|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
41-563 |
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: 997.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 41 IANEPILGYLKDSKERKALEQALKGTASSCEDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVE 120
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 121 TQPKWDRVSIADRLKIWEKAADLMATTYRQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISENiK 200
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSP-A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 201 VTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVF 280
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 281 GDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCS 360
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 361 ACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGGTYSDSKGYFVN 440
Cdd:cd07123 320 AASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 441 PTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDLLETMKLVHTSTKFALTGAVFGQDEDFVKCALQEFKMAAGNFYINDKS 520
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 320546182 521 TGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETFVP 563
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
42-572 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 795.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 42 ANEPILGYLKDSKERKALEQALKGTASSCEDIPIVIGGKEYKTPEVR-YQVMPHDHQHKLASFYYADKKLIEKAIKTAVE 120
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERiPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 121 TQPKWDRVSIADRLKIWEKAADLMATTYRQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISenIK 200
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPIS--AP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 201 VTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVF 280
Cdd:TIGR01236 159 GEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 281 GDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCS 360
Cdd:TIGR01236 239 SDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 361 ACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSP-NLEILAGGTYSDSKGYFV 439
Cdd:TIGR01236 319 AASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPeALTILYGGKYDDSQGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 440 NPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDLLETMKLVHTSTKFALTGAVFGQDEDFVKCALQEFKMAAGNFYINDK 519
Cdd:TIGR01236 399 EPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDK 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 520 STGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETFVPLRDVNYPYM 572
Cdd:TIGR01236 479 CTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYM 531
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
56-561 |
0e+00 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 562.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 56 RKALEQALKGTASS-CEDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRL 134
Cdd:cd07083 1 RRAMREALRRVKEEfGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 135 KIWEKAADLMATTYRQDLNAATMLGqSKTAIQaEIDSAAELIDFIRMNAYFLKEVTKYQPISENIKVTKNSLRYRGIdGF 214
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 215 IAAVSPFNFT-AIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGI 293
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 294 NFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWP 373
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 374 QIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpnLEILAGGTYSDSKGYFVNPTIVLSKDPKDRI 453
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE--GQLVLGGKRLEGEGYFVAPTVVEEVPPKARI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 454 MTEEIFGPVLSIYVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFkmAAGNFYINDKSTGSVVGQQPFGGG 533
Cdd:cd07083 396 AQEEIFGPVLSVIRYKDDDFAEALEVAN-STPYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGF 472
|
490 500
....*....|....*....|....*...
gi 320546182 534 RMSGTNDKAGGPHYILRWTSPQSIKETF 561
Cdd:cd07083 473 KLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
43-561 |
9.21e-131 |
|
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: 391.97 E-value: 9.21e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 43 NEPILGYlKDSKERKALEQALKGTASSC-EDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVET 121
Cdd:cd07124 3 NEPFTDF-ADEENRAAFRAALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 122 QPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQAEIDsAAELIDFIRmnaYFLKEVTKYQP-ISENIK 200
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALL-RRRRFELAAWMVLEVGKNWAEADAD-VAEAIDFLE---YYAREMLRLRGfPVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 201 VTKNSLRYRGIdGFIAAVSPFNF-TAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPV 279
Cdd:cd07124 157 GEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 280 FGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKC 359
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 360 SACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLeiLAGGTYSD--SKGY 437
Cdd:cd07124 316 SACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLElaAEGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 438 FVNPTIVLSKDPKDRIMTEEIFGPVLSiyVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFKmaAGNFYIN 517
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLA--VIKAKDFDEALEIAN-DTEYGLTGGVFSRSPEHLERARREFE--VGNLYAN 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 320546182 518 DKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETF 561
Cdd:cd07124 469 RKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
71-561 |
1.35e-129 |
|
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: 387.56 E-value: 1.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 71 EDIPIVIGGKEYKTPEVRYQ--VMPHDhQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtY 148
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 149 RQDLNAATMLGQSKTAIQAEIDsAAELIDFIRMNAYFLKEVTKYQpISENIKVTKNSLRYRGIdGFIAAVSPFNFTAIGG 228
Cdd:COG1012 82 REELAALLTLETGKPLAEARGE-VDRAADFLRYYAGEARRLYGET-IPSDAPGTRAYVRREPL-GVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 229 NLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWK 307
Cdd:COG1012 159 AWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 308 QVGNNIdnyvnfPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLK 387
Cdd:COG1012 239 AAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 388 IGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGGTY-SDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIY 466
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDA-VAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 467 VYKesDLLETMKLVHtSTKFALTGAVFGQDEDfvkcALQEF--KMAAGNFYINDKSTGsVVGQQPFGGGRMSGTNDKaGG 544
Cdd:COG1012 392 PFD--DEEEAIALAN-DTEYGLAASVFTRDLA----RARRVarRLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGRE-GG 462
|
490
....*....|....*..
gi 320546182 545 PHYILRWTSPQSIKETF 561
Cdd:COG1012 463 REGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
93-557 |
7.94e-118 |
|
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: 356.84 E-value: 7.94e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 93 PHDhQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtYRQDLNAATMLGQSKTAIQA--EID 170
Cdd:pfam00171 14 PAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEE-RKDELAELETLENGKPLAEArgEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 171 SAaelIDFIRmnaYFLKEVTKYQPISENIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTA 249
Cdd:pfam00171 92 RA---IDVLR---YYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAaGNTVVLKPSELT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 MLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvnFPRLTGECGGK 329
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN------LKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 330 NFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKR 409
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 410 ITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALT 489
Cdd:pfam00171 320 VLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAN-DTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546182 490 GAVFGQDED-FVKCALQefkMAAGNFYINDKSTGSVVGqQPFGGGRMSGTNDKaGGPHYILRWTSPQSI 557
Cdd:pfam00171 396 AGVFTSDLErALRVARR---LEAGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
112-557 |
9.98e-115 |
|
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: 348.04 E-value: 9.98e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 112 EKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSKTAIQAEIDSAAELIDfirmnaYFLKE 188
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEE--RREELAALEtleTGKPIEEALGEVARAADTFR------YYAGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 189 VTKY--QPISENIKVTKNSLRYRGIdGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGV 265
Cdd:cd07078 73 ARRLhgEVIPSPDPGELAIVRREPL-GVVGAITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALLLAELLAEAGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 266 PDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIdnyvnfPRLTGECGGKNFHFIHASADVESVVT 345
Cdd:cd07078 152 PPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 346 STIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPnLEI 425
Cdd:cd07078 226 GAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-AKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 426 LAGGTYSDS-KGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALTGAVFGQDEDFVKCAL 504
Cdd:cd07078 305 LCGGKRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFK--DEEEAIELAN-DTEYGLAAGVFTRDLERALRVA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 505 QEFKmaAGNFYINDKSTGsVVGQQPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd07078 382 ERLE--AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
40-561 |
1.00e-112 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 345.38 E-value: 1.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 40 PIANEPILGYlKDSKERKALEQALKGTASSC-EDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTA 118
Cdd:PRK03137 4 PYKHEPFTDF-SVEENVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 119 VETQPKWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKTAIQAEIDsAAELIDFIRmnaYFLKEVTKYqpiSEN 198
Cdd:PRK03137 83 LEAFETWKKWSPEDRARILLRAAAIIRRR-KHEFSAWLVKEAGKPWAEADAD-TAEAIDFLE---YYARQMLKL---ADG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 199 IKVT-----KNSLRYRGIdGFIAAVSPFNF-TAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNF 272
Cdd:PRK03137 155 KPVEsrpgeHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 273 VPADGPVFGDTITASPHLAGINFTGSvptfnrlwKQVGNNI--------DNYVNFPRLTGECGGKNFHFIHASADVESVV 344
Cdd:PRK03137 234 VPGSGSEVGDYLVDHPKTRFITFTGS--------REVGLRIyeraakvqPGQIWLKRVIAEMGGKDAIVVDEDADLDLAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 345 TSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFsSFTSAVIDDKAFKRITGYIEHAKKSPNLe 424
Cdd:PRK03137 306 ESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEGRL- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 425 iLAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSiyVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCAL 504
Cdd:PRK03137 384 -VLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA--FIKAKDFDHALEIAN-NTEYGLTGAVISNNREHLEKAR 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 320546182 505 QEFKmaAGNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETF 561
Cdd:PRK03137 460 REFH--VGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
43-561 |
7.36e-102 |
|
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: 317.58 E-value: 7.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 43 NEPILGYlKDSKERKALEQALKGTASSC-EDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVET 121
Cdd:TIGR01237 3 HEPFTDF-ADEENRQAFFKALATVKEQLgKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 122 QPKWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKTAIQAEIDSAaELIDFIRmnaYFLKEVTKYQPISEN--I 199
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAEVA-EAIDFME---YYARQMIELAKGKPVnsR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 200 KVTKNSLRYRGIdGFIAAVSPFNFT-AIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGP 278
Cdd:TIGR01237 157 EGETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 279 VFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQK 358
Cdd:TIGR01237 236 EVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 359 CSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPnlEILAGGTYSDSKGYF 438
Cdd:TIGR01237 316 CSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG--RLVSGGCGDDSKGYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 439 VNPTIVLSKDPKDRIMTEEIFGPVLSIYvyKESDLLETMKlVHTSTKFALTGAVFGQDEDFVKCALQEFKMaaGNFYIND 518
Cdd:TIGR01237 394 IGPTIFADVDRKARLAQEEIFGPVVAFI--RASDFDEALE-IANNTEYGLTGGVISNNRDHINRAKAEFEV--GNLYFNR 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 320546182 519 KSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETF 561
Cdd:TIGR01237 469 NITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
71-550 |
1.24e-99 |
|
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: 311.82 E-value: 1.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 71 EDIPIVIGGKEykTPEVRYQVM-PHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTyR 149
Cdd:cd07125 32 EAIPIINGEET--ETGEGAPVIdPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAN-R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 150 QDLNAATMLGQSKTAIQAeIDSAAELIDFIRMNAY----FLKEVTKYQPISENikvtkNSLRYRGiDGFIAAVSPFNF-- 223
Cdd:cd07125 109 GELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAqareLFSDPELPGPTGEL-----NGLELHG-RGVFVCISPWNFpl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 224 -TAIGGNLSytpALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPT 301
Cdd:cd07125 182 aIFTGQIAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 302 ---FNRlwkqvgNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEG 378
Cdd:cd07125 259 aklINR------ALAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 379 LVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLeiLAGGTYSDSKGYFVNPTIVlsKDPKDRIMTEEI 458
Cdd:cd07125 333 LKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYFVAPGII--EIVGIFDLTTEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 459 FGPVLSIYVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFKmaAGNFYINDKSTGSVVGQQPFGGGRMSGT 538
Cdd:cd07125 409 FGPILHVIRFKAEDLDEAIEDIN-ATGYGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQPFGGWGLSGT 485
|
490
....*....|..
gi 320546182 539 NDKAGGPHYILR 550
Cdd:cd07125 486 GPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
116-557 |
3.97e-86 |
|
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: 271.80 E-value: 3.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 116 KTAVETQPKWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKTAIQAEIDsAAELIDFIRmnaYFLKEVTKYQ-- 193
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGE-VARAIDTFR---YAAGLADKLGgp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 194 PISENIKVTKNSLRYRGIdGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNF 272
Cdd:cd06534 76 ELPSPDPGGEAYVRREPL-GVVGVITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 273 VPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNnidnyvNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAF 352
Cdd:cd06534 155 VPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE------NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 353 EYCGQKCSACSRMYVPESLWPQIKEGLVceaaklkigdvqdfssftsaviddkafkritgyiehakkspnleilaggtys 432
Cdd:cd06534 229 FNAGQICTAASRLLVHESIYDEFVEKLV---------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 433 dskgyfvnpTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDEDFVKCALQEfkMAAG 512
Cdd:cd06534 257 ---------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEE--EAIALAN-DTEYGLTAGVFTRDLNRALRVAER--LRAG 322
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320546182 513 NFYINDKSTGsVVGQQPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd06534 323 TVYINDSSIG-VGPEAPFGGVKNSGIG-REGGPYGLEEYTRTKTV 365
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
50-557 |
9.87e-75 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 257.05 E-value: 9.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 50 LKDSKERKALEQALKGTASSCEDIPIVIGGkeykTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVS 129
Cdd:PRK11904 530 LNDRSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTP 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 130 IADRLKIWEKAADLMattyrqDLNAATML-------GqsKTaIQAEIDSAAELIDFIRmnaYFLKEVTK--YQPIS---- 196
Cdd:PRK11904 606 VEERAAILERAADLL------EANRAELIalcvreaG--KT-LQDAIAEVREAVDFCR---YYAAQARRlfGAPEKlpgp 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 197 --ENikvtkNSLRYRGiDGFIAAVSPFNFT-AI-GGNLsyTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVN 271
Cdd:PRK11904 674 tgES-----NELRLHG-RGVFVCISPWNFPlAIfLGQV--AAALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQ 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 272 FVPADGPVFGDTITASPHLAGINFTGSVPT---FNRLWKQVGNNIdnyvnFPrLTGECGGKNFHFIHASADVESVVTSTI 348
Cdd:PRK11904 746 LLPGDGATVGAALTADPRIAGVAFTGSTETariINRTLAARDGPI-----VP-LIAETGGQNAMIVDSTALPEQVVDDVV 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 349 RSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLeiLAG 428
Cdd:PRK11904 820 TSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARL--LAQ 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 429 GTYSDS--KGYFVNPTIVLSKDPKDriMTEEIFGPVLSIYVYKESDLLetmKLVHT--STKFALTGAVFGQDEDFVKcAL 504
Cdd:PRK11904 898 LPLPAGteNGHFVAPTAFEIDSISQ--LEREVFGPILHVIRYKASDLD---KVIDAinATGYGLTLGIHSRIEETAD-RI 971
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 505 QEfKMAAGNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSI 557
Cdd:PRK11904 972 AD-RVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-550 |
1.58e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 237.53 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 50 LKDSKERKALEQALKGTASSCEDIPIVIGGKeyKTPEVRYQVM-PHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRV 128
Cdd:COG4230 535 LSDEAVLAALSAALAAAAEKQWQAAPLIAGE--AASGEARPVRnPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSAT 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 129 SIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKT---AIqAEIDSAaelIDFIRmnaYFLKEVtkyqpisENIKVTKNS 205
Cdd:COG4230 613 PVEERAAILERAADLL-EAHRAELMALLVREAGKTlpdAI-AEVREA---VDFCR---YYAAQA-------RRLFAAPTV 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 206 LRYRGIdgfIAAVSPFNF---------TAiggnlsytpALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPA 275
Cdd:COG4230 678 LRGRGV---FVCISPWNFplaiftgqvAA---------ALAaGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPG 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 276 DGPVFGDTITASPHLAGINFTGSVPT---FNRLWKQVGNNIdnyvnfPRLTGECGGKNFHFIHASADVESVVTSTIRSAF 352
Cdd:COG4230 746 DGETVGAALVADPRIAGVAFTGSTETarlINRTLAARDGPI------VPLIAETGGQNAMIVDSSALPEQVVDDVLASAF 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 353 EYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLeiLAGGTYS 432
Cdd:COG4230 820 DSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRL--VHQLPLP 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 433 DS--KGYFVNPTIVLSKDPKDriMTEEIFGPVLSIYVYKESDLletMKLVHT--STKFALTGAVFGQDEDFVKCALQefK 508
Cdd:COG4230 898 EEcaNGTFVAPTLIEIDSISD--LEREVFGPVLHVVRYKADEL---DKVIDAinATGYGLTLGVHSRIDETIDRVAA--R 970
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 320546182 509 MAAGNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILR 550
Cdd:COG4230 971 ARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
76-546 |
2.87e-66 |
|
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: 223.28 E-value: 2.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 76 VIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTyRQDLNAA 155
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEAR-KEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 156 TMLGQSKT---AIqAEIDSAAELIDFIRMNAYFLKEVTkYQPISEN--IKVTKNSLryrgidGFIAAVSPFNF-TAIGGn 229
Cdd:cd07097 83 LTREEGKTlpeAR-GEVTRAGQIFRYYAGEALRLSGET-LPSTRPGveVETTREPL------GVVGLITPWNFpIAIPA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 230 LSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQ 308
Cdd:cd07097 154 WKIAPALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 309 VGNnidnyvNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKI 388
Cdd:cd07097 234 AAA------RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 389 GDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNlEILAGGT--YSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSiy 466
Cdd:cd07097 308 GDALDEGVDIGPVVSERQLEKDLRYIEIARSEGA-KLVYGGErlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAA-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 467 VYKESDLLETMKLVHtSTKFALTGAVFGQDedfVKCAlQEFK--MAAGNFYINDKSTGsVVGQQPFGGGRMSGTNDKAGG 544
Cdd:cd07097 385 VIRVRDYDEALAIAN-DTEFGLSAGIVTTS---LKHA-THFKrrVEAGVVMVNLPTAG-VDYHVPFGGRKGSSYGPREQG 458
|
..
gi 320546182 545 PH 546
Cdd:cd07097 459 EA 460
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
50-554 |
5.76e-61 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 218.58 E-value: 5.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 50 LKDSKERKALEQALKGTASSC-EDIPIVIGGKeykTPEVRYQVM-PHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDR 127
Cdd:PRK11905 532 LSDEATLAALDEALNAFAAKTwHAAPLLAGGD---VDGGTRPVLnPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 128 VSIADRLKIWEKAADLMATTYrQDLNAATMLGQSKTAIQAeIDSAAELIDFIRmnaYFLKEVTKYqpisenikVTKNSLR 207
Cdd:PRK11905 609 TPAAERAAILERAADLMEAHM-PELFALAVREAGKTLANA-IAEVREAVDFLR---YYAAQARRL--------LNGPGHK 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 208 YRGIdgfIAAVSPFNFT-AI-GGNLSytPALM-GNGVLWKPSDTAMLsnwIIF---KIMREAGVPDGVVNFVPADGPVFG 281
Cdd:PRK11905 676 PLGP---VVCISPWNFPlAIfTGQIA--AALVaGNTVLAKPAEQTPL---IAAravRLLHEAGVPKDALQLLPGDGRTVG 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 282 DTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVnfPrLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSA 361
Cdd:PRK11905 748 AALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPV--P-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 362 CSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKspnleilAGGTY-------SDS 434
Cdd:PRK11905 825 LRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRA-------AGRLVhqlplpaETE 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 435 KGYFVNPTIVLSKDPKDriMTEEIFGPVLSIYVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFKmaAGNF 514
Cdd:PRK11905 898 KGTFVAPTLIEIDSISD--LEREVFGPVLHVVRFKADELDRVIDDIN-ATGYGLTFGLHSRIDETIAHVTSRIR--AGNI 972
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 320546182 515 YINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSP 554
Cdd:PRK11905 973 YVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
106-538 |
1.61e-60 |
|
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: 207.42 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQA---EIDSAAElidfirmN 182
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLI-EARADELALLESLDTGKPITLArtrDIPRAAA-------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 183 AYFLKEVTKYQPiSENIKVTKNSLRY--RGIDGFIAAVSPFNF--------TAiggnlsytPAL-MGNGVLWKPSDTAML 251
Cdd:cd07093 88 FRFFADYILQLD-GESYPQDGGALNYvlRQPVGVAGLITPWNLplmlltwkIA--------PALaFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 252 SNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGnnidnyVNFPRLTGECGGKNF 331
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA------PNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 332 HFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRIT 411
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 412 GYIEHAKKSpNLEILAGG----TYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFA 487
Cdd:cd07093 313 GYVELARAE-GATILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEE--EAIELAN-DTPYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 320546182 488 LTGAVFGQDED---FVKCALQefkmaAGNFYIN-----DKSTgsvvgqqPFGGGRMSGT 538
Cdd:cd07093 389 LAAYVWTRDLGrahRVARRLE-----AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
41-555 |
2.55e-60 |
|
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: 208.23 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 41 IANEPILGYLKdskerkalEQALKGTASSCEDIPIvIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVE 120
Cdd:TIGR01238 15 LDNESELKPLE--------AQIHAWADKTWQAAPI-IGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 121 TQPKWDRVSIADRLKIWEKAADLMattyrqDLNAATMLG----QSKTAIQAEIDSAAELIDFIRmnaYFLKEVTKYQPis 196
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLL------ELHMPELMAlcvrEAGKTIHNAIAEVREAVDFCR---YYAKQVRDVLG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 197 enikvtKNSLRYRGIdgfIAAVSPFNFT-AI-GGNLSYTPAlMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVP 274
Cdd:TIGR01238 155 ------EFSVESRGV---FVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 275 ADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFprlTGECGGKNFHFIHASADVESVVTSTIRSAFEY 354
Cdd:TIGR01238 225 GRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 355 CGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEH--AKKSPNLEILAGGTYS 432
Cdd:TIGR01238 302 AGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHmsQTQKKIAQLTLDDSRA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 433 DSKGYFVNPTIVLSKDPKDriMTEEIFGPVLSIYVYKESDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFKmaAG 512
Cdd:TIGR01238 382 CQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKARELDQIVDQIN-QTGYGLTMGVHSRIETTYRWIEKHAR--VG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 320546182 513 NFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQ 555
Cdd:TIGR01238 457 NCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
112-553 |
2.98e-59 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 203.72 E-value: 2.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 112 EKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVT- 190
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIMER--RADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 191 -KYQPISEnikvTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDG 268
Cdd:cd07150 102 eTLPSDSP----GTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 269 VVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGnnidnyVNFPRLTGECGGKNFHFIHASADVESVVTSTI 348
Cdd:cd07150 178 VFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 349 RSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAG 428
Cdd:cd07150 252 FGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA-VAKGAKLLTG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 429 GTYSdskGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALTGAVFGQDEDfvkcalQEFK 508
Cdd:cd07150 331 GKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAK--DAEEALELAN-DTEYGLSAAILTNDLQ------RAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 320546182 509 MA----AGNFYINDkSTGSVVGQQPFGGGRMSGTNdKAGGPHYI-----LRWTS 553
Cdd:cd07150 399 LAerleSGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
86-538 |
6.16e-58 |
|
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: 200.51 E-value: 6.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 86 EVRYqvmPHDhQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSK 162
Cdd:cd07149 2 EVIS---PYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEE--RREEFARTIaleAGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 163 TAIQAEIDSAAELIDF------------IRMNAYflkevtkyqPISENikvtKNSLRYRGIDGFIAAVSPFNFTAiggNL 230
Cdd:cd07149 76 KDARKEVDRAIETLRLsaeeakrlagetIPFDAS---------PGGEG----RIGFTIREPIGVVAAITPFNFPL---NL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 231 S---YTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVptfnrlw 306
Cdd:cd07149 140 VahkVGPAIAaGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSP------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 307 kQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKL 386
Cdd:cd07149 213 -AVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 387 KIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSdskGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIY 466
Cdd:cd07149 292 VVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEG-GARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLN 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320546182 467 VYKesDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSvVGQQPFGGGRMSGT 538
Cdd:cd07149 368 PFD--TLDEAIAMAN-DSPYGLQAGVFTNDLQKALKAARE--LEVGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
93-557 |
7.57e-57 |
|
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: 197.66 E-value: 7.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 93 PHDHQhKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQAEIDSA 172
Cdd:cd07115 4 PATGE-LIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELI-LANADELARLESLDTGKPIRAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 173 AELIDFIRmnaYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTA 249
Cdd:cd07115 82 PRAADTFR---YYAGWADKIE--GEVIPVRGPFLNYtvREPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 MLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGnnidnyVNFPRLTGECGGK 329
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA------GNLKRVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 330 NFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKR 409
Cdd:cd07115 231 SANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 410 ITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALT 489
Cdd:cd07115 311 VLDYVDVGREE-GARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE--EALRIAN-GTEYGLA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320546182 490 GAVFGQdeDFVKCALQEFKMAAGNFYINdkSTGSVVGQQPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd07115 387 AGVWTR--DLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSV 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
111-553 |
2.06e-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: 195.83 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATMLGQS-KTAIQAEIDsAAELIDFIRMNAYFLKEV 189
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEE--RRDEIADWLIRESgSTRPKAAFE-VGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 190 T-KYQPISENIKVtknSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPS-DTAMLSNWIIFKIMREAGVP 266
Cdd:cd07104 79 EgEILPSDVPGKE---SMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 267 DGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNnidnyvNFPRLTGECGGKNFHFIHASADVESVVTS 346
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR------HLKKVALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 347 TIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEIL 426
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAA-GARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 427 AGGTYSdskGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVhTSTKFALTGAVFGQDEDF-VKCALQ 505
Cdd:cd07104 309 TGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFD--DDEEAVELA-NDTEYGLSAAVFTRDLERaMAFAER 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 506 efkMAAGNFYINDKST--GSVVgqqPFGGGRMSGTnDKAGGPHYI-----LRWTS 553
Cdd:cd07104 383 ---LETGMVHINDQTVndEPHV---PFGGVKASGG-GRFGGPASLeefteWQWIT 430
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
112-537 |
2.33e-56 |
|
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: 196.57 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 112 EKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSKT---AIQAE-----IDSAAELIDFIR 180
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYEA--RADELAQAItleMGAPITlarAAQVGlgighLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 181 MNAYFLKEVTKYQPIsenikvtknslryrgidGFIAAVSPFNFTA--IGGNLSytPALM-GNGVLWKPSDTAMLSNWIIF 257
Cdd:cd07138 117 FEERRGNSLVVREPI-----------------GVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 258 KIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSvptfNRLWKQVGNNIDNYVNfpRLTGECGGKNFHFIHAS 337
Cdd:cd07138 178 EILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGS----TRAGKRVAEAAADTVK--RVALELGGKSANIILDD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 338 ADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHA 417
Cdd:cd07138 252 ADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 418 KKSpNLEILAGGTYSD---SKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGAVFG 494
Cdd:cd07138 332 IEE-GARLVAGGPGRPeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY--DDEDEAIAIAN-DTPYGLAGYVWS 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320546182 495 QDEDfvkcALQEF--KMAAGNFYINDkstGSVVGQQPFGGGRMSG 537
Cdd:cd07138 408 ADPE----RARAVarRLRAGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
100-537 |
4.02e-56 |
|
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: 195.60 E-value: 4.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDlNAATM----LGQSKTAIQAEIDSAAEL 175
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRE--RND-EIARLetidNGKPIEEARVDIDSSADC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 176 IDfirmnaYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLS 252
Cdd:cd07090 87 LE------YYAGLAPTLS--GEHVPLPGGSFAYtrREPLGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 253 NWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFH 332
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 333 FIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITG 412
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 413 YIEHAKKSpNLEILAGGTYSDSK-----GYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFA 487
Cdd:cd07090 312 YIESAKQE-GAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE--EVIRRAN-DTTYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 488 LTGAVFGQD---EDFVKCALQefkmaAGNFYINDKSTGSVvgQQPFGGGRMSG 537
Cdd:cd07090 388 LAAGVFTRDlqrAHRVIAQLQ-----AGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
106-557 |
9.71e-56 |
|
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: 194.28 E-value: 9.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtYRQDLnaATML----GQSKTAIQAEIDSAAeliDFIRM 181
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEA-NAEEL--ARLLtleqGKPLAEAQFEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 182 NAYFLKEVTKYQPiSENIKVtknSLRYRGIdGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIM 260
Cdd:cd07106 90 TASLDLPDEVIED-DDTRRV---ELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLCTLKLGELA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 261 REAgVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADV 340
Cdd:cd07106 165 QEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 341 ESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKS 420
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 421 pNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGAVFGQDEDfv 500
Cdd:cd07106 317 -GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARAN-DSEYGLGASVWSSDLE-- 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320546182 501 kcalQEFKMA----AGNFYINdkSTGSVVGQQPFGGGRMSGtNDKAGGPHYILRWTSPQSI 557
Cdd:cd07106 391 ----RAEAVArrleAGTVWIN--THGALDPDAPFGGHKQSG-IGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
99-546 |
4.14e-55 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 193.25 E-value: 4.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQA--EIDSAAELI 176
Cdd:cd07088 25 VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI-RENADELAKLIVEEQGKTLSLArvEVEFTADYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 177 DFIRMNAYFLK-EVTKYQPISENIKVTKNSLryrgidGFIAAVSPFNFTA--IGGNLSytPALM-GNGVLWKPSDTAMLS 252
Cdd:cd07088 104 DYMAEWARRIEgEIIPSDRPNENIFIFKVPI------GVVAGILPWNFPFflIARKLA--PALVtGNTIVIKPSEETPLN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 253 NWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIdnyvnfPRLTGECGGKNFH 332
Cdd:cd07088 176 ALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLELGGKAPA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 333 FIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITG 412
Cdd:cd07088 250 IVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 413 YIEHAKKSpNLEILAGGTYSDS-KGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGA 491
Cdd:cd07088 330 MVERAVEA-GATLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAN-DSEYGLTSY 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 320546182 492 VFGQDEDFVKCALQEFKmaAGNFYINDKSTGSVvgqQPFGGG-RMSGTNDkAGGPH 546
Cdd:cd07088 406 IYTENLNTAMRATNELE--FGETYINRENFEAM---QGFHAGwKKSGLGG-ADGKH 455
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
114-538 |
6.96e-55 |
|
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: 192.18 E-value: 6.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 114 AIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATMLGQSKTAIQ---AEIDSAAELIdfiRMNAYFLKEVT 190
Cdd:cd07145 26 AIEVAEKAKDVMSNLPAYKRYKILMKVAELIER--RKEELAKLLTIEVGKPIKqsrVEVERTIRLF---KLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 191 KYQPISENIKVTKNSLRY--RGIDGFIAAVSPFNFTAiggNLS---YTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAG 264
Cdd:cd07145 101 GETIPVDAYEYNERRIAFtvREPIGVVGAITPFNFPA---NLFahkIAPAIaVGNSVVVKPSSNTPLTAIELAKILEEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 265 VPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNnidnyvNFPRLTGECGGKNFHFIHASADVESVV 344
Cdd:cd07145 178 LPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVALELGGSDPMIVLKDADLERAV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 345 TSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNlE 424
Cdd:cd07145 252 SIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGG-K 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 425 ILAGGTYSDskGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDedfVKCAL 504
Cdd:cd07145 331 ILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE--EAVEIAN-STEYGLQASVFTND---INRAL 402
|
410 420 430
....*....|....*....|....*....|....*...
gi 320546182 505 qefKMA----AGNFYINDkSTGSVVGQQPFGGGRMSGT 538
Cdd:cd07145 403 ---KVAreleAGGVVIND-STRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
77-557 |
1.15e-54 |
|
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: 192.18 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 77 IGGK--EYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNA 154
Cdd:cd07131 3 IGGEwvDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKK--RKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 155 ATM---LGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISEnikvtKNSLRYRGIDGFIAAVSPFNF-TAIGGNL 230
Cdd:cd07131 81 RLVtreMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPN-----KDAMTRRQPIGVVALITPWNFpVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 231 SYtPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQV 309
Cdd:cd07131 156 IF-PALVcGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 310 GNNidnyvnFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIG 389
Cdd:cd07131 235 ARP------NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 390 DVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGGTYSD----SKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSI 465
Cdd:cd07131 309 DGLDEETDMGPLINEAQLEKVLNYNEIG-KEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVAL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 466 YvykESDLLETMKLVHTSTKFALTGAVFgqDEDFVKCALQEFKMAAGNFYINDKSTGSVVgQQPFGGGRMSGTNDKAGGP 545
Cdd:cd07131 388 I---EVSSLEEAIEIANDTEYGLSSAIY--TEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGT 461
|
490
....*....|..
gi 320546182 546 HYILRWTSPQSI 557
Cdd:cd07131 462 TALDAFTEWKAV 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
100-537 |
3.04e-54 |
|
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: 190.34 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLnAATM-------LGQSKtaiqAEIDSA 172
Cdd:cd07103 10 IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI-RERAEDL-ARLLtleqgkpLAEAR----GEVDYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 173 AELIDF-------------------IRMnayflkeVTKYQPIsenikvtknslryrgidGFIAAVSPFNFtaiggnlsyt 233
Cdd:cd07103 84 ASFLEWfaeearriygrtipspapgKRI-------LVIKQPV-----------------GVVAAITPWNF---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 234 PALM-----------GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTF 302
Cdd:cd07103 130 PAAMitrkiapalaaGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 303 NRLWKQVGNNIDnyvnfpRLTGECGGkNFHFI-HASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVC 381
Cdd:cd07103 210 KLLMAQAADTVK------RVSLELGG-NAPFIvFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 382 EAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGP 461
Cdd:cd07103 283 RVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA-VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 462 VLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDedfVKCALQ-----EFKMAAgnfyINdksTGSVVG-QQPFGGGRM 535
Cdd:cd07103 362 VAPIIPFDTED--EVIARAN-DTPYGLAAYVFTRD---LARAWRvaealEAGMVG----IN---TGLISDaEAPFGGVKE 428
|
..
gi 320546182 536 SG 537
Cdd:cd07103 429 SG 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
99-537 |
2.57e-53 |
|
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: 188.57 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVET--QPKWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKT-AIQAEIDsAAEL 175
Cdd:cd07091 31 VICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERD-RDELAALESLDNGKPlEESAKGD-VALS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 176 IDFIRmnaYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLS 252
Cdd:cd07091 109 IKCLR---YYAGWADKIQ--GKTIPIDGNFLAYtrREPIGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 253 NWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvNFPRLTGECGGKNFH 332
Cdd:cd07091 184 ALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS-----NLKKVTLELGGKSPN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 333 FIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITG 412
Cdd:cd07091 259 IVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 413 YIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAV 492
Cdd:cd07091 339 YIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED--EVIERAN-DTEYGLAAGV 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 320546182 493 FGQDED---FVKCALQefkmaAGNFYINdksTGSVVGQQ-PFGGGRMSG 537
Cdd:cd07091 415 FTKDINkalRVSRALK-----AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
100-557 |
1.95e-52 |
|
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: 186.11 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVET-QPKWDRVSIADRLKIWEKAADLMATtYRQDLNAATMLGQSKTAIQAEIDSAAELIDF 178
Cdd:cd07113 28 IASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQSANF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 179 IRmnaYFLKEVTKYQpiSENIKVTKNSL---RY-----RGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTA 249
Cdd:cd07113 107 LR---YFAGWATKIN--GETLAPSIPSMqgeRYtaftrREPVGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 MLSNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGK 329
Cdd:cd07113 182 PLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT------RVTLELGGK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 330 NFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKR 409
Cdd:cd07113 255 NAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 410 ITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALT 489
Cdd:cd07113 335 VCSYLDDARAE-GDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE--ELIQLIN-DTPFGLT 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546182 490 GAVFGQDedfVKCALQEF-KMAAGNFYIN-----DKSTgsvvgqqPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd07113 411 ASVWTNN---LSKALRYIpRIEAGTVWVNmhtflDPAV-------PFGGMKQSGIG-REFGSAFIDDYTELKSV 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
213-537 |
3.54e-52 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 185.11 E-value: 3.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLA 291
Cdd:cd07112 126 GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNidnyvNFPRLTGECGGKNFHFIHASA-DVESVVTSTIRSAFEYCGQKCSACSRMYVPES 370
Cdd:cd07112 206 ALAFTGSTEVGRRFLEYSGQS-----NLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHES 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 371 LWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGG--TYSDSKGYFVNPTIVLSKD 448
Cdd:cd07112 281 IKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGkrVLTETGGFFVEPTVFDGVT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 449 PKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDEDfvkcalQEFKMA----AGNFYINDKSTGSV 524
Cdd:cd07112 360 PDMRIAREEIFGPVLSVITFDSEE--EAVALAN-DSVYGLAASVWTSDLS------RAHRVArrlrAGTVWVNCFDEGDI 430
|
330
....*....|...
gi 320546182 525 vgQQPFGGGRMSG 537
Cdd:cd07112 431 --TTPFGGFKQSG 441
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
78-537 |
3.80e-51 |
|
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: 182.99 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 78 GGKEYKTpevryqVMPHDHQhKLASFYYADKKLIEKAIKTAVET-QPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAAT 156
Cdd:cd07144 21 DGETIKT------VNPSTGE-VIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLV-EKNRDLLAAIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 157 MLGQSKTAIQAEIDSAAELIDFIRmnaYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTP 234
Cdd:cd07144 93 ALDSGKPYHSNALGDLDEIIAVIR---YYAGWADKIQ--GKTIPTSPNKLAYtlHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 235 ALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNI 313
Cdd:cd07144 168 ALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 314 DNyvnfprLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAK-LKIGDVQ 392
Cdd:cd07144 248 KA------VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 393 DFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYS---DSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYK 469
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKE-GAKLVYGGEKApegLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320546182 470 ESDllETMKLVHtSTKFALTGAVFGQD----EDFVKcalqefKMAAGNFYINDKSTGSVvgQQPFGGGRMSG 537
Cdd:cd07144 401 TYE--EAIKKAN-DTTYGLAAAVFTKDirraHRVAR------ELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
97-537 |
4.21e-50 |
|
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: 179.42 E-value: 4.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 97 QHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTYRQDLNA-ATMLGQSKTAIQAEIDSAael 175
Cdd:cd07151 20 GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWlIRESGSTRIKANIEWGAA--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 176 IDFIRMNAYFLKEVTKyqPISENIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKP-SDTAMLSN 253
Cdd:cd07151 97 MAITREAATFPLRMEG--RILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPaSDTPITGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 254 WIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPtfnrlwkqVGNNIDNYV--NFPRLTGECGGKNF 331
Cdd:cd07151 175 LLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTP--------VGRHIGELAgrHLKKVALELGGNNP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 332 HFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRIT 411
Cdd:cd07151 247 FVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 412 GYIEHAKKSpNLEILAGGtysDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGA 491
Cdd:cd07151 327 DKIEQAVEE-GATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE--EALELAN-DTEYGLSGA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 320546182 492 VFGQD-EDFVKCALQefkMAAGNFYINDKStgsvVGQQP---FGGGRMSG 537
Cdd:cd07151 400 VFTSDlERGVQFARR---IDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
93-537 |
4.48e-50 |
|
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: 179.69 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 93 PHDHQhKLASFYYADKKLIEKAIKTAVETQPKWDR-VSIADRLKIWEKAADLMaTTYRQDLNAATML--GQSKTAIQAEI 169
Cdd:cd07082 23 PIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLL-KENKEEVANLLMWeiGKTLKDALKEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 170 DSAaelIDFIRMNAYFLKEVTKYQPISENIKVTKNSLR--YRGIDGFIAAVSPFNFTAiggNLSYT---PAL-MGNGVLW 243
Cdd:cd07082 101 DRT---IDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAqvRREPLGVVLAIGPFNYPL---NLTVSkliPALiMGNTVVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 244 KPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvnfpRLT 323
Cdd:cd07082 175 KPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMK--------RLV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 324 GECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVID 403
Cdd:cd07082 247 LELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 404 DKAFKRITGYIEHAKKSpNLEILAGGTYsdSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHTS 483
Cdd:cd07082 327 PKSADFVEGLIDDAVAK-GATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN--DIEEAIELANKS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 320546182 484 tKFALTGAVFGQDEDfvKCALQEFKMAAGNFYINDKStgsvvgQQ-----PFGGGRMSG 537
Cdd:cd07082 402 -NYGLQASIFTKDIN--KARKLADALEVGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
93-537 |
4.51e-50 |
|
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: 179.17 E-value: 4.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 93 PHDHQHkLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADlMATTYRQDLNAATMLGQSKTAIQA--EID 170
Cdd:cd07094 6 PYDGEV-IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAAD-LLKKRAEEFAKIIACEGGKPIKDArvEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 171 SAaelIDFIRMNAYFLKEVTKYQPISENIKVTKNSLRY--RGIDGFIAAVSPFNFTAiggNLS---YTPAL-MGNGVLWK 244
Cdd:cd07094 84 RA---IDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWtiREPVGVVLAITPFNFPL---NLVahkLAPAIaTGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 245 PSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGnnidnyvnFPRLTG 324
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRIAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 325 ECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDD 404
Cdd:cd07094 230 ELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 405 KAFKRITGYIEHAKKSpNLEILAGGTYSDSkgyFVNPTiVLSKDPKD-RIMTEEIFGPVLSIYVYKESDllETMKLVHtS 483
Cdd:cd07094 310 EAAERVERWVEEAVEA-GARLLCGGERDGA---LFKPT-VLEDVPRDtKLSTEETFGPVVPIIRYDDFE--EAIRIAN-S 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 484 TKFALTGAVFGQDED-FVKCALqefKMAAGNFYINDkSTGSVVGQQPFGGGRMSG 537
Cdd:cd07094 382 TDYGLQAGIFTRDLNvAFKAAE---KLEVGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
91-537 |
6.52e-50 |
|
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: 178.71 E-value: 6.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 91 VMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATMLGQSKTAIQAE-I 169
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALETGNALRTQaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 170 DSAAELIDFIRMNAYFLKEVTkyqpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPS 246
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELK-----GETLPFGPDVLTYtvREPLGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 247 DTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGnnidnyvnfPRL---T 323
Cdd:cd07108 154 EDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLipvS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 324 GECGGKNFHFIHASADVESVVTSTIRSA-FEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVI 402
Cdd:cd07108 224 LELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 403 DDKAFKRITGYIEHAKKSPNLEILAGGTYS----DSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMK 478
Cdd:cd07108 304 SEKQFAKVCGYIDLGLSTSGATVLRGGPLPgegpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDED--EVIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320546182 479 LVHTSTkFALTGAVFGQDedfVKCALQEFK-MAAGNFYINDKstgsvVGQQP---FGGGRMSG 537
Cdd:cd07108 382 MANDSH-YGLAAYVWTRD---LGRALRAAHaLEAGWVQVNQG-----GGQQPgqsYGGFKQSG 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
111-538 |
1.08e-49 |
|
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: 178.34 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMattyRQDLNAATML-----GQSKTAIQAEIDSAAELIDFIRMNAYF 185
Cdd:cd07107 21 VDRAVAAARAAFPEWRATTPLERARMLRELATRL----REHAEELALIdaldcGNPVSAMLGDVMVAAALLDYFAGLVTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 186 LKevtkyqpiSENIKVTKNSLRY--RGIDGFIAAVSPFN----FTAigGNLSyTPALMGNGVLWKPSDTAMLSNWIIFKI 259
Cdd:cd07107 97 LK--------GETIPVGGRNLHYtlREPYGVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 260 MREAgVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASAD 339
Cdd:cd07107 166 AREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 340 VESVVTSTIRSA-FEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAk 418
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 419 KSPNLEILAGGTYSD----SKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFG 494
Cdd:cd07107 318 KREGARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQAN-GVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 320546182 495 QDEDfvkcalQEFKMA----AGNFYINDKST---GSvvgqqPFGGGRMSGT 538
Cdd:cd07107 395 NDIS------QAHRTArrveAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
213-557 |
2.15e-49 |
|
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: 177.43 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNF---TAIGgnlSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASP 288
Cdd:cd07089 125 GVVAAITPWNFpffLNLA---KLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 289 HLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVP 368
Cdd:cd07089 202 RVDMVSFTGSTAVGRRIMAQAAATLK------RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVP 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 369 ESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSDS--KGYFVNPTIVLS 446
Cdd:cd07089 276 RSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDE-GARLVTGGGRPAGldKGFYVEPTLFAD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 447 KDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALTGAVFGQDEDfvkcalQEFKMA----AGNFYINDKSTG 522
Cdd:cd07089 355 VDNDMRIAQEEIFGPVLVVIPYDDDD--EAVRIANDS-DYGLSGGVWSADVD------RAYRVArrirTGSVGINGGGGY 425
|
330 340 350
....*....|....*....|....*....|....*
gi 320546182 523 SVVGqqPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd07089 426 GPDA--PFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
106-537 |
3.66e-49 |
|
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: 177.50 E-value: 3.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPkWDRVSIADRLKIWEKAADLMattyRQDLNAATML---GQSKTAIQAEIDSAaeliDFIRMN 182
Cdd:cd07119 35 EDAKRAIAAARRAFDSGE-WPHLPAQERAALLFRIADKI----REDAEELARLetlNTGKTLRESEIDID----DVANCF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 183 AYFLKEVTKyqPISENIKVTKNSLRYR-----GIDGFIAavsPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWII 256
Cdd:cd07119 106 RYYAGLATK--ETGEVYDVPPHVISRTvrepvGVCGLIT---PWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 257 FKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvnFPRLTGECGGKNFHFIHA 336
Cdd:cd07119 181 FELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGGKNPNIVFA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 337 SADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEH 416
Cdd:cd07119 255 DADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 417 AkKSPNLEILAGGTYSD----SKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAV 492
Cdd:cd07119 335 G-KEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE--EAIRLAN-DTPYGLAGAV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320546182 493 FgqDEDFVKCALQEFKMAAGNFYINDksTGSVVGQQPFGGGRMSG 537
Cdd:cd07119 411 W--TKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
100-537 |
7.09e-48 |
|
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: 173.19 E-value: 7.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPK-WDRVSIADRLKIWEKAADLMattyRQDLNAATML-----GQSKTAIQAEIDSAA 173
Cdd:cd07109 10 FARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLI----REHADELARLesldtGKPLTQARADVEAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 174 elidfiRMNAYFLKEVTKYQ----PISENIKVTKnslrYRGIDGFIAAVSPFNFTA-IGGNlSYTPAL-MGNGVLWKPSD 247
Cdd:cd07109 86 ------RYFEYYGGAADKLHgetiPLGPGYFVYT----VREPHGVTGHIIPWNYPLqITGR-SVAPALaAGNAVVVKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 248 TAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECG 327
Cdd:cd07109 155 DAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVV------PVTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 328 GKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTsAVIDDKAF 407
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLG-PLISAKQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 408 KRITGYIEHAKKSpNLEILAGG---TYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtST 484
Cdd:cd07109 308 DRVEGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFD--DEAEAIALAN-GT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 320546182 485 KFALTGAVFGQDEDfvkcalQEFKMA----AGNFYINDKSTGSVVgQQPFGGGRMSG 537
Cdd:cd07109 384 DYGLVAGVWTRDGD------RALRVArrlrAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
111-544 |
8.73e-48 |
|
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: 172.46 E-value: 8.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSKTAIQAEIDSAAELIDfIRMNAYFLK 187
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKA--NKEELARLIsreTGKPLWEAQTEVAAMAGKID-ISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 188 EVTKYQPISEnikvTKNSLRYRGIdGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVP 266
Cdd:cd07095 79 TGERATPMAQ----GRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 267 DGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYvnfprLTGECGGKNFHFIHASADVESVVTS 346
Cdd:cd07095 154 PGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 347 TIRSAFEYCGQKCSACSRMYVPESLWPQ-IKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRitgYIEHAKKSPNL-- 423
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR---YLLAQQDLLALgg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 424 EILAGGTYSDSKGYFVNPTIVLSKDPKDRiMTEEIFGPVLSIYVYKesDLLETMKLvHTSTKFALTGAVFGQDEDFVKCA 503
Cdd:cd07095 305 EPLLAMERLVAGTAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRYD--DFDEAIAL-ANATRFGLSAGLLSDDEALFERF 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 320546182 504 LQEfkMAAGNFYINDKSTGSvVGQQPFGGGRMSGtNDKAGG 544
Cdd:cd07095 381 LAR--IRAGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
213-537 |
1.08e-47 |
|
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: 172.74 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFN----FTAiggnLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITAS 287
Cdd:cd07114 121 GVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 288 PHLAGINFTGSVPTFNRLWKQVGNNidnyvnFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYV 367
Cdd:cd07114 197 PLVAKIAFTGGTETGRHIARAAAEN------LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 368 PESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGG----TYSDSKGYFVNPTI 443
Cdd:cd07114 271 QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA-REEGARVLTGGerpsGADLGAGYFFEPTI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 444 VLSKDPKDRIMTEEIFGPVLSIYVYK-ESDLLETMklvhTSTKFALTGAVFGQDEDfvkcalQEFKMA----AGNFYIND 518
Cdd:cd07114 350 LADVTNDMRIAQEEVFGPVLSVIPFDdEEEAIALA----NDSEYGLAAGIWTRDLA------RAHRVAraieAGTVWVNT 419
|
330
....*....|....*....
gi 320546182 519 KSTGSVVgqQPFGGGRMSG 537
Cdd:cd07114 420 YRALSPS--SPFGGFKDSG 436
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
114-537 |
1.82e-47 |
|
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: 172.14 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 114 AIKTAVETQPkWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKTAIQA--EIDSAAELIDFIRMNAYFLKEVTk 191
Cdd:cd07118 27 AARKAFDKGP-WPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEGAADLWRYAASLARTLHGDS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 192 yqpiSENIKVTKNSLRYRGIDGFIAAVSPFNFTA--IGGNLSYTPAlMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGV 269
Cdd:cd07118 104 ----YNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 270 VNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTSTIR 349
Cdd:cd07118 179 VNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK------KVSLELGGKNPQIVFADADLDAAADAVVF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 350 SAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGG 429
Cdd:cd07118 253 GVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 430 TYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDEDfvKCALQEFKM 509
Cdd:cd07118 333 RLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD--EAIALAN-DTVYGLSAGVWSKDID--TALTVARRI 407
|
410 420
....*....|....*....|....*...
gi 320546182 510 AAGNFYINDKSTGSVvgQQPFGGGRMSG 537
Cdd:cd07118 408 RAGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
213-538 |
5.37e-47 |
|
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: 171.21 E-value: 5.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNF-TAIGG-NLsyTPALM-GNGVLWKPSDTAMLSNWIIFKIMREA----GVPDGVVNFVPADGPVfGDTIT 285
Cdd:cd07086 135 GVVGVITAFNFpVAVPGwNA--AIALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 286 ASPHLAGINFTGSVPTfnrlWKQVGNNIDNYvnFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRM 365
Cdd:cd07086 212 HDPRVPLVSFTGSTEV----GRRVGETVARR--FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 366 YVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSD--SKGYFVNPTI 443
Cdd:cd07086 286 IVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRIDggEPGNYVEPTI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 444 VLSKDPKDRIMTEEIFGPVLsiYVYKESDLLETMKlVHTSTKFALTGAVFGQD----EDFVKCALQEfkmaAGNFYINDK 519
Cdd:cd07086 365 VTGVTDDARIVQEETFAPIL--YVIKFDSLEEAIA-INNDVPQGLSSSIFTEDlreaFRWLGPKGSD----CGIVNVNIP 437
|
330 340
....*....|....*....|....*
gi 320546182 520 STGSVVGqQPFGG------GRMSGT 538
Cdd:cd07086 438 TSGAEIG-GAFGGeketggGRESGS 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
111-559 |
4.85e-46 |
|
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: 168.26 E-value: 4.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM-LGQSKTAIQA--EI-DSAAELIDFIRMNAYFL 186
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLE--RRDELLDLIqLETGKARRHAfeEVlDVAIVARYYARRAERLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 187 KEVTKYQPISENIKVTKNSlRYRGIDGFIaavSPFNF---TAIGGNLsytPALM-GNGVLWKPSDTAMLSNWIIFKIMRE 262
Cdd:cd07101 98 KPRRRRGAIPVLTRTTVNR-RPKGVVGVI---SPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTALTALWAVELLIE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 263 AGVPDGVVNFVPADGPVFGDTITAspHLAGINFTGSVPTFNRLWKQVGNnidnyvnfpRLTG---ECGGKNFHFIHASAD 339
Cdd:cd07101 171 AGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGR---------RLIGcslELGGKNPMIVLEDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 340 VESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkK 419
Cdd:cd07101 240 LDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA-V 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 420 SPNLEILAGGTYSDSKG-YFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGAVFGQDED 498
Cdd:cd07101 319 AKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRV--ADDDEAIELAN-DTDYGLNASVWTRDGA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546182 499 fVKCALQEfKMAAGNFYIND---KSTGSVvgQQPFGGGRMSGTNDKAgGPHYILRWTSPQSIKE 559
Cdd:cd07101 396 -RGRRIAA-RLRAGTVNVNEgyaAAWASI--DAPMGGMKDSGLGRRH-GAEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
105-517 |
1.32e-45 |
|
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: 167.04 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 105 YADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNA---ATMLGQSKTAIQAEIDSAAELIDFIRM 181
Cdd:cd07102 14 LASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAA--NTDEIAeelTWQMGRPIAQAGGEIRGMLERARYMIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 182 NAyflKEVTKYQPISENIKVTKnSLRYRGIdGFIAAVSPFN---FTAIGgnlSYTPALM-GNGVLWKPSDTAMLSNWIIF 257
Cdd:cd07102 92 IA---EEALADIRVPEKDGFER-YIRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVILKHSPQTPLCGERFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 258 KIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvnFPRLTGECGGKNFHFIHAS 337
Cdd:cd07102 164 AAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 338 ADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHA 417
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 418 KKSPNLEILAGGTYSDSK--GYFVNPTIVLSKDPKDRIMTEEIFGPVLSIyvYKESDLLETMKLVHTStKFALTGAVFGQ 495
Cdd:cd07102 317 IAKGARALIDGALFPEDKagGAYLAPTVLTNVDHSMRVMREETFGPVVGI--MKVKSDAEAIALMNDS-EYGLTASVWTK 393
|
410 420
....*....|....*....|..
gi 320546182 496 DEDfVKCALQEfKMAAGNFYIN 517
Cdd:cd07102 394 DIA-RAEALGE-QLETGTVFMN 413
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
99-538 |
1.89e-44 |
|
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: 164.44 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVETQPK---WDRVSIADRLKIWEKAADLMAttyRQDLNAATM--LGQSKTAiqaEIDSAA 173
Cdd:cd07141 34 KICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIE---RDRAYLASLetLDNGKPF---SKSYLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 174 ELIDFIRMNAYFLKEVTKYQpiSENIKVTKNSLRYRGID--GFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAM 250
Cdd:cd07141 108 DLPGAIKVLRYYAGWADKIH--GKTIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 251 LSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTfNRLWKQVGNNidnyVNFPRLTGECGGKN 330
Cdd:cd07141 186 LTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAGK----SNLKRVTLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 331 FHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRI 410
Cdd:cd07141 261 PNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 411 TGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTiVLSkDPKD--RIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFAL 488
Cdd:cd07141 341 LELIESGKKE-GAKLECGGKRHGDKGYFIQPT-VFS-DVTDdmRIAKEEIFGPVQQIFKFKTID--EVIERAN-NTTYGL 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 489 TGAVFGQDED---FVKCALQefkmaAGNFYINDKSTGSVvgQQPFGGGRMSGT 538
Cdd:cd07141 415 AAAVFTKDIDkaiTFSNALR-----AGTVWVNCYNVVSP--QAPFGGYKMSGN 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
101-537 |
1.60e-43 |
|
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: 161.26 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 101 ASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtYRQDLNAATMLGQSKTAIQAEIDsAAELIDFIR 180
Cdd:cd07147 13 ARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEE-RFEELAETIVLEAGKPIKDARGE-VARAIDTFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 181 MNAyflKEVTKYQPISENIKVTKNSLRYRGI-----DGFIAAVSPFNFTAiggNL---SYTPAL-MGNGVLWKPSDTAML 251
Cdd:cd07147 91 IAA---EEATRIYGEVLPLDISARGEGRQGLvrrfpIGPVSAITPFNFPL---NLvahKVAPAIaAGCPFVLKPASRTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 252 SNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPtfnrlwkqVGNNIDNYVNFPRLTGECGGKNF 331
Cdd:cd07147 165 SALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPA--------VGWDLKARAGKKKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 332 HFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRIT 411
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 412 GYIEHAKKSpNLEILAGGTysdSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALTGA 491
Cdd:cd07147 316 GWVNEAVDA-GAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFD--EALAAVNDS-KFGLQAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 320546182 492 VFGQDedfVKCALQEFK-MAAGNFYINDKSTGSvVGQQPFGGGRMSG 537
Cdd:cd07147 389 VFTRD---LEKALRAWDeLEVGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
99-545 |
1.60e-42 |
|
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: 158.23 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLnaATMLGQSKTAIQAEID-SAAELID 177
Cdd:cd07152 3 VLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLL-EEHADEI--ADWIVRESGSIRPKAGfEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 178 FIRMNAYFLKevtkyQPISENIKVT--KNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPS-DTAMLSN 253
Cdd:cd07152 80 ELHEAAGLPT-----QPQGEILPSApgRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 254 WIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHF 333
Cdd:cd07152 155 VVIARLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLK------KVSLELGGKNALI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 334 IHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGY 413
Cdd:cd07152 228 VLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 414 IEHAKKSpNLEILAGGTYsdsKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVhTSTKFALTGAVF 493
Cdd:cd07152 308 VDDSVAA-GARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE--EAVALA-NDTEYGLSAGII 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 320546182 494 GQDEDFVKcALQEfKMAAGNFYINDKSTGSVVgQQPFGGGRMSGTNDKAGGP 545
Cdd:cd07152 381 SRDVGRAM-ALAD-RLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
106-543 |
3.39e-42 |
|
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: 158.04 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPkWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQAEIdsaAELIDFIRMNAYF 185
Cdd:cd07142 41 EDVDRAVKAARKAFDEGP-WPRMTGYERSRILLRFADLL-EKHADELAALETWDNGKPYEQARY---AEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 186 LKEVTKYQpiSENIKVTKNSLRYRGID--GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMRE 262
Cdd:cd07142 116 AGWADKIH--GMTLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 263 AGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVptfnrlwkQVGNNIDNYV---NFPRLTGECGGKNFHFIHASAD 339
Cdd:cd07142 194 AGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGST--------EVGKIIMQLAaksNLKPVTLELGGKSPFIVCEDAD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 340 VESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDvqdfsSFTSAV-----IDDKAFKRITGYI 414
Cdd:cd07142 266 VDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD-----PFRKGVeqgpqVDKEQFEKILSYI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 415 EHAKKSpNLEILAGGTYSDSKGYFVNPTIVlsKDPKD--RIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAV 492
Cdd:cd07142 341 EHGKEE-GATLITGGDRIGSKGYYIQPTIF--SDVKDdmKIARDEIFGPVQSILKFKTVD--EVIKRAN-NSKYGLAAGV 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 320546182 493 FGQDEDFVKCALQEFKmaAGNFYIN--DKSTGSVvgqqPFGGGRMSGTNDKAG 543
Cdd:cd07142 415 FSKNIDTANTLSRALK--AGTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
106-537 |
4.71e-42 |
|
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: 157.69 E-value: 4.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVET-QPKWDR-VSIADRLKIWEKAADLMATTYrQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNA 183
Cdd:cd07143 41 ATEADVDIAVEVAHAAfETDWGLkVSGSKRGRCLSKLADLMERNL-DYLASIEALDNGKTFGTAKRVDVQASADTFRYYG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 184 YFLKEVTKyQPISENIKVTKNSlRYRGIdGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMRE 262
Cdd:cd07143 120 GWADKIHG-QVIETDIKKLTYT-RHEPI-GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 263 AGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvNFPRLTGECGGKNFHFIHASADVES 342
Cdd:cd07143 197 AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 343 VVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpN 422
Cdd:cd07143 272 AVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAE-G 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 423 LEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHTSTkFALTGAVFGQDedfVKC 502
Cdd:cd07143 351 ATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK--TEEEAIKRANDST-YGLAAAVFTNN---INN 424
|
410 420 430
....*....|....*....|....*....|....*.
gi 320546182 503 ALQ-EFKMAAGNFYINDKSTgsVVGQQPFGGGRMSG 537
Cdd:cd07143 425 AIRvANALKAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
111-537 |
6.13e-41 |
|
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: 153.50 E-value: 6.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATMlgqsktaiQAEIDSAAELIDF-IRMNAYFLKEV 189
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLES--RRDEFIEAM--------MEETGATAAWAGFnVDLAAGMLREA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 190 TKY--QPISENIKVTK---NSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREA 263
Cdd:cd07105 72 ASLitQIIGGSIPSDKpgtLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 264 GVPDGVVNFV---PADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVnfprLtgECGGKNFHFIHASADV 340
Cdd:cd07105 152 GLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVL----L--ELGGKAPAIVLEDADL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 341 ESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDfssftSAVIDDKAFKRITGYIEHAkKS 420
Cdd:cd07105 226 DAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDA-LS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 421 PNLEILAGGTYSDSK-GYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALTGAVFGQDEdf 499
Cdd:cd07105 300 KGAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVK--DEEEAVRIAN-DSEYGLSAAVFTRDL-- 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320546182 500 vkcaLQEFKMA----AGNFYINdkstGSVVG---QQPFGGGRMSG 537
Cdd:cd07105 375 ----ARALAVAkrieSGAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
122-557 |
2.09e-40 |
|
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: 152.38 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 122 QPKWDRVSIADR---LKIWEKA----ADLMATTYRQDLnaatmlGQSKTAIQAEIDSAAELIDFIRMNAYFL--KEVTKY 192
Cdd:cd07099 31 QRAWAALGVEGRaqrLLRWKRAladhADELAELLHAET------GKPRADAGLEVLLALEAIDWAARNAPRVlaPRKVPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 193 QPISENIKVTknsLRYR--GIDGFIaavSPFNF---TAIGgnlSYTPALM-GNGVLWKPSD-TAMLSNWIIfKIMREAGV 265
Cdd:cd07099 105 GLLMPNKKAT---VEYRpyGVVGVI---SPWNYpllTPMG---DIIPALAaGNAVVLKPSEvTPLVGELLA-EAWAAAGP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 266 PDGVVNFVPADGPVFGDTITASPHLagINFTGSVPTFNRLWKQVGNnidnyvnfpRLTG---ECGGKNFHFIHASADVES 342
Cdd:cd07099 175 PQGVLQVVTGDGATGAALIDAGVDK--VAFTGSVATGRKVMAAAAE---------RLIPvvlELGGKDPMIVLADADLER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 343 VVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpN 422
Cdd:cd07099 244 AAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAK-G 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 423 LEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALTGAVFGQDEDFVKc 502
Cdd:cd07099 323 AKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADED--EAIALANDS-RYGLSASVFSRDLARAE- 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 503 ALQEfKMAAGNFYINDKSTGSVVGQQPFGGGRMSGTNdKAGGPHYILRWTSPQSI 557
Cdd:cd07099 399 AIAR-RLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAI 451
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
111-570 |
3.75e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 157.06 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMattyRQDLNaaTMLG-----QSKT---AIqAEIDSAaelIDFIRmn 182
Cdd:PRK11809 684 VEQALESAVNAAPIWFATPPAERAAILERAADLM----EAQMQ--TLMGllvreAGKTfsnAI-AEVREA---VDFLR-- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 183 aYFlkevtkyqpiSENIKVTKNSLRYRGIdGFIAAVSPFNFT-AI-GGNLSytPALM-GNGVLWKPSDTAMLSNWIIFKI 259
Cdd:PRK11809 752 -YY----------AGQVRDDFDNDTHRPL-GPVVCISPWNFPlAIfTGQVA--AALAaGNSVLAKPAEQTPLIAAQAVRI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 260 MREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASAD 339
Cdd:PRK11809 818 LLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPLIAETGGQNAMIVDSSAL 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 340 VESVVTSTIRSAFEYCGQKCSA----CSRMYVPESLWPQIKEGLvceaAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIE 415
Cdd:PRK11809 898 TEQVVADVLASAFDSAGQRCSAlrvlCLQDDVADRTLKMLRGAM----AECRMGNPDRLSTDIGPVIDAEAKANIERHIQ 973
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 416 --HAKKSPNLEILAGGTYSDSKGYFVNPTIVlSKDPKDRiMTEEIFGPVLSIYVYKESDLLETMKLVHtSTKFALTGAVF 493
Cdd:PRK11809 974 amRAKGRPVFQAARENSEDWQSGTFVPPTLI-ELDSFDE-LKREVFGPVLHVVRYNRNQLDELIEQIN-ASGYGLTLGVH 1050
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 494 GQ-DEDFVKCALqefKMAAGNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTS--PQSIKETFVPLRDVNYP 570
Cdd:PRK11809 1051 TRiDETIAQVTG---SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAtrPEDALAVTLARQDAEYP 1127
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
213-537 |
6.71e-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: 151.57 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLA 291
Cdd:cd07139 139 GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREV-GEYLVRHPGVD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNIdnyvnfPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESL 371
Cdd:cd07139 218 KVSFTGSTAAGRRIAAVCGERL------ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 372 WPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSD--SKGYFVNPTIVLSKDP 449
Cdd:cd07139 292 YDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAE-GARLVTGGGRPAglDRGWFVEPTLFADVDN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 450 KDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHTStKFALTGAVFGQDEDF-VKCALQefkMAAGNFYINDKSTGSVVgqq 528
Cdd:cd07139 371 DMRIAQEEIFGPVLSVIPY--DDEDDAVRIANDS-DYGLSGSVWTADVERgLAVARR---IRTGTVGVNGFRLDFGA--- 441
|
....*....
gi 320546182 529 PFGGGRMSG 537
Cdd:cd07139 442 PFGGFKQSG 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
111-538 |
7.01e-40 |
|
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: 150.94 E-value: 7.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTyRQDLNAATMLGQSKT---AIQAEIDSAAELIDFIRMNAYFL- 186
Cdd:cd07092 21 VDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEEN-AEELAALESRNTGKPlhlVRDDELPGAVDNFRFFAGAARTLe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 187 -KEVTKYQPISENIkVTKNSLryrgidGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREaG 264
Cdd:cd07092 100 gPAAGEYLPGHTSM-IRREPI------GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAELAAE-V 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 265 VPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVV 344
Cdd:cd07092 172 LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGKAPVIVFDDADLDAAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 345 TSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKspNLE 424
Cdd:cd07092 246 AGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPA--HAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 425 ILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDEDFVKCAL 504
Cdd:cd07092 324 VLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDED--EAIELAN-DVEYGLASSVWTRDVGRAMRLS 400
|
410 420 430
....*....|....*....|....*....|....
gi 320546182 505 QEFKmaAGNFYINDKstGSVVGQQPFGGGRMSGT 538
Cdd:cd07092 401 ARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
100-571 |
9.92e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 151.19 E-value: 9.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQD-LNAATMLGQSKtAIQ----AEIDSAAE 174
Cdd:PRK13252 35 LATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE--RNDeLAALETLDTGK-PIQetsvVDIVTGAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 175 LIDfirmnaYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNF-TAIGGNLSyTPAL-MGNGVLWKPSDTAM 250
Cdd:PRK13252 112 VLE------YYAGLAPALE--GEQIPLRGGSFVYtrREPLGVCAGIGAWNYpIQIACWKS-APALaAGNAMIFKPSEVTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 251 LSNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLW-------KQVgnnidnyvnfprlT 323
Cdd:PRK13252 183 LTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMaaaaaslKEV-------------T 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 324 GECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVID 403
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 404 DKAFKRITGYIEHAKKSpNLEILAGGTYSD----SKGYFVNPTIVlsKDPKD--RIMTEEIFGPVLSIYVYKESDllETM 477
Cdd:PRK13252 329 FAHRDKVLGYIEKGKAE-GARLLCGGERLTeggfANGAFVAPTVF--TDCTDdmTIVREEIFGPVMSVLTFDDED--EVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 478 KLVHtSTKFALTGAVFGQDedfVKCALQEF-KMAAGNFYINdkSTGSVVGQQPFGGGRMSGT---NDKAGGPHYilrwts 553
Cdd:PRK13252 404 ARAN-DTEYGLAAGVFTAD---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVGGYKQSGIgreNGIATLEHY------ 471
|
490
....*....|....*...
gi 320546182 554 pQSIKETFVPLRDVNYPY 571
Cdd:PRK13252 472 -TQIKSVQVEMGPFQSPF 488
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
100-537 |
3.45e-39 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 149.97 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVET--QPKWDRVSIADRLKIWEKAADLMATTYRQ-----DLNAATMLGQSKTAiqaEIDSA 172
Cdd:PLN02766 49 IARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEElaaldTIDAGKLFALGKAV---DIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 173 AELIdfirmnAYFLKEVTKYQpiSENIKVTKNSLRY--RGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTA 249
Cdd:PLN02766 126 AGLL------RYYAGAADKIH--GETLKMSRQLQGYtlKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 MLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVptfnrlwkQVGNNIDNYV---NFPRLTGEC 326
Cdd:PLN02766 198 PLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGST--------EVGRKIMQAAatsNLKQVSLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 327 GGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKA 406
Cdd:PLN02766 270 GGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 407 FKRITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKF 486
Cdd:PLN02766 350 FEKILSYIEHGKRE-GATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE--EAIKKAN-NTKY 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 320546182 487 ALTGAVFGQDEDFVKCALQEFKmaAGNFYIN-----DKSTgsvvgqqPFGGGRMSG 537
Cdd:PLN02766 426 GLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
111-537 |
6.45e-39 |
|
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: 147.99 E-value: 6.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSKTAIQAEIDSAAELIDFIRMNA-YFL 186
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRE--RKDELARLItleMGKPIAEARAEVEKCAWICRYYAENAeAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 187 KEvtkyQPIseNIKVTKNSLRYRGIdGFIAAVSPFNFT-------AIggnlsytPALM-GNGVLWKPSDTAMLSNWIIFK 258
Cdd:cd07100 79 AD----EPI--ETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfAA-------PNLMaGNTVLLKHASNVPGCALAIEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 259 IMREAGVPDGVVNFVPADGPVFgDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVnfprLtgECGGKNFHFIHASA 338
Cdd:cd07100 145 LFREAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSV----L--ELGGSDPFIVLDDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 339 DVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAK 418
Cdd:cd07100 218 DLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 419 KSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDED 498
Cdd:cd07100 298 AA-GATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE--EAIALAN-DSPFGLGGSVFTTDLE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320546182 499 fvkcalQEFKMA----AGNFYIND--KSTGSVvgqqPFGGGRMSG 537
Cdd:cd07100 374 ------RAERVArrleAGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
111-565 |
2.02e-38 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 148.10 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATmlgqsktaIQAEID----SAAELIDFIRMNA-YF 185
Cdd:PRK09407 56 VEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLE--NREELLDL--------VQLETGkarrHAFEEVLDVALTArYY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 186 LKEVTKYQ---------PIsenikVTKNSLRY--RGIDGFIaavSPFNF---TAIGGNLsytPALM-GNGVLWKP-SDTA 249
Cdd:PRK09407 126 ARRAPKLLaprrragalPV-----LTKTTELRqpKGVVGVI---SPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 mLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITAspHLAGINFTGSVPTFNRLWKQVGnnidnyvnfPRLTG---EC 326
Cdd:PRK09407 195 -LTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAG---------RRLIGfslEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 327 GGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKA 406
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 407 FKRITGYIEHAkKSPNLEILAGG-TYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTK 485
Cdd:PRK09407 343 LETVSAHVDDA-VAKGATVLAGGkARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPV--ADVDEAVERAN-DTP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 486 FALTGAVFGQDEDfVKCALQEfKMAAGNFYINDKST---GSVvgQQPFGGGRMSGtndkAG---GPHYILRWTSPQSIKE 559
Cdd:PRK09407 419 YGLNASVWTGDTA-RGRAIAA-RIRAGTVNVNEGYAaawGSV--DAPMGGMKDSG----LGrrhGAEGLLKYTESQTIAT 490
|
....*..
gi 320546182 560 T-FVPLR 565
Cdd:PRK09407 491 QrVLPLA 497
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
132-543 |
2.17e-38 |
|
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: 146.73 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 132 DRLKIWEKAADLMAttyRQDLNAATML----GQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISENIKvTKNSLR 207
Cdd:cd07146 41 QRSAILNKAAALLE---ARREEFARLItlesGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGK-ARKIFT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 208 YRGIDGFIAAVSPFNF------TAIGgnlsytPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVF 280
Cdd:cd07146 117 LREPLGVVLAITPFNHplnqvaHKIA------PAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 281 GDTITASPHLAGINFTGSVPtfnrlwkqVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCS 360
Cdd:cd07146 191 GDELITHPDVDLVTFTGGVA--------VGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 361 ACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYsdsKGYFVN 440
Cdd:cd07146 263 AVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQ-GARVLLGNQR---QGALYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 441 PTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEFKMAAGNfyINDkS 520
Cdd:cd07146 339 PTVLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISN-STAYGLSSGVCTNDLDTIKRLVERLDVGTVN--VNE-V 412
|
410 420
....*....|....*....|...
gi 320546182 521 TGSVVGQQPFGGGRMSGTNDKAG 543
Cdd:cd07146 413 PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
213-537 |
2.49e-38 |
|
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: 146.73 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLA 291
Cdd:cd07110 122 GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGID 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNIDNyvnfprLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESL 371
Cdd:cd07110 202 KISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 372 WPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGGTYSD--SKGYFVNPTIVLSKDP 449
Cdd:cd07110 276 ADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG-KEEGARLLCGGRRPAhlEKGYFIAPTVFADVPT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 450 KDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALTGAVFGQDE---DFVKCALQefkmaAGNFYINdkSTGSVVG 526
Cdd:cd07110 355 DSRIWREEIFGPVLCVRSFATED--EAIALANDS-EYGLAAAVISRDAercDRVAEALE-----AGIVWIN--CSQPCFP 424
|
330
....*....|.
gi 320546182 527 QQPFGGGRMSG 537
Cdd:cd07110 425 QAPWGGYKRSG 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
77-465 |
6.77e-38 |
|
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: 146.12 E-value: 6.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 77 IGGKEYKTPEVRYQ-VMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAA 155
Cdd:cd07085 5 INGEWVESKTTEWLdVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL-EENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 156 TMLGQSKTAIQA--EIDSAAELIDF-IRMNAYFLKEVtkyqpiSENIKvtknslryRGID--------GFIAAVSPFNFT 224
Cdd:cd07085 84 ITLEHGKTLADArgDVLRGLEVVEFaCSIPHLLKGEY------LENVA--------RGIDtysyrqplGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 225 AIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPtfn 303
Cdd:cd07085 150 AMIPLWMFPMAIaCGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA-VNALLDHPDIKAVSFVGSTP--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 304 rlwkqVGNNIdnY----VNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGL 379
Cdd:cd07085 226 -----VGEYI--YeraaANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 380 VCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKspnleilAGGT------------YSDskGYFVNPTIVLSK 447
Cdd:cd07085 299 VERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVE-------EGAKlvldgrgvkvpgYEN--GNFVGPTILDNV 369
|
410
....*....|....*...
gi 320546182 448 DPKDRIMTEEIFGPVLSI 465
Cdd:cd07085 370 TPDMKIYKEEIFGPVLSI 387
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
210-537 |
4.16e-37 |
|
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: 143.25 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 210 GIDGFIaavSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREA-GVPDGVVNFVPADGPVFGDTITAS 287
Cdd:cd07120 119 GVAGII---VPWNSPVVLLVRSLAPALAaGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVAS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 288 PHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYV 367
Cdd:cd07120 196 PDVDVISFTGSTATGRAIMAAAAPTLK------RLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 368 PESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGG--TYSDSKGYFVNPTIVL 445
Cdd:cd07120 270 QRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGpvTEGLAKGAFLRPTLLE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 446 SKDPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGAVFGQDEDfvkcalQEFKMA----AGNFYINDKst 521
Cdd:cd07120 350 VDDPDADIVQEEIFGPVLTLETF--DDEAEAVALAN-DTDYGLAASVWTRDLA------RAMRVArairAGTVWINDW-- 418
|
330
....*....|....*.
gi 320546182 522 GSVVGQQPFGGGRMSG 537
Cdd:cd07120 419 NKLFAEAEEGGYRQSG 434
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
100-537 |
4.50e-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: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLM---------ATTY------RQDLNAATMLGQSK-- 162
Cdd:cd07559 29 LCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIeenlellavAETLdngkpiRETLAADIPLAIDHfr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 163 ---TAIQAEIDSAAEL-IDFIrmnAYFLKEvtkyqPIsenikvtknslryrgidGFIAAVSPFNFTAIGGNLSYTPALM- 237
Cdd:cd07559 109 yfaGVIRAQEGSLSEIdEDTL---SYHFHE-----PL-----------------GVVGQIIPWNFPLLMAAWKLAPALAa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 238 GNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVptfnrlwkQVGNNIDNYV 317
Cdd:cd07559 164 GNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGST--------TVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 318 --NFPRLTGECGGK--NFHFihasADVESVVTSTIRSAFEYC-------GQKCSACSRMYVPESLWPQIKEGLVCEAAKL 386
Cdd:cd07559 235 aeNLIPVTLELGGKspNIFF----DDAMDADDDFDDKAEEGQlgfafnqGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 387 KIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYS----DSKGYFVNPTIVLSKDPKDRIMTEEIFGPV 462
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546182 463 LSIYVYKESDllETMKLVHtSTKFALTGAVFGQDedfvkcALQEFKMA----AGNFYINdkSTGSVVGQQPFGGGRMSG 537
Cdd:cd07559 390 LAVITFKDEE--EAIAIAN-DTEYGLGGGVWTRD------INRALRVArgiqTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
99-537 |
1.59e-36 |
|
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: 142.21 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTyrQDLNAATMLGQSKTAIQ----AEIDSAAe 174
Cdd:cd07117 28 TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDEN--KELLAMVETLDNGKPIRetraVDIPLAA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 175 liDFIRmnaYFLKEVTKYQPISENIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSN 253
Cdd:cd07117 105 --DHFR---YFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 254 WIIFKIMREAgVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVptfnRLWKQVGNNIDNYVnFPRlTGECGGKNFHF 333
Cdd:cd07117 180 LELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGST----EVGRDVAIAAAKKL-IPA-TLELGGKSANI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 334 IHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGY 413
Cdd:cd07117 253 IFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 414 IEHAKKSpNLEILAGGTYSDS----KGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALT 489
Cdd:cd07117 333 VDIAKEE-GAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED--EVIDMANDS-EYGLG 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 320546182 490 GAVFGQDedfVKCALQEFK-MAAGNFYINdkSTGSVVGQQPFGGGRMSG 537
Cdd:cd07117 409 GGVFTKD---INRALRVARaVETGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
108-548 |
1.42e-35 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 139.83 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 108 KKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQA--EIDSAAELIDfirmnaYF 185
Cdd:PLN02278 61 RAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI-IANKEDLAQLMTLEQGKPLKEAigEVAYGASFLE------YF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 186 LKEVTK-YQPISENIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREA 263
Cdd:PLN02278 134 AEEAKRvYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 264 GVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESV 343
Cdd:PLN02278 214 GIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADLDVA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 344 VTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNL 423
Cdd:PLN02278 288 VKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA-VSKGA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 424 EILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTsTKFALTGAVFGQDED---FV 500
Cdd:PLN02278 367 KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE--EAIAIAND-TEAGLAAYIFTRDLQrawRV 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 320546182 501 KCALqEFKMAAgnfyINDKSTGSVVGqqPFGGGRMSGTNdKAGGPHYI 548
Cdd:PLN02278 444 SEAL-EYGIVG----VNEGLISTEVA--PFGGVKQSGLG-REGSKYGI 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
106-537 |
2.78e-35 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 138.55 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLnaATMLGQ--------SKTAIQAEIDSAAelid 177
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL-EENKEEL--AEVIARetgkplweAATEVTAMINKIA---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 178 fIRMNAYFLKEVTKYQPISENIKVtknsLRYRGiDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWII 256
Cdd:PRK09457 107 -ISIQAYHERTGEKRSEMADGAAV----LRHRP-HGVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 257 FKIMREAGVPDGVVNFVPAdGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYvnfprLTGECGGKNFHFIHA 336
Cdd:PRK09457 181 VKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 337 SADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQ-IKEGLVCEAAKLKIGDV-QDFSSFTSAVIDDKAFKRITgyi 414
Cdd:PRK09457 255 VADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLV--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 415 eHAKKspNLEILAGG-----TYSDSKGYFVNPTIVLSKDPKDRImTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALT 489
Cdd:PRK09457 332 -AAQA--QLLALGGKsllemTQLQAGTGLLTPGIIDVTGVAELP-DEEYFGPLLQVVRY--DDFDEAIRLAN-NTRFGLS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 320546182 490 GAVFGQDEDFVKCALQEFKmaAGNFYINDKSTGSvVGQQPFGGGRMSG 537
Cdd:PRK09457 405 AGLLSDDREDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
97-557 |
3.10e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 138.88 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 97 QHKLASFYYADKKLIEKAIKTAVET--QPKWDRVSIADRLKIWEKAADLMATtYRQDLNAATMLGQSKTAIQAEIDSAAE 174
Cdd:PRK09847 45 QAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEA-HAEELALLETLDTGKPIRHSLRDDIPG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 175 LIDFIRMNAYFLKEV-TKYQPISENikvtKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLS 252
Cdd:PRK09847 124 AARAIRWYAEAIDKVyGEVATTSSH----ELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 253 NWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvNFPRLTGECGGKNFH 332
Cdd:PRK09847 200 AIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 333 FIHASA-DVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRIT 411
Cdd:PRK09847 275 IVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 412 GYIEHAKKSPNLeiLAGGTYSDSKGYfVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFALTGA 491
Cdd:PRK09847 355 SFIREGESKGQL--LLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE--QALQLANDS-QYGLGAA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320546182 492 VFGQdeDFVKCALQEFKMAAGNFYINDKSTGSVVgqQPFGGGRMSGtNDKAGGPHYILRWTSPQSI 557
Cdd:PRK09847 429 VWTR--DLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
213-537 |
7.28e-35 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 137.94 E-value: 7.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLA 291
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNIDnyvnfPrLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESL 371
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 372 WPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILAGGTYSD--SKGYFVNPTIVLSKDP 449
Cdd:PLN02467 307 ASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTA-KSEGATILCGGKRPEhlKKGFFIEPTIITDVTT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 450 KDRIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFGQDEDfvKCALQEFKMAAGNFYINdkSTGSVVGQQP 529
Cdd:PLN02467 386 SMQIWREEVFGPVLCVKTFSTED--EAIELAN-DSHYGLAGAVISNDLE--RCERVSEAFQAGIVWIN--CSQPCFCQAP 458
|
....*...
gi 320546182 530 FGGGRMSG 537
Cdd:PLN02467 459 WGGIKRSG 466
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
113-543 |
4.41e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 136.09 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 113 KAIKTAVETQPkWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQAeidSAAELIDFIRMNAYFLKEVTK- 191
Cdd:PLN02466 102 AAARKAFDEGP-WPKMTAYERSRILLRFADLL-EKHNDELAALETWDNGKPYEQS---AKAELPMFARLFRYYAGWADKi 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 192 ------------YQPISENIkvtknslryrGIDGFIAavsPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFK 258
Cdd:PLN02466 177 hgltvpadgphhVQTLHEPI----------GVAGQII---PWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 259 IMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNidnyvNFPRLTGECGGKNFHFIHASA 338
Cdd:PLN02466 244 LLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS-----NLKPVTLELGGKSPFIVCEDA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 339 DVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDvqdfsSFTSAV-----IDDKAFKRITGY 413
Cdd:PLN02466 319 DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGD-----PFKKGVeqgpqIDSEQFEKILRY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 414 IEHAKKSpNLEILAGGTYSDSKGYFVNPTIVlsKDPKD--RIMTEEIFGPVLSIYVYKesDLLETMKLVHtSTKFALTGA 491
Cdd:PLN02466 394 IKSGVES-GATLECGGDRFGSKGYYIQPTVF--SNVQDdmLIAQDEIFGPVQSILKFK--DLDEVIRRAN-NTRYGLAAG 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 320546182 492 VFGQDEDFVKCALQEFKmaAGNFYIN--DKSTGSVvgqqPFGGGRMSGTNDKAG 543
Cdd:PLN02466 468 VFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
197-517 |
5.25e-34 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 133.71 E-value: 5.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 197 ENIKVTKNSLryrgidGFIAAVSPFNFT--AIGGNLSytPALM-GNGVLWKPSDTAMlSNWIIF-KIMREAGVPDGVVNF 272
Cdd:PRK10090 63 ENILLFKRAL------GVTTGILPWNFPffLIARKMA--PALLtGNTIVIKPSEFTP-NNAIAFaKIVDEIGLPKGVFNL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 273 VPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTSTIRSAF 352
Cdd:PRK10090 134 VLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNIT------KVCLELGGKAPAIVMDDADLDLAVKAIVDSRV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 353 EYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSF-TSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTY 431
Cdd:PRK10090 208 INSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEE-GARVALGGKA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 432 SDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYkesDLLETMKLVHTSTKFALTGAVFGQDEDFVKCALQEFKMaa 511
Cdd:PRK10090 287 VEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAF---DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKF-- 361
|
....*.
gi 320546182 512 GNFYIN 517
Cdd:PRK10090 362 GETYIN 367
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
77-537 |
2.78e-32 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 129.92 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 77 IGGKEYKTpevryqVMPHDhQHKLASFYYADKKLIEKAI---KTAVETQPkWDRVSIADRLKIWEKAADLM-------AT 146
Cdd:cd07140 18 EGGKTYNT------INPTD-GSVICKVSLATVEDVDRAVaaaKEAFENGE-WGKMNARDRGRLMYRLADLMeehqeelAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 147 TYRQDLNAATMLGQsKTAIQAEIDSaaelidfIRmnaYFLKEVTKYQ----PISeNIKVTKN-SLRYRGIDGFIAAVSPF 221
Cdd:cd07140 90 IESLDSGAVYTLAL-KTHVGMSIQT-------FR---YFAGWCDKIQgktiPIN-QARPNRNlTLTKREPIGVCGIVIPW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 222 NFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVP 300
Cdd:cd07140 158 NYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 301 TFNRLWKQVGNNidnyvNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLV 380
Cdd:cd07140 238 IGKHIMKSCAVS-----NLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 381 CEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFG 460
Cdd:cd07140 313 EEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKE-GATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320546182 461 PVLSIYVYKESDLLETMKLVHTsTKFALTGAVFGQDEDfvKCALQEFKMAAGNFYINDKSTGSVVGqqPFGGGRMSG 537
Cdd:cd07140 392 PIMIISKFDDGDVDGVLQRAND-TEYGLASGVFTKDIN--KALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
213-472 |
5.54e-32 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 128.87 E-value: 5.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDTITASPHLA 291
Cdd:PRK13473 140 GVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTStIRsAFEYC--GQKCSACSRMYVPE 369
Cdd:PRK13473 219 MVSLTGSIATGKHVLSAAADSVK------RTHLELGGKAPVIVFDDADLDAVVEG-IR-TFGYYnaGQDCTAACRIYAQR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 370 SLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGGTYSDSKGYFVNPTIVLSKDP 449
Cdd:PRK13473 291 GIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQ 370
|
250 260
....*....|....*....|...
gi 320546182 450 KDRIMTEEIFGPVLSIYVYKESD 472
Cdd:PRK13473 371 DDEIVQREVFGPVVSVTPFDDED 393
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
213-546 |
1.22e-31 |
|
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: 127.90 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPvFGDTITASPHLA 291
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 292 GINFTGSVPTFNRLWKQVGNNIdnyvnfPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESL 371
Cdd:cd07111 228 KVAFTGSTEVGRALRRATAGTG------KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 372 WPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKD 451
Cdd:cd07111 302 AEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE-GADVFQPGADLPSKGPFYPPTLFTNVPPAS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 452 RIMTEEIFGPVLSIYVYKESDllETMKLVHtSTKFALTGAVFgqDEDFVKCALQEFKMAAGNFYINdkSTGSVVGQQPFG 531
Cdd:cd07111 381 RIAQEEIFGPVLVVLTFRTAK--EAVALAN-NTPYGLAASVW--SENLSLALEVALSLKAGVVWIN--GHNLFDAAAGFG 453
|
330
....*....|....*
gi 320546182 532 GGRMSGTNdKAGGPH 546
Cdd:cd07111 454 GYRESGFG-REGGKE 467
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
113-537 |
1.23e-31 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 128.10 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 113 KAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQA--EIDSAAELIDFIRMNA--YFLKE 188
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLM-MEHQDDLARLMTLEQGKPLAEAkgEISYAASFIEWFAEEGkrIYGDT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 189 VTKYQPiSENIKVTKNSLryrgidGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPD 267
Cdd:PRK11241 131 IPGHQA-DKRLIVIKQPI------GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 268 GVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfpRLTGECGGKNFHFIHASADVESVVTST 347
Cdd:PRK11241 204 GVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK------KVSLELGGNAPFIVFDDADLDKAVEGA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 348 IRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAkKSPNLEILA 427
Cdd:PRK11241 278 LASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA-LEKGARVVC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 428 GGTYSDSKGYFVNPTIvLSKDPKD-RIMTEEIFGPVLSIYVYKESDLLETMKlvhTSTKFALTGAVFGQDEDFVkcalqe 506
Cdd:PRK11241 357 GGKAHELGGNFFQPTI-LVDVPANaKVAKEETFGPLAPLFRFKDEADVIAQA---NDTEFGLAAYFYARDLSRV------ 426
|
410 420 430
....*....|....*....|....*....|...
gi 320546182 507 FKMA-AGNFYINDKSTGSVVGQ-QPFGGGRMSG 537
Cdd:PRK11241 427 FRVGeALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
213-496 |
1.71e-31 |
|
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: 127.71 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNF-TAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREA----GVPDGVVNFVPADGPVfGDTITAS 287
Cdd:cd07130 134 GVVGVITAFNFpVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADV-GEALVKD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 288 PHLAGINFTGSVPTfnrlWKQVGNNIDNYvnFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYV 367
Cdd:cd07130 213 PRVPLVSFTGSTAV----GRQVGQAVAAR--FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 368 PESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNlEILAGGTYSDSKGYFVNPTIVlSK 447
Cdd:cd07130 287 HESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIV-EG 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320546182 448 DPKDRIMTEEIFGPVLsiYVYKESDLLETMKLvHTSTKFALTGAVFGQD 496
Cdd:cd07130 365 LSDAPIVKEETFAPIL--YVLKFDTLEEAIAW-NNEVPQGLSSSIFTTD 410
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
93-559 |
3.79e-31 |
|
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: 126.26 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 93 PHDHQHkLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADlMATTYRQDLNAATMLGQSKTAIQA---EI 169
Cdd:cd07098 3 PATGQH-LGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLK-YILENQEEICRVACRDTGKTMVDAslgEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 170 DSAAELIDF-IRMNAYFLKEVTKYQPISENIKVTKnsLRYRGIdGFIAAVSPFNF---TAIGGNLSytpALM-GNGVLWK 244
Cdd:cd07098 81 LVTCEKIRWtLKHGEKALRPESRPGGLLMFYKRAR--VEYEPL-GVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 245 PSD-TAMLSNW---IIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDnyvnfP 320
Cdd:cd07098 155 VSEqVAWSSGFflsIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 321 rLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSA 400
Cdd:cd07098 229 -VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 401 VIDDKAFKRITGYIEHAKKSpNLEILAGGTY----SDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllET 476
Cdd:cd07098 308 MISPARFDRLEELVADAVEK-GARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE--EA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 477 MKLVHtSTKFALTGAVFGQD-EDFVKCALQefkMAAGNFYINDKSTGSVVGQQPFGGGRMSGTnDKAGGPHYILRWTSPQ 555
Cdd:cd07098 385 VEIAN-STEYGLGASVFGKDiKRARRIASQ---LETGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGEEGLRGLCNPK 459
|
....
gi 320546182 556 SIKE 559
Cdd:cd07098 460 SVTE 463
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
91-550 |
4.40e-29 |
|
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: 120.22 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 91 VMPHDHQHkLASFYYADKKLIEKAIKTAVE---TQPKWdrVSIADRLKIWEKAADLMATtyRQD---LNAATMLGQSKTA 164
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHAlflDRNNW--LPAHERIAILERLADLMEE--RADelaLLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 165 IQAEIDSAaelIDFIRMNAYFLKEVTKYQPISENIKVTKNSLRY--RGIDGFIAAVSPFNFTAiggNL---SYTPAL-MG 238
Cdd:cd07148 79 AKVEVTRA---IDGVELAADELGQLGGREIPMGLTPASAGRIAFttREPIGVVVAISAFNHPL---NLivhQVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 239 NGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVfGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIdnyvn 318
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 319 fpRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFT 398
Cdd:cd07148 227 --RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 399 SAVIDDKAFKRITGYIEHAkKSPNLEILAGGTYSDSKGYfvNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMK 478
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEA-VAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLD--EAIA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320546182 479 LVHtSTKFALTGAVFGQDedfVKCALQEFK-MAAGNFYINDKsTGSVVGQQPFGGGRMSGTNdkAGGPHYILR 550
Cdd:cd07148 380 QAN-SLPVAFQAAVFTKD---LDVALKAVRrLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG--TGGIPYTMH 445
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
121-537 |
7.89e-27 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 113.09 E-value: 7.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 121 TQPKWDRVSIADRLkiwEKAADLMAT--TYRQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISEN 198
Cdd:cd07134 10 HALALRASTAAERI---AKLKRLKKAilARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 199 IKV--TKNSLRY--RGIDGFIaavSPFNFTAiggNLSYTP---ALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVV 270
Cdd:cd07134 87 LLLfgTKSKIRYepKGVCLII---SPWNYPF---NLAFGPlvsAIAaGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 271 NFVpadgpvfGDTITASPHLA----GINFTGSvPTfnrlwkqVGNnidnYV------NFPRLTGECGGKNFHFIHASADV 340
Cdd:cd07134 161 VFE-------GDAEVAQALLElpfdHIFFTGS-PA-------VGK----IVmaaaakHLASVTLELGGKSPTIVDETADL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 341 ESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKL--KIGDVQDFSSFTSaVIDDKAFKRITGYIEHAK 418
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLAR-IVNDRHFDRLKGLLDDAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 419 KSpNLEILAGGTySDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVHTSTKfALTGAVFGQDED 498
Cdd:cd07134 301 AK-GAKVEFGGQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPK-PLALYVFSKDKA 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 320546182 499 FVKCALQEfkMAAGNFYINDKSTGSVVGQQPFGGGRMSG 537
Cdd:cd07134 376 NVNKVLAR--TSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
207-557 |
2.06e-26 |
|
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: 112.33 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 207 RYRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAG-VPDGVVNFVPADGPVfGDTI 284
Cdd:cd07084 96 GYRWPYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-MQAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 285 TASPHLAGINFTGSVptfnrlwkQVGNNIDNYVNFPRLTGECGGKNFHFIHASAD-VESVVTSTIRSAFEYCGQKCSACS 363
Cdd:cd07084 175 LLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 364 RMYVPESlwPQiKEGLVcEAAKLKIGDVQDFSSFTSAVIDDKAFKRitgyIEHAKKSPNLEILAGG------TYSDSKGY 437
Cdd:cd07084 247 MLFVPEN--WS-KTPLV-EKLKALLARRKLEDLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGkelknhSIPSIYGA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 438 FVNPTIVLSKDPKDR---IMTEEIFGPVLSIYVYK---ESDLLETMKLVHTStkfaLTGAVFGQDEDFVKCALQEFKMAA 511
Cdd:cd07084 319 CVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKkdqLALVLELLERMHGS----LTAAIYSNDPIFLQELIGNLWVAG 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 320546182 512 GNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSI 557
Cdd:cd07084 395 RTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
99-537 |
2.50e-25 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 109.18 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 99 KLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLkiwEKAADLMATTYRQDLNAATM----LGQSKTAIQAEIDSAAE 174
Cdd:PRK13968 19 QLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRA---QKLRDIGKALRARSEEMAQMitreMGKPINQARAEVAKSAN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 175 LIDFIRMN--AYFLKEVTkyqpISENIKVTknsLRYRGIdGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAML 251
Cdd:PRK13968 96 LCDWYAEHgpAMLKAEPT----LVENQQAV---IEYRPL-GTILAIMPWNFPLWQVMRGAVPILLaGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 252 SNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITaSPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNfprltgECGGKNF 331
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVL------ELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 332 HFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAV----IDDKAF 407
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMarfdLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 408 KRITGYIEHAKKspnleILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTStKFA 487
Cdd:PRK13968 321 HQVEATLAEGAR-----LLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAE--HALELANDS-EFG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 320546182 488 LTGAVFGQDEdfvkcaLQEFKMAA----GNFYINDKSTGSvvGQQPFGGGRMSG 537
Cdd:PRK13968 393 LSATIFTTDE------TQARQMAArlecGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
106-537 |
9.29e-24 |
|
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: 104.46 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 106 ADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMattyrqDLNAATMlgqsktAIQAEID--------SAAEL-- 175
Cdd:cd07116 35 STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRM------EANLEML------AVAETWDngkpvretLAADIpl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 176 -IDFIRmnaYFlKEVTKYQP--ISEnikVTKNSLRYRGID--GFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTA 249
Cdd:cd07116 103 aIDHFR---YF-AGCIRAQEgsISE---IDENTVAYHFHEplGVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 250 MLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTfNRLWKQVGNNidnyvNFPRLTGECGGK 329
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTT-GRLIMQYASE-----NIIPVTLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 330 --NFHFihasADVESVVTSTIRSAFE-------YCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSA 400
Cdd:cd07116 249 spNIFF----ADVMDADDAFFDKALEgfvmfalNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 401 VIDDKAFKRITGYIEHAKKSpNLEILAGGTYS----DSKGYFVNPTIVLsKDPKDRIMTEEIFGPVLSIYVYKESDllET 476
Cdd:cd07116 325 QASLEQLEKILSYIDIGKEE-GAEVLTGGERNelggLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKDEE--EA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 477 MKLVHtSTKFALTGAVFGQDedfvkcALQEFKMA----AGNFYINdkSTGSVVGQQPFGGGRMSG 537
Cdd:cd07116 401 LEIAN-DTLYGLGAGVWTRD------GNTAYRMGrgiqAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
111-517 |
9.88e-24 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 104.84 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 111 IEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMaTTYRQDLNAATMLGQSKTAIQA--EIDSAAELIDF-----IRM-- 181
Cdd:PLN00412 55 VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAIL-KEHKAPIAECLVKEIAKPAKDAvtEVVRSGDLISYtaeegVRIlg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 182 NAYFLkeVTKYQPISENIK---VTKNSLryrgidGFIAAVSPFNFTAiggNLSYT---PALM-GNGVLWKPSDTAMLSNW 254
Cdd:PLN00412 134 EGKFL--VSDSFPGNERNKyclTSKIPL------GVVLAIPPFNYPV---NLAVSkiaPALIaGNAVVLKPPTQGAVAAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 255 IIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSvptfnrlwkQVGNNIDNYVNFPRLTGECGGKNFHFI 334
Cdd:PLN00412 203 HMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG---------DTGIAISKKAGMVPLQMELGGKDACIV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 335 HASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTsAVIDDKAFKRITGYI 414
Cdd:PLN00412 274 LEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDIT-PVVSESSANFIEGLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 415 EHAKKSpnleilaGGTYSDS---KGYFVNPTIVLSKDPKDRIMTEEIFGPVLSiyVYKESDLLETMKLVHTStKFALTGA 491
Cdd:PLN00412 353 MDAKEK-------GATFCQEwkrEGNLIWPLLLDNVRPDMRIAWEEPFGPVLP--VIRINSVEEGIHHCNAS-NFGLQGC 422
|
410 420
....*....|....*....|....*.
gi 320546182 492 VFGQDEDfvKCALQEFKMAAGNFYIN 517
Cdd:PLN00412 423 VFTRDIN--KAILISDAMETGTVQIN 446
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
100-537 |
3.72e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 102.51 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 100 LASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATtyRQDLNAATM---LGQSKTAIQAEIDSAAELI 176
Cdd:PRK09406 14 VKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEA--EADQVAALMtleMGKTLASAKAEALKCAKGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 177 DFIRMNAyflKEVTKYQPI-SENIKVTKNSLRYRGIdGFIAAVSPFNFTAIGGNLSYTPALM-GNGVLWKPSDTAMLSNW 254
Cdd:PRK09406 92 RYYAEHA---EALLADEPAdAAAVGASRAYVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHASNVPQTAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 255 IIFKIMREAGVPDGVVN--FVPADGPvfgDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNfprltgECGGKNFH 332
Cdd:PRK09406 168 YLADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVL------ELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 333 FIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITG 412
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 413 YIEHAKKSpNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSiyVYKESDLLETMKLVHtSTKFALTGAV 492
Cdd:PRK09406 319 QVDDAVAA-GATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVAS--LYRVADIDEAIEIAN-ATTFGLGSNA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 320546182 493 FGQD----EDFVKcalqefKMAAGNFYINdkstGSVVG--QQPFGGGRMSG 537
Cdd:PRK09406 395 WTRDeaeqERFID------DLEAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
219-537 |
7.01e-22 |
|
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: 98.37 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 219 SPFNFTAiggNLSYTP---ALM-GNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDtITASP--Hlag 292
Cdd:cd07087 108 GPWNYPL---QLALAPligAIAaGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATA-LLAEPfdH--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 293 INFTGSVptfnrlwkQVGNNI-----DNYVnfPrLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYV 367
Cdd:cd07087 180 IFFTGSP--------AVGKIVmeaaaKHLT--P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 368 PESLWPQIKEGLVcEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKkspnleILAGGTYSDSKGYfVNPTIVLSK 447
Cdd:cd07087 249 HESIKDELIEELK-KAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK------VVIGGQVDKEERY-IAPTILDDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 448 DPKDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHTSTKfALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSVVGQ 527
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTY--DDLDEAIEFINSRPK-PLALYLFSEDKAVQERVLAE--TSSGGVCVNDVLLHAAIPN 395
|
330
....*....|
gi 320546182 528 QPFGGGRMSG 537
Cdd:cd07087 396 LPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
213-537 |
2.27e-19 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 91.24 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAiggNLSYTPAL----MGNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVfgdtITA-- 286
Cdd:PTZ00381 111 GVVLVIGAWNYPL---NLTLIPLAgaiaAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEV----TTEll 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 287 SPHLAGINFTGSVptfnrlwkQVGNNI-----DNYVnfPrLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSA 361
Cdd:PTZ00381 183 KEPFDHIFFTGSP--------RVGKLVmqaaaENLT--P-CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 362 CSRMYVPESlwpqIKEGLVC---EAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKspnlEILAGGTYSDSKGYf 438
Cdd:PTZ00381 252 PDYVLVHRS----IKDKFIEalkEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 439 VNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTSTKfALTGAVFGQDEDFVKCALQefKMAAGNFYIND 518
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPILPILTYENID--EVLEFINSRPK-PLALYYFGEDKRHKELVLE--NTSSGAVVIND 397
|
330 340
....*....|....*....|...
gi 320546182 519 kstgSVV----GQQPFGGGRMSG 537
Cdd:PTZ00381 398 ----CVFhllnPNLPFGGVGNSG 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
213-543 |
3.78e-19 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 90.66 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNF-TAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREA----GVPDGVVNFVpADGPVFGDTITAS 287
Cdd:PLN02315 156 GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSF-CGGAEIGEAIAKD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 288 PHLAGINFTGSvptfnrlwKQVGNNIDNYVN--FPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRM 365
Cdd:PLN02315 235 TRIPLVSFTGS--------SKVGLMVQQTVNarFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 366 YVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEhAKKSPNLEILAGGTYSDSKGYFVNPTIVl 445
Cdd:PLN02315 307 LLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIE-IIKSQGGKILTGGSAIESEGNFVQPTIV- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 446 SKDPKDRIMTEEIFGPVLsiYVYKESDLLETMKLvHTSTKFALTGAVFGQDEDFVKCALQEFKMAAGNFYINDKSTGSVV 525
Cdd:PLN02315 385 EISPDADVVKEELFGPVL--YVMKFKTLEEAIEI-NNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEI 461
|
330
....*....|....*...
gi 320546182 526 GqQPFGGGRMSGTNDKAG 543
Cdd:PLN02315 462 G-GAFGGEKATGGGREAG 478
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
218-538 |
5.52e-18 |
|
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: 86.50 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 218 VSPFNFTAIggnLSYTPAL----MGNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVFGDTITAspHLAGI 293
Cdd:cd07135 115 IGPWNYPVL---LALSPLVgaiaAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQ--KFDKI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 294 NFTGSVptfnrlwkQVGNNIDNYVN---FPrLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPES 370
Cdd:cd07135 189 FYTGSG--------RVGRIIAEAAAkhlTP-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 371 LWPQIKEGLVCEAAKLKIGDVQDFSSFTSaVIDDKAFKRITGYIEHAKKspnlEILAGGTySDSKGYFVNPTIVLSKDPK 450
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGGANASPDYTR-IVNPRHFNRLKSLLDTTKG----KVVIGGE-MDEATRFIPPTIVSDVSWD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 451 DRIMTEEIFGPVLSIYVYkeSDLLETMKLVHtSTKFALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSVVGQQPF 530
Cdd:cd07135 334 DSLMSEELFGPVLPIIKV--DDLDEAIKVIN-SRDTPLALYIFTDDKSEIDHILTR--TRSGGVVINDTLIHVGVDNAPF 408
|
....*...
gi 320546182 531 GGGRMSGT 538
Cdd:cd07135 409 GGVGDSGY 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
323-537 |
2.14e-17 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 84.97 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 323 TGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSA-----CSrmyvpeslwPQIKEGLVcEAAKLKI-----GDVQ 392
Cdd:cd07132 204 TLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCT---------PEVQEKFV-EALKKTLkefygEDPK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 393 DFSSFtSAVIDDKAFKRITGYIEhakkspNLEILAGGTYsDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesD 472
Cdd:cd07132 274 ESPDY-GRIINDRHFQRLKKLLS------GGKVAIGGQT-DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVN--N 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 473 LLETMKLVHTSTKfALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSVVGQQPFGGGRMSG 537
Cdd:cd07132 344 LDEAIEFINSREK-PLALYVFSNNKKVINKILSN--TSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
73-517 |
5.21e-17 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 84.41 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 73 IPIVIGGKEYKTPEVRY-QVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTY-RQ 150
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFiDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMdKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 151 DLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFlkEVTKYQPiseNIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNL 230
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATL--QMGEYLP---NVSNGVDTYSIREPLGVCAGICPFNFPAMIPLW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 231 SYTPALM-GNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGpvfgDTITA---SPHLAGINFTGSVPTFNRLW 306
Cdd:PLN02419 269 MFPVAVTcGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN----DTVNAicdDEDIRAVSFVGSNTAGMHIY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 307 KQVGnnidnyVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRM-YVPESL-WpqiKEGLVCEAA 384
Cdd:PLN02419 345 ARAA------AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDAKsW---EDKLVERAK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 385 KLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGGTY---SDSKGYFVNPTIVLSKDPKDRIMTEEIFGP 461
Cdd:PLN02419 416 ALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpGYEKGNFIGPTILSGVTPDMECYKEEIFGP 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 320546182 462 VLsiyVYKESDLLETMKLVHTSTKFALTGAVFGQDedfvKCALQEFKM--AAGNFYIN 517
Cdd:PLN02419 496 VL---VCMQANSFDEAISIINKNKYGNGAAIFTSS----GAAARKFQMdiEAGQIGIN 546
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
203-537 |
1.11e-16 |
|
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: 82.53 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 203 KNSLRYRGIdGFIAAVSPFNFTAiggNLSYTP---AL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVnfVPADGP 278
Cdd:cd07133 94 KAEVEYQPL-GVVGIIVPWNYPL---YLALGPliaALaAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA--VVTGGA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 279 VFGDTITASP--HLAginFTGSVptfnrlwkQVGNNI-----DNYVnfPrLTGECGGKNFHFIHASADVESVVTSTIRSA 351
Cdd:cd07133 168 DVAAAFSSLPfdHLL---FTGST--------AVGRHVmraaaENLT--P-VTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 352 FEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKL--KIGDVQDFSSftsaVIDDKAFKRITGYIEHAK-KSPNLEILAG 428
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPDYTS----IINERHYARLQGLLEDARaKGARVIELNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 429 GTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDllETMKLVHTSTK-FALTgaVFGQDEDFVKCALQEf 507
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLD--EAIDYINARPRpLALY--YFGEDKAEQDRVLRR- 384
|
330 340 350
....*....|....*....|....*....|..
gi 320546182 508 kMAAGNFYINDksTGSVVGQ--QPFGGGRMSG 537
Cdd:cd07133 385 -THSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
238-537 |
5.21e-15 |
|
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: 77.54 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 238 GNGVLWKPSDTAMLSNWIIFKIMREAgVPDGVVNFVPADGPVfGDTITASP--HlagINFTGSVPtfnrlwkqVGNnIDN 315
Cdd:cd07136 128 GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEE-NQELLDQKfdY---IFFTGSVR--------VGK-IVM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 316 YVNFPRLTG---ECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQ 392
Cdd:cd07136 194 EAAAKHLTPvtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 393 DFSSFTSaVIDDKAFKRITGYIEHAKkspnleILAGGTYsDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESD 472
Cdd:cd07136 274 ESPDYGR-IINEKHFDRLAGLLDNGK------IVFGGNT-DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLD 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320546182 473 lletmKLVHTSTKFA--LTGAVFGQDEDFVKCALQEFKMAAGnfYINDKSTGSVVGQQPFGGGRMSG 537
Cdd:cd07136 346 -----EAIEIIKSRPkpLALYLFSEDKKVEKKVLENLSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
209-537 |
3.36e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 72.04 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 209 RGIDGFIAAvspFNFTAIGGNLSYTPALM-GNGVLWKP-SDTAMLSNWIIfKIMREAGV-PDGVVNFVPADGPVFGDtit 285
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLaGVPVIVKPaTATAWLTQRMV-KDVVAAGIlPAGALSVVCGSSAGLLD--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 286 aspHLAG---INFTGSVPTFNRLwKQVGNNIDNYVnfpRLTGECGGKNFHFIHASADVES-----VVTSTIRSAFEYCGQ 357
Cdd:PRK11903 222 ---HLQPfdvVSFTGSAETAAVL-RSHPAVVQRSV---RVNVEADSLNSALLGPDAAPGSeafdlFVKEVVREMTVKSGQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 358 KCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFS----SFTSAVIDDKAFKRITGYIEHAkkspnlEILAGGT--- 430
Cdd:PRK11903 295 KCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGvrmgPLVSRAQLAAVRAGLAALRAQA------EVLFDGGgfa 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 431 ---YSDSKGYFVNPTIVLSKDPK--DRIMTEEIFGPVLSIYVYKesDLLETMKLVHTStKFALTGAVFGQDEDFVKCALQ 505
Cdd:PRK11903 369 lvdADPAVAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYR--DAAHALALARRG-QGSLVASVYSDDAAFLAAAAL 445
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 320546182 506 EFKMAAGNFYINDKST-------GSVVGQQPFGG-GRMSG 537
Cdd:PRK11903 446 ELADSHGRVHVISPDVaalhtghGNVMPQSLHGGpGRAGG 485
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
323-538 |
5.03e-13 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 71.29 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 323 TGECGGKNFHFIHASADVESVVTSTIRSAFEYC-GQKCSACSRMYVPESLWPQIKEGLVCEAAKLkIGDVQDFSSFTSAV 401
Cdd:cd07137 205 TLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 402 IDDKAFKRITGYIEHAKKSPnlEILAGGTySDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKesDLLETMKLVH 481
Cdd:cd07137 284 VNSHHFQRLSRLLDDPSVAD--KIVHGGE-RDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVK--KIEESIEIIN 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320546182 482 TSTKfALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSVVGQQPFGGGRMSGT 538
Cdd:cd07137 359 SRPK-PLAAYVFTKNKELKRRIVAE--TSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
325-537 |
6.04e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 67.83 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 325 ECGGKN---FHFIHASADVESVVTSTIRSAFEYC-GQKCSACSRMYVPESLWPQIKEgLVCEAAKLKIGDVQDFSSFTSA 400
Cdd:PLN02203 214 ELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGSCaGQACIAIDYVLVEERFAPILIE-LLKSTIKKFFGENPRESKSMAR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 401 VIDDKAFKRITGYIEhaKKSPNLEILAGGTYsDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYvykesdlleTMKLV 480
Cdd:PLN02203 293 ILNKKHFQRLSNLLK--DPRVAASIVHGGSI-DEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPII---------TVKKI 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320546182 481 HTSTKF------ALTGAVFGQDEDFVKCALQEfkMAAGNFYINDKSTGSVVGQQPFGGGRMSG 537
Cdd:PLN02203 361 EDSIAFinskpkPLAIYAFTNNEKLKRRILSE--TSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
209-544 |
1.07e-10 |
|
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: 64.21 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 209 RGIDGFIAAvspFNFTAIGGNLSYTPALM-GNGVLWKP-SDTAMLSNWIIfKIMREAGV-PDGVVNFVPAD-GPVFgDTI 284
Cdd:cd07128 145 RGVAVHINA---FNFPVWGMLEKFAPALLaGVPVIVKPaTATAYLTEAVV-KDIVESGLlPEGALQLICGSvGDLL-DHL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 285 TASPHLAginFTGSVPTFNRLWKQ---VGNNIdnyvnfpRLTGECGGKNFHFIHASAD---------VESVVTSTIRSAf 352
Cdd:cd07128 220 GEQDVVA---FTGSAATAAKLRAHpniVARSI-------RFNAEADSLNAAILGPDATpgtpefdlfVKEVAREMTVKA- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 353 eycGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKS-------PNLEI 425
Cdd:cd07128 289 ---GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEaevvfggPDRFE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 426 LAGGTYsdSKGYFVNPTIVLSKDP--KDRIMTEEIFGPVLSIYVYkeSDLLETMKLVHTStKFALTGAVFGQDEDFVKCA 503
Cdd:cd07128 366 VVGADA--EKGAFFPPTLLLCDDPdaATAVHDVEAFGPVATLMPY--DSLAEAIELAARG-RGSLVASVVTNDPAFAREL 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 320546182 504 LQEfkMAA--GNFYINDK-----ST--GSVVGQQPFGG-GRmsgtndkAGG 544
Cdd:cd07128 441 VLG--AAPyhGRLLVLNRdsakeSTghGSPLPQLVHGGpGR-------AGG 482
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
208-501 |
2.29e-08 |
|
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: 56.74 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 208 YRGIDGFIAAVSPFNFTAIGGNLSYTPAL-MGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTIT- 285
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLe 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 286 ASPHLagINFTGSVPTFNRLWKQVGNNIdnyvnfpRLtgECGGKNFHFIHAS-ADVESVVTSTIRSAFEYCGQKCSACSR 364
Cdd:cd07126 219 ANPRM--TLFTGSSKVAERLALELHGKV-------KL--EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 365 MYVPESlWpqIKEGLVCEAAKLkiGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGG------TYSDSKGYf 438
Cdd:cd07126 288 LFAHEN-W--VQAGILDKLKAL--AEQRKLEDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGkpltnhSIPSIYGA- 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320546182 439 VNPTIVL-----SKDPKD-RIMTEEIFGPVLSIYVYKESDL---LETMKLVHTStkfaLTGAVFGQDEDFVK 501
Cdd:cd07126 362 YEPTAVFvpleeIAIEENfELVTTEVFGPFQVVTEYKDEQLplvLEALERMHAH----LTAAVVSNDIRFLQ 429
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
238-512 |
2.71e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 50.17 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 238 GNGVLWKPSDTAMLSNWIIFKIMR----EAGVPDGVVNFVpADGPvfGDTITAS----PHLAGINFTGSvPTFnrlwkqv 309
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLA-ADTP--EEPIAQTlatrPEVRIIDFTGS-NAF------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 310 GNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPES---------LWPQIKEGLV 380
Cdd:cd07127 290 GDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 381 CEAAKLkIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGGTYSDSKgyfVNPTIVLSKDPKDRIM-TEEIF 459
Cdd:cd07127 370 AAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDAR---VRTPLLLKLDASDEAAyAEERF 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 320546182 460 GPVLsiYVYKESDLLETMKLVHTS--TKFALTGAVFGQDEDFVKcALQEFKMAAG 512
Cdd:cd07127 446 GPIA--FVVATDSTDHSIELARESvrEHGAMTVGVYSTDPEVVE-RVQEAALDAG 497
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
213-537 |
4.31e-05 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 46.19 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 213 GFIAAVSPFNFTAIggnLSYTPAL----MGNGVLWKPSDTAMLSNWIIFKIMrEAGVPDGVVNFVpaDGPVFGDTITASP 288
Cdd:PLN02174 114 GVVLVISAWNYPFL---LSIDPVIgaisAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVV--EGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 289 HLAGINFTGSVPTFNRLWKQVGNNIDNYVNfprltgECGGKNFHFIHASADVESVVTSTIRSAFEyC--GQKCSACSRMY 366
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTPVVL------ELGGKSPVVVDSDTDLKVTVRRIIAGKWG-CnnGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 367 VPESLWPQIKEGLVCEAAKLkIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPnlEILAGGTySDSKGYFVNPTIVLS 446
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSD--KIVYGGE-KDRENLKIAPTILLD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546182 447 KDPKDRIMTEEIFGPVLSIyvYKESDLLETMKLVHTSTKfALTGAVFGQDEDfvkcaLQE---FKMAAGNFYINDKSTGS 523
Cdd:PLN02174 337 VPLDSLIMSEEIFGPLLPI--LTLNNLEESFDVIRSRPK-PLAAYLFTHNKK-----LKErfaATVSAGGIVVNDIAVHL 408
|
330
....*....|....
gi 320546182 524 VVGQQPFGGGRMSG 537
Cdd:PLN02174 409 ALHTLPFGGVGESG 422
|
|
| |
