|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-533 |
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: 861.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 10 PVNEPVHGYAPGSPERARLESKLKELAENPVDLPMTIGGeKRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAAL 89
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGG-KEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 90 AAAPAWRAMSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDCPCELVDFWRFNVKYARDLLAEQPPANSP 169
Cdd:cd07123 80 EARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 170 GVWNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEV 249
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 250 SEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCS 329
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVGYFV 409
Cdd:cd07123 320 AASRAYVPESLWPE-VKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 410 RPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRYAAGNFYINDK 489
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDK 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1954849083 490 STGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKETLVP 533
Cdd:cd07123 479 PTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
12-543 |
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: 790.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 12 NEPVHGYAPGSPERARLESKLKELAENPVDLPMTIGGEKRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAA 91
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 92 APAWRAMSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDCPCELVDFWRFNVKYARDLLAEQPPANsPGV 171
Cdd:TIGR01236 82 KKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISA-PGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 172 WNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSE 251
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSAS 331
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 332 SRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSC-TVVAGGTYDDSVGYFVR 410
Cdd:TIGR01236 321 SRLYVPHSKWPE-FKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 411 PTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRYAAGNFYINDKS 490
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 491 TGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKETLVPPTDYPYPHMG 543
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-531 |
2.02e-135 |
|
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: 401.43 E-value: 2.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 41 DLPMTIGGEKRMG-GGDRFDVVQPHNHKArLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGpWR 119
Cdd:COG1012 5 EYPLFIGGEWVAAaSGETFDVINPATGEV-LARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE-RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 120 ETLAASTMLGQSKTAQQAEIDCPcELVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNL 199
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 200 PTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTV 278
Cdd:COG1012 161 KLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 279 GnniekyRTYPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGI 356
Cdd:COG1012 241 A------ENLKRVTLELGGKNPAIVLDDADldAAV--EAAVRGAFGNAGQRCTAASRLLVHESIYDE-FVERLVAAAKAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 357 TMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTY-DDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAV 435
Cdd:COG1012 312 KVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 436 HVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAvVGQQPFGGGRASGTNDKAGaP 515
Cdd:COG1012 391 IPFDD--EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGREGG-R 463
|
490
....*....|....*.
gi 1954849083 516 QNLMRWTLTRAIKETL 531
Cdd:COG1012 464 EGLEEYTETKTVTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-530 |
5.01e-127 |
|
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: 380.77 E-value: 5.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 43 PMTIGGEKrMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPWRETL 122
Cdd:cd07083 20 PLVIGGEW-VDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 123 AASTMLGqSKTAQQaEIDCPCELVDFWRFNVKYARDLLAEQPPANS-PGVWNRLDHRPLeGFVYAITPFNFT-AIAGNLP 200
Cdd:cd07083 99 ATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGL-GAGVVISPWNFPvAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 201 TAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGN 280
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 281 NIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGD 360
Cdd:cd07083 256 LAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEP-VLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 361 VTDLSNFIGAVIDERSFAKNKAAIDraHADPSCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYED 440
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIE--HGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 441 DQYDEMLAQMESVSdYALTGSVIAGDRAAAAYTMEKLryAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 520
Cdd:cd07083 413 DDFAEALEVANSTP-YGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRR 489
|
490
....*....|
gi 1954849083 521 WTLTRAIKET 530
Cdd:cd07083 490 FLEMKAVAER 499
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-529 |
2.13e-100 |
|
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: 312.62 E-value: 2.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 11 VNEPVHGYAPGSpERARLESKLKEL-AENPVDLPMTIGGeKRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAAL 89
Cdd:cd07124 2 RNEPFTDFADEE-NRAAFRAALARVrEELGREYPLVIGG-KEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 90 AAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDCpCELVDFWRFnvkYARDLLAEQPPANS- 168
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADADV-AEAIDFLEY---YAREMLRLRGFPVEm 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 169 -PGVWNRLDHRPLeGFVYAITPFNF-TAIAGNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDG 246
Cdd:cd07124 155 vPGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 247 IEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTYPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQ 324
Cdd:cd07124 234 EEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADldEAA--EGIVRSAFGFQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 325 GQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPscTVVAGGTYDDS 404
Cdd:cd07124 312 GQKCSACSRVIVHESVYDE-FLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG--RLLLGGEVLEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 405 V--GYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAG 482
Cdd:cd07124 389 AaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VG 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1954849083 483 NFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKE 529
Cdd:cd07124 464 NLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
51-527 |
1.10e-98 |
|
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: 306.38 E-value: 1.10e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 51 RMGGGDRFDVVQPHNHKArLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQ 130
Cdd:pfam00171 2 VDSESETIEVINPATGEV-IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEER-KDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 131 SKTAQQAEIDCPcELVDFWRFNVKYARDLLAEQPPaNSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNV 209
Cdd:pfam00171 80 GKPLAEARGEVD-RAIDVLRYYAGLARRLDGETLP-SDPGRLAYTRREPL-GVVGAITPWNFPLLLPAWKIAPALAaGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 210 VVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIekyrtyP 289
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------K 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 290 RMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIG 369
Cdd:pfam00171 231 RVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDE-FVEKLVEAAKKLKVGDPLDPDTDMG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 370 AVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQ 449
Cdd:pfam00171 310 PLISKAQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954849083 450 MESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAVVGqQPFGGGRASGTNDKAGaPQNLMRWTLTRAI 527
Cdd:pfam00171 387 AND-TEYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGREGG-PYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
98-527 |
1.49e-93 |
|
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: 292.19 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPWRETLAASTM-LGQSKTAQQAEIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNRLD 176
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVA---RAADTFRYYAGLARRLHGEVIPSPDPGELAIVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07078 94 REPL-GVVGAITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIekyrtyPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSR 333
Cdd:cd07078 173 HPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADldAAV--KGAVFGAFGNAGQVCTAASR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDS-VGYFVRPT 412
Cdd:cd07078 245 LLVHESIYDE-FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDA-KAEGAKLLCGGKRLEGgKGYFVPPT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTG 492
Cdd:cd07078 323 VLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELAND-TEYGLAAGVFTRDLERALRVAERLE--AGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1954849083 493 AvVGQQPFGGGRASGTNdKAGAPQNLMRWTLTRAI 527
Cdd:cd07078 398 A-EPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
41-531 |
3.91e-83 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 267.96 E-value: 3.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 41 DLPMTIGGEkRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPWRE 120
Cdd:PRK03137 36 DYPLIIGGE-RITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 121 tLAASTMLGQSKTAQQAEIDCpCELVDFWRFnvkYARDLL---AEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIA 196
Cdd:PRK03137 115 -FSAWLVKEAGKPWAEADADT-AEAIDFLEY---YARQMLklaDGKPVESRPGEHNRYFYIPL-GVGVVISPWNFpFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 197 GNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGStktfqylwK 276
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS--------R 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 277 TVGNNI--EKYRTYP------RMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEE 348
Cdd:PRK03137 261 EVGLRIyeRAAKVQPgqiwlkRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDE-VLEK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 349 FAAEIDGITMGDVTDlSNFIGAVIDERSFAKNKAAIDRAHADPSctVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEY 428
Cdd:PRK03137 340 VVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGR--LVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 429 FGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEklRYAAGNFYINDKSTGAVVGQQPFGGGRASGT 508
Cdd:PRK03137 417 FGPVVAFIKAKD--FDHALEIANN-TEYGLTGAVISNNREHLEKARR--EFHVGNLYFNRGCTGAIVGYHPFGGFNMSGT 491
|
490 500
....*....|....*....|...
gi 1954849083 509 NDKAGAPQNLMRWTLTRAIKETL 531
Cdd:PRK03137 492 DSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
41-529 |
8.08e-75 |
|
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: 245.93 E-value: 8.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 41 DLPMTIGGEkRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRE 120
Cdd:TIGR01237 32 TYPLVINGE-RVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRR-RH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 121 TLAASTMLGQSKTAQQAEIDCpCELVDFWRFnvkYARDL--LAEQPPANS-PGVWNRLDHRPLeGFVYAITPFNFT-AIA 196
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEADAEV-AEAIDFMEY---YARQMieLAKGKPVNSrEGETNQYVYTPT-GVTVVISPWNFPfAIM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 197 GNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWK 276
Cdd:TIGR01237 185 VGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 277 TVGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGI 356
Cdd:TIGR01237 265 RAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDE-VVERFVEITESL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 357 TMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpsCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVH 436
Cdd:TIGR01237 344 KVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAE--GRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 437 VYEDdqYDEMLaQMESVSDYALTGSVIAGDRaaAAYTMEKLRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQ 516
Cdd:TIGR01237 422 RASD--FDEAL-EIANNTEYGLTGGVISNNR--DHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPD 496
|
490
....*....|...
gi 1954849083 517 NLMRWTLTRAIKE 529
Cdd:TIGR01237 497 YLALFMQAKTVTE 509
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
23-520 |
3.44e-72 |
|
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: 239.02 E-value: 3.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 23 PERARLESKLKELAENPVDLPMTIGGEKRmgGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDD 102
Cdd:cd07125 15 PLEALADALKAFDEKEWEAIPIINGEETE--TGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 103 RAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPansPGVWNRLDHRPL 180
Cdd:cd07125 93 RAEILEKAADLLEAN-RGELIALAAAEAGKTLADAdaEVR---EAIDFCRYYAAQARELFSDPEL---PGPTGELNGLEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 181 EG---FVyAITPFNF-TAI-AGNlpTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVAL 254
Cdd:cd07125 166 HGrgvFV-CISPWNFpLAIfTGQ--IAAALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 255 EHRDLAGIHFTGSTKTFQYLWKTvgnNIEKYRTYPRMVGETGGKDFVVAHPSADRA-----VLKTAltrgsFEYQGQKCS 329
Cdd:cd07125 243 AHPRIDGVIFTGSTETAKLINRA---LAERDGPILPLIAETGGKNAMIVDSTALPEqavkdVVQSA-----FGSAGQRCS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWnsgfkEEFAAEIDG----ITMGDVTDLSNFIGAVIDERSFAKNKA--AIDRAHAdpscTVVAGGTYDD 403
Cdd:cd07125 315 ALRLLYLQEEIA-----ERFIEMLKGamasLKVGDPWDLSTDVGPLIDKPAGKLLRAhtELMRGEA----WLIAPAPLDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 404 SVGYFVRPTVVEcsDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGN 483
Cdd:cd07125 386 GNGYFVAPGIIE--IVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDINA-TGYGLTLGIHSRDEREIEYWRERVE--AGN 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 1954849083 484 FYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 520
Cdd:cd07125 461 LYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
98-513 |
5.60e-68 |
|
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: 223.65 E-value: 5.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPWRETLAASTM-LGQSKTAQQAEIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNRLD 176
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVA---RAIDTFRYAAGLADKLGGPELPSPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd06534 90 REPL-GVVGVITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIekyrtyPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSR 333
Cdd:cd06534 169 HPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADldAAV--EGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAaeidgitmgdvtdlsnfigavidersfaknkaaidrahadpsctvvaggtyddsvgyfvrpTV 413
Cdd:cd06534 241 LLVHESIYDE-FVEKLV-------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 414 VECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGa 493
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALAND-TEYGLTAGVFTRDLNRALRVAERLR--AGTVYINDSSIG- 332
|
410 420
....*....|....*....|
gi 1954849083 494 VVGQQPFGGGRASGTNDKAG 513
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGG 352
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
98-507 |
8.47e-60 |
|
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: 203.92 E-value: 8.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELL---AGPWRETLAASTmlGQSKTAQQAEIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNR 174
Cdd:cd07104 19 TPPQERAAILRKAAEILeerRDEIADWLIRES--GSTRPKAAFEVG---AAIAILREAAGLPRRPEGEILPSDVPGKESM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSP-TQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEV 252
Cdd:cd07104 94 VRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSrTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 253 ALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYrtyprmVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSA 330
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKV------ALELGGNNPLIVLDDADldLAV--SAAAFGAFLHQGQICMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 331 SSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDdsvGYFVR 410
Cdd:cd07104 245 AGRILVHESVYDE-FVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAA-GARLLTGGTYE---GLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 411 PTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKS 490
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVE-LANDTEYGLSAAVFTRDLERAMAFAERLE--TGMVHINDQT 394
|
410
....*....|....*....
gi 1954849083 491 T--GAVVgqqPFGGGRASG 507
Cdd:cd07104 395 VndEPHV---PFGGVKASG 410
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
104-507 |
8.55e-56 |
|
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: 193.92 E-value: 8.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 104 AAIILRAAELLAG--------PWRETLAastmlgqsktaqQAEIdcpceLVDFWRFNVKYARDLLAEQPPANSPGVWNRL 175
Cdd:cd07114 53 ADLIEANAEELAEletrdngkLIRETRA------------QVRY-----LAEWYRYYAGLADKIEGAVIPVDKGDYLNFT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPtQTHAAVL-LMQLLEEAGLPKGVINLVTGDGIEVSEVA 253
Cdd:cd07114 116 RREPL-GVVAAITPWNSPLLLLAKKLAPALaAGNTVVLKPSE-HTPASTLeLAKLAEEAGFPPGVVNVVTGFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYrtyprmVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSR 333
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAENLAPV------TLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVVAGG----TYDDSVGYFV 409
Cdd:cd07114 268 LLVQRSIYDE-FVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGA-RVLTGGerpsGADLGAGYFF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 410 RPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIND- 488
Cdd:cd07114 346 EPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALAND-SEYGLAAGIWTRDLARAHRVARAIE--AGTVWVNTy 420
|
410
....*....|....*....
gi 1954849083 489 KSTGAVVgqqPFGGGRASG 507
Cdd:cd07114 421 RALSPSS---PFGGFKDSG 436
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
100-507 |
3.42e-54 |
|
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: 189.46 E-value: 3.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 100 FDDRAAIILRAAELLAGpwRETLAASTMLGQSKTAQQAEIDCPCELVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRP 179
Cdd:cd07150 42 PSERERILLKAAEIMER--RADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 180 LeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRD 258
Cdd:cd07150 120 L-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 259 LAGIHFTGSTKTFQYLWKTVGNNIEKYrtyprmVGETGGKD--FVVAHPSADRAVlkTALTRGSFEYQGQKCSASSRAYV 336
Cdd:cd07150 199 VRMVTFTGSTAVGREIAEKAGRHLKKI------TLELGGKNplIVLADADLDYAV--RAAAFGAFMHQGQICMSASRIIV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 337 PASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDdsvGYFVRPTVVEC 416
Cdd:cd07150 271 EEPVYDE-FVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAK-GAKLLTGGKYD---GNFYQPTVLTD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 417 SDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKS--TGAV 494
Cdd:cd07150 346 VTPDMRIFREETFGPVTSVIPAKD--AEEALE-LANDTEYGLSAAILTNDLQRAFKLAERLE--SGMVHINDPTilDEAH 420
|
410
....*....|...
gi 1954849083 495 VgqqPFGGGRASG 507
Cdd:cd07150 421 V---PFGGVKASG 430
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
46-507 |
5.27e-54 |
|
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: 189.77 E-value: 5.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEkRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAAS 125
Cdd:cd07097 5 IDGE-WVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEAR-KEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 126 TMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIAGnLPTA 202
Cdd:cd07097 83 LTREEGKTLPEArgEVT---RAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPL-GVVGLITPWNFpIAIPA-WKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 203 PALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNN 281
Cdd:cd07097 158 PALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 282 IEKYRTyprmvgETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMG 359
Cdd:cd07097 238 GARVQL------EMGGKNPLVVLDDADldLAV--ECAVQGAFFSTGQRCTASSRLIVTEGIHDR-FVEALVERTKALKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 360 DVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYD-DSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVY 438
Cdd:cd07097 309 DALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 439 EDdqYDEMLAQMESVsDYALTGSVIAGDRAAAaytMEKLRYA-AGNFYINDKSTGaVVGQQPFGGGRASG 507
Cdd:cd07097 389 RD--YDEALAIANDT-EFGLSAGIVTTSLKHA---THFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSS 451
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
98-508 |
6.64e-54 |
|
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: 188.96 E-value: 6.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPAN-SPGVWNR 174
Cdd:cd07149 40 LPAYERAEILERAAQLLEER-REEFARTIALEAGKPIKDArkEVD---RAIETLRLSAEEAKRLAGETIPFDaSPGGEGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDH---RPLeGFVYAITPFNF----------TAIAGnlptapalmGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINL 241
Cdd:cd07149 116 IGFtirEPI-GVVAAITPFNFplnlvahkvgPAIAA---------GNAVVLKPASQTPLSALKLAELLLEAGLPKGALNV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 242 VTGDGIEVSEVALEHRDLAGIHFTGSTKtfqylwktVGNNIEKYRTYPRMVGETGGKDFVVAHPSADravLKTALTR--- 318
Cdd:cd07149 186 VTGSGETVGDALVTDPRVRMISFTGSPA--------VGEAIARKAGLKKVTLELGSNAAVIVDADAD---LEKAVERcvs 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 319 GSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAG 398
Cdd:cd07149 255 GAFANAGQVCISVQRIFVHEDIYDE-FLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEA-VEGGARLLTG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 399 GTYDdsvGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLR 478
Cdd:cd07149 333 GKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDT--LDEAIAMAND-SPYGLQAGVFTNDLQKALKAARELE 406
|
410 420 430
....*....|....*....|....*....|
gi 1954849083 479 yaAGNFYINDKSTgAVVGQQPFGGGRASGT 508
Cdd:cd07149 407 --VGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
177-507 |
4.47e-51 |
|
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: 181.26 E-value: 4.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07112 122 REPL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtypRMVGETGGKD-FVVAH--PSADRAVLKTALtrGSFEYQGQKCSASS 332
Cdd:cd07112 201 HMDVDALAFTGSTEVGRRFLEYSGQSNLK-----RVWLECGGKSpNIVFAdaPDLDAAAEAAAA--GIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIwnsgfKEEF----AAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGG--TYDDSVG 406
Cdd:cd07112 274 RLLVHESI-----KDEFlekvVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGkrVLTETGG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 407 YFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYI 486
Cdd:cd07112 348 FFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVA-LANDSVYGLAASVWTSDLSRAHRVARRLR--AGTVWV 422
|
330 340
....*....|....*....|.
gi 1954849083 487 NDKSTGAVvgQQPFGGGRASG 507
Cdd:cd07112 423 NCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
46-522 |
7.10e-51 |
|
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: 181.39 E-value: 7.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEKRMG-GGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLA- 123
Cdd:cd07131 3 IGGEWVDSaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKR-KEELAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 124 -ASTMLGQSKTAQQAEIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIAGNLpT 201
Cdd:cd07131 82 lVTREMGKPLAEGRGDVQ---EAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPI-GVVALITPWNFpVAIPSWK-I 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 202 APALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGn 280
Cdd:cd07131 157 FPALVcGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 281 niekyRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGD 360
Cdd:cd07131 236 -----RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE-FLKRFVERAKRLRVGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 361 VTDLSNFIGAVIDERSFAK--NKAAIDRAHADPSCT---VVAGGTYDDsvGYFVRPTVVECSDPANEVFTTEYFGPFLAv 435
Cdd:cd07131 310 GLDEETDMGPLINEAQLEKvlNYNEIGKEEGATLLLggeRLTGGGYEK--GYFVEPTVFTDVTPDMRIAQEEIFGPVVA- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 436 hVYEDDQYDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAVVgQQPFGGGRASGTNDKAGAP 515
Cdd:cd07131 387 -LIEVSSLEEAIE-IANDTEYGLSSAIYTEDVNKAFRARRDLE--AGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGT 461
|
....*..
gi 1954849083 516 QNLMRWT 522
Cdd:cd07131 462 TALDAFT 468
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
98-507 |
2.40e-50 |
|
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: 179.17 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLagpwRE---TLAASTMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVW 172
Cdd:cd07103 38 TTARERAAILRRWADLI----REraeDLARLLTLEQGKPLAEArgEVD---YAASFLEWFAEEARRIYGRTIPSPAPGKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 173 NRLDHRPLeGFVYAITPFNFTAiagNLPT---APAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIE 248
Cdd:cd07103 111 ILVIKQPV-GVVAAITPWNFPA---AMITrkiAPALaAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 249 VSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYrtypRMvgETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQ 326
Cdd:cd07103 187 IGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV----SL--ELGGNAPFIVFDDADldKAV--DGAIASKFRNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 327 KCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVVAGGTYDDSVG 406
Cdd:cd07103 259 TCVCANRIYVHESIYDE-FVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGA-KVLTGGKRLGLGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 407 YFVRPTVV-ECSDPAnEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRYaaGNFY 485
Cdd:cd07103 337 YFYEPTVLtDVTDDM-LIMNEETFGPVAPIIPFDTE--DEVIARAND-TPYGLAAYVFTRDLARAWRVAEALEA--GMVG 410
|
410 420
....*....|....*....|...
gi 1954849083 486 INdksTGAVVG-QQPFGGGRASG 507
Cdd:cd07103 411 IN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
98-527 |
1.79e-49 |
|
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: 177.38 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPWRETLAASTM-----LGQSKTAQQAEIdcpcelVDFWRFNVKYARDLLAEQPPANSPGVW 172
Cdd:cd07139 57 LSPAERAAVLRRLADALEARADELARLWTAengmpISWSRRAQGPGP------AALLRYYAALARDFPFEERRPGSGGGH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 173 NRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDgIEVSE 251
Cdd:cd07139 131 VLVRREPV-GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSAS 331
Cdd:cd07139 209 YLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 332 SRAYVPASIWnSGFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVVAGGTYDDSV--GYFV 409
Cdd:cd07139 283 TRILVPRSRY-DEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGA-RLVTGGGRPAGLdrGWFV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 410 RPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDK 489
Cdd:cd07139 361 EPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE--DDAVR-IANDSDYGLSGSVWTADVERGLAVARRIR--TGTVGVNGF 435
|
410 420 430
....*....|....*....|....*....|....*...
gi 1954849083 490 STGAVVgqqPFGGGRASGTNDKAGaPQNLMRWTLTRAI 527
Cdd:cd07139 436 RLDFGA---PFGGFKQSGIGREGG-PEGLDAYLETKSI 469
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
98-522 |
3.04e-49 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 175.94 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELL------AGPW--RETlaastmlGQSKTAQQAEIDCPCELVdfwrfnvkYARDLLAEQPP---- 165
Cdd:cd07152 32 TPPRERAAVLRRAADLLeehadeIADWivRES-------GSIRPKAGFEVGAAIGEL--------HEAAGLPTQPQgeil 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 166 ANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSP-TQTHAAVLLMQLLEEAGLPKGVINLVT 243
Cdd:cd07152 97 PSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDPrTPVSGGVVIARLFEEAGLPAGVLHVLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 244 GDGiEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTyprmvgETGGKDFVVAHPSADRAVLKTALTRGSFEY 323
Cdd:cd07152 176 GGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL------ELGGKNALIVLDDADLDLAASNGAWGAFLH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 324 QGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSfAKNKAAIDRAHADPSCTVVAGGTYDd 403
Cdd:cd07152 249 QGQICMAAGRHLVHESVADA-YTAKLAAKAKHLPVGDPATGQVALGPLINARQ-LDRVHAIVDDSVAAGARLEAGGTYD- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 404 svGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGN 483
Cdd:cd07152 326 --GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVA-LANDTEYGLSAGIISRDVGRAMALADRLR--TGM 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 1954849083 484 FYINDKSTGAVVgQQPFGGGRASGTNDKAGAPQNLMRWT 522
Cdd:cd07152 399 LHINDQTVNDEP-HNPFGGMGASGNGSRFGGPANWEEFT 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
98-508 |
4.67e-49 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 175.83 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKT-AQQAEIDCPCELVDFwRFNVKYARDLLAEQPPaNSPGVWNRLD 176
Cdd:cd07093 38 MSPAERARILHKVADLIEAR-ADELALLESLDTGKPiTLARTRDIPRAAANF-RFFADYILQLDGESYP-QDGGALNYVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNftaiagnLP-------TAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIE 248
Cdd:cd07093 115 RQPV-GVAGLITPWN-------LPlmlltwkIAPALaFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 249 VSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTyprmvgETGGKDFVVAHPSADR-AVLKTALtRGSFEYQGQK 327
Cdd:cd07093 187 AGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL------ELGGKNPNIVFADADLdRAVDAAV-RSSFSNNGEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 328 CSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGG----TYDD 403
Cdd:cd07093 260 CLAGSRILVQRSIYDE-FLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE-GATILTGGgrpeLPDL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 404 SVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVsDYALTGSVIAGDRAAAAYTMEKLRyaAGN 483
Cdd:cd07093 338 EGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDT-PYGLAAYVWTRDLGRAHRVARRLE--AGT 412
|
410 420 430
....*....|....*....|....*....|
gi 1954849083 484 FYIN-----DKSTgavvgqqPFGGGRASGT 508
Cdd:cd07093 413 VWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
99-507 |
2.00e-48 |
|
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: 174.09 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAgPWRETLAASTMLGQSK---TAQQAEIDCpceLVDFWRFNVKYARDLLAEQPPANsPGVWNRL 175
Cdd:cd07108 39 PARERGKLLARIADALE-ARSEELARLLALETGNalrTQARPEAAV---LADLFRYFGGLAGELKGETLPFG-PDVLTYT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGIEVSEVAL 254
Cdd:cd07108 114 VREPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 255 EHRDLAGIHFTGSTKTFQYLWKTVGnniekyrtyPRMVG---ETGGKDFVVAHPSAD-RAVLKTALTRGSFEYQGQKCSA 330
Cdd:cd07108 192 DHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvslELGGKSPMIVFPDADlDDAVDGAIAGMRFTRQGQSCTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 331 SSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGT----YDDSVG 406
Cdd:cd07108 263 GSRLFVHEDIYDA-FLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 407 YFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYI 486
Cdd:cd07108 342 FFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDEVIA-MANDSHYGLAAYVWTRDLGRALRAAHALE--AGWVQV 416
|
410 420
....*....|....*....|.
gi 1954849083 487 NdKSTGAVVGQQpFGGGRASG 507
Cdd:cd07108 417 N-QGGGQQPGQS-YGGFKQSG 435
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
93-507 |
4.85e-48 |
|
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: 172.71 E-value: 4.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 93 PAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIdcpcEL---VDFWRFNVKYARDLLAEQppaNSP 169
Cdd:cd07106 33 PGWSATPLEERRAALLAIADAIEAN-AEELARLLTLEQGKPLAEAQF----EVggaVAWLRYTASLDLPDEVIE---DDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 170 GVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGiE 248
Cdd:cd07106 105 TRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGD-E 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 249 VSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKC 328
Cdd:cd07106 182 LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 329 SASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYF 408
Cdd:cd07106 256 AAIKRLYVHESIYDE-FCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK-GAKVLAGGEPLDGPGYF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 409 VRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINd 488
Cdd:cd07106 334 IPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE--DEVIARAND-SEYGLGASVWSSDLERAEAVARRLE--AGTVWIN- 407
|
410
....*....|....*....
gi 1954849083 489 kSTGAVVGQQPFGGGRASG 507
Cdd:cd07106 408 -THGALDPDAPFGGHKQSG 425
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-527 |
5.07e-48 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 179.62 E-value: 5.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 22 SPERARLESKLKELAENPVDLPMTIGGekrmgGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFD 101
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 102 DRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQ--AEIDcpcELVDFWRFNVKYARDLLAEQPPANSP-GVWNRLDHR 178
Cdd:PRK11904 608 ERAAILERAADLLEAN-RAELIALCVREAGKTLQDaiAEVR---EAVDFCRYYAAQARRLFGAPEKLPGPtGESNELRLH 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLEGFVyAITPFNFT-AI-AGnlPTAPALM-GNVVVWKPSPtQT----HAAVllmQLLEEAGLPKGVINLVTGDGIEVSE 251
Cdd:PRK11904 684 GRGVFV-CISPWNFPlAIfLG--QVAAALAaGNTVIAKPAE-QTpliaAEAV---KLLHEAGIPKDVLQLLPGDGATVGA 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVGNniekyRTYP--RMVGETGGKDFVVAHPSADR-AVLKTALTrGSFEYQGQKC 328
Cdd:PRK11904 757 ALTADPRIAGVAFTGSTETARIINRTLAA-----RDGPivPLIAETGGQNAMIVDSTALPeQVVDDVVT-SAFRSAGQRC 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 329 SASSRAYVPASIwnsgfkeefaAE--IDGI-------TMGDVTDLSNFIGAVIDERSFAKNKAAIDRahADPSCTVVAGG 399
Cdd:PRK11904 831 SALRVLFVQEDI----------ADrvIEMLkgamaelKVGDPRLLSTDVGPVIDAEAKANLDAHIER--MKREARLLAQL 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 400 TYDDS--VGYFVRPTVVECSDPAneVFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKL 477
Cdd:PRK11904 899 PLPAGteNGHFVAPTAFEIDSIS--QLEREVFGPILHVIRYKASDLDKVIDAINA-TGYGLTLGIHSRIEETADRIADRV 975
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1954849083 478 RyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAI 527
Cdd:PRK11904 976 R--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
98-507 |
6.25e-48 |
|
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: 172.91 E-value: 6.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPANSPGVWNRL 175
Cdd:cd07118 40 MSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIE---GAADLWRYAASLARTLHGDSYNNLGDDMLGLV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFTA--IAGNLPTAPAlMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVA 253
Cdd:cd07118 116 LREPI-GVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprmVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASS 332
Cdd:cd07118 194 TEHPDVDMVSFTGSTRVGKAIAAAAARNLKK-------VSlELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVGYFVRPT 412
Cdd:cd07118 267 RLLVHESIADA-FVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESVsDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTG 492
Cdd:cd07118 346 IFTDVTPDMAIAREEIFGPVLSVLTFDT--VDEAIALANDT-VYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDG 420
|
410
....*....|....*
gi 1954849083 493 AVvgQQPFGGGRASG 507
Cdd:cd07118 421 SP--ELPFGGFKQSG 433
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
98-508 |
1.21e-47 |
|
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: 172.15 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDCPCELvdfWRFNVKYARDLLAEQPPA-NSPGVWNR 174
Cdd:cd07145 40 LPAYKRYKILMKVAELIERR-KEELAKLLTIEVGKPIKQSrvEVERTIRL---FKLAAEEAKVLRGETIPVdAYEYNERR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 L---DHRPLeGFVYAITPFNFTAiagNLPT---APAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGI 247
Cdd:cd07145 116 IaftVREPI-GVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 248 EVSEVALEHRDLAGIHFTGSTKtfqylwktVGNNIEKY--RTYPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEY 323
Cdd:cd07145 192 EVGDEIVTNPKVNMISFTGSTA--------VGLLIASKagGTGKKVALELGGSDPMIVLKDADleRAV--SIAVRGRFEN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 324 QGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDD 403
Cdd:cd07145 262 AGQVCNAVKRILVEEEVYDK-FLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDA-VEKGGKILYGGKRDE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 404 svGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRYaaGN 483
Cdd:cd07145 340 --GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTNDINRALKVARELEA--GG 412
|
410 420
....*....|....*....|....*
gi 1954849083 484 FYINDkSTGAVVGQQPFGGGRASGT 508
Cdd:cd07145 413 VVIND-STRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
98-514 |
2.83e-47 |
|
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: 170.53 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELL---AGPWRETLAASTmlGQSKTAQQAEIDCPCELVDFwrfNVKYARDLLAEQPPANsPGVWNR 174
Cdd:cd07095 19 LSLEERAAILRRFAELLkanKEELARLISRET--GKPLWEAQTEVAAMAGKIDI---SIKAYHERTGERATPM-AQGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVA 253
Cdd:cd07095 93 LRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGR-ETGEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYrtyprMVGETGGKDFVVAHPSAD-RAVLKTALtRGSFEYQGQKCSASS 332
Cdd:cd07095 171 AAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADiDAAAYLIV-QSAFLTAGQRCTCAR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSGFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSvGYFVRPT 412
Cdd:cd07095 245 RLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAG-TAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPAnEVFTTEYFGPFLAVHVYEDdqYDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTG 492
Cdd:cd07095 324 IIDVTDAA-DVPDEEIFGPLLQVYRYDD--FDEAIA-LANATRFGLSAGLLSDDEALFERFLARIR--AGIVNWNRPTTG 397
|
410 420
....*....|....*....|..
gi 1954849083 493 AvVGQQPFGGGRASGtNDKAGA 514
Cdd:cd07095 398 A-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
98-507 |
5.93e-47 |
|
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: 169.93 E-value: 5.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGpWRETLAASTMLGQSKTAQQAE-IDCPcELVDFWRFNVKYARDLLAEQPPAnSPGVWNRLD 176
Cdd:cd07115 38 MDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARrLDVP-RAADTFRYYAGWADKIEGEVIPV-RGPFLNYTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07115 115 REPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSAD-RAVLKTALTrGSFEYQGQKCSASSRA 334
Cdd:cd07115 194 HPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFADADlDAAVRAAAT-GIFYNQGQMCTAGSRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 335 YVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPTVV 414
Cdd:cd07115 267 LVHESIYDE-FLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE-GARLLTGGKRPGARGFFVEPTIF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 415 ECSDPANEVFTTEYFGPFLAVHVYEDdqyDEMLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTGAV 494
Cdd:cd07115 345 AAVPPEMRIAQEEIFGPVVSVMRFRD---EEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRF 417
|
410
....*....|...
gi 1954849083 495 VGQQPFGGGRASG 507
Cdd:cd07115 418 DPGSPFGGYKQSG 430
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
103-507 |
6.33e-47 |
|
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: 169.92 E-value: 6.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 103 RAAIILRAAELLaGPWRETLAASTMLGQSKTAQQA--EIDcpcELVDFWRFNVKYARDLLAEQPPAN-SPGVWNRLD--- 176
Cdd:cd07094 45 RMAILERAADLL-KKRAEEFAKIIACEGGKPIKDArvEVD---RAIDTLRLAAEEAERIRGEEIPLDaTQGSDNRLAwti 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAiagNLPT---APAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEV 252
Cdd:cd07094 121 REPV-GVVLAITPFNFPL---NLVAhklAPAIaTGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 253 ALEHRDLAGIHFTGSTKtfqylwktVGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASS 332
Cdd:cd07094 197 FAADERVAMLSFTGSAA--------VGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVgyfVRPT 412
Cdd:cd07094 269 RIYVHEELYDE-FIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEA-VEAGARLLCGGERDGAL---FKPT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDkSTG 492
Cdd:cd07094 344 VLEDVPRDTKLSTEETFGPVVPIIRYDD--FEEAIRIANS-TDYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSA 417
|
410
....*....|....*
gi 1954849083 493 AVVGQQPFGGGRASG 507
Cdd:cd07094 418 FRTDWMPFGGVKESG 432
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
98-507 |
1.06e-46 |
|
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: 169.35 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPW---RETLAASTmlGQSK-TAQQAEIDCPCELVDFWrfnVKYARDLLAEQ--PPANSPGV 171
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKeelRALLVAEV--GAPVmTARAMQVDGPIGHLRYF---ADLADSFPWEFdlPVPALRGG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 172 WNR--LDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIE 248
Cdd:cd07089 114 PGRrvVRREPV-GVVAAITPWNFPFFLNLAKLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 249 VSEVALEHRDLAGIHFTGSTktfqylwkTVGNNIEKY--RTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQ 326
Cdd:cd07089 193 VGEALTTDPRVDMVSFTGST--------AVGRRIMAQaaATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 327 KCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDD-SV 405
Cdd:cd07089 265 GCALTTRLLVPRSRYDE-VVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPAGlDK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 406 GYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFY 485
Cdd:cd07089 344 GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVR-IANDSDYGLSGGVWSADVDRAYRVARRIR--TGSVG 418
|
410 420
....*....|....*....|...
gi 1954849083 486 INdksTGAVVG-QQPFGGGRASG 507
Cdd:cd07089 419 IN---GGGGYGpDAPFGGYKQSG 438
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
174-522 |
1.12e-46 |
|
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: 169.67 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 174 RLDHRPLE-----GFVYAITPFNF-TAIAG-NLptAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEA----GLPKGVINL 241
Cdd:cd07086 122 RPGHRLMEqwnplGVVGVITAFNFpVAVPGwNA--AIALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 242 VTGDGiEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGnniekyRTYPRMVGETGGKDFVVAHPSAD-----RAVLktal 316
Cdd:cd07086 200 VTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVA------RRFGRVLLELGGNNAIIVMDDADldlavRAVL---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 317 tRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVV 396
Cdd:cd07086 269 -FAAVGTAGQRCTTTRRLIVHESVYDE-FLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 397 AGGTY--DDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESVSdYALTGSVIAGDRAAAAYTM 474
Cdd:cd07086 346 TGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS--LEEAIAINNDVP-QGLSSSIFTEDLREAFRWL 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1954849083 475 EKLRYAAGNFYINDKSTGAVVGqQPFGGGRASGTNDKAG--APQNLMRWT 522
Cdd:cd07086 423 GPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGsdAWKQYMRRS 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
103-487 |
1.21e-46 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 169.37 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 103 RAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDCPCelvDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPL 180
Cdd:cd07088 59 RAAYLRKLADLIREN-ADELAKLIVEEQGKTLSLArvEVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 181 eGFVYAITPFNFTA--IAGNLptAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHR 257
Cdd:cd07088 135 -GVVAGILPWNFPFflIARKL--APALVtGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 DLAGIHFTGSTKTFQYLWKTVGNNIEKYRTyprmvgETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSRAY 335
Cdd:cd07088 212 KVGMISLTGSTEAGQKIMEAAAENITKVSL------ELGGKAPAIVMKDADldLAV--KAIVDSRIINCGQVCTCAERVY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 336 VPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDS-VGYFVRPTVV 414
Cdd:cd07088 284 VHEDIYDE-FMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEA-GATLLTGGKRPEGeKGYFYEPTVL 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 415 ECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRYaaGNFYIN 487
Cdd:cd07088 362 TNVRQDMEIVQEEIFGPVLPVVKFSS--LDEAIELAND-SEYGLTSYIYTENLNTAMRATNELEF--GETYIN 429
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
98-507 |
3.33e-46 |
|
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: 168.64 E-value: 3.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDCPCELVDFwRFnvkYARDLLAEQPPANS--PGVWNRL 175
Cdd:cd07119 56 LPAQERAALLFRIADKIRED-AEELARLETLNTGKTLRESEIDIDDVANCF-RY---YAGLATKETGEVYDvpPHVISRT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPS---PTQTHAavlLMQLLEEAGLPKGVINLVTGDGIEVSE 251
Cdd:cd07119 131 VREPV-GVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSevtPLTTIA---LFELIEEAGLPAGVVNLVTGSGATVGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprmVG-ETGGKDFVVAHPSAD-RAVLKTALTrGSFEYQGQKCS 329
Cdd:cd07119 207 ELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK-------VAlELGGKNPNIVFADADfETAVDQALN-GVFFNAGQVCS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSV---G 406
Cdd:cd07119 279 AGSRLLVEESIHDK-FVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 407 YFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAqmeSVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYI 486
Cdd:cd07119 358 YFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA---NDTPYGLAGAVWTKDIARANRVARRLR--AGTVWI 432
|
410 420
....*....|....*....|.
gi 1954849083 487 NDksTGAVVGQQPFGGGRASG 507
Cdd:cd07119 433 ND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
46-508 |
2.37e-44 |
|
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: 163.38 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEKRMGGGDRF-DVVQPHNhKARLGTYANATQQDAQDAIDAALAA-APAWRAMSFDDRAAIILRAAELLAGPwRETLA 123
Cdd:cd07113 4 IDGRPVAGQSEKRlDITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQH-GEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 124 ASTMLGQSKT---AQQAEIDCPcelVDFWRFNVKYARDLLAE--QPPANSPG--VWNRLDHRPLEGFVYAITPFNFTAIA 196
Cdd:cd07113 82 QLETLCSGKSihlSRAFEVGQS---ANFLRYFAGWATKINGEtlAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 197 GNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVALEHRDLAGIHFTGSTKTFQYLW 275
Cdd:cd07113 159 AVWKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 276 KTVGNNIEkyrtypRMVGETGGKD--FVVAHPSADRAVlkTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEI 353
Cdd:cd07113 238 RQAASDLT------RVTLELGGKNaaAFLKDADIDWVV--EGLLTAGFLHQGQVCAAPERFYVHRSKFDE-LVTKLKQAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 354 DGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFL 433
Cdd:cd07113 309 SSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 434 AVHVYEDdqyDEMLAQMESVSDYALTGSVIAGDRAAAaytmekLRYA----AGNFYINDKS--TGAVvgqqPFGGGRASG 507
Cdd:cd07113 388 SFVPYED---EEELIQLINDTPFGLTASVWTNNLSKA------LRYIprieAGTVWVNMHTflDPAV----PFGGMKQSG 454
|
.
gi 1954849083 508 T 508
Cdd:cd07113 455 I 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
99-527 |
4.32e-44 |
|
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: 162.01 E-value: 4.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIDCPCELVDFWrfnVKYARDLLAEQ---PPANSPGVWN 173
Cdd:cd07099 38 GVEGRAQRLLRWKRALADH-ADELAEllHAETGKPRADAGLEVLLALEAIDWA---ARNAPRVLAPRkvpTGLLMPNKKA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 174 RLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEV 252
Cdd:cd07099 114 TVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 253 ALEHR-DLagIHFTGSTKTfqylWKTVGNNIEKYRTyPRMVgETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCS 329
Cdd:cd07099 192 LIDAGvDK--VAFTGSVAT----GRKVMAAAAERLI-PVVL-ELGGKDPMIVLADADleRAA--AAAVWGAMVNAGQTCI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERsfaknKAAIDRAHADPS----CTVVAGGTYDDSV 405
Cdd:cd07099 262 SVERVYVHESVYDE-FVARLVAKARALRPGADDIGDADIGPMTTAR-----QLDIVRRHVDDAvakgAKALTGGARSNGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 406 GYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFY 485
Cdd:cd07099 336 GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIA-LANDSRYGLSASVFSRDLARAEAIARRLE--AGAVS 410
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1954849083 486 INDKSTGAVVGQQPFGGGRASGTNDKAGAPqNLMRWTLTRAI 527
Cdd:cd07099 411 INDVLLTAGIPALPFGGVKDSGGGRRHGAE-GLREFCRPKAI 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
99-529 |
1.21e-43 |
|
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: 160.94 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAeIDCPCELVDFWRFNVKYARDLLAEQPPANS-PGVW-NRLD 176
Cdd:cd07101 38 PFAERAAVFLRFHDLVLER-RDELLDLIQLETGKARRHA-FEEVLDVAIVARYYARRAERLLKPRRRRGAiPVLTrTTVN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07101 116 RRPK-GVVGVISPWNYPLTLAVSDAIPALLaGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDlaGIHFTGSTKTFQYLWKTVGNniekyrtypRMVG---ETGGKD--FVVAHPSADRAVlkTALTRGSFEYQGQKCSA 330
Cdd:cd07101 195 NAD--YVMFTGSTATGRVVAERAGR---------RLIGcslELGGKNpmIVLEDADLDKAA--AGAVRACFSNAGQLCVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 331 SSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVG-YFV 409
Cdd:cd07101 262 IERIYVHESVYDE-FVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK-GATVLAGGRARPDLGpYFY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 410 RPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIND- 488
Cdd:cd07101 340 EPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELAND-TDYGLNASVWTRDGARGRRIAARLR--AGTVNVNEg 414
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1954849083 489 --KSTGAVvgQQPFGGGRASGTNDKAGaPQNLMRWTLTRAIKE 529
Cdd:cd07101 415 yaAAWASI--DAPMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
165-507 |
1.26e-43 |
|
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: 161.32 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 165 PANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKP-SPTQTHAAVLLMQLLEEAGLPKGVINLV 242
Cdd:cd07151 116 PSDVPGKENRVYREPL-GVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 243 TGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKD-FVV-AHPSADRAVLKTALtrGS 320
Cdd:cd07151 195 VGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK------KVALELGGNNpFVVlEDADIDAAVNAAVF--GK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 321 FEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGT 400
Cdd:cd07151 267 FLHQGQICMAINRIIVHEDVYDE-FVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEE-GATLLVGGE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 401 YDDSVgyfVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAqmeSVSDYALTGSVIAGD--RAAAAytmeKLR 478
Cdd:cd07151 345 AEGNV---LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA---NDTEYGLSGAVFTSDleRGVQF----ARR 414
|
330 340 350
....*....|....*....|....*....|..
gi 1954849083 479 YAAGNFYINDKStgavVGQQP---FGGGRASG 507
Cdd:cd07151 415 IDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
99-487 |
1.68e-43 |
|
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: 160.49 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIDCPCELVDFWrfnVKYARDLLAEQPPANSPGVWNRLD 176
Cdd:cd07102 38 PLEERKAIVTRAVELLAAN-TDEIAEelTWQMGRPIAQAGGEIRGMLERARYM---ISIAEEALADIRVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFN---FTAIAGnlpTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEV 252
Cdd:cd07102 114 REPL-GVVLIIAPWNypyLTAVNA---VIPALLaGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 253 ALEHRDLAGIHFTGSTKTFQYLWKTVGnniekyrtyPRMVG---ETGGKDFVVAHPSADravLKTA---LTRGSFEYQGQ 326
Cdd:cd07102 189 LIADPRIDHVSFTGSVAGGRAIQRAAA---------GRFIKvglELGGKDPAYVRPDAD---LDAAaesLVDGAFFNSGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 327 KCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAID-------RAHADPsctvvAGG 399
Cdd:cd07102 257 SCCSIERIYVHESIYDA-FVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakgaRALIDG-----ALF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 400 TYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLry 479
Cdd:cd07102 331 PEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIALMND-SEYGLTASVWTKDIARAEALGEQL-- 405
|
....*...
gi 1954849083 480 AAGNFYIN 487
Cdd:cd07102 406 ETGTVFMN 413
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
46-507 |
5.32e-43 |
|
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: 159.66 E-value: 5.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEKRMGGGDRFDVVQPHNHKaRLGTYANATQQDAQDAIDAALAA-APAWRAMSFDDRAAIILRAAELLAgPWRETLAA 124
Cdd:cd07082 6 INGEWKESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 125 STML--GQSKTAQQAEIDCPCELVDfwrfnvkYARDLLAEQPPANSPGVWNRLDHR--------PLeGFVYAITPFN--- 191
Cdd:cd07082 84 LLMWeiGKTLKDALKEVDRTIDYIR-------DTIEELKRLDGDSLPGDWFPGTKGkiaqvrrePL-GVVLAIGPFNypl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 192 ---FTAIAgnlptaPAL-MGNVVVWKPsPTQTHAAVLLM-QLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTG 266
Cdd:cd07082 156 nltVSKLI------PALiMGNTVVFKP-ATQGVLLGIPLaEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 267 STKtfqylwktVGNNIEKYRTYPRMVGETGGKDFVVAHPSADravLKTALTR---GSFEYQGQKCSASSRAYVPASIWNS 343
Cdd:cd07082 229 STE--------VGNRLKKQHPMKRLVLELGGKDPAIVLPDAD---LELAAKEivkGALSYSGQRCTAIKRVLVHESVADE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 344 gFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDdsVGYFVRPTVVECSDPANEV 423
Cdd:cd07082 298 -LVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAK-GATVLNGGGRE--GGNLIYPTLLDPVTPDMRL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 424 FTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKStgavvgQQ----- 498
Cdd:cd07082 374 AWEEPFGPVLPIIRVNDI--EEAIE-LANKSNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhf 442
|
....*....
gi 1954849083 499 PFGGGRASG 507
Cdd:cd07082 443 PFLGRKDSG 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
98-507 |
5.47e-43 |
|
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: 159.32 E-value: 5.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDCPcELVDFWRFNVKYARDLLAEQPPANsPGVWNRLDH 177
Cdd:cd07109 39 LSPAERGRLLLRIARLIREH-ADELARLESLDTGKPLTQARADVE-AAARYFEYYGGAADKLHGETIPLG-PGYFVYTVR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 178 RPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEH 256
Cdd:cd07109 116 EPH-GVTGHIIPWNYPLQITGRSVAPALaAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 257 RDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYV 336
Cdd:cd07109 195 PGVDHISFTGSVETGIAVMRAAAENVV------PVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 337 PASIWNSgFKEEFAAEIDGITMG-DVTDLSnfIGAVIDERSFAKNKAAIDRAHADpSCTVVAGG---TYDDSVGYFVRPT 412
Cdd:cd07109 269 HRSIYDE-VLERLVERFRALRVGpGLEDPD--LGPLISAKQLDRVEGFVARARAR-GARIVAGGriaEGAPAGGYFVAPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTG 492
Cdd:cd07109 345 LLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIA-LANGTDYGLVAGVWTRDGDRALRVARRLR--AGQVFVNNYGAG 419
|
410
....*....|....*
gi 1954849083 493 AVVgQQPFGGGRASG 507
Cdd:cd07109 420 GGI-ELPFGGVKKSG 433
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
24-520 |
1.11e-42 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 163.57 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 24 ERARLESKLKELAENPVDLPMTIGGEKRmgGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDR 103
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAAPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 104 AAIILRAAELLAGPwRETLAASTMLGQSKTAQ--QAEIdcpCELVDFWRFnvkYA---RDLLAeqppanspgvwNRLDHR 178
Cdd:COG4230 618 AAILERAADLLEAH-RAELMALLVREAGKTLPdaIAEV---REAVDFCRY---YAaqaRRLFA-----------APTVLR 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLeGFVYAITPFNFT-AI-AGnlPTAPALM-GNVVVWKPSPtQT----HAAVllmQLLEEAGLPKGVINLVTGDGIEVSE 251
Cdd:COG4230 680 GR-GVFVCISPWNFPlAIfTG--QVAAALAaGNTVLAKPAE-QTpliaARAV---RLLHEAGVPADVLQLLPGDGETVGA 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVgnnIEKYRTYPRMVGETGGKDfvvahpsadrA--VLKTALT--------RGSF 321
Cdd:COG4230 753 ALVADPRIAGVAFTGSTETARLINRTL---AARDGPIVPLIAETGGQN----------AmiVDSSALPeqvvddvlASAF 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 322 EYQGQKCSASSRAYVPasiwnsgfkEEFAAEIdgITM----------GDVTDLSNFIGAVIDERSFAKNKAAIDRAHADP 391
Cdd:COG4230 820 DSAGQRCSALRVLCVQ---------EDIADRV--LEMlkgamaelrvGDPADLSTDVGPVIDAEARANLEAHIERMRAEG 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 392 scTVVAGGTYDDSV--GYFVRPTVVECSDPanEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTGSV---Iagd 466
Cdd:COG4230 889 --RLVHQLPLPEECanGTFVAPTLIEIDSI--SDLEREVFGPVLHVVRYKADELDKVIDAINA-TGYGLTLGVhsrI--- 960
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1954849083 467 RAAAAYTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 520
Cdd:COG4230 961 DETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
168-508 |
1.15e-42 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 158.31 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 168 SPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPsPTQTHAAVLLMQLLEEAGLPKGVINLVTGDG 246
Cdd:cd07107 105 GGRNLHYTLREPY-GVVARIVAFNHPLMFAAAKIAAPLAaGNTVVVKP-PEQAPLSALRLAELAREVLPPGVFNILPGDG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 247 IEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIeKYRTYprmvgETGGKDFVVAHPSADRAVLKTALTRG-SFEYQG 325
Cdd:cd07107 183 ATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI-KHVTL-----ELGGKNALIVFPDADPEAAADAAVAGmNFTWCG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 326 QKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSV 405
Cdd:cd07107 257 QSCGSTSRLFVHESIYDE-VLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 406 ---GYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVsDYALTGSVIAGDRAAAAYTMEKLRyaAG 482
Cdd:cd07107 336 legGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANGV-EYGLTAAIWTNDISQAHRTARRVE--AG 410
|
330 340
....*....|....*....|....*....
gi 1954849083 483 NFYINDKST---GAvvgqqPFGGGRASGT 508
Cdd:cd07107 411 YVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
99-507 |
1.53e-42 |
|
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: 158.05 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGpwRETLAASTM---LGQSKT-AQQAEIDCPcelVDFWRFNVKYARDLLAEQPPANSpgvwnR 174
Cdd:cd07138 56 SVEERAALLERIAEAYEA--RADELAQAItleMGAPITlARAAQVGLG---IGHLRAAADALKDFEFEERRGNS-----L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNFTA--IAGNLptAPALM-GNVVVWKPS---PTQthaAVLLMQLLEEAGLPKGVINLVTGDGIE 248
Cdd:cd07138 126 VVREPI-GVCGLITPWNWPLnqIVLKV--APALAaGCTVVLKPSevaPLS---AIILAEILDEAGLPAGVFNLVNGDGPV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 249 VSEVALEHRDLAGIHFTGSTKtfqylwktVGNNIEKY--RTYPRMVGETGGKDFVVAHPSADravLKTALTRG---SFEY 323
Cdd:cd07138 200 VGEALSAHPDVDMVSFTGSTR--------AGKRVAEAaaDTVKRVALELGGKSANIILDDAD---LEKAVPRGvaaCFAN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 324 QGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTY-- 401
Cdd:cd07138 269 SGQSCNAPTRMLVPRSRYAE-AEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEE-GARLVAGGPGrp 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 402 -DDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRya 480
Cdd:cd07138 347 eGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE--DEAIA-IANDTPYGLAGYVWSADPERARAVARRLR-- 421
|
410 420
....*....|....*....|....*..
gi 1954849083 481 AGNFYINDkstGAVVGQQPFGGGRASG 507
Cdd:cd07138 422 AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
29-525 |
9.07e-41 |
|
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: 153.91 E-value: 9.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 29 ESKLKELAENPVDLPMTigGEKRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIIL 108
Cdd:TIGR01238 26 AQIHAWADKTWQAAPII--GHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 109 RAAELLAGPwRETLAASTMLGQSKTAQQAeIDCPCELVDFWRFNVKYARDLLAEQPpanspgvwnrldHRPLeGFVYAIT 188
Cdd:TIGR01238 104 RLADLLELH-MPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEFS------------VESR-GVFVCIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 189 PFNFT-AIAGNLPTAPALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGS 267
Cdd:TIGR01238 169 PWNFPlAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 268 TKTFQYLWKTVGNniekyRTYPR--MVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSGF 345
Cdd:TIGR01238 249 TEVAQLINQTLAQ-----REDAPvpLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 346 KEEFAAeIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDraHADPSCTVVAGGTYDDSV----GYFVRPTVVECSDPAN 421
Cdd:TIGR01238 324 TMIQGA-MQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE--HMSQTQKKIAQLTLDDSRacqhGTFVAPTLFELDDIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 422 evFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTGSVIAgdRAAAAYTMEKLRYAAGNFYINDKSTGAVVGQQPFG 501
Cdd:TIGR01238 401 --LSEEVFGPVLHVVRYKARELDQIVDQINQ-TGYGLTMGVHS--RIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475
|
490 500
....*....|....*....|....
gi 1954849083 502 GGRASGTNDKAGAPQNLMRWTLTR 525
Cdd:TIGR01238 476 GQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-507 |
1.33e-40 |
|
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: 151.96 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGpWRETLAAstmlgqsktAQQAEIDCPCELVDfwrFNVKYARDLLAE-----------QPPA 166
Cdd:cd07105 19 TPPSERRDILLKAADLLES-RRDEFIE---------AMMEETGATAAWAG---FNVDLAAGMLREaaslitqiiggSIPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 167 NSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVT-- 243
Cdd:cd07105 86 DKPGTLAMVVKEPV-GVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 244 -GDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKYrtyprmVGETGGKDFVVAHPSAD--RAVLKTALtrGS 320
Cdd:cd07105 165 pEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPV------LLELGGKAPAIVLEDADldAAANAALF--GA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 321 FEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTdlsnfIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGT 400
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADE-FVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKGAKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 401 YDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqyDEMLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRYa 480
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKD---EEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIES- 386
|
410 420 430
....*....|....*....|....*....|
gi 1954849083 481 aGNFYINdkstGAVVG---QQPFGGGRASG 507
Cdd:cd07105 387 -GAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-514 |
2.21e-40 |
|
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: 151.74 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 102 DRAAIILRAAELLAGPWREtlAASTM---LGQSKTAQQAEIDCPCelvDFWRFNVKYARDLLAEQPPA-NSPGVWNRL-- 175
Cdd:cd07146 41 QRSAILNKAAALLEARREE--FARLItleSGLCLKDTRYEVGRAA---DVLRFAAAEALRDDGESFSCdLTANGKARKif 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHR-PLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVA 253
Cdd:cd07146 116 TLRePL-GVVLAITPFNHPLNQVAHKIAPAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGSTKtfqylwktVGNNIEKYRTYPRMVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSAS 331
Cdd:cd07146 195 ITHPDVDLVTFTGGVA--------VGKAIAATAGYKRQLLELGGNDPLIVMDDADleRAA--TLAVAGSYANSGQRCTAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 332 SRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDdsvGYFVRP 411
Cdd:cd07146 265 KRILVHESVADE-FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQ-GARVLLGNQRQ---GALYAP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 412 TVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVSdYALTGSVIAGDRAAAAYTMEKLRYAAGNfyINDkST 491
Cdd:cd07146 340 TVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNSTA-YGLSSGVCTNDLDTIKRLVERLDVGTVN--VNE-VP 413
|
410 420
....*....|....*....|...
gi 1954849083 492 GAVVGQQPFGGGRASGTNDKAGA 514
Cdd:cd07146 414 GFRSELSPFGGVKDSGLGGKEGV 436
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
99-538 |
2.61e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 153.11 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLA----ASTmlGQSKTAQQAEIdcpCELVDFWRFNVKYARDLLAeqpPANSPGVW-- 172
Cdd:PRK09407 74 PVRERAAVLLRFHDLVLEN-REELLdlvqLET--GKARRHAFEEV---LDVALTARYYARRAPKLLA---PRRRAGALpv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 173 ---NRLDHRPLeGFVYAITPFNF---TAIAGNLptaPALM-GNVVVWKPSpTQT-HAAVLLMQLLEEAGLPKGVINLVTG 244
Cdd:PRK09407 145 ltkTTELRQPK-GVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPD-SQTpLTALAAVELLYEAGLPRDLWQVVTG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 245 DGIEVSEVALEHRDlaGIHFTGSTKTFQYLWKTVGnniekyrtyPRMVG---ETGGKDFVVAHPSADRAVLKTALTRGSF 321
Cdd:PRK09407 220 PGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAG---------RRLIGfslELGGKNPMIVLDDADLDKAAAGAVRACF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 322 EYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTY 401
Cdd:PRK09407 289 SNAGQLCISIERIYVHESIYDE-FVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAK-GATVLAGGKA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 402 DDSVG-YFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRya 480
Cdd:PRK09407 367 RPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERAND-TPYGLNASVWTGDTARGRAIAARIR-- 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954849083 481 AGNFYIND------KSTGAvvgqqPFGGGRASGTNDKAGApQNLMRWTLTRAIKETLVPPTDYP 538
Cdd:PRK09407 442 AGTVNVNEgyaaawGSVDA-----PMGGMKDSGLGRRHGA-EGLLKYTESQTIATQRVLPLAPP 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-536 |
5.27e-40 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 155.79 E-value: 5.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 26 ARLESKLKELAENPVD-LPMTIGGEKrmgGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRA 104
Cdd:PRK11905 539 AALDEALNAFAAKTWHaAPLLAGGDV---DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERA 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 105 AIILRAAELLagpwrE----TLAASTMLGQSKTAQQAeIDCPCELVDFWRFNVKYARDLLAEQPpanspgvwnrldHRPL 180
Cdd:PRK11905 616 AILERAADLM-----EahmpELFALAVREAGKTLANA-IAEVREAVDFLRYYAAQARRLLNGPG------------HKPL 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 181 eGFVYAITPFNFT-AI-AGNLptAPALM-GNVVVWKPSPtQT----HAAVllmQLLEEAGLPKGVINLVTGDGIEVSEVA 253
Cdd:PRK11905 678 -GPVVCISPWNFPlAIfTGQI--AAALVaGNTVLAKPAE-QTpliaARAV---RLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGSTKTFQYLWKTVgnnIEKYRTYPRMVGETGGKDFVVAHPSA-----DRAVLKTAltrgsFEYQGQKC 328
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQRTL---AKRSGPPVPLIAETGGQNAMIVDSSAlpeqvVADVIASA-----FDSAGQRC 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 329 SASSRAYVpasiwnsgfKEEFAAEIdgITM----------GDVTDLSNFIGAVIDERSFAKNKAAID--RAHADPSCTVV 396
Cdd:PRK11905 823 SALRVLCL---------QEDVADRV--LTMlkgamdelriGDPWRLSTDVGPVIDAEAQANIEAHIEamRAAGRLVHQLP 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 397 AGGTYDDsvGYFVRPTVVECSDPAneVFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTG---SVIagDRAAAAYT 473
Cdd:PRK11905 892 LPAETEK--GTFVAPTLIEIDSIS--DLEREVFGPVLHVVRFKADELDRVIDDINA-TGYGLTFglhSRI--DETIAHVT 964
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 474 MeklRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRwtLTRAIKETLVPPTD 536
Cdd:PRK11905 965 S---RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGR--LVREAPTPIPPAHE 1022
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
119-507 |
1.09e-39 |
|
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: 150.19 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 119 RETLAASTMLGQSKTAQQA--EID-CPCELvdfwRFNVKYARDLL--AEQPpanSPGVWNRLDHRPLeGFVYAITPFNFT 193
Cdd:cd07120 59 AERLARLLALENGKILGEArfEISgAISEL----RYYAGLARTEAgrMIEP---EPGSFSLVLREPM-GVAGIIVPWNSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 194 AIAGNLPTAPALM-GNVVVWKPSP--TQTHAAVllMQLLEEA-GLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTK 269
Cdd:cd07120 131 VVLLVRSLAPALAaGCTVVVKPAGqtAQINAAI--IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 270 TfqylwktvGNNI--EKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKE 347
Cdd:cd07120 209 T--------GRAImaAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE-VRD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 348 EFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDD--SVGYFVRPTVVECSDPANEVFT 425
Cdd:cd07120 280 RLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 426 TEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKstGAVVGQQPFGGGRA 505
Cdd:cd07120 360 EEIFGPVLTLETFDDE--AEAVALAND-TDYGLAASVWTRDLARAMRVARAIR--AGTVWINDW--NKLFAEAEEGGYRQ 432
|
..
gi 1954849083 506 SG 507
Cdd:cd07120 433 SG 434
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
99-507 |
3.38e-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: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEID-CpcelVDFWRFNVKYARDLLAEQPpANSPGVWNRL 175
Cdd:cd07100 19 SFAERAALLRKLADLLRER-KDELARliTLEMGKPIAEARAEVEkC----AWICRYYAENAEAFLADEP-IETDAGKAYV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFtaiagnlP-------TAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGV-INL-VTGD 245
Cdd:cd07100 93 RYEPL-GVVLGIMPWNF-------PfwqvfrfAAPNLMaGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLlIDSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 246 GIEVsevALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVGETGGKD-FVVAhPSAD--RAVlKTAlTRGSFE 322
Cdd:cd07100 165 QVEA---IIADPRVRGVTLTGSERAGRAVAAEAGKNLKK------SVLELGGSDpFIVL-DDADldKAV-KTA-VKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 323 YQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVidersfaKNKAAIDRAHA------DPSCTVV 396
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDE-FLEKFVEAMAALKVGDPMDEDTDLGPL-------ARKDLRDELHEqveeavAAGATLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 397 AGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEK 476
Cdd:cd07100 305 LGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIA-LANDSPFGLGGSVFTTDLERAERVARR 381
|
410 420 430
....*....|....*....|....*....|...
gi 1954849083 477 LRyaAGNFYIND--KSTGAVvgqqPFGGGRASG 507
Cdd:cd07100 382 LE--AGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
46-507 |
4.26e-39 |
|
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: 149.03 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEKRMG-GGDRFDVVQPHNHKArLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAA-------ELLA-- 115
Cdd:cd07559 5 INGEWVAPsKGEYFDNYNPVNGKV-LCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIAdrieenlELLAva 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 116 ------GPWRETLAAstmlgqsktaqqaeiDCPCElVDFWRFnvkYARDLLAEQppanspGVWNRLD--------HRPLe 181
Cdd:cd07559 84 etldngKPIRETLAA---------------DIPLA-IDHFRY---FAGVIRAQE------GSLSEIDedtlsyhfHEPL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSpTQTHAAVL-LMQLLEEAgLPKGVINLVTGDGIEVSEVALEHRDL 259
Cdd:cd07559 138 GVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKPA-SQTPLSILvLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 260 AGIHFTGSTktfqylwkTVGNNIEKY---RTYPRMVgETGGK-------DFVVAHPSADRAVLKTALtrGSFEYQGQKCS 329
Cdd:cd07559 216 AKLAFTGST--------TVGRLIMQYaaeNLIPVTL-ELGGKspniffdDAMDADDDFDDKAEEGQL--GFAFNQGEVCT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGG----TYDDSV 405
Cdd:cd07559 285 CPSRALVQESIYDE-FIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGerltLGGLDK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 406 GYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDrAAAAYTMEKlRYAAGNFY 485
Cdd:cd07559 363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE--EEAIA-IANDTEYGLGGGVWTRD-INRALRVAR-GIQTGRVW 437
|
490 500
....*....|....*....|..
gi 1954849083 486 INdkSTGAVVGQQPFGGGRASG 507
Cdd:cd07559 438 VN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
103-507 |
6.84e-39 |
|
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: 147.88 E-value: 6.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 103 RAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDcpcelVD----FWRFNVKYARDLLAEQPPA---NSPGVWNRL 175
Cdd:cd07110 43 RAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAWD-----VDdvagCFEYYADLAEQLDAKAERAvplPSEDFKARV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVAL 254
Cdd:cd07110 117 RREPV-GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 255 EHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSAD--RAVLKTALtrGSFEYQGQKCSASS 332
Cdd:cd07110 196 AHPGIDKISFTGSTATGSQVMQAAAQDIK------PVSLELGGKSPIIVFDDADleKAVEWAMF--GCFWNNGQICSATS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSV--GYFVR 410
Cdd:cd07110 268 RLLVHESIADA-FLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEE-GARLLCGGRRPAHLekGYFIA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 411 PTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkS 490
Cdd:cd07110 346 PTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIA-LANDSEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--C 418
|
410
....*....|....*..
gi 1954849083 491 TGAVVGQQPFGGGRASG 507
Cdd:cd07110 419 SQPCFPQAPWGGYKRSG 435
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
44-507 |
9.88e-39 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 147.75 E-value: 9.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 44 MTIGGEKRMGGGDRFDVVQPHNHKArLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLA 123
Cdd:PRK13473 5 LLINGELVAGEGEKQPVYNPATGEV-LAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEEN-ADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 124 ASTMLGQSKTAQQA-EIDCPCeLVDFWRFNVKYARDLlaEQPPAN--SPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLP 200
Cdd:PRK13473 83 RLESLNCGKPLHLAlNDEIPA-IVDVFRFFAGAARCL--EGKAAGeyLEGHTSMIRRDPV-GVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 201 TAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVG 279
Cdd:PRK13473 159 LAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 280 NNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMG 359
Cdd:PRK13473 238 DSVK------RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDD-LVAKLAAAVATLKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 360 DVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYE 439
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 440 DDqyDEMLAQMESvSDYALTGSVIAGD-----RAAAaytmeklRYAAGNFYINDKSTgaVVGQQPFGGGRASG 507
Cdd:PRK13473 391 DE--DQAVRWAND-SDYGLASSVWTRDvgrahRVSA-------RLQYGCTWVNTHFM--LVSEMPHGGQKQSG 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-507 |
4.40e-38 |
|
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: 145.52 E-value: 4.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDCPCElVDFWRFNVKYARDLLAEQPP-ANSPGVWNRld 176
Cdd:cd07090 38 TSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVDIDSS-ADCLEYYAGLAPTLSGEHVPlPGGSFAYTR-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVALE 255
Cdd:cd07090 114 REPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIeKYRTYprmvgETGGKDFVVAHPSAD--RAVlKTALTrGSFEYQGQKCSASSR 333
Cdd:cd07090 192 HPDVAKVSFTGSVPTGKKVMSAAAKGI-KHVTL-----ELGGKSPLIIFDDADleNAV-NGAMM-ANFLSQGQVCSNGTR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTY---DDSV--GYF 408
Cdd:cd07090 264 VFVQRSIKDE-FTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE-GAKVLCGGERvvpEDGLenGFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 409 VRPTV-VECSDPAnEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIN 487
Cdd:cd07090 342 VSPCVlTDCTDDM-TIVREEIFGPVMSILPFDTE--EEVIR-RANDTTYGLAAGVFTRDLQRAHRVIAQLQ--AGTCWIN 415
|
410 420
....*....|....*....|
gi 1954849083 488 DKSTGAVvgQQPFGGGRASG 507
Cdd:cd07090 416 TYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
146-508 |
3.46e-37 |
|
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: 142.85 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 146 VDFWRFNVKYARDLlaEQPPANS--PGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAA 222
Cdd:cd07092 85 VDNFRFFAGAARTL--EGPAAGEylPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 223 VLLMQLLEEaGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVV 302
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGKAPVI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 303 AHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKA 382
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDE-FVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 383 AIDRAHADpsCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVsDYALTGSV 462
Cdd:cd07092 314 FVERAPAH--ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELANDV-EYGLASSV 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1954849083 463 IAGDRAAAAYTMEKLRYaaGNFYINDKstGAVVGQQPFGGGRASGT 508
Cdd:cd07092 389 WTRDVGRAMRLSARLDF--GTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
98-507 |
1.37e-36 |
|
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: 141.58 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKT-AQQAEIDCPcELVDFWRFNVKYArDLLAEQPPANSPGVWNRLD 176
Cdd:cd07091 62 MDPRERGRLLNKLADLIERD-RDELAALESLDNGKPlEESAKGDVA-LSIKCLRYYAGWA-DKIQGKTIPIDGNFLAYTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07091 139 REPI-GVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGN-NIEKyrtyprMVGETGGKDFVVAHPSADravLKTAL---TRGSFEYQGQKCSAS 331
Cdd:cd07091 218 HMDVDKIAFTGSTAVGRTIMEAAAKsNLKK------VTLELGGKSPNIVFDDAD---LDKAVewaAFGIFFNQGQCCCAG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 332 SRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVGYFVRP 411
Cdd:cd07091 289 SRIFVQESIYDE-FVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESG-KKEGATLLTGGERHGSKGYFIQP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 412 TVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLaQMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdksT 491
Cdd:cd07091 367 TVFTDVKDDMKIAKEEIFGPVVTILKFKTE--DEVI-ERANDTEYGLAAGVFTKDINKALRVSRALK--AGTVWVN---T 438
|
410
....*....|....*..
gi 1954849083 492 GAVVGQQ-PFGGGRASG 507
Cdd:cd07091 439 YNVFDAAvPFGGFKQSG 455
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
177-527 |
9.54e-36 |
|
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: 139.59 E-value: 9.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07143 142 HEPI-GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVG-NNIEKyrtyprMVGETGGKDFVVAHPSAD--RAVLKTAltRGSFEYQGQKCSASS 332
Cdd:cd07143 221 HMDIDKVAFTGSTLVGRKVMEAAAkSNLKK------VTLELGGKSPNIVFDDADleSAVVWTA--YGIFFNHGQVCCAGS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPT 412
Cdd:cd07143 293 RIYVQEGIYDK-FVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAE-GATVETGGKRHGNEGYFIEPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDDQydEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTg 492
Cdd:cd07143 371 IFTDVTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKRAND-STYGLAAAVFTNNINNAIRVANALK--AGTVWVNCYNL- 444
|
330 340 350
....*....|....*....|....*....|....*
gi 1954849083 493 aVVGQQPFGGGRASGTNDKAGApQNLMRWTLTRAI 527
Cdd:cd07143 445 -LHHQVPFGGYKQSGIGRELGE-YALENYTQIKAV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
98-514 |
1.30e-34 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 136.08 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEI-DCPCeLVDFWRFNVKYARDLLAEQPPANSPGVWNRLd 176
Cdd:cd07142 62 MTGYERSRILLRFADLLEKH-ADELAALETWDNGKPYEQARYaEVPL-AARLFRYYAGWADKIHGMTLPADGPHHVYTL- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07142 139 HEPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIAS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTYprmvgETGGKDFVVAHPSA--DRAVLKTALtrGSFEYQGQKCSASSR 333
Cdd:cd07142 218 HMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTL-----ELGGKSPFIVCEDAdvDKAVELAHF--ALFFNQGQCCCAGSR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVGYFVRPTV 413
Cdd:cd07142 291 TFVHESIYDE-FVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHG-KEEGATLITGGDRIGSKGYYIQPTI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 414 VECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLaQMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIN--DKST 491
Cdd:cd07142 369 FSDVKDDMKIARDEIFGPVQSILKFKT--VDEVI-KRANNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVNcyDVFD 443
|
410 420
....*....|....*....|...
gi 1954849083 492 GAVvgqqPFGGGRASGTNDKAGA 514
Cdd:cd07142 444 ASI----PFGGYKMSGIGREKGI 462
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
44-507 |
1.68e-34 |
|
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: 135.66 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 44 MTIGGE-KRMGGGDRFDVVQPHNHKArLGTYANATQQDAQDAIDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETL 122
Cdd:cd07117 3 LFINGEwVKGSSGETIDSYNPANGET-LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDEN-KELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 123 AASTMLGQSKTAQQAE-IDCPCElVDFWRFnvkYARDLLAEQppanspGVWNRLD--------HRPLeGFVYAITPFNFT 193
Cdd:cd07117 81 AMVETLDNGKPIRETRaVDIPLA-ADHFRY---FAGVIRAEE------GSANMIDedtlsivlREPI-GVVGQIIPWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 194 AIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKtfq 272
Cdd:cd07117 150 FLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTE--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 273 yLWKTVGNNIEKyRTYPRMVgETGGKDFVVAHPSA--DRAVLKTALtrGSFEYQGQKCSASSRAYVPASIWNSgFKEEFA 350
Cdd:cd07117 226 -VGRDVAIAAAK-KLIPATL-ELGGKSANIIFDDAnwDKALEGAQL--GILFNQGQVCCAGSRIFVQEGIYDE-FVAKLK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 351 AEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGG---TYDDSV-GYFVRPTVVECSDPANEVFTT 426
Cdd:cd07117 300 EKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEE-GAKILTGGhrlTENGLDkGFFIEPTLIVNVTNDMRVAQE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 427 EYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTGAVVGQQPFGGGRAS 506
Cdd:cd07117 379 EIFGPVATVIKFKTE--DEVID-MANDSEYGLGGGVFTKDINRALRVARAVE--TGRVWVN--TYNQIPAGAPFGGYKKS 451
|
.
gi 1954849083 507 G 507
Cdd:cd07117 452 G 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
120-507 |
2.65e-34 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 134.09 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 120 ETLAASTMLGQSKTAQQAEIDCPCElVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFT--AIAG 197
Cdd:PRK10090 13 SEISALIVEEGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRAL-GVTTGILPWNFPffLIAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 198 NLptAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWK 276
Cdd:PRK10090 91 KM--APALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 277 TVGNNIEKYRTyprmvgETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGI 356
Cdd:PRK10090 169 AAAKNITKVCL------ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ-FVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 357 TMGDVTDLSNF-IGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAV 435
Cdd:PRK10090 242 QFGNPAERNDIaMGPLINAAALERVEQKVARAVEE-GARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 436 HVYedDQYDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRYaaGNFYINDKSTGAVvgqQPFGGG-RASG 507
Cdd:PRK10090 321 VAF--DTLEEAIA-MANDSDYGLTSSIYTQNLNVAMKAIKGLKF--GETYINRENFEAM---QGFHAGwRKSG 385
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
101-525 |
3.69e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 138.18 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 101 DDRAAIILRAAELLAGPW--------RETlaastmlGQSKTAQQAEIDcpcELVDFWRFNVKYARDLLAEQppanspgvw 172
Cdd:PRK11809 704 AERAAILERAADLMEAQMqtlmgllvREA-------GKTFSNAIAEVR---EAVDFLRYYAGQVRDDFDND--------- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 173 nrlDHRPLeGFVYAITPFNFT-AI-AGNLPTAPAlMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVS 250
Cdd:PRK11809 765 ---THRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVG 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 251 EVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIE-KYRTYPrMVGETGGKDFVVAHPSA-------DraVLKTAltrgsFE 322
Cdd:PRK11809 840 AALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIP-LIAETGGQNAMIVDSSAlteqvvaD--VLASA-----FD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 323 YQGQKCSASSRAYVpasiwnsgfkEEFAAE---------IDGITMGDVTDLSNFIGAVIDersfAKNKAAID------RA 387
Cdd:PRK11809 912 SAGQRCSALRVLCL----------QDDVADrtlkmlrgaMAECRMGNPDRLSTDIGPVID----AEAKANIErhiqamRA 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 388 HADPSCTVVAGGTYDDSVGYFVRPTVVECSDPANevFTTEYFGPFLAVHVYEDDQYDEMLAQMESvSDYALTGSV---Ia 464
Cdd:PRK11809 978 KGRPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYNRNQLDELIEQINA-SGYGLTLGVhtrI- 1053
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954849083 465 gDRAAAAYTMeklRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTR 525
Cdd:PRK11809 1054 -DETIAQVTG---SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
175-514 |
3.93e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 135.09 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNFtaiAGNLPTA---PALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGdGIEVS 250
Cdd:PRK09457 130 LRHRPH-GVVAVFGPYNF---PGHLPNGhivPALLaGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 251 EVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCS 329
Cdd:PRK09457 205 KALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK------ILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSGFKEEFAAEIDGITMGDV-TDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVGyF 408
Cdd:PRK09457 279 CARRLLVPQGAQGDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTG-L 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 409 VRPTVVECSDPAnEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESVSdYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIND 488
Cdd:PRK09457 358 LTPGIIDVTGVA-ELPDEEYFGPLLQVVRYDD--FDEAIRLANNTR-FGLSAGLLSDDREDYDQFLLEIR--AGIVNWNK 431
|
330 340
....*....|....*....|....*.
gi 1954849083 489 KSTGAvVGQQPFGGGRASGtNDKAGA 514
Cdd:PRK09457 432 PLTGA-SSAAPFGGVGASG-NHRPSA 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
182-507 |
8.27e-34 |
|
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: 133.52 E-value: 8.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAiagNL---PTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDgIEVSEVALEHR 257
Cdd:cd07147 125 GPVSAITPFNFPL---NLvahKVAPAIaAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 DLAGIHFTGSTKtfqylwktVGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVP 337
Cdd:cd07147 201 RIKLLSFTGSPA--------VGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 338 ASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVgyfVRPTVVECS 417
Cdd:cd07147 273 RSVYDE-FKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEA-VDAGAKLLTGGKRDGAL---LEPTILEDV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 418 DPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAvVGQ 497
Cdd:cd07147 348 PPDMEVNCEEVFGPVVTVEPYDD--FDEALAAVND-SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDH 421
|
330
....*....|
gi 1954849083 498 QPFGGGRASG 507
Cdd:cd07147 422 MPYGGVKDSG 431
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
102-448 |
1.17e-33 |
|
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: 133.41 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 102 DRAAIILRAAELLAGPWREtLAASTMLGQSKTAQQA--EIDCPCELVDFwrfNVKYARDLLAEQPPANSPGVWNRLDHRP 179
Cdd:cd07085 61 KRQQVMFKFRQLLEENLDE-LARLITLEHGKTLADArgDVLRGLEVVEF---ACSIPHLLKGEYLENVARGIDTYSYRQP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 180 LeGFVYAITPFNFTAIAGN--LPTAPALmGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVALEHR 257
Cdd:cd07085 137 L-GVVAGITPFNFPAMIPLwmFPMAIAC-GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK-EAVNALLDHP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 DLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVP 337
Cdd:cd07085 214 DIKAVSFVGSTPVGEYIYERAAANGK------RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 338 ASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGT-----YDDsvGYFVRPT 412
Cdd:cd07085 288 GDEADE-WIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvkvpgYEN--GNFVGPT 364
|
330 340 350
....*....|....*....|....*....|....*.
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVhVYEDDqYDEMLA 448
Cdd:cd07085 365 ILDNVTPDMKIYKEEIFGPVLSI-VRVDT-LDEAIA 398
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
102-507 |
5.32e-33 |
|
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: 131.76 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 102 DRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDCPCELVDFWRFNVKYArDLLAEQPPANSPGVWNRLDHRPLe 181
Cdd:cd07144 69 ERGELLDKLADLVEKN-RDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWA-DKIQGKTIPTSPNKLAYTLHEPY- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLA 260
Cdd:cd07144 146 GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNNIeKYRTYprmvgETGGKD--FVVAHPSADRAVLKTALtrGSFEYQGQKCSASSRAYVPA 338
Cdd:cd07144 226 KIAFTGSTATGRLVMKAAAQNL-KAVTL-----ECGGKSpaLVFEDADLDQAVKWAAA--GIMYNSGQNCTATSRIYVQE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 339 SIWNSgFKEEFAAEI-DGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVVAGGT---YDDSVGYFVRPTVV 414
Cdd:cd07144 298 SIYDK-FVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEkapEGLGKGYFIPPTIF 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 415 ECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALtgsviagdrAAAAYTmEKLRYA--------AGNFYI 486
Cdd:cd07144 376 TDVPQDMRIVKEEIFGPVVVISKFKT--YEEAIKKAND-TTYGL---------AAAVFT-KDIRRAhrvareleAGMVWI 442
|
410 420
....*....|....*....|.
gi 1954849083 487 NDKSTGAVvgQQPFGGGRASG 507
Cdd:cd07144 443 NSSNDSDV--GVPFGGFKMSG 461
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
182-507 |
9.37e-31 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 125.39 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLA 260
Cdd:PRK09847 159 GVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDID 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNNIEKyrtypRMVGETGGK--DFVVAH-PSADRAVLKTAltRGSFEYQGQKCSASSRAYVP 337
Cdd:PRK09847 239 AIAFTGSTRTGKQLLKDAGDSNMK-----RVWLEAGGKsaNIVFADcPDLQQAASATA--AGIFYNQGQVCIAGTRLLLE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 338 ASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDErsfaknkaaidrAHADPSCTVVAGGTYDDSV---------GYF 408
Cdd:PRK09847 312 ESIADE-FLALLKQQAQNWQPGHPLDPATTMGTLIDC------------AHADSVHSFIREGESKGQLlldgrnaglAAA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 409 VRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAqmeSVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIND 488
Cdd:PRK09847 379 IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA---NDSQYGLGAAVWTRDLSRAHRMSRRLK--AGSVFVNN 453
|
330
....*....|....*....
gi 1954849083 489 KSTGAVVgqQPFGGGRASG 507
Cdd:PRK09847 454 YNDGDMT--VPFGGYKQSG 470
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
99-507 |
1.35e-30 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 124.46 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIdcpCELVDFWRFNVKYARDLLAEQP--PANSPGVWNR 174
Cdd:PRK09406 43 TFAQRARWANAAADLLEAE-ADQVAAlmTLEMGKTLASAKAEA---LKCAKGFRYYAEHAEALLADEPadAAAVGASRAY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVIN--LVTGDGIevsE 251
Cdd:PRK09406 119 VRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQtlLVGSGAV---E 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVGETGGKDFVVAHPSAD--RAVlKTALTrGSFEYQGQKCS 329
Cdd:PRK09406 195 AILRDPRVAAATLTGSEPAGRAVAAIAGDEIKK------TVLELGGSDPFIVMPSADldRAA-ETAVT-ARVQNNGQSCI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVGYFV 409
Cdd:PRK09406 267 AAKRFIVHADVYDA-FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA-VAAGATILCGGKRPDGPGWFY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 410 RPTVVECSDPANEVFTTEYFGPFLAvhVYEDDQYDEMLAqMESVSDYALTGSVIAGDRAaaaytmEKLRYA----AGNFY 485
Cdd:PRK09406 345 PPTVITDITPDMRLYTEEVFGPVAS--LYRVADIDEAIE-IANATTFGLGSNAWTRDEA------EQERFIddleAGQVF 415
|
410 420
....*....|....*....|....
gi 1954849083 486 INdkstGAVVG--QQPFGGGRASG 507
Cdd:PRK09406 416 IN----GMTVSypELPFGGVKRSG 435
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
182-507 |
4.21e-30 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 123.69 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLA 260
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNNIEkyrtyPRMVgETGGKDFVVAHPSAD--RAVLKTALtrGSFEYQGQKCSASSRAYVPA 338
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMVK-----PVSL-ELGGKSPIIVFDDVDldKAVEWAMF--GCFWTNGQICSATSRLLVHE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 339 SIwNSGFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDD--SVGYFVRPTVVEC 416
Cdd:PLN02467 305 RI-ASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSE-GATILCGGKRPEhlKKGFFIEPTIITD 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 417 SDPANEVFTTEYFGPFLAVHVYEDDqyDEMLaQMESVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTGAVVG 496
Cdd:PLN02467 383 VTTSMQIWREEVFGPVLCVKTFSTE--DEAI-ELANDSHYGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFC 455
|
330
....*....|.
gi 1954849083 497 QQPFGGGRASG 507
Cdd:PLN02467 456 QAPWGGIKRSG 466
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
174-440 |
8.83e-30 |
|
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: 122.32 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 174 RLDHRPLE-----GFVYAITPFNF-TAIAG-NlpTAPALM-GNVVVWKPSPTQTHAAVLLMQL----LEEAGLPKGVINL 241
Cdd:cd07130 121 RPGHRMMEqwnplGVVGVITAFNFpVAVWGwN--AAIALVcGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 242 VTGDGiEVSEVALEHRDLAGIHFTGSTKTfqylWKTVGNNIEKYrtYPRMVGETGGKDFVVAHPSAD-----RAVLKTAL 316
Cdd:cd07130 199 VCGGA-DVGEALVKDPRVPLVSFTGSTAV----GRQVGQAVAAR--FGRSLLELGGNNAIIVMEDADldlavRAVLFAAV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 317 trGSfeyQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPScTVV 396
Cdd:cd07130 272 --GT---AGQRCTTTRRLIVHESIYDE-VLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVL 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1954849083 397 AGGTYDDSVGYFVRPTVVECSDPAnEVFTTEYFGPFLAVHVYED 440
Cdd:cd07130 345 FGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDT 387
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
177-508 |
1.84e-29 |
|
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: 121.30 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:cd07141 143 HEPV-GVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNNIEKyrtypRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAY 335
Cdd:cd07141 222 HPDIDKVAFTGSTEVGKLIQQAAGKSNLK-----RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTF 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 336 VPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPTVVe 415
Cdd:cd07141 297 VQESIYDE-FVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKE-GAKLECGGKRHGDKGYFIQPTVF- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 416 cSDPANE--VFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTGA 493
Cdd:cd07141 374 -SDVTDDmrIAKEEIFGPVQQIFKFKT--IDEVIERANN-TTYGLAAAVFTKDIDKAITFSNALR--AGTVWVN--CYNV 445
|
330
....*....|....*
gi 1954849083 494 VVGQQPFGGGRASGT 508
Cdd:cd07141 446 VSPQAPFGGYKMSGN 460
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
182-508 |
2.02e-29 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 121.34 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLA 260
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNniekyrTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASI 340
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 341 WNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPTVVECSDPA 420
Cdd:PLN02278 316 YDK-FAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSK-GAKVLLGGKRHSLGGTFYEPTVLGDVTED 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 421 NEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAGDRAAAAYTMEKLRYaaGNFYINDKSTGAVVGqqPF 500
Cdd:PLN02278 394 MLIFREEVFGPVAPLTRFKTE--EEAIA-IANDTEAGLAAYIFTRDLQRAWRVSEALEY--GIVGVNEGLISTEVA--PF 466
|
....*...
gi 1954849083 501 GGGRASGT 508
Cdd:PLN02278 467 GGVKQSGL 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
177-507 |
5.33e-29 |
|
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: 119.81 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVALE 255
Cdd:cd07111 145 WKPV-GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALAN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKTFQYLWKTVGNniekyrTYPRMVGETGGKDFVVAHPSA--DRAVlkTALTRGSFEYQGQKCSASSR 333
Cdd:cd07111 223 HPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKSPFIVFDDAdlDSAV--EGIVDAIWFNQGQVCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 334 AYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSvGYFVRPTV 413
Cdd:cd07111 295 LLVQESVAEE-LIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 414 VECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAqMESVSDYALTGSVIAgDRAAAAYTMeKLRYAAGNFYINdkSTGA 493
Cdd:cd07111 373 FTNVPPASRIAQEEIFGPVLVVLTFRTA--KEAVA-LANNTPYGLAASVWS-ENLSLALEV-ALSLKAGVVWIN--GHNL 445
|
330
....*....|....
gi 1954849083 494 VVGQQPFGGGRASG 507
Cdd:cd07111 446 FDAAAGFGGYRESG 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
98-513 |
1.81e-28 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 119.14 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDCPCeLVDFWRFNVKYARDLLAEQPPANSPGVWNRLdH 177
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPM-FARLFRYYAGWADKIHGLTVPADGPHHVQTL-H 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 178 RPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEH 256
Cdd:PLN02466 194 EPI-GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 257 RDLAGIHFTGSTKTFQYLWKTVGNNIEKYRTYprmvgETGGKD-FVVAHPS-ADRAV--LKTALtrgsFEYQGQKCSASS 332
Cdd:PLN02466 273 MDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKSpFIVCEDAdVDKAVelAHFAL----FFNQGQCCCAGS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIdRAHADPSCTVVAGGTYDDSVGYFVRPT 412
Cdd:PLN02466 344 RTFVHERVYDE-FVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI-KSGVESGATLECGGDRFGSKGYYIQPT 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIN--DKS 490
Cdd:PLN02466 422 VFSNVQDDMLIAQDEIFGPVQSILKFKD--LDEVIRRANN-TRYGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVF 496
|
410 420
....*....|....*....|...
gi 1954849083 491 TGAVvgqqPFGGGRASGTNDKAG 513
Cdd:PLN02466 497 DAAI----PFGGYKMSGIGREKG 515
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
202-507 |
1.83e-27 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 115.36 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 202 APAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGiEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGN 280
Cdd:PRK13252 164 APALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 281 NIeKYRTyprMvgETGGKDFVVAHPSAD--RAVlkTALTRGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITM 358
Cdd:PRK13252 243 SL-KEVT---M--ELGGKSPLIVFDDADldRAA--DIAMLANFYSSGQVCTNGTRVFVQKSIKAA-FEARLLERVERIRI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 359 GDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTY----DDSVGYFVRPTV-VECSDP---ANEvfttEYFG 430
Cdd:PRK13252 314 GDPMDPATNFGPLVSFAHRDKVLGYIEKGKAE-GARLLCGGERltegGFANGAFVAPTVfTDCTDDmtiVRE----EIFG 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1954849083 431 PFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTGAVVGQQPFGGGRASG 507
Cdd:PRK13252 389 PVMSVLTFDDE--DEVIARAND-TEYGLAAGVFTADLSRAHRVIHQLE--AGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
98-527 |
1.95e-26 |
|
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: 112.59 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 98 MSFDDRAAIILRAAELLAGPWRE-------------TLAASTMLGQSktaqqaeidcpcelVDFWRFNVKYARDLLAEQP 164
Cdd:cd07140 64 MNARDRGRLMYRLADLMEEHQEElatiesldsgavyTLALKTHVGMS--------------IQTFRYFAGWCDKIQGKTI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 165 PANsPGVWNR---LDHRPLEGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVIN 240
Cdd:cd07140 130 PIN-QARPNRnltLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVIN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 241 LVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVG-NNIEKYRTyprmvgETGGKD--FVVAHPSADRAVlKTALT 317
Cdd:cd07140 209 ILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKKVSL------ELGGKSplIIFADCDMDKAV-RMGMS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 318 rGSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVA 397
Cdd:cd07140 282 -SVFFNKGENCIAAGRLFVEESIHDE-FVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERG-VKEGATLVY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 398 GGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLaQMESVSDYALTGSVIAGDRAAAAYTMEKL 477
Cdd:cd07140 359 GGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVL-QRANDTEYGLASGVFTKDINKALYVSDKL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1954849083 478 RyaAGNFYINDKSTGAVVGqqPFGGGRASGTNDKAGApQNLMRWTLTRAI 527
Cdd:cd07140 438 E--AGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLGE-EALNEYLKTKTV 482
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
92-527 |
3.49e-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: 111.18 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 92 APAWRAMSFDDRAAIILRAAELLAgPWRETLAASTMLGQSKTAQQAEIDCPCELVDFWRFNVKYARDLlaEQPPANSPGV 171
Cdd:cd07084 12 TKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRI--PHEPGNHLGQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 172 WNRLD-HRPL--EGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAG-LPKGVINLVTGDG 246
Cdd:cd07084 89 GLKQQsHGYRwpYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 247 iEVSEVALEHRDLAGIHFTGSTKTFQYLWktvgNNIEKYRTYprmvGETGGKDFVVAHPSADR-AVLKTALTRGSFEYQG 325
Cdd:cd07084 169 -KTMQALLLHPNPKMVLFTGSSRVAEKLA----LDAKQARIY----LELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 326 QKCSASSRAYVPASIWNSGFKEEFAAEIDGITMGDVTdlsnfIGAVIDERSFAKnkaaIDRAHADPSCTVVAGG------ 399
Cdd:cd07084 240 QKCTAQSMLFVPENWSKTPLVEKLKALLARRKLEDLL-----LGPVQTFTTLAM----IAHMENLLGSVLLFSGkelknh 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 400 TYDDSVGYFVRPTVVECSDPAN---EVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVSDyALTGSVIAGDRAAAAYTMEK 476
Cdd:cd07084 311 SIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG-SLTAAIYSNDPIFLQELIGN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1954849083 477 LRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAI 527
Cdd:cd07084 390 LWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
154-508 |
5.03e-25 |
|
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: 107.69 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 154 KYARDllaEQPPANSPGVWN---RLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLL 229
Cdd:cd07135 83 KWAKD---EKVKDGPLAFMFgkpRIRKEPL-GVVLIIGPWNYPVLLALSPLVGAIAaGCTVVLKPSELTPHTAALLAELV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 230 EEAgLPKGVINLVTGdGIEVSEVALEHR-DLagIHFTGSTktfqylwkTVGNNI----EKYRTyPrMVGETGGKDFVVAH 304
Cdd:cd07135 159 PKY-LDPDAFQVVQG-GVPETTALLEQKfDK--IFYTGSG--------RVGRIIaeaaAKHLT-P-VTLELGGKSPVIVT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 305 PSADravLKTALTR---GSFEYQGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFiGAVIDERSFAKNK 381
Cdd:cd07135 225 KNAD---LELAAKRilwGKFGNAGQICVAPDYVLVDPSVYDE-FVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 382 AAIDRAHADpsctVVAGGTYDDSVgYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVsDYALTGS 461
Cdd:cd07135 300 SLLDTTKGK----VVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL--DEAIKVINSR-DTPLALY 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1954849083 462 VIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGT 508
Cdd:cd07135 372 IFTDDKSEIDHILTRTR--SGGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
182-507 |
1.05e-24 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 107.30 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLA 260
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNNIEKYRTyprmvgETGGKDFVVAHPSAD-RAVLKTALTrGSFEYQGQKCSASSRAYVPAS 339
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCAKDIKKVSL------ELGGNAPFIVFDDADlDKAVEGALA-SKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 340 IWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVGYFVRPTV-VECSD 418
Cdd:PRK11241 301 VYDR-FAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA-LEKGARVVCGGKAHELGGNFFQPTIlVDVPA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 419 PAnEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRYaaGNFYINdksTGAVVGQ- 497
Cdd:PRK11241 379 NA-KVAKEETFGPLAPLFRFKDE--ADVIAQAND-TEFGLAAYFYARDLSRVFRVGEALEY--GIVGIN---TGIISNEv 449
|
330
....*....|
gi 1954849083 498 QPFGGGRASG 507
Cdd:PRK11241 450 APFGGIKASG 459
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
175-507 |
1.26e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 106.87 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 175 LDHRPLeGFVYAITPFNF---TAIAGNLPTApaLMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSE 251
Cdd:PRK13968 122 IEYRPL-GTILAIMPWNFplwQVMRGAVPIL--LAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 VALEHRdLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVGETGGKD--FVVAHPSADRAVlKTALTrGSFEYQGQKCS 329
Cdd:PRK13968 199 MINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDpfIVLNDADLELAV-KAAVA-GRYQNTGQVCA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 330 ASSRAYVPASIwNSGFKEEFAAEIDGITMGDVTDLSNFIG--AVIDERSFAKNKAaidRAHADPSCTVVAGGTYDDSVGY 407
Cdd:PRK13968 270 AAKRFIIEEGI-ASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQV---EATLAEGARLLLGGEKIAGAGN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 408 FVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDQYDEMLAqmeSVSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYIN 487
Cdd:PRK13968 346 YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELA---NDSEFGLSATIFTTDETQARQMAARLE--CGGVFIN 420
|
330 340
....*....|....*....|
gi 1954849083 488 DKStgAVVGQQPFGGGRASG 507
Cdd:PRK13968 421 GYC--ASDARVAFGGVKKSG 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
173-529 |
1.47e-24 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 106.62 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 173 NRLDHRPLeGFVYAITPFN--FTAIAGnlPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEA----GLPKGVINLVTGD 245
Cdd:cd07098 114 ARVEYEPL-GVVGAIVSWNypFHNLLG--PIIAALFaGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 246 GiEVSEVALEHRDLAGIHFTGStktfqylwKTVGNNIEK--YRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEY 323
Cdd:cd07098 191 P-ETAEALTSHPVIDHITFIGS--------PPVGKKVMAaaAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 324 QGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTY-- 401
Cdd:cd07098 262 SGQNCIGIERVIVHEKIYDK-LLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADA-VEKGARLLAGGKRyp 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 402 --DDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRy 479
Cdd:cd07098 340 hpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANS-TEYGLGASVFGKDIKRARRIASQLE- 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1954849083 480 aAGNFYINDKSTGAVVGQQPFGGGRASGTnDKAGAPQNLMRWTLTRAIKE 529
Cdd:cd07098 416 -TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
99-507 |
1.57e-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: 106.77 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 99 SFDDRAAIILRAA-------ELLA--------GPWRETLAASTMLGqsktaqqaeidcpcelVDFWRFnvkYARDLLAEQ 163
Cdd:cd07116 58 SVAERANILNKIAdrmeanlEMLAvaetwdngKPVRETLAADIPLA----------------IDHFRY---FAGCIRAQE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 164 ppanspGVWNRLD--------HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSpTQTHAAVL-LMQLLEEAg 233
Cdd:cd07116 119 ------GSISEIDentvayhfHEPL-GVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPA-EQTPASILvLMELIGDL- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 234 LPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIekyrtYPRMVgETGGK------DFVVAHPSA 307
Cdd:cd07116 190 LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IPVTL-ELGGKspniffADVMDADDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 308 --DRAVLKTALtrgsFEY-QGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAI 384
Cdd:cd07116 264 ffDKALEGFVM----FALnQGEVCTCPSRALIQESIYDR-FMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 385 DRAHADpSCTVVAGGTY----DDSVGYFVRPTVVECSDPAnEVFTTEYFGPFLAVHVYEDdqYDEMLAqMESVSDYALTG 460
Cdd:cd07116 339 DIGKEE-GAEVLTGGERnelgGLLGGGYYVPTTFKGGNKM-RIFQEEIFGPVLAVTTFKD--EEEALE-IANDTLYGLGA 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1954849083 461 SVIAGDrAAAAYTMEKlRYAAGNFYINdkSTGAVVGQQPFGGGRASG 507
Cdd:cd07116 414 GVWTRD-GNTAYRMGR-GIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
182-509 |
1.35e-21 |
|
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: 97.49 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAiagNL---PTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHR 257
Cdd:cd07148 126 GVVVAISAFNHPL---NLivhQVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 dLAGIHFTGSTKTFQYLwktvgnnieKYRTYP--RMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAY 335
Cdd:cd07148 203 -VAFFSFIGSARVGWML---------RSKLAPgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 336 VPASIwNSGFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAhADPSCTVVAGGTYDDSVGYfvRPTVVe 415
Cdd:cd07148 273 VPAEI-ADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEA-VAAGARLLCGGKRLSDTTY--APTVL- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 416 cSDPANE--VFTTEYFGPFLAVHVYEDdqYDEMLAQMESVsDYALTGSVIAGDRAAAAYTMEKLryAAGNFYINDKsTGA 493
Cdd:cd07148 348 -LDPPRDakVSTQEIFGPVVCVYSYDD--LDEAIAQANSL-PVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAF 420
|
330
....*....|....*.
gi 1954849083 494 VVGQQPFGGGRASGTN 509
Cdd:cd07148 421 RVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
136-507 |
5.39e-21 |
|
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: 95.29 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 136 QAEIDCPCELVDfwrfnvKYARDLLAEQPPANSPGVwNRLDHRPLeGFVYAITPFNF---TAIAgnlPTAPALM-GNVVV 211
Cdd:cd07087 64 LGEIDHALKHLK------KWMKPRRVSVPLLLQPAK-AYVIPEPL-GVVLIIGPWNYplqLALA---PLIGAIAaGNTVV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 212 WKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGiEVSEVALEHR-DLagIHFTGSTKtfqylwktVGNNIekyrtypr 290
Cdd:cd07087 133 LKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGV-EVATALLAEPfDH--IFFTGSPA--------VGKIV-------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 291 MVG----------ETGGKDFVVAHPSADravLKTALTR---GSFEYQGQKCSASSRAYVPASIwnsgfKEEFAAEI-DGI 356
Cdd:cd07087 193 MEAaakhltpvtlELGGKSPCIVDKDAN---LEVAARRiawGKFLNAGQTCIAPDYVLVHESI-----KDELIEELkKAI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 357 T--MGDVTDLSNFIGAVIDERSFAKNKAAIDRAhadpscTVVAGGTYDDSvGYFVRPTVVECSDPANEVFTTEYFGPFLA 434
Cdd:cd07087 265 KefYGEDPKESPDYGRIINERHFDRLASLLDDG------KVVIGGQVDKE-ERYIAPTILDDVSPDSPLMQEEIFGPILP 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954849083 435 VHVYEDdqYDEMLAQMESVSDyALTGSVIAGDRAAAAYTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASG 507
Cdd:cd07087 338 ILTYDD--LDEAIEFINSRPK-PLALYLFSEDKAVQERVLAETS--SGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
177-507 |
1.87e-20 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 94.50 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALE 255
Cdd:PLN02766 156 KEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIAS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLAGIHFTGSTKtfqylwktVGNNIEKY--RTYPRMVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASS 332
Cdd:PLN02766 235 HMDVDKVSFTGSTE--------VGRKIMQAaaTSNLKQVSlELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASS 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpSCTVVAGGTYDDSVGYFVRPT 412
Cdd:PLN02766 307 RVYVQEGIYDE-FVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKRE-GATLLTGGKPCGDKGYYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDPANEVFTTEYFGPFLAVHVYEddQYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRyaAGNFYINdkSTG 492
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKFK--TVEEAIKKANN-TKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVN--CYF 457
|
330
....*....|....*
gi 1954849083 493 AVVGQQPFGGGRASG 507
Cdd:PLN02766 458 AFDPDCPFGGYKMSG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
179-383 |
7.21e-20 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 92.51 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLeGFVYAITPFNFTAiagNLPT---APALM-GNVVVWKPsPTQTHAAVLLM-QLLEEAGLPKGVINLVTGDGIEVSEVA 253
Cdd:PLN00412 158 PL-GVVLAIPPFNYPV---NLAVskiAPALIaGNAVVLKP-PTQGAVAALHMvHCFHLAGFPKGLISCVTGKGSEIGDFL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 254 LEHRDLAGIHFTGStktfqylwkTVGNNIEKyrtYPRMVG---ETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSA 330
Cdd:PLN00412 233 TMHPGVNCISFTGG---------DTGIAISK---KAGMVPlqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTA 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954849083 331 SSRAYVPASIWNSgFKEEFAAEIDGITMG------DVTDL-----SNFI-GAVIDersfAKNKAA 383
Cdd:PLN00412 301 VKVVLVMESVADA-LVEKVNAKVAKLTVGppeddcDITPVvsessANFIeGLVMD----AKEKGA 360
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
179-507 |
1.62e-19 |
|
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: 91.56 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLEGFVYAITPFNFtAIAGNLPT-APALMGNV-VVWKPSPTQTHAAVLLMQLLEEAG-LPKGVINLVTGDGIEVSEvALE 255
Cdd:cd07128 143 PRRGVAVHINAFNF-PVWGMLEKfAPALLAGVpVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLD-HLG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 256 HRDLagIHFTGSTKTFQYLwktvgnniekyRTYPRMVGEtgGKDFVVAHPSADRAVLKTALTRGSFEYQ----------- 324
Cdd:cd07128 221 EQDV--VAFTGSAATAAKL-----------RAHPNIVAR--SIRFNAEADSLNAAILGPDATPGTPEFDlfvkevaremt 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 325 ---GQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpsCTVVAGG-- 399
Cdd:cd07128 286 vkaGQKCTAIRRAFVPEARVDA-VIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE--AEVVFGGpd 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 400 -----TYDDSVGYFVRPTVVECSDP--ANEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVSdyaLTGSVIAGDRAAAAY 472
Cdd:cd07128 363 rfevvGADAEKGAFFPPTLLLCDDPdaATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS---LVASVVTNDPAFARE 439
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1954849083 473 TMEKLRYAAGNFYINDKST-------GAVVGQQPFGG-GRASG 507
Cdd:cd07128 440 LVLGAAPYHGRLLVLNRDSakestghGSPLPQLVHGGpGRAGG 482
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-507 |
6.56e-19 |
|
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: 89.21 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 164 PPANSPGVWNRLDHRPlEGFVYAITPFNF---TAIAgnlPTAPALM-GNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVi 239
Cdd:cd07134 85 TPLLLFGTKSKIRYEP-KGVCLIISPWNYpfnLAFG---PLVSAIAaGNTAILKPSELTPHTSAVIAKIIREAFDEDEV- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 240 NLVTGDgIEVSEVALE----HrdlagIHFTGSTktfqylwkTVGnniekyrtypRMVG------------ETGGKDFVVA 303
Cdd:cd07134 160 AVFEGD-AEVAQALLElpfdH-----IFFTGSP--------AVG----------KIVMaaaakhlasvtlELGGKSPTIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 304 HPSADravLKTA---LTRGSFEYQGQKCSASSRAYVPASIwNSGFKEEFAAEIDGITMGDVTDLSNF-IGAVIDERSFAK 379
Cdd:cd07134 216 DETAD---LKKAakkIAWGKFLNAGQTCIAPDYVFVHESV-KDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 380 NKAAIDRAHADpSCTVVAGGTYDDSvGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALT 459
Cdd:cd07134 292 LKGLLDDAVAK-GAKVEFGGQFDAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYED--LDEVIEYINA-KPKPLA 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1954849083 460 GSVIAGDRAAAAYTMEklRYAAGNFYINDKSTGAVVGQQPFGGGRASG 507
Cdd:cd07134 367 LYVFSKDKANVNKVLA--RTSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
144-524 |
6.90e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 86.43 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 144 ELVDFWRFNVKYARDLLAEQPPANSPG-----VWNRLdhrpleGFVYAITPFNF-TAIAGNLPTAPALMGNVVVWKPSPT 217
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERPNhmmmeVWNPL------GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 218 QTHAAV----LLMQLLEEAGLPKGVINLVTGdGIEVSE-VALEHRdLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMV 292
Cdd:PLN02315 193 TPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEaIAKDTR-IPLVSFTGSSKVGLMVQQTVNARFGK------CL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 293 GETGGKDFVVAHPSAD-----RAVLKTALTRGsfeyqGQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNF 367
Cdd:PLN02315 265 LELSGNNAIIVMDDADiqlavRSVLFAAVGTA-----GQRCTTCRRLLLHESIYDD-VLEQLLTVYKQVKIGDPLEKGTL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 368 IGAVIDERS---FAKNKAAIdrahADPSCTVVAGGTYDDSVGYFVRPTVVECSdPANEVFTTEYFGPFLavHVYEDDQYD 444
Cdd:PLN02315 339 LGPLHTPESkknFEKGIEII----KSQGGKILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 445 EMLAQMESVSDyALTGSVIAGDRAAAAYTMEKLRYAAGNFYINDKSTGAVVGQQpFGGGRASGTNDKAGA---PQNLMRW 521
Cdd:PLN02315 412 EAIEINNSVPQ-GLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAGSdswKQYMRRS 489
|
...
gi 1954849083 522 TLT 524
Cdd:PLN02315 490 TCT 492
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
179-507 |
1.37e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.44 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLEGFVYAITPFNFTAIAGNLPTAPALMGNV-VVWKPSPTQTHAAVLLMQLLEEAG-LPKGVINLVTGDGIEVSEvALEH 256
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLD-HLQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 257 RDLagIHFTGSTKTFQYLwktvgnniekyRTYPRMVGEtgGKDFVVAHPSADRAVLKTALTRGSFEYQ------------ 324
Cdd:PRK11903 226 FDV--VSFTGSAETAAVL-----------RSHPAVVQR--SVRVNVEADSLNSALLGPDAAPGSEAFDlfvkevvremtv 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 325 --GQKCSASSRAYVPASIWNSgFKEEFAAEIDGITMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADpsCTVVAGGT-- 400
Cdd:PRK11903 291 ksGQKCTAIRRIFVPEALYDA-VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ--AEVLFDGGgf 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 401 ----YDDSVGYFVRPTVVECSDP--ANEVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVSdyaLTGSVIAGDRAAAAYTM 474
Cdd:PRK11903 368 alvdADPAVAACVGPTLLGASDPdaATAVHDVEVFGPVATLLPYRDAAHALALARRGQGS---LVASVYSDDAAFLAAAA 444
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1954849083 475 EKLRYAAGNFYINDKSTGA-------VVGQQPFGG-GRASG 507
Cdd:PRK11903 445 LELADSHGRVHVISPDVAAlhtghgnVMPQSLHGGpGRAGG 485
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
136-507 |
1.57e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 82.38 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 136 QAEIDCPCELVDfwrfnvKYARDLLAEQPPANSPGVwNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKP 214
Cdd:PTZ00381 73 VAEIEHLLKHLD------EYLKPEKVDTVGVFGPGK-SYIIPEPL-GVVLVIGAWNYPLNLTLIPLAGAIAaGNTVVLKP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 215 SPTQTHAAVLLMQLLEEAgLPKGVINLVTGdGIEVSEVALEHR-DLagIHFTGSTKTFQYLWKTVGNNIekyrtYPRMVg 293
Cdd:PTZ00381 145 SELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENL-----TPCTL- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 294 ETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIwNSGFKEEFAAEIDGItMGDVTDLSNFIGAVID 373
Cdd:PTZ00381 215 ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI-KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 374 ERSFAKNKAAIDRaHADpscTVVAGGTYDDSVGYfVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESV 453
Cdd:PTZ00381 293 EFHTKRLAELIKD-HGG---KVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYEN--IDEVLEFINSR 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1954849083 454 SDyALTGSVIAGDRAAAAYTMEKLryAAGNFYINDKSTGAVVGQQPFGGGRASG 507
Cdd:PTZ00381 366 PK-PLALYYFGEDKRHKELVLENT--SSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
160-487 |
2.71e-15 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 78.63 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 160 LAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFTAIAG--NLPTApALMGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKG 237
Cdd:PLN02419 230 MGEYLPNVSNGVDTYSIREPL-GVCAGICPFNFPAMIPlwMFPVA-VTCGNTFILKPSEKDPGASVILAELAMEAGLPDG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 238 VINLVTGDGIEVSEVAlEHRDLAGIHFTGSTKTFQYLWKTVGNNIEkyrtypRMVGETGGKDFVVAHPSADRAVLKTALT 317
Cdd:PLN02419 308 VLNIVHGTNDTVNAIC-DDEDIRAVSFVGSNTAGMHIYARAAAKGK------RIQSNMGAKNHGLVLPDANIDATLNALL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 318 RGSFEYQGQKCSA-SSRAYV-PASIWNSGFKEEfaAEIDGITMGDV--TDLSNFIGAVIDERSFAKNKAAID---RAHAD 390
Cdd:PLN02419 381 AAGFGAAGQRCMAlSTVVFVgDAKSWEDKLVER--AKALKVTCGSEpdADLGPVISKQAKERICRLIQSGVDdgaKLLLD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 391 PSCTVVAGgtYDDsvGYFVRPTVVECSDPANEVFTTEYFGPFLAvhVYEDDQYDEMLAQMESvSDYAlTGSVIAGDRAAA 470
Cdd:PLN02419 459 GRDIVVPG--YEK--GNFIGPTILSGVTPDMECYKEEIFGPVLV--CMQANSFDEAISIINK-NKYG-NGAAIFTSSGAA 530
|
330
....*....|....*..
gi 1954849083 471 AYTMEkLRYAAGNFYIN 487
Cdd:PLN02419 531 ARKFQ-MDIEAGQIGIN 546
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
182-527 |
1.70e-13 |
|
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: 72.91 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEhRDLA 260
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 261 GIHFTGSTKTFQYLWKTVGNNIEKyrtyprmvgETGGKDFVVAHPS-ADRAVLKTALTRGSFEYQGQKCSASSRAYVPAS 339
Cdd:cd07126 223 MTLFTGSSKVAERLALELHGKVKL---------EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 340 IWNSGFKEEFAA-----EIDGITMGDVTDLSNfigavidersfAKNKAAIDRAHADPSCTVVAGG------TYDDSVGYf 408
Cdd:cd07126 294 WVQAGILDKLKAlaeqrKLEDLTIGPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGkpltnhSIPSIYGA- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 409 VRPTVV-----ECSDPAN-EVFTTEYFGPFLAVHVYEDDQYDEMLAQMESVsDYALTGSVIAGD----RAAAAYTMEKLR 478
Cdd:cd07126 362 YEPTAVfvpleEIAIEENfELVTTEVFGPFQVVTEYKDEQLPLVLEALERM-HAHLTAAVVSNDirflQEVLANTVNGTT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1954849083 479 YAAgnfyINDKSTGAVVGQ--QPFGGGRASGTndkaGAPQNL-MRWTLTRAI 527
Cdd:cd07126 441 YAG----IRARTTGAPQNHwfGPAGDPRGAGI----GTPEAIrLVWSCHREI 484
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
182-507 |
4.50e-13 |
|
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: 71.38 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 182 GFVYAITPFNFT----------AIAGnlptapalmGNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGdGIEVSE 251
Cdd:cd07136 102 GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 252 vALEHRDLAGIHFTGSTKTfqylWKTVGNNIEKYRTyPrmVG-ETGGKDFVVAHPSADravLKTALTR---GSFEYQGQK 327
Cdd:cd07136 171 -ELLDQKFDYIFFTGSVRV----GKIVMEAAAKHLT-P--VTlELGGKSPCIVDEDAN---LKLAAKRivwGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 328 CSASSRAYVPASIwnsgfKEEFAAEIDG-IT--MGDVTDLSNFIGAVIDERSFAKNKAAIDRAhadpscTVVAGGTYDDS 404
Cdd:cd07136 240 CVAPDYVLVHESV-----KEKFIKELKEeIKkfYGEDPLESPDYGRIINEKHFDRLAGLLDNG------KIVFGGNTDRE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 405 VGYfVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDdqYDEMLAQMESvSDYALTGSVIAGDRAAAAYTMEKLRYAAGnf 484
Cdd:cd07136 309 TLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTYDT--LDEAIEIIKS-RPKPLALYLFSEDKKVEKKVLENLSFGGG-- 382
|
330 340
....*....|....*....|...
gi 1954849083 485 YINDKSTGAVVGQQPFGGGRASG 507
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
152-507 |
3.66e-12 |
|
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: 68.28 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 152 NVKYARDLLAE--QPPANSPGVW-----NRLDHRPLeGFVYAITPFNF---TAIAgnlPTAPAL-MGNVVVWKPSPTQTH 220
Cdd:cd07133 67 GIKHARKHLKKwmKPSRRHVGLLflpakAEVEYQPL-GVVGIIVPWNYplyLALG---PLIAALaAGNRVMIKPSEFTPR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 221 AAVLLMQLLEEAGLPKgVINLVTGD---GIEVSEVALEHrdlagIHFTGSTKtfqylwktVGnniekyrtypRMVG---- 293
Cdd:cd07133 143 TSALLAELLAEYFDED-EVAVVTGGadvAAAFSSLPFDH-----LLFTGSTA--------VG----------RHVMraaa 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 294 --------ETGGKDFVVAHPSADravLKTALTR---GSFEYQGQKCSASSRAYVPAsiwnsGFKEEFAAEI--------- 353
Cdd:cd07133 199 enltpvtlELGGKSPAIIAPDAD---LAKAAERiafGKLLNAGQTCVAPDYVLVPE-----DKLEEFVAAAkaavakmyp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 354 DGITMGDVTdlsnfigAVIDERSFAKNKAAIDRAhADPSCTVV--AGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGP 431
Cdd:cd07133 271 TLADNPDYT-------SIINERHYARLQGLLEDA-RAKGARVIelNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 432 FLAVHVYEDdqydemlaqMESVSDYaltgsVIAGDRAAAAYTM-------EKL--RYAAGNFYINDKSTGAVVGQQPFGG 502
Cdd:cd07133 343 ILPILTYDS---------LDEAIDY-----INARPRPLALYYFgedkaeqDRVlrRTHSGGVTINDTLLHVAQDDLPFGG 408
|
....*
gi 1954849083 503 GRASG 507
Cdd:cd07133 409 VGASG 413
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
189-502 |
1.67e-10 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 63.33 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 189 PFNFTAIAGNlpTAPAL-MGNVVVWKPSPTQTHAAVLLMQL----LEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIH 263
Cdd:cd07129 118 PLAFSVAGGD--TASALaAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 264 FTGSTKTFQYLWKTVGNniekyRTYPRMV-GETGGKDFVVAHPSA--DRAV-----LKTALTRGSfeyqGQKCSASSRAY 335
Cdd:cd07129 196 FTGSRRGGRALFDAAAA-----RPEPIPFyAELGSVNPVFILPGAlaERGEaiaqgFVGSLTLGA----GQFCTNPGLVL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 336 VPASIWNSGFKEEFA---AEIDGITMgdvtdLSNFIgavidERSFAKNKAAIdRAHADPscTVVAGGTYDDSvGYFVRPT 412
Cdd:cd07129 267 VPAGPAGDAFIAALAealAAAPAQTM-----LTPGI-----AEAYRQGVEAL-AAAPGV--RVLAGGAAAEG-GNQAAPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 413 VVECSDP---ANEVFTTEYFGPFLAVHVYEDDqyDEMLAQMESVSDyALTGSVIA--GDRAAAAYTMEKLRYAAGNFYIN 487
Cdd:cd07129 333 LFKVDAAaflADPALQEEVFGPASLVVRYDDA--AELLAVAEALEG-QLTATIHGeeDDLALARELLPVLERKAGRLLFN 409
|
330
....*....|....*.
gi 1954849083 488 DKSTG-AVVGQQPFGG 502
Cdd:cd07129 410 GWPTGvEVCPAMVHGG 425
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
189-433 |
7.89e-09 |
|
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: 58.00 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 189 PFNFT------AIAGnlptapalmGNVVVWKPSPTQTHAAVLLMQLLeeaglPKGVIN----LVTGdGIEVSEVALEHR- 257
Cdd:cd07132 113 PLQLTlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAELI-----PKYLDKecypVVLG-GVEETTELLKQRf 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 DLagIHFTGSTktfqylwkTVGNNI----EKYRTypRMVGETGGKDFVVAHPSADravLKTALTR---GSFEYQGQKCSA 330
Cdd:cd07132 178 DY--IFYTGST--------SVGKIVmqaaAKHLT--PVTLELGGKSPCYVDKSCD---IDVAARRiawGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 331 SSraYVpasIWNSGFKEEFAAEIDGIT---MGDVTDLSNFIGAVIDERSFAKNKAAIDrahadpSCTVVAGGTYDDSVGY 407
Cdd:cd07132 243 PD--YV---LCTPEVQEKFVEALKKTLkefYGEDPKESPDYGRIINDRHFQRLKKLLS------GGKVAIGGQTDEKERY 311
|
250 260
....*....|....*....|....*.
gi 1954849083 408 fVRPTVVECSDPANEVFTTEYFGPFL 433
Cdd:cd07132 312 -IAPTVLTDVKPSDPVMQEEIFGPIL 336
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
207-514 |
2.84e-08 |
|
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: 56.33 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 207 GNVVVWKPSPtqthAAVLLMQL--------LEEAGLPKGVINLVTGD-GIEVSEVALEHRDLAGIHFTGSTKtfqylwkt 277
Cdd:cd07127 221 GNPVIVKPHP----AAILPLAItvqvarevLAEAGFDPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNA-------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 278 VGNNIEKYRTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPAS-IWNS----GFKE---EF 349
Cdd:cd07127 289 FGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgIQTDdgrkSFDEvaaDL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 350 AAEIDGItMGDVTDLSNFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVgyfVR-PTVVECSDPANEVFTTEY 428
Cdd:cd07127 369 AAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDAR---VRtPLLLKLDASDEAAYAEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 429 FGPFLAVHVYEDDQYDEMLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRYAAGNFYINdkSTGAVVGQQP--FGGGRAS 506
Cdd:cd07127 445 FGPIAFVVATDSTDHSIELARESVREHGAMTVGVYSTDPEVVERVQEAALDAGVALSIN--LTGGVFVNQSaaFSDFHGT 522
|
....*...
gi 1954849083 507 GTNDKAGA 514
Cdd:cd07127 523 GANPAANA 530
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
179-435 |
4.59e-06 |
|
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: 48.95 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGdGIEVSEVALEHR 257
Cdd:cd07137 101 PL-GVVLVISAWNFPFLLSLEPVIGAIaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 -DlaGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVGETGGKDFVVAHPSADravLKTALTR---GSFEY-QGQKCSASS 332
Cdd:cd07137 178 wD--KIFFTGSPRVGRIIMAAAAKHLTP------VTLELGGKCPVIVDSTVD---LKVAVRRiagGKWGCnNGQACIAPD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 333 RAYVPasiwnsgfkEEFAAE-IDGIT------MGDVTDLSNFIGAVIDERSFAKNKAAIDrahaDPSCT--VVAGGTYDD 403
Cdd:cd07137 247 YVLVE---------ESFAPTlIDALKntlekfFGENPKESKDLSRIVNSHHFQRLSRLLD----DPSVAdkIVHGGERDE 313
|
250 260 270
....*....|....*....|....*....|...
gi 1954849083 404 SvGYFVRPTVVeCSDP-ANEVFTTEYFGPFLAV 435
Cdd:cd07137 314 K-NLYIEPTIL-LDPPlDSSIMTEEIFGPLLPI 344
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
179-507 |
6.16e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.89 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 179 PLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHAAVLLMQLLEEAgLPKGVINLVTGDGIEVSevALEHR 257
Cdd:PLN02174 112 PL-GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETT--ALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 258 DLAGIHFTGSTKTFQYLWKTVGNNIEKyrtyprMVGETGGKDFVVAHPSADRAVLKTALTRGSFE-YQGQKCSA-----S 331
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISpdyilT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 332 SRAYVPASIwnSGFKEEFaAEIDGITMGDVTDLSNfigaVIDERSFAKNKAAIDRAHAdpSCTVVAGGTYDDSvGYFVRP 411
Cdd:PLN02174 262 TKEYAPKVI--DAMKKEL-ETFYGKNPMESKDMSR----IVNSTHFDRLSKLLDEKEV--SDKIVYGGEKDRE-NLKIAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 412 TVVECSDPANEVFTTEYFGPFLAVHVYED--DQYDEMLAQMESVSDYALTGSVIAGDRAAAAYTmeklryaAGNFYINDK 489
Cdd:PLN02174 332 TILLDVPLDSLIMSEEIFGPLLPILTLNNleESFDVIRSRPKPLAAYLFTHNKKLKERFAATVS-------AGGIVVNDI 404
|
330
....*....|....*...
gi 1954849083 490 STGAVVGQQPFGGGRASG 507
Cdd:PLN02174 405 AVHLALHTLPFGGVGESG 422
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
46-527 |
7.29e-04 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 42.34 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 46 IGGEKRMGGGDRFDVVQPHNHKARLGTYANATQQDAQDAIDAALAAAPAWRAMSfDDRAAIILRAAELLAGPWRETLAAS 125
Cdd:COG0506 494 AAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA-AAAAAAAAAAAAAEAAEAALLLAAA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 126 TMLGQSKTAQQAEIDcpCELVDFWRFNVKYARDLLAEQPPANSPGVWNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPAL 205
Cdd:COG0506 573 AAEAAAAAALAAAAA--EAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 206 MGNVVVWKPSPTQTHAAVLLMQLLEEAGLPKGVINLVTGDGIEVSEVALEHRDLAGIHFTGSTKTFQYLWKTVGNNIeky 285
Cdd:COG0506 651 AAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAA--- 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 286 RTYPRMVGETGGKDFVVAHPSADRAVLKTALTRGSFEYQGQKCSASSRAYVPASIWnsgfKEEFAAEIDGITMGDVTDLS 365
Cdd:COG0506 728 AAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADL----VILLLALAAAAAALLVGGPG 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 366 NFIGAVIDERSFAKNKAAIDRAHADPSCTVVAGGTYDDSVGYFVRPTVVECSDPANEVFTTEYFGPFLAVHVYEDDqYDE 445
Cdd:COG0506 804 AAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALAL-DLA 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954849083 446 MLAQMESVSDYALTGSVIAGDRAAAAYTMEKLRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTR 525
Cdd:COG0506 883 ALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAA 962
|
..
gi 1954849083 526 AI 527
Cdd:COG0506 963 AA 964
|
|
| |
