLRFAAGNFYVNDKPTGAVVGRQPFGGARGSGT 506
Cdd:TIGR01237 414 FGPVVAFIRASD--FDEALEIAN-NTEYGLTGGVISNNRDHINRA--KAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGT 488
|
490 500
....*....|....*....|...
gi 489997281 507 NDKAGSPLNLLRWTSARSIKETF 529
Cdd:TIGR01237 489 DSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
39-518 |
1.18e-77 |
|
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: 253.66 E-value: 1.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 39 PIDLPHVIGGRHRmgDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPw 118
Cdd:cd07125 31 WEAIPIINGEETE--TGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAN- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 119 REKIAAATMLGQSKSVYQAeIDAVCELIDFWRFNVAFARQILEQQPISGP-GEWNRIDYRPlDGFVYAITPFNF-TSI-A 195
Cdd:cd07125 108 RGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPtGELNGLELHG-RGVFVCISPWNFpLAIfT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 196 GNlpTAPALM-GNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHL 273
Cdd:cd07125 186 GQ--IAAALAaGNTVIAKPA-EQTpLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 274 WQWvgtNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAE 353
Cdd:cd07125 263 NRA---LAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 354 LRYGDITDLSNYGGALIDQRAFvKNVDA-IERAKGAAAVTVAVggEYDDSEGYFVRPTVLLsddpTDESFVI--EYFGPL 430
Cdd:cd07125 340 LKVGDPWDLSTDVGPLIDKPAG-KLLRAhTELMRGEAWLIAPA--PLDDGNGYFVAPGIIE----IVGIFDLttEVFGPI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 431 LSVHVYPDERYEQILDVI-DTGsrYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPTGAVVGRQPFGGARGSGTNDK 509
Cdd:cd07125 413 LHVIRFKAEDLDEAIEDInATG--YGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQPFGGWGLSGTGPK 488
|
....*....
gi 489997281 510 AGSPLNLLR 518
Cdd:cd07125 489 AGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
94-525 |
1.18e-60 |
|
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: 204.39 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKsVYQAEIDAVCELIDFWRFNVAFARQILE-QQPISGPGEWN 172
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEER-REELAALETLETGK-PIEEALGEVARAIDTFRYAAGLADKLGGpELPSPDPGGEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDV 251
Cdd:cd06534 87 YVRREPL-GVVGVITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTATFGHLWQWVGTNIGryhsypRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVS 331
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAAENLK------PVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 332 RAFIAHSVWqrmgDELLAKAAelrygditdlsnyggalidqrafvknvdaierakgaaavtvavggeyddsegyfvrpTV 411
Cdd:cd06534 240 RLLVHESIY----DEFVEKLV---------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 412 LLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPTGA 491
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALAN-DTEYGLTAGVFTRDLNRALRVAERLR--AGTVYINDSSIGV 333
|
410 420 430
....*....|....*....|....*....|....
gi 489997281 492 VVGrQPFGGARGSGTNdKAGSPLNLLRWTSARSI 525
Cdd:cd06534 334 GPE-APFGGVKNSGIG-REGGPYGLEEYTRTKTV 365
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-525 |
3.40e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 215.06 E-value: 3.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 22 SPERTRLRTELASLADHPIDLPHVIGGrhrmgDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFD 101
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 102 ERAAVFLRAADLLAGPWREKIAAATMLGqSKSVYQAeIDAVCELIDFWRFNVAFARQILEQ-QPISGP-GEWNRIDYRPL 179
Cdd:PRK11904 608 ERAAILERAADLLEANRAELIALCVREA-GKTLQDA-IAEVREAVDFCRYYAAQARRLFGApEKLPGPtGESNELRLHGR 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 180 DGFVyAITPFNFT-SI-AGnlPTAPALM-GNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALAD 255
Cdd:PRK11904 686 GVFV-CISPWNFPlAIfLG--QVAAALAaGNTVIAKPA-EQTpLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTAD 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 256 PRLAGIHFTGSTATFGHLWQwvgTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFI 335
Cdd:PRK11904 762 PRIAGVAFTGSTETARIINR---TLAARDGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFV 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 336 AHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFvKNVDA-IERAKGAAAVTVAVGGEYDDSEGYFVRPTVLLS 414
Cdd:PRK11904 839 QEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAK-ANLDAhIERMKREARLLAQLPLPAGTENGHFVAPTAFEI 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 415 DDPTD-ESfviEYFGPLLSVHVYPDERYEQILDVI-DTGsrYALTGAV---IADDRQAVltaLDRLRfaAGNFYVNDKPT 489
Cdd:PRK11904 918 DSISQlER---EVFGPILHVIRYKASDLDKVIDAInATG--YGLTLGIhsrIEETADRI---ADRVR--VGNVYVNRNQI 987
|
490 500 510
....*....|....*....|....*....|....*.
gi 489997281 490 GAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSARSI 525
Cdd:PRK11904 988 GAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
94-505 |
1.60e-56 |
|
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: 195.06 E-value: 1.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGpwREKIAAATMLGQSKSVY---QAEIDAVCELIdfwRFNVAFARQIL-EQQPISGPG 169
Cdd:cd07104 15 AWAATPPQERAAILRKAAEILEE--RRDEIADWLIRESGSTRpkaAFEVGAAIAIL---REAAGLPRRPEgEILPSDVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 EWNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSI-TQTLAAYLTMQLLEAAGLPPGVINLVTGDGFA 247
Cdd:cd07104 90 KESMVRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSrTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGSE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 248 VSDVALADPRLAGIHFTGSTATFGHlwqwVGTNIGRYHSYPRLvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKC 327
Cdd:cd07104 169 IGDALVEHPRVRMISFTGSTAVGRH----IGELAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAfVKNVDA-IERAKGAAAvTVAVGGEYDdseGYF 406
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQ-VDRVHAiVEDAVAAGA-RLLTGGTYE---GLF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 407 VRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVND 486
Cdd:cd07104 318 YQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVE-LANDTEYGLSAAVFTRDLERAMAFAERLE--TGMVHIND 392
|
410 420
....*....|....*....|.
gi 489997281 487 KPT--GAVVgrqPFGGARGSG 505
Cdd:cd07104 393 QTVndEPHV---PFGGVKASG 410
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
28-523 |
1.02e-55 |
|
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: 195.13 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 28 LRTELASLADHPIDLPHVIGGRHRmGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVF 107
Cdd:TIGR01238 24 LEAQIHAWADKTWQAAPIIGHSYK-ADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 108 LRAADLLAGPWREKIAAATMlgQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPIsgpgewnridyRPLDGFVyAIT 187
Cdd:TIGR01238 103 DRLADLLELHMPELMALCVR--EAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV-----------ESRGVFV-CIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 188 PFNF--TSIAGNLPTAPAlMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTG 265
Cdd:TIGR01238 169 PWNFplAIFTGQISAALA-AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 266 STATFghlwQWVGTNIGRYHSYP-RLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMG 344
Cdd:TIGR01238 248 STEVA----QLINQTLAQREDAPvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 345 DELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIE--RAKGAAAVTVAVGGEYDDSEGYFVRPTVLLSDDPTDESf 422
Cdd:TIGR01238 324 TMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEhmSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAELS- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 423 vIEYFGPLLSVHVYPDERYEQILDVIDTgSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPTGAVVGRQPFGGAR 502
Cdd:TIGR01238 403 -EEVFGPVLHVVRYKARELDQIVDQINQ-TGYGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQG 478
|
490 500
....*....|....*....|.
gi 489997281 503 GSGTNDKAGSPLNLLRWTSAR 523
Cdd:TIGR01238 479 LSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
94-505 |
3.08e-55 |
|
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: 192.54 E-value: 3.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGpwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIL-EQQPISGPGEWN 172
Cdd:cd07150 36 AWAATTPSERERILLKAAEIMER--RADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRgETLPSDSPGTVS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDV 251
Cdd:cd07150 114 MSVRRPL-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYhsyprlVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVS 331
Cdd:cd07150 193 LVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI------TLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSAS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 332 RAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALID--QRAFVKNVDAIERAKGAAAVTvavGGEYDdseGYFVRP 409
Cdd:cd07150 267 RIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISprQVERIKRQVEDAVAKGAKLLT---GGKYD---GNFYQP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLSDDPTDESFVIEYFGPLLSVHVYPDerYEQILDVIDTgSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKP- 488
Cdd:cd07150 341 TVLTDVTPDMRIFREETFGPVTSVIPAKD--AEEALELAND-TEYGLSAAILTNDLQRAFKLAERLE--SGMVHINDPTi 415
|
410
....*....|....*...
gi 489997281 489 -TGAVVgrqPFGGARGSG 505
Cdd:cd07150 416 lDEAHV---PFGGVKASG 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-518 |
2.74e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.17 E-value: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 26 TRLRTELASLADHPIDLPHVIGGRHRmgDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAA 105
Cdd:PRK11905 539 AALDEALNAFAAKTWHAAPLLAGGDV--DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAA 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 106 VFLRAADLLAGPWREKIAAAtMLGQSKSVYQAeIDAVCELIDFWRFNVAFARQILEQQPIsgpgewnridyRPLdGFVYA 185
Cdd:PRK11905 617 ILERAADLMEAHMPELFALA-VREAGKTLANA-IAEVREAVDFLRYYAAQARRLLNGPGH-----------KPL-GPVVC 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 186 ITPFNFtsiagnlPTA-------PALM-GNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADP 256
Cdd:PRK11905 683 ISPWNF-------PLAiftgqiaAALVaGNTVLAKPA-EQTpLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADP 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 257 RLAGIHFTGSTATFGHLWQWVGTNIGRyhsYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIA 336
Cdd:PRK11905 755 RIAGVMFTGSTEVARLIQRTLAKRSGP---PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQ 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 337 HSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAfVKNVDA-IERAKGAAAVTVAVGGEYDDSEGYFVRPTVLLSD 415
Cdd:PRK11905 832 EDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA-QANIEAhIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEID 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 416 DPTD-ESfviEYFGPLLSVHVYPDERYEQILDVI-DTGsrYALTGAV---IaDDRqaVLTALDRLRfaAGNFYVNDKPTG 490
Cdd:PRK11905 911 SISDlER---EVFGPVLHVVRFKADELDRVIDDInATG--YGLTFGLhsrI-DET--IAHVTSRIR--AGNIYVNRNIIG 980
|
490 500
....*....|....*....|....*....
gi 489997281 491 AVVGRQPFGGaRG-SGTNDKAGSPLNLLR 518
Cdd:PRK11905 981 AVVGVQPFGG-EGlSGTGPKAGGPLYLGR 1008
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
93-506 |
2.00e-53 |
|
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: 188.33 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAALPFDERAAVFLRAADLLAgpwREKIAAATMLGQS--KSVYQAEIDaVCELIDFWRFNVAFARQIL-EQQPISGPG 169
Cdd:cd07131 51 PEWRKVPAPRRAEYLFRAAELLK---KRKEELARLVTREmgKPLAEGRGD-VQEAIDMAQYAAGEGRRLFgETVPSELPN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 EWNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAV 248
Cdd:cd07131 127 KDAMTRRQPI-GVVALITPWNFPVAIPSWKIFPALVcGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALADPRLAGIHFTGSTATfghlWQWVGTNIGRYHSYPRLvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCS 328
Cdd:cd07131 206 GEALVEHPDVDVVSFTGSTEV----GERIGETCARPNKRVAL--EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGE----YDDSEG 404
Cdd:cd07131 280 ATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGA-TLLLGGErltgGGYEKG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 405 YFVRPTVLLSDDPTDESFVIEYFGPLLSvhVYPDERYEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYV 484
Cdd:cd07131 359 YFVEPTVFTDVTPDMRIAQEEIFGPVVA--LIEVSSLEEAIEIAN-DTEYGLSSAIYTEDVNKAFRARRDLE--AGITYV 433
|
410 420
....*....|....*....|..
gi 489997281 485 NDKPTGAVVgRQPFGGARGSGT 506
Cdd:cd07131 434 NAPTIGAEV-HLPFGGVKKSGN 454
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
24-523 |
1.28e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 193.23 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 24 ERTRLRTELASLADHPIDLPHVIGGRhrMGDGERIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDER 103
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAAPLIAGE--AASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 104 AAVFLRAADLL--------------AGpwrekiaaatmlgqsKSvYQAEIDAVCELIDFWRFNVAFARQILEqqpisgpg 169
Cdd:COG4230 618 AAILERAADLLeahraelmallvreAG---------------KT-LPDAIAEVREAVDFCRYYAAQARRLFA-------- 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 ewNRIDYRPLdGFVYAITPFNFtsiagnlP-------TAPALM-GNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINL 240
Cdd:COG4230 674 --APTVLRGR-GVFVCISPWNF-------PlaiftgqVAAALAaGNTVLAKPA-EQTpLIAARAVRLLHEAGVPADVLQL 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 241 VTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQwvgTNIGRYHSYPRLVGETGGKDFVVAHASARP-----DVlrtal 315
Cdd:COG4230 743 LPGDGETVGAALVADPRIAGVAFTGSTETARLINR---TLAARDGPIVPLIAETGGQNAMIVDSSALPeqvvdDV----- 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 316 IRGAFDYQGQKCSAVSRAFIAHSVWQRMgDELLAKA-AELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVA 394
Cdd:COG4230 815 LASAFDSAGQRCSALRVLCVQEDIADRV-LEMLKGAmAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQ 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 395 VGGEYDDSEGYFVRPTVLLSDDPTD-ESfviEYFGPLLsvHVYpdeRY--EQILDVIDT--GSRYALTGAV---IaDDRQ 466
Cdd:COG4230 894 LPLPEECANGTFVAPTLIEIDSISDlER---EVFGPVL--HVV---RYkaDELDKVIDAinATGYGLTLGVhsrI-DETI 964
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489997281 467 AvlTALDRLRfaAGNFYVNDKPTGAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSAR 523
Cdd:COG4230 965 D--RVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATER 1017
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
96-506 |
4.39e-52 |
|
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: 183.95 E-value: 4.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 96 AALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQIL-EQQPISG-PGEWNR 173
Cdd:cd07149 38 KSLPAYERAEILERAAQLLEER-REEFARTIALEAGKPIKDARKE-VDRAIETLRLSAEEAKRLAgETIPFDAsPGGEGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDY---RPLdGFVYAITPFNFTSiagNL---PTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:cd07149 116 IGFtirEPI-GVVAAITPFNFPL---NLvahKVGPAIAaGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07149 192 TVGDALVTDPRVRMISFTGSPA--------VGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGD----ITDLsnygGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDds 402
Cdd:cd07149 264 CISVQRIFVHEDIYDEFLERFVAATKKLVVGDpldeDTDV----GPMISEAEAERIEEWVEEAVEGGA-RLLTGGKRD-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 403 eGYFVRPTVLLSDDPTDESFVIEYFGPLLSVhvypdERYEQILDVID--TGSRYALTGAVIADDRQAVLTALDRLRfaAG 480
Cdd:cd07149 337 -GAILEPTVLTDVPPDMKVVCEEVFAPVVSL-----NPFDTLDEAIAmaNDSPYGLQAGVFTNDLQKALKAARELE--VG 408
|
410 420
....*....|....*....|....*.
gi 489997281 481 NFYVNDKPTgAVVGRQPFGGARGSGT 506
Cdd:cd07149 409 GVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
44-512 |
1.03e-50 |
|
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: 180.84 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 44 HVIGGRHRMGDGERIDVVQPHrHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLagpwREKIA 123
Cdd:cd07086 1 GVIGGEWVGSGGETFTSRNPA-NGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL----RKKKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 124 AatmLGQSKS-----VYQAEIDAVCELIDFWRFNVAFARQILEQQ-PISGPGEWNRIDYRPLdGFVYAITPFNF-TSIAG 196
Cdd:cd07086 76 A---LGRLVSlemgkILPEGLGEVQEMIDICDYAVGLSRMLYGLTiPSERPGHRLMEQWNPL-GVVGVITAFNFpVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 197 -NLptAPALM-GNTVIWKPSITQTLAAYLTMQLLEAA----GLPPGVINLVTGDGfAVSDVALADPRLAGIHFTGSTATf 270
Cdd:cd07086 152 wNA--AIALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEV- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 271 GHlwqWVGTNIGRYHSypRLVGETGGKDFVVAHASARPD-VLRTALIrGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLA 349
Cdd:cd07086 228 GR---RVGETVARRFG--RVLLELGGNNAIIVMDDADLDlAVRAVLF-AAVGTAGQRCTTTRRLIVHESVYDEFLERLVK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 350 KAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEY--DDSEGYFVRPTVLlsDDPTDESFVI--E 425
Cdd:cd07086 302 AYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGG-TVLTGGKRidGGEPGNYVEPTIV--TGVTDDARIVqeE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 426 YFGPLLSVHVYPDerYEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRFAAGNFYVNDKPTGAVVGrQPFGGARGSG 505
Cdd:cd07086 379 TFAPILYVIKFDS--LEEAIA-INNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
....*..
gi 489997281 506 TNDKAGS 512
Cdd:cd07086 455 GGRESGS 461
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-511 |
2.21e-50 |
|
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: 179.48 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 102 ERAAVFLRAADLLAgpwREKIAAATML----GQSKSVYQAEIDAVCeliDFWRFNVAFARQILEQQ---PISGPGEWNRI 174
Cdd:cd07146 41 QRSAILNKAAALLE---ARREEFARLItlesGLCLKDTRYEVGRAA---DVLRFAAAEALRDDGESfscDLTANGKARKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 175 --DYRPLdGFVYAITPFNF--TSIAGNLptAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07146 115 ftLREPL-GVVLAITPFNHplNQVAHKI--APAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07146 192 DELITHPDVDLVTFTGGVA--------VGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDdseGYFVRP 409
Cdd:cd07146 264 VKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGA-RVLLGNQRQ---GALYAP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLSDDPTDESFVIEYFGPLLSVHVYPDerYEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRFAAGNfyVNDKPt 489
Cdd:cd07146 340 TVLDHVPPDAELVTEETFGPVAPVIRVKD--LDEAIAISN-STAYGLSSGVCTNDLDTIKRLVERLDVGTVN--VNEVP- 413
|
410 420
....*....|....*....|..
gi 489997281 490 GAVVGRQPFGGARGSGTNDKAG 511
Cdd:cd07146 414 GFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
93-525 |
8.06e-50 |
|
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: 177.80 E-value: 8.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAALPFDERAAVFLRAADLLAGPwREKIAAATML--GQSKSVYQAEIDAVCELIDFWRFNvafARQILEQQPISG--- 167
Cdd:cd07099 32 RAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAetGKPRADAGLEVLLALEAIDWAARN---APRVLAPRKVPTgll 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 168 -PGEWNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDG 245
Cdd:cd07099 108 mPNKKATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 246 fAVSdVALADPRLAGIHFTGSTATfghlwqwvGTNIGRYHSyPRL---VGETGGKDFVVAHASARPDVLRTALIRGAFDY 322
Cdd:cd07099 187 -ATG-AALIDAGVDKVAFTGSVAT--------GRKVMAAAA-ERLipvVLELGGKDPMIVLADADLERAAAAAVWGAMVN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRafvkNVDAIER------AKGAaavTVAVG 396
Cdd:cd07099 256 AGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTAR----QLDIVRRhvddavAKGA---KALTG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 397 GEYDDSEGYFVRPTVLLsdDPTDESFVI--EYFGPLLSVHVYPDEryEQILDVIDtGSRYALTGAVIADDRQAVLTALDR 474
Cdd:cd07099 329 GARSNGGGPFYEPTVLT--DVPHDMDVMreETFGPVLPVMPVADE--DEAIALAN-DSRYGLSASVFSRDLARAEAIARR 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489997281 475 LRfaAGNFYVNDKPTGAVVGRQPFGGARGSGTNDKAGsPLNLLRWTSARSI 525
Cdd:cd07099 404 LE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHG-AEGLREFCRPKAI 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
94-521 |
2.14e-49 |
|
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: 176.33 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLL---AGPWREKIAAATMLGQSKSvyQAEIDAVcelIDFWRFNVAFARQILEQQPISGPGE 170
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLeehADEIADWIVRESGSIRPKA--GFEVGAA---IGELHEAAGLPTQPQGEILPSAPGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSI-TQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAV 248
Cdd:cd07152 103 LSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDPrTPVSGGVVIARLFEEAGLPAGVLHVLPGGA-DA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALADPRLAGIHFTGSTATfGHLwqwVGTNIGRYhsYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCS 328
Cdd:cd07152 181 GEALVEDPNVAMISFTGSTAV-GRK---VGEAAGRH--LKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAfVKNVDAIERAKGAAAVTVAVGGEYDdseGYFVR 408
Cdd:cd07152 255 AAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQ-LDRVHAIVDDSVAAGARLEAGGTYD---GLFYR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 409 PTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKP 488
Cdd:cd07152 331 PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE-EAV--ALANDTEYGLSAGIISRDVGRAMALADRLR--TGMLHINDQT 405
|
410 420 430
....*....|....*....|....*....|....*...
gi 489997281 489 TGAVVgRQPFGGARGSGTNDKAGSPLNL-----LRWTS 521
Cdd:cd07152 406 VNDEP-HNPFGGMGASGNGSRFGGPANWeeftqWQWVT 442
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
94-506 |
3.44e-49 |
|
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: 176.22 E-value: 3.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA---EIDAVCEliDFwRFNVAFARQILEQQPISGPGE 170
Cdd:cd07093 34 GWSRMSPAERARILHKVADLIEAR-ADELALLESLDTGKPITLArtrDIPRAAA--NF-RFFADYILQLDGESYPQDGGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07093 110 LNYVLRQPV-GVAGLITPWNLPLMLLTWKIAPALaFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSyprlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07093 189 AALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL------ELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGG----EYDDSEGY 405
Cdd:cd07093 263 GSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGA-TILTGGgrpeLPDLEGGY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 406 FVRPTVLLsdDPTDESFVI--EYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFY 483
Cdd:cd07093 342 FVEPTVIT--GLDNDSRVAqeEIFGPVVTVIPFDDE--EEAIE-LANDTPYGLAAYVWTRDLGRAHRVARRLE--AGTVW 414
|
410 420
....*....|....*....|....*...
gi 489997281 484 VN-----DKptgavvgRQPFGGARGSGT 506
Cdd:cd07093 415 VNcwlvrDL-------RTPFGGVKASGI 435
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
44-512 |
3.46e-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: 3.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 44 HVIGGRHRMGDGE-RIDVVQPHRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPwREKI 122
Cdd:cd07113 2 HFIDGRPVAGQSEkRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQH-GEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 123 AAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQ-----PISGPGEWNRIDYRPLDGFVYAITPFNFTSIAGN 197
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsiPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 198 LPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSDVALADPRLAGIHFTGSTATfghlwqw 276
Cdd:cd07113 161 WKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVAT------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 277 vGTNIGR--YHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAEL 354
Cdd:cd07113 233 -GKKIGRqaASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 355 RYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVH 434
Cdd:cd07113 312 QVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 435 VYPDEryEQILDVIDTgSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKP--TGAVvgrqPFGGARGSGTNDKAGS 512
Cdd:cd07113 391 PYEDE--EELIQLIND-TPFGLTASVWTNNLSKALRYIPRIE--AGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS 461
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
46-505 |
8.97e-49 |
|
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: 175.45 E-value: 8.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 46 IGGRHRMGDGERIDVVQPHRHAaRLGTLTN-ATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAgPWREKIAA 124
Cdd:cd07082 6 INGEWKESSGKTIEVYSPIDGE-VIGSVPAlSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLK-ENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 125 ATML--GQSKSVYQAEIDAVCELIDFwrfnVAFARQILEQQPIsgPGEWNR-------IDYR-PLdGFVYAITPFN---- 190
Cdd:cd07082 84 LLMWeiGKTLKDALKEVDRTIDYIRD----TIEELKRLDGDSL--PGDWFPgtkgkiaQVRRePL-GVVLAIGPFNypln 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 191 --FTSIAgnlptaPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGST 267
Cdd:cd07082 157 ltVSKLI------PALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 268 AtfghlwqwVGTNIGRYHSYPRLVGETGGKD--FVVAHAsarpDVLRTA--LIRGAFDYQGQKCSAVSRAFIAHSVWQRM 343
Cdd:cd07082 231 E--------VGNRLKKQHPMKRLVLELGGKDpaIVLPDA----DLELAAkeIVKGALSYSGQRCTAIKRVLVHESVADEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 344 GDELLAKAAELRYGDITDLSNYGGALIDQRA--FVKNV--DAIEraKGAaavTVAVGGEYDdsEGYFVRPTVLlsDDPTD 419
Cdd:cd07082 299 VELLKEEVAKLKVGMPWDNGVDITPLIDPKSadFVEGLidDAVA--KGA---TVLNGGGRE--GGNLIYPTLL--DPVTP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 420 ESFVI--EYFGPLLsvhvyPDERYEQILDVID--TGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDKPtgavvgr 495
Cdd:cd07082 370 DMRLAweEPFGPVL-----PIIRVNDIEEAIElaNKSNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------- 435
|
490
....*....|....*.
gi 489997281 496 Q------PFGGARGSG 505
Cdd:cd07082 436 QrgpdhfPFLGRKDSG 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
95-505 |
2.69e-48 |
|
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: 173.97 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAeIDAVCELIDFWRFNVAFA-RQILEQQPISGPGEWNR 173
Cdd:cd07097 53 WRRTSPEARADILDKAGDELEAR-KEELARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEAlRLSGETLPSTRPGVEVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKP-SITQTLAAYLTmQLLEAAGLPPGVINLVTGDGFAVSDV 251
Cdd:cd07097 131 TTREPL-GVVGLITPWNFPIAIPAWKIAPALAyGNTVVFKPaELTPASAWALV-EILEEAGLPAGVFNLVMGSGSEVGQA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSyprlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVS 331
Cdd:cd07097 209 LVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL------EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 332 RAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYD-DSEGYFVRPT 410
Cdd:cd07097 283 RLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKrPDEGYYLAPA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 411 VLLSDDPTDESFVIEYFGPLLSVHVYPDerYEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNdKPTG 490
Cdd:cd07097 363 LFAGVTNDMRIAREEIFGPVAAVIRVRD--YDEALAIAN-DTEFGLSAGIVTTSLKHATHFKRRVE--AGVVMVN-LPTA 436
|
410
....*....|....*
gi 489997281 491 AVVGRQPFGGARGSG 505
Cdd:cd07097 437 GVDYHVPFGGRKGSS 451
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
95-523 |
1.41e-47 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 178.24 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPWRekiaaaTMLG-----QSKSVYQAeIDAVCELIDFWRFNVAFARQileqqpisgpg 169
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQMQ------TLMGllvreAGKTFSNA-IAEVREAVDFLRYYAGQVRD----------- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 EWNRIDYRPLdGFVYAITPFNFT-SI-AGNLPTAPAlMGNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:PRK11809 760 DFDNDTHRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPA-EQTpLIAAQAVRILLEAGVPAGVVQLLPGRGE 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTATFGHLWQwvgtNI-GRYHSYPR---LVGETGGKDFVVAHASARPDVLRTALIRGAFDY 322
Cdd:PRK11809 837 TVGAALVADARVRGVMFTGSTEVARLLQR----NLaGRLDPQGRpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDS 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRA---FVKNVDAIeRAKGAAAVTVAVGGEY 399
Cdd:PRK11809 913 AGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAkanIERHIQAM-RAKGRPVFQAARENSE 991
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 400 DDSEGYFVRPTvLLSDDPTDEsFVIEYFGPLLSVHVYPDERYEQILDVIDtGSRYALTGAV---IaDDRQAVLTAldrlR 476
Cdd:PRK11809 992 DWQSGTFVPPT-LIELDSFDE-LKREVFGPVLHVVRYNRNQLDELIEQIN-ASGYGLTLGVhtrI-DETIAQVTG----S 1063
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489997281 477 FAAGNFYVNDKPTGAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSAR 523
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
94-505 |
1.87e-47 |
|
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: 171.46 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLagpwREK---IAAATMLGQSKSVYQA--EIDAVCELIDFwrfnvaFARQILEQQ----P 164
Cdd:cd07103 34 TWRKTTARERAAILRRWADLI----RERaedLARLLTLEQGKPLAEArgEVDYAASFLEW------FAEEARRIYgrtiP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 165 ISGPGEWNRIDYRPLdGFVYAITPFNFTSiagNLPT---APAL-MGNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVIN 239
Cdd:cd07103 104 SPAPGKRILVIKQPV-GVVAAITPWNFPA---AMITrkiAPALaAGCTVVLKPA-EETpLSALALAELAEEAGLPAGVLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 240 LVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGA 319
Cdd:cd07103 179 VVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNAPFIVFDDADLDKAVDGAIASK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 320 FDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERA--KGAaavTVAVGG 397
Cdd:cd07103 253 FRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAvaKGA---KVLTGG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 398 EYDDSEGYFVRPTVLLsdDPTDESFVI--EYFGPLLSVHVYPDERyeqilDVI----DTgsRYALTGAVIADDRQAVLTA 471
Cdd:cd07103 330 KRLGLGGYFYEPTVLT--DVTDDMLIMneETFGPVAPIIPFDTED-----EVIaranDT--PYGLAAYVFTRDLARAWRV 400
|
410 420 430
....*....|....*....|....*....|....*
gi 489997281 472 LDRLRFaaGNFYVND-KPTGAVVgrqPFGGARGSG 505
Cdd:cd07103 401 AEALEA--GMVGINTgLISDAEA---PFGGVKESG 430
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
54-485 |
2.96e-46 |
|
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: 168.60 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 54 DGERIDVVQPHRHAArLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKS 133
Cdd:cd07088 11 SGETIDVLNPATGEV-VATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIREN-ADELAKLIVEEQGKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 134 VYQA--EIDAVCeliDFWRFNVAFARQIL-EQQPISGPGEWNRIDYRPLdGFVYAITPFNFT--SIAGNLptAPALM-GN 207
Cdd:cd07088 89 LSLArvEVEFTA---DYIDYMAEWARRIEgEIIPSDRPNENIFIFKVPI-GVVAGILPWNFPffLIARKL--APALVtGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 208 TVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRyhsy 287
Cdd:cd07088 163 TIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 288 PRLvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGG 367
Cdd:cd07088 239 VSL--ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 368 ALIDQRAfVKNVDAI-ERAKGAAAvTVAVGGEYDDSE-GYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYP--DERYEQ 443
Cdd:cd07088 317 PLVNEAA-LDKVEEMvERAVEAGA-TLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSslDEAIEL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489997281 444 ILDvidtgSRYALTGAVIADDRQAVLTALDRLRFaaGNFYVN 485
Cdd:cd07088 395 AND-----SEYGLTSYIYTENLNTAMRATNELEF--GETYIN 429
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
92-506 |
5.64e-46 |
|
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: 167.53 E-value: 5.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPWREKIAAATM-----LGQSKsvyqAEIDAVCELIDFwrfnVAFARQILEQQPI- 165
Cdd:cd07145 34 KDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIevgkpIKQSR----VEVERTIRLFKL----AAEEAKVLRGETIp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 166 --SGPGEWNRIDY---RPLdGFVYAITPFNF--TSIAGNLptAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGV 237
Cdd:cd07145 106 vdAYEYNERRIAFtvrEPI-GVVGAITPFNFpaNLFAHKI--APAIaVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 238 INLVTGDGFAVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRY--HSYPRLVGETGGKDFVVAHASARPDVLRTAL 315
Cdd:cd07145 183 INVVTGYGSEVGDEIVTNPKVNMISFTGSTA--------VGLLIASKagGTGKKVALELGGSDPMIVLKDADLERAVSIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 316 IRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAfVKNV-DAIERAKGAAAVtVA 394
Cdd:cd07145 255 VRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA-VERMeNLVNDAVEKGGK-IL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 395 VGGEYDdsEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTgSRYALTGAVIADDRQAVLTALDR 474
Cdd:cd07145 333 YGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTNDINRALKVARE 407
|
410 420 430
....*....|....*....|....*....|..
gi 489997281 475 LRFaaGNFYVNDKPTgAVVGRQPFGGARGSGT 506
Cdd:cd07145 408 LEA--GGVVINDSTR-FRWDNLPFGGFKKSGI 436
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
95-525 |
4.19e-45 |
|
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: 164.92 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGpWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIL-EQQPISGPGewnr 173
Cdd:cd07115 35 WSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAADTFRYYAGWADKIEgEVIPVRGPF---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDY--RPLDGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD 250
Cdd:cd07115 110 LNYtvREPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAV 330
Cdd:cd07115 190 ALVEHPDVDKITFTGSTAVGRKIMQGAAGNL------KRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 331 SRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAvGGEYDDSEGYFVRPT 410
Cdd:cd07115 264 SRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLT-GGKRPGARGFFVEPT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 411 VLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNdkPTG 490
Cdd:cd07115 343 IFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALR-IANGTEYGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYN 415
|
410 420 430
....*....|....*....|....*....|....*
gi 489997281 491 AVVGRQPFGGARGSGTNDKAGSPLnLLRWTSARSI 525
Cdd:cd07115 416 RFDPGSPFGGYKQSGFGREMGREA-LDEYTEVKSV 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
95-505 |
4.38e-44 |
|
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: 162.34 E-value: 4.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAG---------------PWREkiaaatMLGQSKSVyqaeidavcelIDFWRFNVAFARQI 159
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEAnaeelaeletrdngkLIRE------TRAQVRYL-----------AEWYRYYAGLADKI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 160 LEQ-QPISGPGEWNRIDYRPLdGFVYAITPFN--FTSIAGNLptAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPP 235
Cdd:cd07114 100 EGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspLLLLAKKL--APALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 236 GVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYhsyprlVGETGGKDFVVAHASARPDVLRTAL 315
Cdd:cd07114 177 GVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV------TLELGGKSPNIVFDDADLDAAVNGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 316 IRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAV 395
Cdd:cd07114 251 VAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGA-RVLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 396 GGE----YDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAV-IADDRQAVLT 470
Cdd:cd07114 330 GGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIA-LANDSEYGLAAGIwTRDLARAHRV 406
|
410 420 430
....*....|....*....|....*....|....*.
gi 489997281 471 AlDRLRfaAGNFYVND-KPTGAVVgrqPFGGARGSG 505
Cdd:cd07114 407 A-RAIE--AGTVWVNTyRALSPSS---PFGGFKDSG 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
95-505 |
5.69e-44 |
|
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: 161.54 E-value: 5.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRfnvAFARQILEQQPIS-GPGEWNR 173
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEAN-AEELARLLTLEQGKPLAEAQFE-VGGAVAWLR---YTASLDLPDEVIEdDDTRRVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAaylTMQLLEAAG--LPPGVINLVTGDGfAVSD 250
Cdd:cd07106 110 LRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLC---TLKLGELAQevLPPGVLNVVSGGD-ELGP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAV 330
Cdd:cd07106 185 ALTSHPDIRKISFTGSTATGKKVMASAAKTL------KRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 331 SRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPT 410
Cdd:cd07106 259 KRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGA-KVLAGGEPLDGPGYFIPPT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 411 VLlsDDPTDESFVI--EYFGPLLSVHVYPDERyeqilDVID--TGSRYALTGAVIADDR-QAVLTAldrLRFAAGNFYVN 485
Cdd:cd07106 338 IV--DDPPEGSRIVdeEQFGPVLPVLKYSDED-----EVIAraNDSEYGLGASVWSSDLeRAEAVA---RRLEAGTVWIN 407
|
410 420
....*....|....*....|
gi 489997281 486 DKptGAVVGRQPFGGARGSG 505
Cdd:cd07106 408 TH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
94-505 |
1.86e-43 |
|
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: 160.46 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGPGEWNR 173
Cdd:cd07112 41 VWSRLSPAERKAVLLRLADLIEAH-RDELALLETLDMGKPISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDvA 252
Cdd:cd07112 120 ITREPL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGE-A 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 253 LA-DPRLAGIHFTGSTATFGHLWQWVG-TNIgryhsyPRLVGETGGKD-FVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07112 198 LGlHMDVDALAFTGSTEVGRRFLEYSGqSNL------KRVWLECGGKSpNIVFADAPDLDAAAEAAAAGIFWNQGEVCSA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGE--YDDSEGYFV 407
Cdd:cd07112 272 GSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGA-RLVAGGKrvLTETGGFFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 408 RPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDk 487
Cdd:cd07112 351 EPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE-EAV--ALANDSVYGLAASVWTSDLSRAHRVARRLR--AGTVWVNC- 424
|
410
....*....|....*...
gi 489997281 488 pTGAVVGRQPFGGARGSG 505
Cdd:cd07112 425 -FDEGDITTPFGGFKQSG 441
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
95-505 |
2.39e-43 |
|
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: 160.20 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA--EIDAVcelIDFWRFNVAFARQIL-EQQPISGPGEW 171
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEGA---ADLWRYAASLARTLHgDSYNNLGDDML 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNFTS--IAGNLPTAPAlMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07118 113 GLVLREPI-GVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRY--HSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKC 327
Cdd:cd07118 191 QAMTEHPDVDMVSFTGSTR--------VGKAIAAAaaRNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDS-EGYF 406
Cdd:cd07118 263 NSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGA-TLLLGGERLASaAGLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 407 VRPTVLLSDDPTDESFVIEYFGPLLSVHVYpDERYEQILDVIDTGsrYALTGAVIADDRQAVLTALDRLRfaAGNFYVND 486
Cdd:cd07118 342 YQPTIFTDVTPDMAIAREEIFGPVLSVLTF-DTVDEAIALANDTV--YGLSAGVWSKDIDTALTVARRIR--AGTVWVNT 416
|
410
....*....|....*....
gi 489997281 487 KPTGAVvgRQPFGGARGSG 505
Cdd:cd07118 417 FLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
93-505 |
4.22e-43 |
|
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: 158.97 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAALPFDERAAVFLRAADLLaGPWREKIAAATMLGQSKSVY--QAEIDAVCELIDFwrfNVAFARQILEQQPISGPGE 170
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELL-KANKEELARLISRETGKPLWeaQTEVAAMAGKIDI---SIKAYHERTGERATPMAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFtsiAGNLPTA---PALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGf 246
Cdd:cd07095 90 RAVLRHRPH-GVMAVFGPFNF---PGHLPNGhivPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGR- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTATFGHLWQWVGtniGRYHSYprLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07095 165 ETGEALAAHEGIDGLLFTGSAATGLLLHRQFA---GRPGKI--LALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWqrmGDELL----AKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVaVGGEYDDS 402
Cdd:cd07095 240 CTCARRLIVPDGAV---GDAFLerlvEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL-LAMERLVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 403 EGYFVRPTVLL---SDDPTDEsfviEYFGPLLSVHVYPDerYEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRfaA 479
Cdd:cd07095 316 GTAFLSPGIIDvtdAADVPDE----EIFGPLLQVYRYDD--FDEAIA-LANATRFGLSAGLLSDDEALFERFLARIR--A 386
|
410 420
....*....|....*....|....*.
gi 489997281 480 GNFYVNDKPTGAvVGRQPFGGARGSG 505
Cdd:cd07095 387 GIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
94-505 |
4.37e-43 |
|
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: 159.45 E-value: 4.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAgPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFnvaFARQILEQQPISGPGEWNR 173
Cdd:cd07108 34 EWAATPARERGKLLARIADALE-ARSEELARLLALETGNALRTQARPEAAVLADLFRY---FGGLAGELKGETLPFGPDV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDY---RPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLeAAGLPPGVINLVTGDGfAVS 249
Cdd:cd07108 110 LTYtvrEPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDAPLAVLLLAEIL-AQVLPAGVLNVITGYG-EEC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALAD-PRLAGIHFTGSTATFGHLWQWVGtnigryhsyPRLVG---ETGGKDFVVAHASARPD-VLRTALIRGAFDYQG 324
Cdd:cd07108 187 GAALVDhPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvslELGGKSPMIVFPDADLDdAVDGAIAGMRFTRQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 325 QKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGG----EYD 400
Cdd:cd07108 258 QSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTSGATVLRGGplpgEGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 401 DSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyeqilDVIDTG--SRYALTGAVIADDRQAVLTALDRLRfa 478
Cdd:cd07108 338 LADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDED-----EVIAMAndSHYGLAAYVWTRDLGRALRAAHALE-- 410
|
410 420
....*....|....*....|....*..
gi 489997281 479 AGNFYVNDkpTGAVVGRQPFGGARGSG 505
Cdd:cd07108 411 AGWVQVNQ--GGGQQPGQSYGGFKQSG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
95-505 |
5.78e-43 |
|
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: 159.14 E-value: 5.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLaGPWREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQIL-------EQQPISG 167
Cdd:cd07094 37 RRALPPHERMAILERAADLL-KKRAEEFAKIIACEGGKPIKDARVE-VDRAIDTLRLAAEEAERIRgeeipldATQGSDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 168 PGEWNRIDyrPLdGFVYAITPFNFTSiagNLPT---APAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTG 243
Cdd:cd07094 115 RLAWTIRE--PV-GVVLAITPFNFPL---NLVAhklAPAIaTGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 244 DGFAVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQ 323
Cdd:cd07094 189 EREVLGDAFAADERVAMLSFTGSAA--------VGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 324 GQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERA--KGAAAVTvavGGEYDD 401
Cdd:cd07094 261 GQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAveAGARLLC---GGERDG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 402 SegyFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRFAAGN 481
Cdd:cd07094 338 A---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDF--EEAIR-IANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVM 411
|
410 420
....*....|....*....|....
gi 489997281 482 fyVNDKPTgAVVGRQPFGGARGSG 505
Cdd:cd07094 412 --VNDSSA-FRTDWMPFGGVKESG 432
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
94-506 |
9.03e-43 |
|
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: 158.69 E-value: 9.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLagpwREKiaaATMLGQSKSV-----YQAEIDAVCELIDFWRFNVAFARQILEQQPISGP 168
Cdd:cd07107 34 EWRATTPLERARMLRELATRL----REH---AEELALIDALdcgnpVSAMLGDVMVAAALLDYFAGLVTELKGETIPVGG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEWNRIDYRPLdGFVYAITPFN--FTSIAGNLpTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVTGDGF 246
Cdd:cd07107 107 RNLHYTLREPY-GVVARIVAFNhpLMFAAAKI-AAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGA-FDYQGQ 325
Cdd:cd07107 184 TAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI------KHVTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 326 KCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDD---S 402
Cdd:cd07107 258 SCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGpalE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 403 EGYFVRPTVLlsDDPTDESFVI--EYFGPLLSVHVYPDEryEQILDVIDtGSRYALTGAVIADD-RQAVLTAlDRLRfaA 479
Cdd:cd07107 338 GGFYVEPTVF--ADVTPGMRIAreEIFGPVLSVLRWRDE--AEMVAQAN-GVEYGLTAAIWTNDiSQAHRTA-RRVE--A 409
|
410 420 430
....*....|....*....|....*....|.
gi 489997281 480 GNFYVNDkptgavVGRQ----PFGGARGSGT 506
Cdd:cd07107 410 GYVWING------SSRHflgaPFGGVKNSGI 434
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
92-505 |
2.10e-42 |
|
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: 157.85 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPwREKI--AAATMLGQSKSVYQAEIDAVCELID-FWRFNVAFARQILeqqPISGP 168
Cdd:cd07151 45 QKEWAATLPQERAEILEKAAQILEER-RDEIveWLIRESGSTRIKANIEWGAAMAITReAATFPLRMEGRIL---PSDVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEWNRIdYRPLDGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSI-TQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:cd07151 121 GKENRV-YREPLGVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPASdTPITGGLLLAKIFEEAGLPKGVLNVVVGAGS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSD--VALADPRLagIHFTGSTAtfghlwqwVGTNIGRYHSYP--RLVGETGGKDFVVAHASARPDVLRTALIRGAFDY 322
Cdd:cd07151 200 EIGDafVEHPVPRL--ISFTGSTP--------VGRHIGELAGRHlkKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGeydDS 402
Cdd:cd07151 270 QGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGA-TLLVGG---EA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 403 EGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDrqavltaLDR-LRFA--- 478
Cdd:cd07151 346 EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALE-LANDTEYGLSGAVFTSD-------LERgVQFArri 415
|
410 420 430
....*....|....*....|....*....|.
gi 489997281 479 -AGNFYVNDKPtgavVGRQP---FGGARGSG 505
Cdd:cd07151 416 dAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
92-505 |
4.94e-42 |
|
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: 157.09 E-value: 4.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQILEQQPISGPGEW 171
Cdd:cd07119 50 SGEWPHLPAQERAALLFRIADKIRED-AEELARLETLNTGKTLRESEID-IDDVANCFRYYAGLATKETGEVYDVPPHVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD 250
Cdd:cd07119 128 SRTVREPV-GVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAV 330
Cdd:cd07119 207 ELAESPDVDLVSFTGGTATGRSIMRAAAGNV------KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 331 SRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALI--DQRAFVKNVDAIERAKGAaavTVAVGGE-YDDSE---G 404
Cdd:cd07119 281 SRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVsaEHREKVLSYIQLGKEEGA---RLVCGGKrPTGDElakG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 405 YFVRPTVLlsdDPTDESFVI---EYFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADDRQAVLTALDRLRfaAGN 481
Cdd:cd07119 358 YFVEPTIF---DDVDRTMRIvqeEIFGPVLTVERFDTEE-EAIRLANDT--PYGLAGAVWTKDIARANRVARRLR--AGT 429
|
410 420
....*....|....*....|....*
gi 489997281 482 FYVND-KPTGAvvgRQPFGGARGSG 505
Cdd:cd07119 430 VWINDyHPYFA---EAPWGGYKQSG 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
95-505 |
1.53e-40 |
|
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: 152.73 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQ--ILEQQPISGPGEwN 172
Cdd:cd07139 54 WPRLSPAERAAVLRRLADALEAR-ADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpFEERRPGSGGGH-V 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSDV 251
Cdd:cd07139 132 LVRREPV-GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYhsyprlVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVS 331
Cdd:cd07139 210 LVRHPGVDKVSFTGSTAAGRRIAAVCGERLARV------TLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 332 RAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEY--DDSEGYFVRP 409
Cdd:cd07139 284 RILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGA-RLVTGGGRpaGLDRGWFVEP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNdkpt 489
Cdd:cd07139 363 TLFADVDNDMRIAQEEIFGPVLSVIPYDDED-DAV--RIANDSDYGLSGSVWTADVERGLAVARRIR--TGTVGVN---- 433
|
410
....*....|....*..
gi 489997281 490 GAVVGRQ-PFGGARGSG 505
Cdd:cd07139 434 GFRLDFGaPFGGFKQSG 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
93-505 |
2.86e-40 |
|
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: 151.63 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAaLPFDERAAVFLRAADLLAGPWrEKIAAATML--GQSKSVYQAEIDAVceLIDFWRF------NVAFARQILEQQP 164
Cdd:cd07089 35 GDWS-TDAEERARCLRQLHEALEARK-EELRALLVAevGAPVMTARAMQVDG--PIGHLRYfadladSFPWEFDLPVPAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 165 ISGPGEwNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTG 243
Cdd:cd07089 111 RGGPGR-RVVRREPV-GVVAAITPWNFPFFLNLAKLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 244 DGFAVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRYHS--YPRLVGETGGKDFVVAHASARPDVLRTALIRGAFD 321
Cdd:cd07089 189 SDNAVGEALTTDPRVDMVSFTGSTA--------VGRRIMAQAAatLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 322 YQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALI--DQRAFVKNVDAIERAKGAaavTVAVGGEY 399
Cdd:cd07089 261 NAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLIsaAQRDRVEGYIARGRDEGA---RLVTGGGR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 400 DDS--EGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRf 477
Cdd:cd07089 338 PAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD-EAV--RIANDSDYGLSGGVWSADVDRAYRVARRIR- 413
|
410 420 430
....*....|....*....|....*....|
gi 489997281 478 aAGNFYVNdkptGAVVGR--QPFGGARGSG 505
Cdd:cd07089 414 -TGSVGIN----GGGGYGpdAPFGGYKQSG 438
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
94-505 |
8.96e-40 |
|
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: 149.53 E-value: 8.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLagpwRE------KIAAATM---LGQSKsvyqAEIDAVCELIDFWRFNvafARQILEQQP 164
Cdd:cd07100 14 AWRKTSFAERAALLRKLADLL----RErkdelaRLITLEMgkpIAEAR----AEVEKCAWICRYYAEN---AEAFLADEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 165 ISGPGEWNRIDYRPLdGFVYAITPFNFtsiagnlP-------TAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPG 236
Cdd:cd07100 83 IETDAGKAYVRYEPL-GVVLGIMPWNF-------PfwqvfrfAAPNLMaGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 237 V-INL-VTGDgfAVSDVaLADPRLAGIHFTGSTATfGhlwQWVGTNIGRYhsYPRLVGETGGKD-FVVAhASARPDVLRT 313
Cdd:cd07100 155 VfQNLlIDSD--QVEAI-IADPRVRGVTLTGSERA-G---RAVAAEAGKN--LKKSVLELGGSDpFIVL-DDADLDKAVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 314 ALIRGAFDYQGQKCSAVSRaFIAH-SVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvT 392
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKR-FIVHeDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGA-T 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 393 VAVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTgSRYALTGAVIADDRQAVLTAL 472
Cdd:cd07100 303 LLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALAND-SPFGLGGSVFTTDLERAERVA 379
|
410 420 430
....*....|....*....|....*....|...
gi 489997281 473 DRLRfaAGNFYVNDkpTGAVVGRQPFGGARGSG 505
Cdd:cd07100 380 RRLE--AGMVFING--MVKSDPRLPFGGVKRSG 408
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
94-527 |
1.45e-38 |
|
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: 147.07 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAeIDAVCELIDFWRFNVAFARQILEQQPISG--PG-E 170
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLER-RDELLDLIQLETGKARRHA-FEEVLDVAIVARYYARRAERLLKPRRRRGaiPVlT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07101 111 RTTVNRRPK-GVVGVISPWNYPLTLAVSDAIPALLaGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DvALADpRLAGIHFTGSTATfghlwqwvGTNIGRyHSYPRLVG---ETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07101 190 G-AIVD-NADYVMFTGSTAT--------GRVVAE-RAGRRLIGcslELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAF---VKNVDAiERAKGAaavTVAVGGEYDDSE 403
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLdrvTAHVDD-AVAKGA---TVLAGGRARPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 G-YFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDErYEQILDVIDTgsRYALTGAVIADDRQAVLTALDRLRfaAGNF 482
Cdd:cd07101 335 GpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD-DEAIELANDT--DYGLNASVWTRDGARGRRIAARLR--AGTV 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489997281 483 YVND--KPTGAVVGrQPFGGARGSGTNDKAGsPLNLLRWTSARSIKE 527
Cdd:cd07101 410 NVNEgyAAAWASID-APMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
95-485 |
1.99e-38 |
|
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: 146.62 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAA--ATMLGQSKSVYQAEIDAVCELIDFWrfnVAFARQILEQQPISGPGEWN 172
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAAN-TDEIAEelTWQMGRPIAQAGGEIRGMLERARYM---ISIAEEALADIRVPEKDGFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 R-IDYRPLdGFVYAITPFN---FTSIAGnlpTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfA 247
Cdd:cd07102 110 RyIRREPL-GVVLIIAPWNypyLTAVNA---VIPALLaGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSH-E 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 248 VSDVALADPRLAGIHFTGSTATfghlwqwvGTNIGRYHSyPRLVG---ETGGKDfvvaHASARPDV-LRTA---LIRGAF 320
Cdd:cd07102 185 TSAALIADPRIDHVSFTGSVAG--------GRAIQRAAA-GRFIKvglELGGKD----PAYVRPDAdLDAAaesLVDGAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 321 DYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRA--FVKNVDAIERAKGAAAVTVAVGGE 398
Cdd:cd07102 252 FNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAadFVRAQIADAIAKGARALIDGALFP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 399 YDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVH-VYPDEryEQILDVIDtgSRYALTGAVIADDRQAVLTALDRLrf 477
Cdd:cd07102 332 EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMkVKSDA--EAIALMND--SEYGLTASVWTKDIARAEALGEQL-- 405
|
....*...
gi 489997281 478 AAGNFYVN 485
Cdd:cd07102 406 ETGTVFMN 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
94-525 |
4.43e-38 |
|
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: 145.55 E-value: 4.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIleQQPISG---PGE 170
Cdd:cd07092 34 SWRRTTPAERSKALLKLADAIEEN-AEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTL--EGPAAGeylPGH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLeAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07092 111 TSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAELA-AEVLPPGVVNVVCGGGASAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSyprlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07092 189 DALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL------ELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAavTVAVGGEYDDSEGYFVRP 409
Cdd:cd07092 263 ACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHA--RVLTGGRRAEGPGYFYEP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDRLRFaaGNFYVNDKpt 489
Cdd:cd07092 341 TVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIE-LANDVEYGLASSVWTRDVGRAMRLSARLDF--GTVWVNTH-- 413
|
410 420 430
....*....|....*....|....*....|....*.
gi 489997281 490 GAVVGRQPFGGARGSGTNdKAGSPLNLLRWTSARSI 525
Cdd:cd07092 414 IPLAAEMPHGGFKQSGYG-KDLSIYALEDYTRIKHV 448
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
95-505 |
3.22e-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: 143.64 E-value: 3.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQ---AEIDAVcelIDFWRFnvaFARQILEQQpisgpGEW 171
Cdd:cd07559 54 WGKTSVAERANILNKIADRIEEN-LELLAVAETLDNGKPIREtlaADIPLA---IDHFRY---FAGVIRAQE-----GSL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRID--------YRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVT 242
Cdd:cd07559 122 SEIDedtlsyhfHEPL-GVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 243 GDGFAVSDVALADPRLAGIHFTGSTATfghlwqwvGTNIGRYHSyPRLVG---ETGGK--DFVVAHASARPDVLRTALIR 317
Cdd:cd07559 200 GFGSEAGKPLASHPRIAKLAFTGSTTV--------GRLIMQYAA-ENLIPvtlELGGKspNIFFDDAMDADDDFDDKAEE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 318 G----AFDyQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTV 393
Cdd:cd07559 271 GqlgfAFN-QGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGA-EV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 394 AVGGEY----DDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDrqaVL 469
Cdd:cd07559 349 LTGGERltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE--EEAIA-IANDTEYGLGGGVWTRD---IN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489997281 470 TAldrLRFA----AGNFYVN---DKPTGAvvgrqPFGGARGSG 505
Cdd:cd07559 423 RA---LRVArgiqTGRVWVNcyhQYPAHA-----PFGGYKKSG 457
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
93-505 |
3.53e-37 |
|
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: 143.26 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAALPFDERAAvFLRA-ADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQILEQQPISGPGEW 171
Cdd:cd07110 33 PRWKKTTGAERAK-YLRAiAEGVRER-REELAELEARDNGKPLDEAAWD-VDDVAGCFEYYADLAEQLDAKAERAVPLPS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYR----PLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:cd07110 110 EDFKARvrrePV-GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07110 189 EAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI------KPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDD--SEG 404
Cdd:cd07110 263 CSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGA-RLLCGGRRPAhlEKG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 405 YFVRPTVlLSDDPTD-ESFVIEYFGPLLSVHVYPDERyEQILDVIDtgSRYALTGAVIADDRQAVLTALDRLRfaAGNFY 483
Cdd:cd07110 342 YFIAPTV-FADVPTDsRIWREEIFGPVLCVRSFATED-EAIALAND--SEYGLAAAVISRDAERCDRVAEALE--AGIVW 415
|
410 420
....*....|....*....|..
gi 489997281 484 VNdkPTGAVVGRQPFGGARGSG 505
Cdd:cd07110 416 IN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
94-505 |
1.00e-36 |
|
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: 141.18 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGpWREKIAAATMlgqsksvyqAEIDAVceliDFW-RFNVAFARQIL------------ 160
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLES-RRDEFIEAMM---------EETGAT----AAWaGFNVDLAAGMLreaaslitqiig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 161 EQQPISGPGEWNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVIN 239
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPV-GVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 240 LVT---GDGFAVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGR---YHSYPRLVgETGGKDFVVAHASARPDVLRT 313
Cdd:cd07105 160 VVThspEDAPEVVEALIAHPAVRKVNFTGSTR--------VGRIIAEtaaKHLKPVLL-ELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 314 ALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDitdlsNYGGALIDQRAFVKNVDAIERAKGAAAVTV 393
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 394 AVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTgSRYALTGAVIADD-RQAVLTAl 472
Cdd:cd07105 306 VGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIAND-SEYGLSAAVFTRDlARALAVA- 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 489997281 473 DRLRFAA---GNFYVNDKPTGavvgrqPFGGARGSG 505
Cdd:cd07105 382 KRIESGAvhiNGMTVHDEPTL------PHGGVKSSG 411
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
94-525 |
2.90e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 141.55 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAeIDAVCELIDFWRFNVAFARQILEQQPISG--PG-E 170
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDLVLEN-REELLDLVQLETGKARRHA-FEEVLDVALTARYYARRAPKLLAPRRRAGalPVlT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNF---TSIAGNLPtapALM-GNTVIWKPSiTQT-LAAYLTMQLLEAAGLPPGVINLVTGDG 245
Cdd:PRK09407 147 KTTELRQPK-GVVGVISPWNYpltLAVSDAIP---ALLaGNAVVLKPD-SQTpLTALAAVELLYEAGLPRDLWQVVTGPG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 246 FAVSD--VALADprlaGIHFTGSTATfGhlwQWVGTNIGRyhsypRLVG---ETGGKDFVVAHASARPDVLRTALIRGAF 320
Cdd:PRK09407 222 PVVGTalVDNAD----YLMFTGSTAT-G---RVLAEQAGR-----RLIGfslELGGKNPMIVLDDADLDKAAAGAVRACF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 321 DYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQR------AFVKnvDAieRAKGAaavTVA 394
Cdd:PRK09407 289 SNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAqletvsAHVD--DA--VAKGA---TVL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 395 VGGEYDDSEG-YFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDErYEQILDVIDTgsRYALTGAVIADDRQAVLTALD 473
Cdd:PRK09407 362 AGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV-DEAVERANDT--PYGLNASVWTGDTARGRAIAA 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489997281 474 RLRfaAGNFYVND--KPTGAVVGrQPFGGARGSGTNDKAGsPLNLLRWTSARSI 525
Cdd:PRK09407 439 RIR--AGTVNVNEgyAAAWGSVD-APMGGMKDSGLGRRHG-AEGLLKYTESQTI 488
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
92-505 |
1.37e-35 |
|
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: 138.52 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVcELIDFWRFNVAFARQILEQQPISGPGEW 171
Cdd:cd07109 33 ESGWLRLSPAERGRLLLRIARLIREH-ADELARLESLDTGKPLTQARADVE-AAARYFEYYGGAADKLHGETIPLGPGYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNF-TSIAGNlPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVS 249
Cdd:cd07109 111 VYTVREPH-GVTGHIIPWNYpLQITGR-SVAPALaAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DVALADPRLAGIHFTGSTATfghlwqwvGTNIGRY---HSYPrLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07109 189 AALVAHPGVDHISFTGSVET--------GIAVMRAaaeNVVP-VTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYG---DITDLsnygGALID--QRAFVKNVDAIERAKGAAAVTVAVGGEYDD 401
Cdd:cd07109 260 CSAGSRLLVHRSIYDEVLERLVERFRALRVGpglEDPDL----GPLISakQLDRVEGFVARARARGARIVAGGRIAEGAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 402 SEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGN 481
Cdd:cd07109 336 AGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEA-EAI--ALANGTDYGLVAGVWTRDGDRALRVARRLR--AGQ 410
|
410 420
....*....|....*....|....
gi 489997281 482 FYVNDKPTGAVVGRqPFGGARGSG 505
Cdd:cd07109 411 VFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
102-512 |
1.51e-35 |
|
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: 138.82 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 102 ERAAVFLRAADLLAGPWrEKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGPGEWNRIDYRPLdG 181
Cdd:cd07143 69 KRGRCLSKLADLMERNL-DYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPI-G 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 182 FVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAG 260
Cdd:cd07143 147 VCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 261 IHFTGSTAtfghlwqwVGTNIGRYHSYPRLVG---ETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAH 337
Cdd:cd07143 227 VAFTGSTL--------VGRKVMEAAAKSNLKKvtlELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 338 SVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPTVlLSDDP 417
Cdd:cd07143 299 GIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTI-FTDVT 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 418 TDESFVI-EYFGPLLSVHVYPDERyeqilDVIDTG--SRYALTGAVIADD-RQAVLTAldrLRFAAGNFYVNDKPTgaVV 493
Cdd:cd07143 377 EDMKIVKeEIFGPVVAVIKFKTEE-----EAIKRAndSTYGLAAAVFTNNiNNAIRVA---NALKAGTVWVNCYNL--LH 446
|
410
....*....|....*....
gi 489997281 494 GRQPFGGARGSGTNDKAGS 512
Cdd:cd07143 447 HQVPFGGYKQSGIGRELGE 465
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
95-505 |
2.45e-35 |
|
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: 138.02 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFnvafARQILEQQPISGPGEWNRI 174
Cdd:cd07138 52 WSATSVEERAALLERIAEAYEAR-ADELAQAITLEMGAPITLARAAQVGLGIGHLRA----AADALKDFEFEERRGNSLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 175 DYRPLdGFVYAITPFNFT--SIAGNLptAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDV 251
Cdd:cd07138 127 VREPI-GVCGLITPWNWPlnQIVLKV--APALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 ALADPRLAGIHFTGSTAtfghlwqwVGTNIGRY--HSYPRLVGETGGKdfvvahaSAR---PDV-LRTAL---IRGAFDY 322
Cdd:cd07138 204 LSAHPDVDMVSFTGSTR--------AGKRVAEAaaDTVKRVALELGGK-------SANiilDDAdLEKAVprgVAACFAN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERA--KGAaavTVAVGGEY- 399
Cdd:cd07138 269 SGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGieEGA---RLVAGGPGr 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 400 --DDSEGYFVRPTVLLSDDPTDEsfvI---EYFGPLLSVHVYPDEryEQILDvIDTGSRYALTGAVIADDRQAVLTALDR 474
Cdd:cd07138 346 peGLERGYFVKPTVFADVTPDMT---IareEIFGPVLSIIPYDDE--DEAIA-IANDTPYGLAGYVWSADPERARAVARR 419
|
410 420 430
....*....|....*....|....*....|.
gi 489997281 475 LRfaAGNFYVNDKPTGAvvgRQPFGGARGSG 505
Cdd:cd07138 420 LR--AGQVHINGAAFNP---GAPFGGYKQSG 445
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
46-505 |
3.12e-35 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 137.73 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 46 IGGRHRMGDGERIDVVQPhRHAARLGTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAVFLRAADLLAGPwREKIAAA 125
Cdd:PRK13473 7 INGELVAGEGEKQPVYNP-ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEEN-ADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 126 TMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIleQQPISG---PGEWNRIDYRPLdGFVYAITPFNFTSIAGNLPTAP 202
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCL--EGKAAGeylEGHTSMIRRDPV-GVVASIAPWNYPLMMAAWKLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 203 ALM-GNTVIWKPSITQTLAAyLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNI 281
Cdd:PRK13473 162 ALAaGNTVVLKPSEITPLTA-LKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 282 GRYHSyprlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITD 361
Cdd:PRK13473 241 KRTHL------ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 362 LSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEry 441
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE-- 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489997281 442 EQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRFaaGNFYVNDKptGAVVGRQPFGGARGSG 505
Cdd:PRK13473 393 DQAVRWAN-DSDYGLASSVWTRDVGRAHRVSARLQY--GCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
95-505 |
3.81e-35 |
|
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: 137.44 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLagpwREK---IAAATMLGQSKSVYQA--EIDAVCELIDFWrfnvAFARQILEQQPISGPG 169
Cdd:cd07090 35 WSATSGMERGRILRKAADLL----RERndeIARLETIDNGKPIEEArvDIDSSADCLEYY----AGLAPTLSGEHVPLPG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 EwnRIDY---RPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDG 245
Cdd:cd07090 107 G--SFAYtrrEPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 246 fAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQ 325
Cdd:cd07090 184 -ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI------KHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 326 KCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSE-- 403
Cdd:cd07090 257 VCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGA-KVLCGGERVVPEdg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 ---GYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADDRQAVLTALDRLRfaAG 480
Cdd:cd07090 336 lenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE-EVIRRANDT--TYGLAAGVFTRDLQRAHRVIAQLQ--AG 410
|
410 420
....*....|....*....|....*...
gi 489997281 481 NFYVN---DKPTGAvvgrqPFGGARGSG 505
Cdd:cd07090 411 TCWINtynISPVEV-----PFGGYKQSG 433
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
95-505 |
3.91e-35 |
|
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: 137.73 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQ-AEIDaVCELIDFWRFNVAFARQILEQQPISGPGEWNR 173
Cdd:cd07091 59 WRKMDPRERGRLLNKLADLIERD-RDELAALESLDNGKPLEEsAKGD-VALSIKCLRYYAGWADKIQGKTIPIDGNFLAY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDYRPLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSDVA 252
Cdd:cd07091 137 TRREPI-GVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFG-PTAGAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 253 LAD-PRLAGIHFTGSTATfGHLWQWVG--TNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07091 215 ISShMDVDKIAFTGSTAV-GRTIMEAAakSNL------KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRP 409
Cdd:cd07091 288 GSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGA-TLLTGGERHGSKGYFIQP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 410 TVLLsdDPTDESFVI--EYFGPLLSVhvypdERYEQILDVIDTG--SRYALTGAVIADDRQAVLTALDRLRfaAGNFYVN 485
Cdd:cd07091 367 TVFT--DVKDDMKIAkeEIFGPVVTI-----LKFKTEDEVIERAndTEYGLAAGVFTKDINKALRVSRALK--AGTVWVN 437
|
410 420
....*....|....*....|.
gi 489997281 486 dkpTGAVVGRQ-PFGGARGSG 505
Cdd:cd07091 438 ---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
96-505 |
4.79e-35 |
|
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: 136.99 E-value: 4.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 96 AALPFDERAAVFLRAADLLAgPWREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFARQIL-EQQPI----SGPGE 170
Cdd:cd07147 38 RALPAHRRAAILLHCVARLE-ERFEELAETIVLEAGKPIKDARGE-VARAIDTFRIAAEEATRIYgEVLPLdisaRGEGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSiagNL---PTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTgdgf 246
Cdd:cd07147 116 QGLVRRFPI-GPVSAITPFNFPL---NLvahKVAPAIaAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLP---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALA---DPRLAGIHFTGSTAtfghlwqwVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQ 323
Cdd:cd07147 188 CSRDDADLlvtDERIKLLSFTGSPA--------VGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 324 GQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDdse 403
Cdd:cd07147 260 GQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGA-KLLTGGKRD--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 GYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYpdERYEQILDVIDTgSRYALTGAVIADDRQAVLTALDRLRfaAGNFY 483
Cdd:cd07147 336 GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAVND-SKFGLQAGVFTRDLEKALRAWDELE--VGGVV 410
|
410 420
....*....|....*....|..
gi 489997281 484 VNDKPTGAvVGRQPFGGARGSG 505
Cdd:cd07147 411 INDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
93-505 |
1.17e-34 |
|
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: 135.93 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 93 SDWAALPfDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA--EIDAVcelIDFWRFNVAFARQILEQQPISGPGE 170
Cdd:cd07120 35 TDWAHDP-RLRARVLLELADAFEAN-AERLARLLALENGKILGEArfEISGA---ISELRYYAGLARTEAGRMIEPEPGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKP-SITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAV 248
Cdd:cd07120 110 FSLVLREPM-GVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINAAIIRILAEIPSLPAGVVNLFTESGSEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALADPRLAGIHFTGSTATfghlwqwvGTNIGR--YHSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07120 189 AAHLVASPDVDVISFTGSTAT--------GRAIMAaaAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDqRAFVKNVD-AIERAKGAAAVTVAVGGEYDD--SE 403
Cdd:cd07120 261 CMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLID-RANVDRVDrMVERAIAAGAEVVLRGGPVTEglAK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 GYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERyEQIldVIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFY 483
Cdd:cd07120 340 GAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA-EAV--ALANDTDYGLAASVWTRDLARAMRVARAIR--AGTVW 414
|
410 420
....*....|....*....|..
gi 489997281 484 VNDKptGAVVGRQPFGGARGSG 505
Cdd:cd07120 415 INDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-511 |
1.79e-34 |
|
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: 135.70 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIL-EQQPISGPGEWNR 173
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKH-ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHgMTLPADGPHHVYT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IdYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSDVA 252
Cdd:cd07142 138 L-HEPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFG-PTAGAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 253 LADPRLAG-IHFTGSTAtfghlwqwVGTNIGRYHSYPRLVG---ETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCS 328
Cdd:cd07142 215 IASHMDVDkVAFTGSTE--------VGKIIMQLAAKSNLKPvtlELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCC 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVR 408
Cdd:cd07142 287 AGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGA-TLITGGDRIGSKGYYIQ 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 409 PTVLlsDDPTDESFVI--EYFGPLLSVhvypdERYEQILDVID--TGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYV 484
Cdd:cd07142 366 PTIF--SDVKDDMKIArdEIFGPVQSI-----LKFKTVDEVIKraNNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWV 436
|
410 420
....*....|....*....|....*....
gi 489997281 485 N--DKPTGAVvgrqPFGGARGSGTNDKAG 511
Cdd:cd07142 437 NcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
94-505 |
3.35e-33 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 132.39 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA--EIDAVCELIDFwrfNV-AFARQILEQQPiSGPGE 170
Cdd:PRK09457 52 AWARLSFEERQAIVERFAALLEEN-KEELAEVIARETGKPLWEAatEVTAMINKIAI---SIqAYHERTGEKRS-EMADG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 171 WNRIDYRPLdGFVYAITPFNFtsiAGNLPTA---PALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDgf 246
Cdd:PRK09457 127 AAVLRHRPH-GVVAVFGPYNF---PGHLPNGhivPALLaGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGG-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALAD-PRLAGIHFTGSTATFGHLWQWVGTNIGRYhsyprLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQ 325
Cdd:PRK09457 201 RETGKALAAhPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 326 KCSAVSRAFIAHSVWqrmGDELLAK----AAELRYGDI-TDLSNYGGALIDQRAFVKNVDAIER--AKGAAAVTVAVgge 398
Cdd:PRK09457 276 RCTCARRLLVPQGAQ---GDAFLARlvavAKRLTVGRWdAEPQPFMGAVISEQAAQGLVAAQAQllALGGKSLLEMT--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 399 YDDSEGYFVRPTVL---LSDDPTDEsfviEYFGPLLSVHVYPDerYEQILDVI-DTgsRYALTGAVIADDRQAVLTALDR 474
Cdd:PRK09457 350 QLQAGTGLLTPGIIdvtGVAELPDE----EYFGPLLQVVRYDD--FDEAIRLAnNT--RFGLSAGLLSDDREDYDQFLLE 421
|
410 420 430
....*....|....*....|....*....|..
gi 489997281 475 LRfaAGnfYVN-DKPTGAVVGRQPFGGARGSG 505
Cdd:PRK09457 422 IR--AG--IVNwNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
181-505 |
4.71e-32 |
|
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: 129.05 E-value: 4.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 181 GFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVAlADPRLA 259
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALA-NHPGVD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 260 GIHFTGSTAtfghlwqwVGTNIGRY--HSYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAH 337
Cdd:cd07111 228 KVAFTGSTE--------VGRALRRAtaGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 338 SVWQRMGDELLAKAAELRYGDITDLSNYGGALID--QRAFVKNVDAIERAKGAAAVTVAvggeyDD--SEGYFVRPTvLL 413
Cdd:cd07111 300 SVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDpaQLKRIRELVEEGRAEGADVFQPG-----ADlpSKGPFYPPT-LF 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 414 SDDPTDESFV-IEYFGPLLSVHVY--PDERYEqildvIDTGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNDkpTG 490
Cdd:cd07111 374 TNVPPASRIAqEEIFGPVLVVLTFrtAKEAVA-----LANNTPYGLAASVWSENLSLALEVALSLK--AGVVWING--HN 444
|
330
....*....|....*
gi 489997281 491 AVVGRQPFGGARGSG 505
Cdd:cd07111 445 LFDAAAGFGGYRESG 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
46-505 |
9.20e-32 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 128.31 E-value: 9.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 46 IGGRHRMGD-GERIDVVQPH--RHAARL--GTLTNATHADAAAAVEAAMSAKSDWAALPFDERAAvFLRAadlLAGPWRE 120
Cdd:PLN02467 12 IGGEWREPVlGKRIPVVNPAteETIGDIpaATAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAK-YLRA---IAAKITE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 121 K---IAAATMLGQSKSVYQAE--IDAVCELIDFWRfNVAFARQILEQQPISGPGEW--NRIDYRPLdGFVYAITPFNFTS 193
Cdd:PLN02467 88 RkseLAKLETLDCGKPLDEAAwdMDDVAGCFEYYA-DLAEALDAKQKAPVSLPMETfkGYVLKEPL-GVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 194 IAGNLPTAPALM-GNTVIWKPSitqTLAAYLTMQLLEAA---GLPPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTAT 269
Cdd:PLN02467 166 LMATWKVAPALAaGCTAVLKPS---ELASVTCLELADICrevGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 270 fghlwqwvGTNIGRYHS-YPRLVG-ETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDEL 347
Cdd:PLN02467 243 --------GRKIMTAAAqMVKPVSlELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 348 LAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDD--SEGYFVRPTVLLSDDPTDESFVIE 425
Cdd:PLN02467 315 VKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGA-TILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 426 YFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADDRQAVltalDRL--RFAAGNFYVN-DKPTGAvvgRQPFGGAR 502
Cdd:PLN02467 394 VFGPVLCVKTFSTED-EAIELANDS--HYGLAGAVISNDLERC----ERVseAFQAGIVWINcSQPCFC---QAPWGGIK 463
|
...
gi 489997281 503 GSG 505
Cdd:PLN02467 464 RSG 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
92-505 |
1.21e-31 |
|
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: 127.91 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGPGEW 171
Cdd:cd07144 59 ESWWSKVTGEERGELLDKLADLVEKN-RDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSD 250
Cdd:cd07144 138 AYTLHEPY-GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYG-AVAG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALAD-PRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA 329
Cdd:cd07144 216 SALAEhPDVDKIAFTGSTATGRLVMKAAAQNL------KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWQRMGDELLAKAAE-LRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGE---YDDSEGY 405
Cdd:cd07144 290 TSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEkapEGLGKGY 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 406 FVRPTVLLsdDPTDESFVI--EYFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADDRQAVLTALDRLRfaAGNFY 483
Cdd:cd07144 369 FIPPTIFT--DVPQDMRIVkeEIFGPVVVISKFKTYE-EAIKKANDT--TYGLAAAVFTKDIRRAHRVARELE--AGMVW 441
|
410 420
....*....|....*....|..
gi 489997281 484 VNDKPTGAVvgRQPFGGARGSG 505
Cdd:cd07144 442 INSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
94-433 |
1.27e-31 |
|
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: 127.63 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPWrEKIAAATMLGQSKSVYQA--EIDAVCELIDFwrfnvAFARQIL---EQQPISGP 168
Cdd:cd07085 53 AWSATPVLKRQQVMFKFRQLLEENL-DELARLITLEHGKTLADArgDVLRGLEVVEF-----ACSIPHLlkgEYLENVAR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEWNRIDYRPLdGFVYAITPFNFTSIAGN--LPTAPALmGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:cd07085 127 GIDTYSYRQPL-GVVAGITPFNFPAMIPLwmFPMAIAC-GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVsDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSYprlvgeTGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:cd07085 205 AV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQAL------GGAKNHAVVMPDADLEQTANALVGAAFGAAGQR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAK--GAAAV----TVAVGGEyd 400
Cdd:cd07085 278 CMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVeeGAKLVldgrGVKVPGY-- 355
|
330 340 350
....*....|....*....|....*....|....*
gi 489997281 401 dSEGYFVRPTVLlsDDPTDESFVI--EYFGPLLSV 433
Cdd:cd07085 356 -ENGNFVGPTIL--DNVTPDMKIYkeEIFGPVLSI 387
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
95-505 |
1.77e-30 |
|
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: 124.10 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFnvaFARQILEQQpisgpGEWNRI 174
Cdd:cd07117 54 WRKTTVAERANILNKIADIIDEN-KELLAMVETLDNGKPIRETRAVDIPLAADHFRY---FAGVIRAEE-----GSANMI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 175 DYRPLD-------GFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVTGDGF 246
Cdd:cd07117 125 DEDTLSivlrepiGVVGQIIPWNFPFLMAAWKLAPALaAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRyHSYPRLVGET---GGKDFVVAHASARPDVLRTALIRGAFDYQ 323
Cdd:cd07117 204 KSGEYLLNHPGLDKLAFTGSTE--------VGRDVAI-AAAKKLIPATlelGGKSANIIFDDANWDKALEGAQLGILFNQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 324 GQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGG----EY 399
Cdd:cd07117 275 GQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGA-KILTGGhrltEN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 400 DDSEGYFVRPTVLLSddPTDESFVI--EYFGPLLSVHVYPDERyeqilDVIDTG--SRYALTGAVIADDRQAVLTALDRL 475
Cdd:cd07117 354 GLDKGFFIEPTLIVN--VTNDMRVAqeEIFGPVATVIKFKTED-----EVIDMAndSEYGLGGGVFTKDINRALRVARAV 426
|
410 420 430
....*....|....*....|....*....|...
gi 489997281 476 RfaAGNFYVN---DKPTGAvvgrqPFGGARGSG 505
Cdd:cd07117 427 E--TGRVWVNtynQIPAGA-----PFGGYKKSG 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
178-506 |
2.04e-30 |
|
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: 124.00 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 178 PLDG--FVY----------AITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGD 244
Cdd:cd07141 132 PMDGdfFTYtrhepvgvcgQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 245 GfAVSDVALAD-PRLAGIHFTGSTATfGHLWQWVG--TNIgryhsyPRLVGETGGKDFVVAHASARPD-VLRTALIrGAF 320
Cdd:cd07141 212 G-PTAGAAISShPDIDKVAFTGSTEV-GKLIQQAAgkSNL------KRVTLELGGKSPNIVFADADLDyAVEQAHE-ALF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 321 DYQGQKCSAVSRAFIAHSVWqrmgDELLAKAAEL----RYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVG 396
Cdd:cd07141 283 FNMGQCCCAGSRTFVQESIY----DEFVKRSVERakkrVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 397 GEYDDsEGYFVRPTVLlsDDPTDESFVI--EYFGPLLSVHvypdeRYEQILDVID--TGSRYALTGAVIADDRQAVLTAL 472
Cdd:cd07141 359 KRHGD-KGYFIQPTVF--SDVTDDMRIAkeEIFGPVQQIF-----KFKTIDEVIEraNNTTYGLAAAVFTKDIDKAITFS 430
|
330 340 350
....*....|....*....|....*....|....*
gi 489997281 473 DRLRfaAGNFYVNdkpTGAVVGRQ-PFGGARGSGT 506
Cdd:cd07141 431 NALR--AGTVWVN---CYNVVSPQaPFGGYKMSGN 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
95-436 |
1.32e-29 |
|
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: 121.54 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLagpwREKIAAatmLGQSKS-----VYQAEIDAVCELIDFWRFNVAFARQI---------- 159
Cdd:cd07130 50 WRDVPAPKRGEIVRQIGDAL----RKKKEA---LGKLVSlemgkILPEGLGEVQEMIDICDFAVGLSRQLygltipserp 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 160 ----LEQqpisgpgeWNridyrPLdGFVYAITPFNF-TSIAG-NlpTAPALM-GNTVIWKPSITQTLAAYLTMQL----L 228
Cdd:cd07130 123 ghrmMEQ--------WN-----PL-GVVGVITAFNFpVAVWGwN--AAIALVcGNVVVWKPSPTTPLTAIAVTKIvarvL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 229 EAAGLPPGVINLVTGDGfAVSDVALADPRLAGIHFTGSTATfGHLwqwVGTNIGRYHSypRLVGETGGKDFVVAHASARP 308
Cdd:cd07130 187 EKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAV-GRQ---VGQAVAARFG--RSLLELGGNNAIIVMEDADL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 309 D-VLRTALIrGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKG 387
Cdd:cd07130 260 DlAVRAVLF-AAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKS 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489997281 388 AAAvTVAVGGEYDDSEGYFVRPTVL--LSDDPtdesfVI--EYFGPLLSVHVY 436
Cdd:cd07130 339 QGG-TVLFGGKVIDGPGNYVEPTIVegLSDAP-----IVkeETFAPILYVLKF 385
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
177-503 |
2.55e-29 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 119.84 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 177 RPLdGFVYAITPFNFTS--IAGNLptAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVAL 253
Cdd:PRK10090 70 RAL-GVTTGILPWNFPFflIARKM--APALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 254 ADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRA 333
Cdd:PRK10090 147 GNPKVAMVSMTGSVSAGEKIMAAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 334 FIAHSVWQRMGDELLAKAAELRYGDITDLSNYG-GALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPTVL 412
Cdd:PRK10090 221 YVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 413 LSDDPTDESFVIEYFGPLLsvhvyPDERYEQILDVIDTG--SRYALTGAVIADDRQAVLTALDRLRFaaGNFYVNDKPTG 490
Cdd:PRK10090 300 LDVRQEMSIMHEETFGPVL-----PVVAFDTLEEAIAMAndSDYGLTSSIYTQNLNVAMKAIKGLKF--GETYINRENFE 372
|
330
....*....|....*....
gi 489997281 491 AVVG------RQPFGGARG 503
Cdd:PRK10090 373 AMQGfhagwrKSGIGGADG 391
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
94-506 |
4.64e-28 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 117.48 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA--EIDAVCELIDFW-----RFN-------VAFARQI 159
Cdd:PLN02278 77 SWSKLTASERSKILRRWYDLIIAN-KEDLAQLMTLEQGKPLKEAigEVAYGASFLEYFaeeakRVYgdiipspFPDRRLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 160 LEQQPIsgpgewnridyrpldGFVYAITPFNF-----TSIAGnlptaPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGL 233
Cdd:PLN02278 156 VLKQPV---------------GVVGAITPWNFplamiTRKVG-----PALAaGCTVVVKPSELTPLTALAAAELALQAGI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 234 PPGVINLVTGDGFAVSDVALADPRLAGIHFTGSTAtfghlwqwVGTNI--GRYHSYPRLVGETGGKDFVVAHASARPDVL 311
Cdd:PLN02278 216 PPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTA--------VGKKLmaGAAATVKRVSLELGGNAPFIVFDDADLDVA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 312 RTALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAfVKNV-----DAIerAK 386
Cdd:PLN02278 288 VKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA-VQKVeshvqDAV--SK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 387 GAaavTVAVGGEYDDSEGYFVRPTVLlsDDPTDESFVI--EYFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADD 464
Cdd:PLN02278 365 GA---KVLLGGKRHSLGGTFYEPTVL--GDVTEDMLIFreEVFGPVAPLTRFKTEE-EAIAIANDT--EAGLAAYIFTRD 436
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489997281 465 RQAVLTALDRLRFaaGNFYVNDKPTGAVVGrqPFGGARGSGT 506
Cdd:PLN02278 437 LQRAWRVSEALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
92-525 |
7.77e-27 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 113.84 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILEQQPISGPGEW 171
Cdd:PRK09847 72 RGDWSLSSPAKRKAVLNKLADLMEAH-AEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHEL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD 250
Cdd:PRK09847 151 AMIVREPV-GVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALADPRLAGIHFTGSTATFGHLWQWVGTNigryhSYPRLVGETGGKDFVVAHASArPDVLR--TALIRGAFDYQGQKCS 328
Cdd:PRK09847 230 ALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADC-PDLQQaaSATAAGIFYNQGQVCI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIEraKGAAAVTVAVGGEYDDSEGYfVR 408
Cdd:PRK09847 304 AGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR--EGESKGQLLLDGRNAGLAAA-IG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 409 PTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTgSRYALTGAVIADDrqavLTALDRL--RFAAGNFYVND 486
Cdd:PRK09847 381 PTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRD----LSRAHRMsrRLKAGSVFVNN 453
|
410 420 430
....*....|....*....|....*....|....*....
gi 489997281 487 KPTGAVVgrQPFGGARGSGtNDKAGSPLNLLRWTSARSI 525
Cdd:PRK09847 454 YNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
95-505 |
4.04e-26 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 111.51 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLagpwREK---IAAATMLGQSKSVYQAE-IDAV--CELIDFWrfnVAFARQIL-EQQPISG 167
Cdd:PRK13252 60 WAAMTAMERSRILRRAVDIL----RERndeLAALETLDTGKPIQETSvVDIVtgADVLEYY---AGLAPALEgEQIPLRG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 168 pGEWNRIDYRPLdGFVYAITPFNF-TSIAGnLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDG 245
Cdd:PRK13252 133 -GSFVYTRREPL-GVCAGIGAWNYpIQIAC-WKSAPALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 246 fAVSDVALADPRLAGIHFTGSTATfghlwqwvgtniGRY------HSYPRLVGETGGKDFVVAHASARPDVLRTALIRGA 319
Cdd:PRK13252 210 -RVGAWLTEHPDIAKVSFTGGVPT------------GKKvmaaaaASLKEVTMELGGKSPLIVFDDADLDRAADIAMLAN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 320 FDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGG-- 397
Cdd:PRK13252 277 FYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGA-RLLCGGer 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 398 --EYDDSEGYFVRPTVLlsDDPTDESFVI--EYFGPLLSVHVYPDERyeqilDVID--TGSRYALTGAVIADDrqavLTA 471
Cdd:PRK13252 356 ltEGGFANGAFVAPTVF--TDCTDDMTIVreEIFGPVMSVLTFDDED-----EVIAraNDTEYGLAAGVFTAD----LSR 424
|
410 420 430
....*....|....*....|....*....|....*....
gi 489997281 472 LDRL--RFAAGNFYVN---DKPTGAvvgrqPFGGARGSG 505
Cdd:PRK13252 425 AHRVihQLEAGICWINtwgESPAEM-----PVGGYKQSG 458
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
92-439 |
1.67e-25 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 109.46 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 92 KSDWAALPFDERAAVFLRAADLLAGPWrEKIAAATMLGQSKSVYQAEIDAVCELIDFWRFnvaFARQILEQQpisgpGEW 171
Cdd:cd07116 51 KEAWGKTSVAERANILNKIADRMEANL-EMLAVAETWDNGKPVRETLAADIPLAIDHFRY---FAGCIRAQE-----GSI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRID--------YRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSiTQTLAAYLTMQLLEAAGLPPGVINLVT 242
Cdd:cd07116 122 SEIDentvayhfHEPL-GVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPA-EQTPASILVLMELIGDLLPPGVVNVVN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 243 GDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsYPRLVgETGGK------DFVVAHASARPDVLRTALI 316
Cdd:cd07116 200 GFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IPVTL-ELGGKspniffADVMDADDAFFDKALEGFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 317 RGAFDyQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALI--DQRAFVKNVDAIERAKGAaavTVA 394
Cdd:cd07116 274 MFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQAslEQLEKILSYIDIGKEEGA---EVL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489997281 395 VGGEY----DDSEGYFVRPTVLLSDDPTdESFVIEYFGPLLSVHVYPDE 439
Cdd:cd07116 350 TGGERnelgGLLGGGYYVPTTFKGGNKM-RIFQEEIFGPVLAVTTFKDE 397
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
95-527 |
1.05e-24 |
|
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: 107.00 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVfLRA--ADLLAGpwREKIAAATMLGQSKSVYQA---EIDAVCELIdfwRFNVAFARQILEQQPISGP- 168
Cdd:cd07098 34 WAKTSFAERRKV-LRSllKYILEN--QEEICRVACRDTGKTMVDAslgEILVTCEKI---RWTLKHGEKALRPESRPGGl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEW---NRIDYRPLdGFVYAITPFN--FTSIAGnlPTAPALM-GNTVIWKPS--ITQTLAAYLTM--QLLEAAGLPPGVI 238
Cdd:cd07098 108 LMFykrARVEYEPL-GVVGAIVSWNypFHNLLG--PIIAALFaGNAIVVKVSeqVAWSSGFFLSIirECLAACGHDPDLV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 239 NLVTGdgFAVSDVAL-ADPRLAGIHFTGSTAtfghlwqwVGTNIGR--YHSYPRLVGETGGKDFVVAHASARPDVLRTAL 315
Cdd:cd07098 185 QLVTC--LPETAEALtSHPVIDHITFIGSPP--------VGKKVMAaaAESLTPVVLELGGKDPAIVLDDADLDQIASII 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 316 IRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKN----VDAIEraKGAaav 391
Cdd:cd07098 255 MRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLeelvADAVE--KGA--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 392 TVAVGGEY----DDSEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDtGSRYALTGAVIADDRQA 467
Cdd:cd07098 330 RLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIAN-STEYGLGASVFGKDIKR 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 468 VLTALDRLRfaAGNFYVNDKPTGAVVGRQPFGGARGSGTnDKAGSPLNLLRWTSARSIKE 527
Cdd:cd07098 407 ARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
95-505 |
1.65e-24 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 106.53 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQA--EIDAVCELIDfWrfnvaFARqilEQQPISG---PG 169
Cdd:PRK11241 64 WRALTAKERANILRRWFNLMMEH-QDDLARLMTLEQGKPLAEAkgEISYAASFIE-W-----FAE---EGKRIYGdtiPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 170 ewNRIDYR------PLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVT 242
Cdd:PRK11241 134 --HQADKRlivikqPI-GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 243 GDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIgryhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDY 322
Cdd:PRK11241 211 GSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI------KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERA--KGAaavTVAVGGEYD 400
Cdd:PRK11241 285 AGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADAleKGA---RVVCGGKAH 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 401 DSEGYFVRPTVLLsDDPTDESFVI-EYFGPLLSVHVYPDERyEQILDVIDTgsRYALTGAVIADDRQAVLTALDRLRFaa 479
Cdd:PRK11241 362 ELGGNFFQPTILV-DVPANAKVAKeETFGPLAPLFRFKDEA-DVIAQANDT--EFGLAAYFYARDLSRVFRVGEALEY-- 435
|
410 420
....*....|....*....|....*..
gi 489997281 480 GNFYVNdkpTGAVVGR-QPFGGARGSG 505
Cdd:PRK11241 436 GIVGIN---TGIISNEvAPFGGIKASG 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
95-505 |
2.50e-24 |
|
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: 106.04 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAgPWREKIAAATMLgQSKSVYQAEIDA-VCELIDFWRFNVAFARQILEQQ-PISGPGEWN 172
Cdd:cd07140 61 WGKMNARDRGRLMYRLADLME-EHQEELATIESL-DSGAVYTLALKThVGMSIQTFRYFAGWCDKIQGKTiPINQARPNR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDY---RPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAV 248
Cdd:cd07140 139 NLTLtkrEPI-GVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALADPRLAGIHFTGSTATFGHLWQWVGTNigryhSYPRLVGETGGKDFVVAHASARPD-VLRTALIRGAFDyQGQKC 327
Cdd:cd07140 218 GQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSPLIIFADCDMDkAVRMGMSSVFFN-KGENC 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFV 407
Cdd:cd07140 292 IAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGA-TLVYGGKQVDRPGFFF 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 408 RPTVLlsDDPTDESFVI--EYFGPLLSVHVYPDERYEQILDVIDtGSRYALTGAVIADDRQAVLTALDRLRfaAGNFYVN 485
Cdd:cd07140 371 EPTVF--TDVEDHMFIAkeESFGPIMIISKFDDGDVDGVLQRAN-DTEYGLASGVFTKDINKALYVSDKLE--AGTVFVN 445
|
410 420
....*....|....*....|
gi 489997281 486 DKPTGAVVGrqPFGGARGSG 505
Cdd:cd07140 446 TYNKTDVAA--PFGGFKQSG 463
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
95-505 |
3.18e-24 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 105.99 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAGPWREkIAAATMlgqsKSVYQAEIDAVCELI---DFWRFNVAFARQILEQQPI----SG 167
Cdd:PLN00412 69 WAKTPLWKRAELLHKAAAILKEHKAP-IAECLV----KEIAKPAKDAVTEVVrsgDLISYTAEEGVRILGEGKFlvsdSF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 168 PGEwNRIDY-----RPLdGFVYAITPFNFTSiagNLPT---APALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVI 238
Cdd:PLN00412 144 PGN-ERNKYcltskIPL-GVVLAIPPFNYPV---NLAVskiAPALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 239 NLVTGDGFAVSDVALADPRLAGIHFTGSTatfghlwqwVGTNIGRYHSYPRLVGETGGKDFVVAHASARPDVLRTALIRG 318
Cdd:PLN00412 219 SCVTGKGSEIGDFLTMHPGVNCISFTGGD---------TGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 319 AFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYG------DITDL-----SNYGGALIDqrafvknvDAieRAKG 387
Cdd:PLN00412 290 GFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGppeddcDITPVvsessANFIEGLVM--------DA--KEKG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 388 AAAVTvavggEYdDSEGYFVRPtvLLSDDPTDESFVI--EYFGPLLSV-HVYPDEryEQILDVidTGSRYALTGAVIADD 464
Cdd:PLN00412 360 ATFCQ-----EW-KREGNLIWP--LLLDNVRPDMRIAweEPFGPVLPViRINSVE--EGIHHC--NASNFGLQGCVFTRD 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489997281 465 RQAVLTALDRLRfaAGNFYVNDKPtgavvGRQ----PFGGARGSG 505
Cdd:PLN00412 428 INKAILISDAME--TGTVQINSAP-----ARGpdhfPFQGLKDSG 465
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
174-505 |
4.07e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 105.33 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 IDYRPLdGFVYAITPFNF---TSIAGNLPTApaLMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSD 250
Cdd:PRK13968 122 IEYRPL-GTILAIMPWNFplwQVMRGAVPIL--LAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 vALADPRLAGIHFTGSTATfghlwqwvGTNIGRYH--SYPRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCS 328
Cdd:PRK13968 199 -MINDSRIAAVTVTGSVRA--------GAAIGAQAgaALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGG--ALIDQRAFVKNVDAIERAKGAaavTVAVGGEYDDSEGYF 406
Cdd:PRK13968 270 AAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQVEATLAEGA---RLLLGGEKIAGAGNY 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 407 VRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTgSRYALTGAVI-ADDRQAVLTAldrLRFAAGNFYVN 485
Cdd:PRK13968 347 YAPTVLANVTPEMTAFREELFGPVAAITVAKDA--EHALELAND-SEFGLSATIFtTDETQARQMA---ARLECGGVFIN 420
|
330 340
....*....|....*....|
gi 489997281 486 DkpTGAVVGRQPFGGARGSG 505
Cdd:PRK13968 421 G--YCASDARVAFGGVKKSG 438
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
95-511 |
9.60e-24 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 104.89 E-value: 9.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 95 WAALPFDERAAVFLRAADLLAgPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQIleqQPISGPGEWN-- 172
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKI---HGLTVPADGPhh 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 -RIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSD 250
Cdd:PLN02466 189 vQTLHEPI-GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFG-PTAG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 251 VALAD----PRLAgihFTGSTATfGHLWQWVGTNigryHSYPRLVGETGGKD-FVV---AHASARPDVLRTALirgaFDY 322
Cdd:PLN02466 267 AALAShmdvDKLA---FTGSTDT-GKIVLELAAK----SNLKPVTLELGGKSpFIVcedADVDKAVELAHFAL----FFN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 QGQKCSAVSRAFIAHSVWqrmgDELL--AKAAELR--YGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGE 398
Cdd:PLN02466 335 QGQCCCAGSRTFVHERVY----DEFVekAKARALKrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGA-TLECGGD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 399 YDDSEGYFVRPTVLlsDDPTDESFVI--EYFGPLLSVHVYPDeryeqILDVID--TGSRYALTGAVIADDRQAVLTALDR 474
Cdd:PLN02466 410 RFGSKGYYIQPTVF--SNVQDDMLIAqdEIFGPVQSILKFKD-----LDEVIRraNNTRYGLAAGVFTQNLDTANTLSRA 482
|
410 420 430
....*....|....*....|....*....|....*....
gi 489997281 475 LRfaAGNFYVN--DKPTGAVvgrqPFGGARGSGTNDKAG 511
Cdd:PLN02466 483 LR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
94-525 |
1.67e-23 |
|
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: 103.09 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAgPWREKIAAATMLGQSKSVYQAEiDAVCELIDFWRFNVAFARQILEQQPISGPGEWNR 173
Cdd:cd07084 14 AARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 ID---YRPLDGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAG-LPPGVINLVTGDGFAV 248
Cdd:cd07084 92 QQshgYRWPYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 249 SDVALaDPRLAGIHFTGSTATfghlWQWVGTNIgryhSYPRLVGETGGKDFVVAHASARP-DVLRTALIRGAFDYQGQKC 327
Cdd:cd07084 172 QALLL-HPNPKMVLFTGSSRV----AEKLALDA----KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFiAHSVWQRMG--DELLAKAAELRYGDITDlsnygGALI--DQRAFVKNVDAIERAKGAAAVTVAVGGEYDDSE 403
Cdd:cd07084 243 TAQSMLF-VPENWSKTPlvEKLKALLARRKLEDLLL-----GPVQtfTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 GYFVRPTVLLSDDPTD---ESFVIEYFGPLLSVHVYPDERYEQILDVIDTGSRyALTGAVIADDRQAVLTALDRLRFAAG 480
Cdd:cd07084 317 GACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG-SLTAAIYSNDPIFLQELIGNLWVAGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489997281 481 NFYVNDKPTGAVVGRQPFGGARGSGTNDKAGSPLNLLRWTSARSI 525
Cdd:cd07084 396 TYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
94-505 |
2.64e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 102.89 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 94 DWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDAVcELIDFWRFNVAFARQILEQQPISGPGEWNR 173
Cdd:PRK09406 38 DYRTTTFAQRARWANAAADLLEAE-ADQVAALMTLEMGKTLASAKAEAL-KCAKGFRYYAEHAEALLADEPADAAAVGAS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 174 ---IDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWK--PSITQTlAAYLTmQLLEAAGLPPGVI-NLVTGDGf 246
Cdd:PRK09406 116 rayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhaSNVPQT-ALYLA-DLFRRAGFPDGCFqTLLVGSG- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVaLADPRLAGIHFTGSTATfghlWQWVGTNIGRyhSYPRLVGETGGKDFVVAHASArpDVLRTALIRGAFDYQ--G 324
Cdd:PRK09406 192 AVEAI-LRDPRVAAATLTGSEPA----GRAVAAIAGD--EIKKTVLELGGSDPFIVMPSA--DLDRAAETAVTARVQnnG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 325 QKCSAVSRaFIAHS-VWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSE 403
Cdd:PRK09406 263 QSCIAAKR-FIVHAdVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGA-TILCGGKRPDGP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 GYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDerYEQILDVIDtGSRYALTGAVIADDrqavltALDRLRFA----A 479
Cdd:PRK09406 341 GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIAN-ATTFGLGSNAWTRD------EAEQERFIddleA 411
|
410 420
....*....|....*....|....*...
gi 489997281 480 GNFYVNdkptGAVVGRQ--PFGGARGSG 505
Cdd:PRK09406 412 GQVFIN----GMTVSYPelPFGGVKRSG 435
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
181-511 |
1.50e-22 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 100.61 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 181 GFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSI-TQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRL 258
Cdd:TIGR04284 143 GVVGAITPWNFPHQINLAKLGPALAaGNTVVLKPAPdTPWCAAVLGELIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 259 AGIHFTGSTATfghlwqwvgtniGRY------HSYPRLVGETGGKDFVVAHASARpdvLRTALIRGAFD---YQGQKCSA 329
Cdd:TIGR04284 223 DMVSFTGSTAT------------GRAvmadaaATLKKVFLELGGKSAFIVLDDAD---LAAACSMAAFTvcmHAGQGCAI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 330 VSRAFIAHSVWqrmgDELLAKAAE----LRYGDITDLSNYGGALID--QRAFVKNVDAIERAKGAaavTVAVGG--EYDD 401
Cdd:TIGR04284 288 TTRLVVPRARY----DEAVAAAAAtmgsIKPGDPADPGTVCGPVISarQRDRVQSYLDLAVAEGG---RFACGGgrPADR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 402 SEGYFVRPTVLLSDDPTDESFVIEYFGPLLSV--HVYPDERYEqildvIDTGSRYALTGAVIADDRQAVLTALDRLRfaA 479
Cdd:TIGR04284 361 DRGFFVEPTVIAGLDNNARVAREEIFGPVLTViaHDGDDDAVR-----IANDSPYGLSGTVFGADPERAAAVAARVR--T 433
|
330 340 350
....*....|....*....|....*....|....
gi 489997281 480 GNFYVNdkptGAV--VGRQPFGGARGSGTNDKAG 511
Cdd:TIGR04284 434 GTVNVN----GGVwySADAPFGGYKQSGIGREMG 463
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
172-507 |
1.89e-22 |
|
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: 100.19 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDY--RPLDGFVYAITPFNFTSiagNL---PTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDG 245
Cdd:cd07148 115 GRIAFttREPIGVVVAISAFNHPL---NLivhQVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 246 fAVSDVALADPRLAGIHFTGSTATFGHLWQWV--GTnigryhsypRLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQ 323
Cdd:cd07148 192 -AVAEKLVTDPRVAFFSFIGSARVGWMLRSKLapGT---------RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 324 GQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSE 403
Cdd:cd07148 262 GQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 404 GYfvRPTVLLsdDPTDESFV--IEYFGPLlsVHVYPderYEQILDVIDTGSR--YALTGAVIADDRQAVLTALDRLrfAA 479
Cdd:cd07148 341 TY--APTVLL--DPPRDAKVstQEIFGPV--VCVYS---YDDLDEAIAQANSlpVAFQAAVFTKDLDVALKAVRRL--DA 409
|
330 340
....*....|....*....|....*...
gi 489997281 480 GNFYVNDkPTGAVVGRQPFGGARGSGTN 507
Cdd:cd07148 410 TAVMVND-HTAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
181-505 |
4.70e-21 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 96.43 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 181 GFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGfAVSDVALADPR-L 258
Cdd:PLN02766 160 GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFG-PTAGAAIASHMdV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 259 AGIHFTGSTAtfghlwqwVGTNIGRYHSYPRLVG---ETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSAVSRAFI 335
Cdd:PLN02766 239 DKVSFTGSTE--------VGRKIMQAAATSNLKQvslELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 336 AHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAvTVAVGGEYDDSEGYFVRPTVLLsd 415
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFT-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 416 DPTDESFVI--EYFGPLLSVHvypdeRYEQILDVIDTG--SRYALTGAVIADDRQAVLTALDRLRfaAGNFYVNdkPTGA 491
Cdd:PLN02766 388 DVTEDMKIAqdEIFGPVMSLM-----KFKTVEEAIKKAnnTKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVN--CYFA 458
|
330
....*....|....
gi 489997281 492 VVGRQPFGGARGSG 505
Cdd:PLN02766 459 FDPDCPFGGYKMSG 472
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
173-506 |
1.35e-19 |
|
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: 91.51 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVTGdgfAVSDV 251
Cdd:cd07135 103 RIRKEPL-GVVLIIGPWNYPVLLALSPLVGAIAaGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQG---GVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 -ALADPRLAGIHFTGSTAtfghlwqwVGTNIGRY---HSYPrLVGETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKC 327
Cdd:cd07135 178 tALLEQKFDKIFYTGSGR--------VGRIIAEAaakHLTP-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQIC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGgALIDQRAFVKNVDAIERAKGaaavTVAVGGEYDDSEgYFV 407
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYT-RIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 408 RPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIDTGSRyALTGAVIADDRQAVLTALDRLRfaAGNFYVNDK 487
Cdd:cd07135 323 PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL--DEAIKVINSRDT-PLALYIFTDDKSEIDHILTRTR--SGGVVINDT 397
|
330
....*....|....*....
gi 489997281 488 PTGAVVGRQPFGGARGSGT 506
Cdd:cd07135 398 LIHVGVDNAPFGGVGDSGY 416
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
119-505 |
2.41e-18 |
|
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: 87.58 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 119 REKIAAA--TMLGQSKS-VYQAEIDAVCELIDFWRFNVafaRQILEQQPIS-----GPGEwNRIDYRPLdGFVYAITPFN 190
Cdd:cd07087 37 EEEIAAAlyADLGKPPAeAYLTEIAVVLGEIDHALKHL---KKWMKPRRVSvplllQPAK-AYVIPEPL-GVVLIIGPWN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 191 F---TSIAgnlPTAPALM-GNTVIWKPSITqtlaAYLTMQLLE---AAGLPPGVINLVTGDGfAVSDvALADPRLAGIHF 263
Cdd:cd07087 112 YplqLALA---PLIGAIAaGNTVVLKPSEL----APATSALLAkliPKYFDPEAVAVVEGGV-EVAT-ALLAEPFDHIFF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 264 TGSTAtfghlwqwVGTNIGRY---HSYPrLVGETGGKDFVVAHASARPDVlrTA--LIRGAFDYQGQKCSAVSRAFIAHS 338
Cdd:cd07087 183 TGSPA--------VGKIVMEAaakHLTP-VTLELGGKSPCIVDKDANLEV--AArrIAWGKFLNAGQTCIAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 339 VWQRMGDELlAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKgaaavtVAVGGEYDDSEGYFVrPTVLlsDDPT 418
Cdd:cd07087 252 IKDELIEEL-KKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK------VVIGGQVDKEERYIA-PTIL--DDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 419 DESFVI--EYFGPLLSVHVYPDEryEQILDVIDTGSRyALTGAVIADDRQAVLTALDRLRFaaGNFYVNDKPTGAVVGRQ 496
Cdd:cd07087 322 PDSPLMqeEIFGPILPILTYDDL--DEAIEFINSRPK-PLALYLFSEDKAVQERVLAETSS--GGVCVNDVLLHAAIPNL 396
|
....*....
gi 489997281 497 PFGGARGSG 505
Cdd:cd07087 397 PFGGVGNSG 405
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
139-512 |
7.03e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 86.43 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 139 IDAVCELIDFWRFNVAFARQ-----ILEQQPISGPGE-WNridyrPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIW 211
Cdd:PLN02315 114 IGEVQEIIDMCDFAVGLSRQlngsiIPSERPNHMMMEvWN-----PL-GIVGVITAFNFPCAVLGWNACIALVcGNCVVW 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 212 KPSITQTLAAYLTMQL----LEAAGLPPGVINLVTGdGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRYhsy 287
Cdd:PLN02315 188 KGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKC--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 288 prLVGETGGKDFVVAHASARPDVLRTALIrGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGG 367
Cdd:PLN02315 264 --LLELSGNNAIIVMDDADIQLAVRSVLF-AAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 368 AL---IDQRAFVKNVDAIeRAKGAAAVTvavGGEYDDSEGYFVRPTVlLSDDPTDESFVIEYFGPLLsvHVYPDERYEQI 444
Cdd:PLN02315 341 PLhtpESKKNFEKGIEII-KSQGGKILT---GGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVL--YVMKFKTLEEA 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489997281 445 LDvIDTGSRYALTGAVIADDRQAVLTALDRLRFAAGNFYVNDKPTGAVVGrQPFGGARGSGTNDKAGS 512
Cdd:PLN02315 414 IE-INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-505 |
7.96e-17 |
|
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: 82.66 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 164 PISGPGEWNRIDYRPlDGFVYAITPFNF---TSIAgnlPTAPALM-GNTVIWKPS-ITQTLAAYLTmQLLEAAgLPPGVI 238
Cdd:cd07134 86 PLLLFGTKSKIRYEP-KGVCLIISPWNYpfnLAFG---PLVSAIAaGNTAILKPSeLTPHTSAVIA-KIIREA-FDEDEV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 239 NLVTGDgFAVSDvALADPRLAGIHFTGSTAtfghlwqwvgtnIGRY-------HsyprLVG---ETGGKDFVVAHASArp 308
Cdd:cd07134 160 AVFEGD-AEVAQ-ALLELPFDHIFFTGSPA------------VGKIvmaaaakH----LASvtlELGGKSPTIVDETA-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 309 DVLRTA--LIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDL--SNYGGaLIDQRAFVKNVDAIER 384
Cdd:cd07134 220 DLKKAAkkIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKasPDLAR-IVNDRHFDRLKGLLDD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 385 AKGAAAvTVAVGGEYDDSEGYFVrPTVLlsDDPTDESFVI--EYFGPLLSVHVYpdERYEQILDVIDTGSRyALTGAVIA 462
Cdd:cd07134 299 AVAKGA-KVEFGGQFDAAQRYIA-PTVL--TNVTPDMKIMqeEIFGPVLPIITY--EDLDEVIEYINAKPK-PLALYVFS 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489997281 463 DDRQAVLTALDRLrfAAGNFYVNDKPTGAVVGRQPFGGARGSG 505
Cdd:cd07134 372 KDKANVNKVLART--SSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
166-505 |
9.42e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 79.69 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 166 SGPGEwNRIDYRPLdGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPS-----ITQTLAAYLTMQLleaaglPPGVIN 239
Cdd:PTZ00381 98 FGPGK-SYIIPEPL-GVVLVIGAWNYPLNLTLIPLAGAIAaGNTVVLKPSelsphTSKLMAKLLTKYL------DPSYVR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 240 LVTGdGFAVSdVALADPRLAGIHFTGSTAtfghlwqwVGTNIGRYHSyPRLVG---ETGGKDFVVAHASARPDVLRTALI 316
Cdd:PTZ00381 170 VIEG-GVEVT-TELLKEPFDHIFFTGSPR--------VGKLVMQAAA-ENLTPctlELGGKSPVIVDKSCNLKVAARRIA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 317 RGAFDYQGQKCSAVSRAFiahsVWQRMGDELLAKAAELR---YGDITDLSNYGGALIDQRAFVKNVDAIERAKGaaavTV 393
Cdd:PTZ00381 239 WGKFLNAGQTCVAPDYVL----VHRSIKDKFIEALKEAIkefFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGG----KV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 394 AVGGEYDDSEGYfVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDEryEQILDVIdtGSR-YALTGAVIADDRQAVLTAL 472
Cdd:PTZ00381 311 VYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENI--DEVLEFI--NSRpKPLALYYFGEDKRHKELVL 385
|
330 340 350
....*....|....*....|....*....|...
gi 489997281 473 DRLrfAAGNFYVNDKPTGAVVGRQPFGGARGSG 505
Cdd:PTZ00381 386 ENT--SSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
178-466 |
3.51e-14 |
|
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: 75.00 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 178 PLDGFVYAITPFNFtSIAGNLPT-APALM-GNTVIWKPSiTQTlaAYLT---MQLLEAAG-LPPGVINLVTGDgfaVSDv 251
Cdd:cd07128 143 PRRGVAVHINAFNF-PVWGMLEKfAPALLaGVPVIVKPA-TAT--AYLTeavVKDIVESGlLPEGALQLICGS---VGD- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 252 aLADpRLAG---IHFTGSTATFGHLwqwvgtnigRYHsyPRLVG-------ETGGKDFVVAHASARPDVLRTAL-IRGAF 320
Cdd:cd07128 215 -LLD-HLGEqdvVAFTGSAATAAKL---------RAH--PNIVArsirfnaEADSLNAAILGPDATPGTPEFDLfVKEVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 321 D----YQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALI--DQRAFVKnvDAIERAKgAAAVTVA 394
Cdd:cd07128 282 RemtvKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVsrEQREDVR--AAVATLL-AEAEVVF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 395 VGGEY------DDSEGYFVRPTVLLSDDPTDESFV--IEYFGPLLSVHVYPDEryEQILDVIDTGsRYALTGAVIADDRQ 466
Cdd:cd07128 359 GGPDRfevvgaDAEKGAFFPPTLLLCDDPDAATAVhdVEAFGPVATLMPYDSL--AEAIELAARG-RGSLVASVVTNDPA 435
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
178-467 |
8.71e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 73.97 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 178 PLDGFVYAITPFNFTSIAGNLPTAPALM-GNTVIWKPSITQTLAAYLTMQLLEAAG-LPPGVINLVTG------DGFAVS 249
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLaGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGssagllDHLQPF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 250 DValadprlagIHFTGSTATFGHLwqwvgtnigryHSYPRLVGETggkdfvvAHASARPDVLRTALI-------RGAFDY 322
Cdd:PRK11903 227 DV---------VSFTGSAETAAVL-----------RSHPAVVQRS-------VRVNVEADSLNSALLgpdaapgSEAFDL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 323 ------------QGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAA 390
Cdd:PRK11903 280 fvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 391 VtVAVGGEY-----DDSEGYFVRPTVLLSDDPTDESFV--IEYFGPLLSVHVYPDEryEQILDVIDTGsRYALTGAVIAD 463
Cdd:PRK11903 360 V-LFDGGGFalvdaDPAVAACVGPTLLGASDPDAATAVhdVEVFGPVATLLPYRDA--AHALALARRG-QGSLVASVYSD 435
|
....
gi 489997281 464 DRQA 467
Cdd:PRK11903 436 DAAF 439
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
172-505 |
1.82e-13 |
|
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: 72.52 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 172 NRIDYRPLdGFVYAITPFNF---TSIAgnlPTAPAL-MGNTVIWKPS-ITQTLAAYLTmQLLEAAgLPPGVINLVTGDGf 246
Cdd:cd07133 95 AEVEYQPL-GVVGIIVPWNYplyLALG---PLIAALaAGNRVMIKPSeFTPRTSALLA-ELLAEY-FDEDEVAVVTGGA- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 avsDVALADPRLAGIH--FTGSTAtfghlwqwVGtnigryhsypRLVG------------ETGGKDFVVAHASARPDVLR 312
Cdd:cd07133 168 ---DVAAAFSSLPFDHllFTGSTA--------VG----------RHVMraaaenltpvtlELGGKSPAIIAPDADLAKAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 313 TALIRGAFDYQGQKCSAVSRAFIAHSVWQRMGDELLAKAAElRYGDITDLSNYgGALIDQRAFVKNVDAIE--RAKGAAA 390
Cdd:cd07133 227 ERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAK-MYPTLADNPDY-TSIINERHYARLQGLLEdaRAKGARV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 391 VTVAVGGEYDDSEGYFVrPTVLLsdDPTDESFVI--EYFGPLLSVHVYPDerYEQILDVIDTGSR----YALTGAviADD 464
Cdd:cd07133 305 IELNPAGEDFAATRKLP-PTLVL--NVTDDMRVMqeEIFGPILPILTYDS--LDEAIDYINARPRplalYYFGED--KAE 377
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489997281 465 RQAVLTaldrlRFAAGNFYVNDKPTGAVVGRQPFGGARGSG 505
Cdd:cd07133 378 QDRVLR-----RTHSGGVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
20-431 |
4.06e-13 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 72.09 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 20 PKSPERTRLRT-------ELASLADHPIDLPHVIGGRHRMGDGER-IDVVQPHRH--AARLGTLTNATHADAAAAVEAAM 89
Cdd:PLN02419 85 PLRPQFLALRSswlstspEQSTQPQMPPRVPNLIGGSFVESQSSSfIDVINPATQevVSKVPLTTNEEFKAAVSAAKQAF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 90 SAksdWAALPFDERAAVFLRAADLLAGPwREKIAAATMLGQSKSVYQAEIDaVCELIDFWRFNVAFAR-QILEQQPISGP 168
Cdd:PLN02419 165 PL---WRNTPITTRQRVMLKFQELIRKN-MDKLAMNITTEQGKTLKDSHGD-IFRGLEVVEHACGMATlQMGEYLPNVSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 169 GEWNRIDYRPLdGFVYAITPFNFTSIAG--NLPTApALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGF 246
Cdd:PLN02419 240 GVDTYSIREPL-GVCAGICPFNFPAMIPlwMFPVA-VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTND 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 247 AVSDVAlADPRLAGIHFTGSTATFGHLWQWVGTNIGRYHSyprlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQK 326
Cdd:PLN02419 318 TVNAIC-DDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 327 CSAVSR-AFIAHS-VWQrmgDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGE-----Y 399
Cdd:PLN02419 391 CMALSTvVFVGDAkSWE---DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgY 467
|
410 420 430
....*....|....*....|....*....|..
gi 489997281 400 DdsEGYFVRPTVLLSDDPTDESFVIEYFGPLL 431
Cdd:PLN02419 468 E--KGNFIGPTILSGVTPDMECYKEEIFGPVL 497
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
188-500 |
1.14e-12 |
|
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: 69.88 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 188 PFNFtSIAGNlPTAPAL-MGNTVIWK--PSITQT--LAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVALADPRLAGIH 262
Cdd:cd07129 118 PLAF-SVAGG-DTASALaAGCPVVVKahPAHPGTseLVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 263 FTGSTAtfghlwqwvgtnigryhsyprlvgetGGKdFVVAHASARPD---------------VLRTALI-RGAFDYQ--- 323
Cdd:cd07129 196 FTGSRR--------------------------GGR-ALFDAAAARPEpipfyaelgsvnpvfILPGALAeRGEAIAQgfv 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 324 -------GQKC----------SAVSRAFIAHSVwqrmgdELLAKAAELRygditdLSNYGGAlidqRAFVKNVDAIErak 386
Cdd:cd07129 249 gsltlgaGQFCtnpglvlvpaGPAGDAFIAALA------EALAAAPAQT------MLTPGIA----EAYRQGVEALA--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 387 GAAAVTVAVGGEyDDSEGYFVRPTVLLSDDPT---DESFVIEYFGPLLSVHVYPDEryEQILDVIDT--GSryaLTGAVI 461
Cdd:cd07129 310 AAPGVRVLAGGA-AAEGGNQAAPTLFKVDAAAflaDPALQEEVFGPASLVVRYDDA--AELLAVAEAleGQ---LTATIH 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489997281 462 AD--DRQAVLTALDRLRFAAGNFYVNDKPTG-AVVGRQPFGG 500
Cdd:cd07129 384 GEedDLALARELLPVLERKAGRLLFNGWPTGvEVCPAMVHGG 425
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
176-525 |
1.79e-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: 66.37 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 176 YRPLDGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLVTGDGFAVSDVAL- 253
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLe 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 254 ADPRLagIHFTGSTATFGHLWQWVGTNIgryhsypRLvgETGGKDFVVAHasarPDVLRTALI-----RGAFDYQGQKCS 328
Cdd:cd07126 219 ANPRM--TLFTGSSKVAERLALELHGKV-------KL--EDAGFDWKILG----PDVSDVDYVawqcdQDAYACSGQKCS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 329 AVSRAFiAHSVWQRMG--DELLAKAAELRYGDITdlsnYGGAL-IDQRAFVKNVDAIERAKGAaavTVAVGG----EYDD 401
Cdd:cd07126 284 AQSILF-AHENWVQAGilDKLKALAEQRKLEDLT----IGPVLtWTTERILDHVDKLLAIPGA---KVLFGGkpltNHSI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 402 SEGY-FVRPT---VLLSDDPTDESFVI---EYFGPLLSVHVYPDERYEQILDVIDTGSRYaLTGAVIADDR---QAVLTA 471
Cdd:cd07126 356 PSIYgAYEPTavfVPLEEIAIEENFELvttEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIrflQEVLAN 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489997281 472 LDRLRFAAGnfyVNDKPTGAVVGR--QPFGGARGSGTndkaGSPLNL-LRWTSARSI 525
Cdd:cd07126 435 TVNGTTYAG---IRARTTGAPQNHwfGPAGDPRGAGI----GTPEAIrLVWSCHREI 484
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
2-518 |
2.16e-09 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 60.45 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 2 DAITQVPVPANEPVHDYAPKSPERTRLRTELASLADHPIDLPHVIGGRHRMGDGERIDVVQPHRHAARLGTLTNATHADA 81
Cdd:COG0506 451 PLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAA 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 82 AAAVEAAMSAKSDWAALPfdERAAVFLRAADLLAGPWREKIAAATMLGQSKSVYQAEIDAVCELIDFWRFNVAFARQILE 161
Cdd:COG0506 531 AAAAAAAAAAAAAAAAAA--AAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAP 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 162 QQPISGPGEWNRIDYRPLDGFVYAITPFNFTSIAGNLPTAPALMGNTVIWKPSITQTLAAYLTMQLLEAAGLPPGVINLV 241
Cdd:COG0506 609 PPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLG 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 242 TGDGFAVSDVALADPRLAGIHFTGSTATFGHLWQWVGTNIGRyhsyPRLVGETGGKDFVVAHASARPDVLRTALIRGAFD 321
Cdd:COG0506 689 AGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAA----AAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASA 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 322 YQGQKCSAVSRAFIAHSVWQRMGDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKGAAAVTVAVGGEYDD 401
Cdd:COG0506 765 SASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVP 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 402 SEGYFVRPTVLLSDDPTDESFVIEYFGPLLSVHVYPDERYEQILDVIDTGSRYALTGAVIADDRQAVLTAldrlRFAAGN 481
Cdd:COG0506 845 GLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRV----GGGGGG 920
|
490 500 510
....*....|....*....|....*....|....*..
gi 489997281 482 FYVNDKPTGAVVGRQPFGGARGSGTNDKAGSPLNLLR 518
Cdd:COG0506 921 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLAL 957
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
173-505 |
4.33e-09 |
|
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: 58.67 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 173 RIDYRPLdGFVYAITPFNFT----------SIAGnlptapalmGNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVT 242
Cdd:cd07136 95 YIYYEPY-GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 243 GDGfAVSDvALADPRLAGIHFTGSTAtfghlwqwVGTNIGRyHSYPRLVG---ETGGKDFVVAHASARpdvLRTALIR-- 317
Cdd:cd07136 164 GGV-EENQ-ELLDQKFDYIFFTGSVR--------VGKIVME-AAAKHLTPvtlELGGKSPCIVDEDAN---LKLAAKRiv 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 318 -GAFDYQGQKCSAVSRAFIAHSVWQRMgDELLAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKgaaavtVAVG 396
Cdd:cd07136 230 wGKFLNAGQTCVAPDYVLVHESVKEKF-IKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK------IVFG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 397 GEYDDSEGYfVRPTVLlsDDPTDESFVI--EYFGPLLSVHVypderYEQILDVIDTGSRYA--LTGAVIADDRQAVLTAL 472
Cdd:cd07136 303 GNTDRETLY-IEPTIL--DNVTWDDPVMqeEIFGPILPVLT-----YDTLDEAIEIIKSRPkpLALYLFSEDKKVEKKVL 374
|
330 340 350
....*....|....*....|....*....|...
gi 489997281 473 DRLRFAAGnfYVNDKPTGAVVGRQPFGGARGSG 505
Cdd:cd07136 375 ENLSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
206-433 |
3.34e-04 |
|
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: 43.24 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 206 GNTVIWKPSITQTLAAYLTMQ----LLEAAGLPPGVINLVTGDGFAVSDVALA-DPRLAGIHFTGSTAtFGhlwQWVGTN 280
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQvareVLAEAGFDPNLVTLAADTPEEPIAQTLAtRPEVRIIDFTGSNA-FG---DWLEAN 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 281 IGRYHSYPrlvgETGGKDFVVAHASARPDVLRTALIRGAFDYQGQKCSA-----VSRAFIAHSVWQRMGDEL---LAKAA 352
Cdd:cd07127 297 ARQAQVYT----EKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTpqniyVPRDGIQTDDGRKSFDEVaadLAAAI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 353 ELRYGDITDLSNYGGALIDQRAfvknVDAIERAKGAAAVTVAVGG-EYDDSEGYFVRPTVLLSDDPTDES-FVIEYFGPL 430
Cdd:cd07127 373 DGLLADPARAAALLGAIQSPDT----LARIAEARQLGEVLLASEAvAHPEFPDARVRTPLLLKLDASDEAaYAEERFGPI 448
|
...
gi 489997281 431 LSV 433
Cdd:cd07127 449 AFV 451
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
178-505 |
7.60e-04 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 42.34 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 178 PLdGFVYAITPFNFTSIAGNLPTAPAL-MGNTVIWKPSITQTLAAYLTMQLLEAAgLPPGVINLVTGdgfAVSDV-ALAD 255
Cdd:PLN02174 112 PL-GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG---AVTETtALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 256 PRLAGIHFTGSTatfghlwqwvgtNIGRY-------HSYPrLVGETGGKDFVVAHASARPDVLRTALIRGAFD-YQGQKC 327
Cdd:PLN02174 187 QKWDKIFYTGSS------------KIGRVimaaaakHLTP-VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQAC 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 328 SAVSRAFIAHSVWQRMGDELlAKAAELRYGDITDLSNYGGALIDQRAFVKNVDAIERAKgaAAVTVAVGGEyDDSEGYFV 407
Cdd:PLN02174 254 ISPDYILTTKEYAPKVIDAM-KKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKE--VSDKIVYGGE-KDRENLKI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489997281 408 RPTVLLsDDPTDeSFVI--EYFGPLLSVhVYPDERYEQiLDVIDTGSRyALTGAVIADDRQAvltaldRLRFA----AGN 481
Cdd:PLN02174 330 APTILL-DVPLD-SLIMseEIFGPLLPI-LTLNNLEES-FDVIRSRPK-PLAAYLFTHNKKL------KERFAatvsAGG 398
|
330 340
....*....|....*....|....
gi 489997281 482 FYVNDKPTGAVVGRQPFGGARGSG 505
Cdd:PLN02174 399 IVVNDIAVHLALHTLPFGGVGESG 422
|
|
| |
