|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-535 |
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: 838.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 10 PVNEPVHSYAPGSPERARLEAKLKELAENPIELPMTIGGERRMGGGErVDVVQPHNHRAVIGTFAGATEQDAQDAVDAAL 89
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNT-GKQVMPHDHAHVLATYHYADAALVEKAIEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 90 AAAPAWRAMSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLLAEQPPANSP 169
Cdd:cd07123 80 EARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 170 GVWNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAV 249
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 250 SEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYRSYPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCS 329
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 330 ATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSVGYFV 409
Cdd:cd07123 320 AASRAYVPESLWPE-VKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 410 RPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespEGYDAMLDQMESVSAYALTGSVIANDRAAAAHTMEKLRYAAGNFYI 489
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVYVYPD---SDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYI 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1717797354 490 NDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKETLV 535
Cdd:cd07123 476 NDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFV 521
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
12-546 |
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: 762.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 12 NEPVHSYAPGSPERARLEAKLKELAENPIELPMTIGGERRMGGGERVDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAA 91
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 92 APAWRAMSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLLAEQPPANsPGV 171
Cdd:TIGR01236 82 KKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISA-PGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 172 WNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSE 251
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 252 VALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYRSYPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSAT 331
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTC-EIVAGGSYDDSVGYFVR 410
Cdd:TIGR01236 321 SRLYVPHSKWPE-FKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEAlTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegYDAMLDQMESVSAYALTGSVIANDRAAAAHTMEKLRYAAGNFYIN 490
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDK---YKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYIN 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717797354 491 DKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKETLVAPVEYGYPHMG 546
Cdd:TIGR01236 477 DKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
98-534 |
4.89e-131 |
|
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: 390.26 E-value: 4.89e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGpWRETLAASTMLGQSKTAQQAEIDTPcELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDH 177
Cdd:COG1012 62 TPPAERAAILLRAADLLEE-RREELAALLTLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:COG1012 140 EPL-GVVGAITPWNFPLALAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVGGNIekyrsyPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRA 334
Cdd:COG1012 219 PDVDKISFTGSTAVGRRIAAAAAENL------KRVTLELGGKNPAIVLDDADldAAV--EAAVRGAFGNAGQRCTAASRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSY-DDSVGYFVRPTV 413
Cdd:COG1012 291 LVHESIYDE-FVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKS 493
Cdd:COG1012 369 LADVTPDMRIAREEIFGPVLSVIPFDDE-----EEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGT 440
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1717797354 494 TGAvVGQQPFGGGRASGTNDKAGaPQNLMRWTLTRAIKETL 534
Cdd:COG1012 441 TGA-VPQAPFGGVKQSGIGREGG-REGLEEYTETKTVTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
61-533 |
4.18e-120 |
|
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: 363.05 E-value: 4.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 61 VQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPWRETLAASTMLGqSKTAQQaEID 140
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 141 TPCELVDFWRFNVAYARDLLAEQPPANS-PGVWNRLDHRPLeGFVYAITPFNFT-AIAGNLPTAPALMGNVVVWKPSPTQ 218
Cdd:cd07083 115 DVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGL-GAGVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 219 THSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYRSYPRIVGETGGK 298
Cdd:cd07083 194 VVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 299 DFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFA 378
Cdd:cd07083 274 NAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEP-VLERLLKRAERLSVGPPEENGTDLGPVIDAEQEA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 379 KNKAAIDRAKADPTceIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegYDAMLDQMESVSA 458
Cdd:cd07083 353 KVLSYIEHGKNEGQ--LVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDD---FAEALEVANSTPY 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717797354 459 YALTGSVIANDraaaAHTMEKLR-YAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKET 533
Cdd:cd07083 428 GLTGGVYSRKR----EHLEEARReFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMKAVAER 499
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
98-530 |
4.90e-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: 304.84 E-value: 4.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPcELVDFWRFNVAYARDLLAEQPPaNSPGVWNRLDH 177
Cdd:pfam00171 48 TPAAERAAILRKAADLLEER-KDELAELETLENGKPLAEARGEVD-RAIDVLRYYAGLARRLDGETLP-SDPGRLAYTRR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:pfam00171 125 EPL-GVVGAITPWNFPLLLPAWKIAPALAaGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVGGNIekyrsyPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYI 336
Cdd:pfam00171 204 PDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 337 PASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTVIVC 416
Cdd:pfam00171 278 HESIYDE-FVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLAN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 417 TDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGA 496
Cdd:pfam00171 356 VTPDMRIAQEEIFGPVLSVIRFKDE-----EEAIEIAND-TEYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGD 427
|
410 420 430
....*....|....*....|....*....|....
gi 1717797354 497 VVGqQPFGGGRASGTNDKAGaPQNLMRWTLTRAI 530
Cdd:pfam00171 428 ADG-LPFGGFKQSGFGREGG-PYGLEEYTEVKTV 459
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-532 |
1.59e-93 |
|
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: 294.90 E-value: 1.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 11 VNEPVHSYAPGSpERARLEAKLKEL-AENPIELPMTIGGERRMGGGErVDVVQPHNHRAVIGTFAGATEQDAQDAVDAAL 89
Cdd:cd07124 2 RNEPFTDFADEE-NRAAFRAALARVrEELGREYPLVIGGKEVRTEEK-IESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 90 AAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTpCELVDFWRFnvaYARDLLAEQPPANS- 168
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADADV-AEAIDFLEY---YAREMLRLRGFPVEm 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 169 -PGVWNRLDHRPLeGFVYAITPFNF-TAIAGNLPTAPALMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDG 246
Cdd:cd07124 155 vPGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 247 IAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYRSYPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQ 324
Cdd:cd07124 234 EEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADldEAA--EGIVRSAFGFQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 325 GQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTceIVAGGSYDDS 404
Cdd:cd07124 312 GQKCSACSRVIVHESVYDE-FLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGR--LLLGGEVLEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 405 V--GYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLDQMESVSaYALTGSVIANDRAAAAHTMEKLRy 482
Cdd:cd07124 389 AaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD-----FDEALEIANDTE-YGLTGGVFSRSPEHLERARREFE- 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 483 aAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKE 532
Cdd:cd07124 462 -VGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
98-530 |
4.61e-92 |
|
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: 288.34 E-value: 4.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTpCELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDH 177
Cdd:cd07078 17 LPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEV-ARAADTFRYYAGLARRLHGEVIPSPDPGELAIVRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:cd07078 95 EPL-GVVGAITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVGGNIekyrsyPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRA 334
Cdd:cd07078 174 PRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADldAAV--KGAVFGAFGNAGQVCTAASRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPtCEIVAGGSYDDS-VGYFVRPTV 413
Cdd:cd07078 246 LVHESIYDE-FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-AKLLCGGKRLEGgKGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKS 493
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDE-----EEAIELAND-TEYGLAAGVFTRDLERALRVAERLE--AGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1717797354 494 TGAvVGQQPFGGGRASGTNdKAGAPQNLMRWTLTRAI 530
Cdd:cd07078 396 VGA-EPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
60-534 |
2.06e-82 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 266.03 E-value: 2.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 60 VVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPWREtLAASTMLGQSKTAQQAEI 139
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE-FSAWLVKEAGKPWAEADA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 140 DTpCELVDFWRFnvaYARDLL---AEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIAGNLPTAPALMGNVVVWKPS 215
Cdd:PRK03137 133 DT-AEAIDFLEY---YARQMLklaDGKPVESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 216 PTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGS----TRTFQHLWKTVGGNIEkyrsYPRI 291
Cdd:PRK03137 208 SDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSrevgLRIYERAAKVQPGQIW----LKRV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 292 VGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDlSNFIGAV 371
Cdd:PRK03137 284 IAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDE-VLEKVVELTKELTVGNPED-NAYMGPV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 372 IDDRSFAKNKAAIDRAKAdpTCEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLD 451
Cdd:PRK03137 362 INQASFDKIMSYIEIGKE--EGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD-----FDHALE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 452 QMESvSAYALTGSVIANDRaaaahtmEKLRYA-----AGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTL 526
Cdd:PRK03137 435 IANN-TEYGLTGAVISNNR-------EHLEKArrefhVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQ 506
|
....*...
gi 1717797354 527 TRAIKETL 534
Cdd:PRK03137 507 AKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
58-532 |
2.75e-77 |
|
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: 252.48 E-value: 2.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 58 VDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA 137
Cdd:TIGR01237 48 IVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 138 EIDTpCELVDFWRFnvaYARDL--LAEQPPANS-PGVWNRLDHRPLeGFVYAITPFNFT-AIAGNLPTAPALMGNVVVWK 213
Cdd:TIGR01237 127 DAEV-AEAIDFMEY---YARQMieLAKGKPVNSrEGETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 214 PSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGS----TRTFQHLWKTVGGNiekyRSYP 289
Cdd:TIGR01237 202 PAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSrevgTRIFERAAKVQPGQ----KHLK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 290 RIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIG 369
Cdd:TIGR01237 278 RVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDE-VVERFVEITESLKVGPPDSADVYVG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 370 AVIDDRSFAKNKAAIDRAKADptCEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAM 449
Cdd:TIGR01237 357 PVIDQKSFNKIMEYIEIGKAE--GRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASD-----FDEA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 450 LDQMESvSAYALTGSVIANDRAAAAHTmeKLRYAAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRA 529
Cdd:TIGR01237 430 LEIANN-TEYGLTGGVISNNRDHINRA--KAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKT 506
|
...
gi 1717797354 530 IKE 532
Cdd:TIGR01237 507 VTE 509
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-523 |
1.42e-69 |
|
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: 232.47 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 16 HSYAPGSPERARLEAKLKELAENPIELPMTIGGERRMGGGErvDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAW 95
Cdd:cd07125 8 RIFDLEVPLEALADALKAFDEKEWEAIPIINGEETETGEGA--PVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 96 RAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAeIDTPCELVDFWRFNVAYARDLLAEQPPansPGVWNRL 175
Cdd:cd07125 86 SATPVEERAEILEKAADLLEAN-RGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPEL---PGPTGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLEG---FVyAITPFNF-TAI-AGNlpTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAV 249
Cdd:cd07125 161 NGLELHGrgvFV-CISPWNFpLAIfTGQ--IAAALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 250 SEVALNHPALAGIHFTGSTRTFQHLWKTvggNIEKYRSYPRIVGETGGKDFVVAHPSADRA-----VLKTAltrgsFEFQ 324
Cdd:cd07125 238 GEALVAHPRIDGVIFTGSTETAKLINRA---LAERDGPILPLIAETGGKNAMIVDSTALPEqavkdVVQSA-----FGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 325 GQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTceIVAGGSYDDS 404
Cdd:cd07125 310 GQRCSALRLLYLQEEIAER-FIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAW--LIAPAPLDDG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 405 VGYFVRPTVIvcTDPGNEVFTDEYFGPILAVYVYEdesPEGYDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaA 484
Cdd:cd07125 387 NGYFVAPGII--EIVGIFDLTTEVFGPILHVIRFK---AEDLDEAIEDINA-TGYGLTLGIHSRDEREIEYWRERVE--A 458
|
490 500 510
....*....|....*....|....*....|....*....
gi 1717797354 485 GNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 523
Cdd:cd07125 459 GNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
98-516 |
1.99e-66 |
|
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: 219.79 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTpCELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDH 177
Cdd:cd06534 13 LPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGEV-ARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:cd06534 91 EPL-GVVGVITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVGGNIekyrsyPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRA 334
Cdd:cd06534 170 PRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADldAAV--EGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWnsgfkEEFAAEVDgiamgdvtdlsnfigaviddrsfaknkaaidrakadptceivaggsyddsvgyfvrpTVI 414
Cdd:cd06534 242 LVHESIY-----DEFVEKLV---------------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 415 VCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKST 494
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDE-----EEAIALAND-TEYGLTAGVFTRDLNRALRVAERLR--AGTVYINDSSI 331
|
410 420
....*....|....*....|..
gi 1717797354 495 GaVVGQQPFGGGRASGTNDKAG 516
Cdd:cd06534 332 G-VGPEAPFGGVKNSGIGREGG 352
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
98-510 |
2.91e-59 |
|
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: 202.76 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELL---AGPWRETLAASTmlGQSKTAQQAEIDtpcELVDFWRFNVAYARDLLAEQPPANSPGVWNR 174
Cdd:cd07104 19 TPPQERAAILRKAAEILeerRDEIADWLIRES--GSTRPKAAFEVG---AAIAILREAAGLPRRPEGEILPSDVPGKESM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 175 LDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSP-TQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEV 252
Cdd:cd07104 94 VRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSrTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 253 ALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSA 330
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKK------VALELGGNNPLIVLDDADldLAV--SAAAFGAFLHQGQICMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 331 TSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDdsvGYFVR 410
Cdd:cd07104 245 AGRILVHESVYDE-FVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAA-GARLLTGGTYE---GLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegydamldqmESV-----SAYALTGSVIANDRAAAAHTMEKLRyaAG 485
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDE-----------EAVelandTEYGLSAAVFTRDLERAMAFAERLE--TG 386
|
410 420
....*....|....*....|....*..
gi 1717797354 486 NFYINDKST--GAVVgqqPFGGGRASG 510
Cdd:cd07104 387 MVHINDQTVndEPHV---PFGGVKASG 410
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
100-510 |
6.55e-55 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 191.39 E-value: 6.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 100 FDDRAAIILRAAELLAGpwRETLAASTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDHRP 179
Cdd:cd07150 42 PSERERILLKAAEIMER--RADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 180 LeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPA 258
Cdd:cd07150 120 L-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 259 LAGIHFTGSTRTFQHLWKTVGGNIEKYrsypriVGETGGKD--FVVAHPSADRAVlkTALTRGSFEFQGQKCSATSRAYI 336
Cdd:cd07150 199 VRMVTFTGSTAVGREIAEKAGRHLKKI------TLELGGKNplIVLADADLDYAV--RAAAFGAFMHQGQICMSASRIIV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 337 PASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDdsvGYFVRPTVIVC 416
Cdd:cd07150 271 EEPVYDE-FVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAK-GAKLLTGGKYD---GNFYQPTVLTD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 417 TDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKS--T 494
Cdd:cd07150 346 VTPDMRIFREETFGPVTSVIPAKDAE----EAL--ELANDTEYGLSAAILTNDLQRAFKLAERLE--SGMVHINDPTilD 417
|
410
....*....|....*.
gi 1717797354 495 GAVVgqqPFGGGRASG 510
Cdd:cd07150 418 EAHV---PFGGVKASG 430
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
104-510 |
5.79e-53 |
|
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: 186.60 E-value: 5.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 104 AAIILRAAELLAG--------PWRETLAastmlgqsktaqQAEIdtpceLVDFWRFNVAYARDLLAEQPPANSPGVWNRL 175
Cdd:cd07114 53 ADLIEANAEELAEletrdngkLIRETRA------------QVRY-----LAEWYRYYAGLADKIEGAVIPVDKGDYLNFT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVAL 254
Cdd:cd07114 116 RREPL-GVVAAITPWNSPLLLLAKKLAPALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 255 NHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRA 334
Cdd:cd07114 195 EHPLVAKIAFTGGTETGRHIARAAAENLA------PVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGG----SYDDSVGYFVR 410
Cdd:cd07114 269 LVQRSIYDE-FVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREE-GARVLTGGerpsGADLGAGYFFE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYIN 490
Cdd:cd07114 347 PTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-EAIALAND-----SEYGLAAGIWTRDLARAHRVARAIE--AGTVWVN 418
|
410 420
....*....|....*....|.
gi 1717797354 491 D-KSTGAVVgqqPFGGGRASG 510
Cdd:cd07114 419 TyRALSPSS---PFGGFKDSG 436
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
98-530 |
3.69e-52 |
|
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: 184.70 E-value: 3.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPWRET--LAASTMLGQSKTAQQAEIDTPcelVDFWRFNVAYARDLLAEQPPANSPGVWNRL 175
Cdd:cd07139 57 LSPAERAAVLRRLADALEARADELarLWTAENGMPISWSRRAQGPGP---AALLRYYAALARDFPFEERRPGSGGGHVLV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDgIAVSEVAL 254
Cdd:cd07139 134 RREPV-GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 255 NHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRA 334
Cdd:cd07139 212 RHPGVDKVSFTGSTAAGRRIAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWnSGFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSV--GYFVRPT 412
Cdd:cd07139 286 LVPRSRY-DEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAE-GARLVTGGGRPAGLdrGWFVEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 413 VIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDK 492
Cdd:cd07139 364 LFADVDNDMRIAQEEIFGPVLSVIPYDDED----DAV--RIANDSDYGLSGSVWTADVERGLAVARRIR--TGTVGVNGF 435
|
410 420 430
....*....|....*....|....*....|....*...
gi 1717797354 493 STGAVVgqqPFGGGRASGTNDKAGaPQNLMRWTLTRAI 530
Cdd:cd07139 436 RLDFGA---PFGGFKQSGIGREGG-PEGLDAYLETKSI 469
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
59-510 |
6.05e-52 |
|
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: 183.99 E-value: 6.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 59 DVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAE 138
Cdd:cd07097 17 ENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEAR-KEELARLLTREEGKTLPEAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 139 IDTpCELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIAGnLPTAPALM-GNVVVWKPSP 216
Cdd:cd07097 96 GEV-TRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPL-GVVGLITPWNFpIAIPA-WKIAPALAyGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 217 TQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYRSyprivgETG 296
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL------EMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 297 GKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDD 374
Cdd:cd07097 247 GKNPLVVLDDADldLAV--ECAVQGAFFSTGQRCTASSRLIVTEGIHDR-FVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 375 RSFAKNKAAIDRAKADPTcEIVAGGSYDDSV--GYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLDQ 452
Cdd:cd07097 324 RQLEKDLRYIEIARSEGA-KLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD-----YDEALAI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717797354 453 MESVSaYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGaVVGQQPFGGGRASG 510
Cdd:cd07097 398 ANDTE-FGLSAGIVTTSLKHATHFKRRVE--AGVVMVNLPTAG-VDYHVPFGGRKGSS 451
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
59-511 |
1.92e-51 |
|
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: 182.41 E-value: 1.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 59 DVVQPHnHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA- 137
Cdd:cd07149 2 EVISPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEER-REEFARTIALEAGKPIKDAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 138 -EIDtpcELVDFWRFNVAYARDLLAEQPPAN-SPGVWNRLDH---RPLeGFVYAITPFNF----------TAIAGnlpta 202
Cdd:cd07149 80 kEVD---RAIETLRLSAEEAKRLAGETIPFDaSPGGEGRIGFtirEPI-GVVAAITPFNFplnlvahkvgPAIAA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 203 palmGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRtfqhlwktVGGNI 282
Cdd:cd07149 151 ----GNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPA--------VGEAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 283 EKYRSYPRIVGETGGKDFVVAHPSADravLKTALTR---GSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMG 359
Cdd:cd07149 219 ARKAGLKKVTLELGSNAAVIVDADAD---LEKAVERcvsGAFANAGQVCISVQRIFVHEDIYDE-FLERFVAATKKLVVG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 360 DVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDdsvGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYE 439
Cdd:cd07149 295 DPLDEDTDVGPMISEAEAERIEEWVEEAVEG-GARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717797354 440 DespegYDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTgAVVGQQPFGGGRASGT 511
Cdd:cd07149 371 T-----LDEAIAMAND-SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
98-510 |
2.98e-51 |
|
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: 181.86 E-value: 2.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLagpwRE---TLAASTMLGQSKTAQQA--EIDTpceLVDFWRFNVAYARDLLAEQPPANSPGVW 172
Cdd:cd07103 38 TTARERAAILRRWADLI----REraeDLARLLTLEQGKPLAEArgEVDY---AASFLEWFAEEARRIYGRTIPSPAPGKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 173 NRLDHRPLeGFVYAITPFNFTAiagNLPT---APAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIA 248
Cdd:cd07103 111 ILVIKQPV-GVVAAITPWNFPA---AMITrkiAPALaAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 249 VSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQ 326
Cdd:cd07103 187 IGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGGNAPFIVFDDADldKAV--DGAIASKFRNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 327 KCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVG 406
Cdd:cd07103 259 TCVCANRIYVHESIYDE-FVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAK-GAKVLTGGKRLGLGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 407 YFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLdQMESVSAYALTGSVIANDRAAAAHTMEKLRYaaGN 486
Cdd:cd07103 337 YFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE-----DEVI-ARANDTPYGLAAYVFTRDLARAWRVAEALEA--GM 408
|
410 420
....*....|....*....|....*
gi 1717797354 487 FYINdksTGAVVG-QQPFGGGRASG 510
Cdd:cd07103 409 VGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
91-510 |
1.79e-50 |
|
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: 179.65 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 91 AAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDTpceLVDFWRFNVAYARDLLAEQppaNS 168
Cdd:cd07106 31 AFPGWSATPLEERRAALLAIADAIEAN-AEELARLLTLEQGKPLAEAqfEVGG---AVAWLRYTASLDLPDEVIE---DD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 169 PGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGD-- 245
Cdd:cd07106 104 DTRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGde 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 246 -GIAVSEvalnHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQ 324
Cdd:cd07106 182 lGPALTS----HPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 325 GQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTcEIVAGGSYDDS 404
Cdd:cd07106 252 GQVCAAIKRLYVHESIYDE-FCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGA-KVLAGGEPLDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 405 VGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaA 484
Cdd:cd07106 330 PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED----EVI--ARANDSEYGLGASVWSSDLERAEAVARRLE--A 401
|
410 420
....*....|....*....|....*.
gi 1717797354 485 GNFYINdkSTGAVVGQQPFGGGRASG 510
Cdd:cd07106 402 GTVWIN--THGALDPDAPFGGHKQSG 425
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-530 |
6.45e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 182.32 E-value: 6.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 22 SPERARLEAKLKELAENPIELPMTIGGERRMGggervDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFD 101
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIINGEGEAR-----PVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAeIDTPCELVDFWRFNVAYARDLLAEQPPANSP-GVWNRLDHRPL 180
Cdd:PRK11904 608 ERAAILERAADLLEAN-RAELIALCVREAGKTLQDA-IAEVREAVDFCRYYAAQARRLFGAPEKLPGPtGESNELRLHGR 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 EGFVyAITPFNF-TAI-AGnlPTAPALM-GNVVVWKPSPtQT----HSAVllmRLLEEAGLPKGVINLVTGDGIAVSEVA 253
Cdd:PRK11904 686 GVFV-CISPWNFpLAIfLG--QVAAALAaGNTVIAKPAE-QTpliaAEAV---KLLHEAGIPKDVLQLLPGDGATVGAAL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRTFQHLWKTVGGniekyRSYPRI--VGETGGKDFVVAHPSADR-AVLKTALTrGSFEFQGQKCSA 330
Cdd:PRK11904 759 TADPRIAGVAFTGSTETARIINRTLAA-----RDGPIVplIAETGGQNAMIVDSTALPeQVVDDVVT-SAFRSAGQRCSA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 331 TSRAYIPasiwnsgfkEEFAAEVdgIAM----------GDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTceIVAGGS 400
Cdd:PRK11904 833 LRVLFVQ---------EDIADRV--IEMlkgamaelkvGDPRLLSTDVGPVIDAEAKANLDAHIERMKREAR--LLAQLP 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 401 YDDS--VGYFVRPTVIVCTDPgnEVFTDEYFGPILAVYVYEdesPEGYDAMLDQMESvSAYALTGSVIANDRAAAAHTME 478
Cdd:PRK11904 900 LPAGteNGHFVAPTAFEIDSI--SQLEREVFGPILHVIRYK---ASDLDKVIDAINA-TGYGLTLGIHSRIEETADRIAD 973
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1717797354 479 KLRyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAI 530
Cdd:PRK11904 974 RVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
59-525 |
7.78e-49 |
|
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: 176.00 E-value: 7.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 59 DVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLA--ASTMLGQSKTAQQ 136
Cdd:cd07131 17 DSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKR-KEELArlVTREMGKPLAEGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 137 AEIDtpcELVDFWRFNVAYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNF-TAIAGNLpTAPALM-GNVVVWKP 214
Cdd:cd07131 96 GDVQ---EAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPI-GVVALITPWNFpVAIPSWK-IFPALVcGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 215 SPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGgniekyRSYPRIVGE 294
Cdd:cd07131 171 AEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 295 TGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDD 374
Cdd:cd07131 245 MGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE-FLKRFVERAKRLRVGDGLDEETDMGPLINE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 375 RSFAKNKAAIDRAK---ADPTC--EIVAGGSYDDsvGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYE--DESPEGYD 447
Cdd:cd07131 324 AQLEKVLNYNEIGKeegATLLLggERLTGGGYEK--GYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSslEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717797354 448 AmldqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAVVgQQPFGGGRASGTNDKAGAPQNLMRWT 525
Cdd:cd07131 402 D--------TEYGLSSAIYTEDVNKAFRARRDLE--AGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
98-511 |
9.67e-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: 175.06 E-value: 9.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKT-AQQAEIDTPCELVDFwRFNVAYARDLLAEQPPaNSPGVWNRLD 176
Cdd:cd07093 38 MSPAERARILHKVADLIEAR-ADELALLESLDTGKPiTLARTRDIPRAAANF-RFFADYILQLDGESYP-QDGGALNYVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNftaiagnLP-------TAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIA 248
Cdd:cd07093 115 RQPV-GVAGLITPWN-------LPlmlltwkIAPALaFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 249 VSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKYrSYprivgETGGKDFVVAHPSADR-AVLKTALtRGSFEFQGQK 327
Cdd:cd07093 187 AGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPV-SL-----ELGGKNPNIVFADADLdRAVDAAV-RSSFSNNGEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 328 CSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSV-- 405
Cdd:cd07093 260 CLAGSRILVQRSIYDE-FLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE-GATILTGGGRPELPdl 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 406 --GYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLRya 483
Cdd:cd07093 338 egGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEE-EAIELAND-----TPYGLAAYVWTRDLGRAHRVARRLE-- 409
|
410 420 430
....*....|....*....|....*....|...
gi 1717797354 484 AGNFYIN-----DKSTgavvgqqPFGGGRASGT 511
Cdd:cd07093 410 AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
102-510 |
5.49e-48 |
|
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: 173.17 E-value: 5.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAAELLAGPwRETLAASTMLGQSKT-AQQAEIDTPcELVDFWRFNvAYARDLLAEQPPANSPGVWNRLDHRPL 180
Cdd:cd07112 49 ERKAVLLRLADLIEAH-RDELALLETLDMGKPiSDALAVDVP-SAANTFRWY-AEAIDKVYGEVAPTGPDALALITREPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 eGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPAL 259
Cdd:cd07112 126 -GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 260 AGIHFTGSTRTFQHLWKTVGGNIEKyrsypRIVGETGGKD-FVVAH--PSADRAVLKTALtrGSFEFQGQKCSATSRAYI 336
Cdd:cd07112 205 DALAFTGSTEVGRRFLEYSGQSNLK-----RVWLECGGKSpNIVFAdaPDLDAAAEAAAA--GIFWNQGEVCSAGSRLLV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 337 PASIwnsgfKEEFAAEVDGIA----MGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGS--YDDSVGYFVR 410
Cdd:cd07112 278 HESI-----KDEFLEKVVAAArewkPGDPLDPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGKrvLTETGGFFVE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYIN 490
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEE----EAV--ALANDSVYGLAASVWTSDLSRAHRVARRLR--AGTVWVN 423
|
410 420
....*....|....*....|
gi 1717797354 491 DKSTGAVvgQQPFGGGRASG 510
Cdd:cd07112 424 CFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
98-525 |
7.76e-48 |
|
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: 172.09 E-value: 7.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELL------AGPW--RETLAAstmlgQSKtaqqAEIDTPCELVDFWrfnVAYArdlLAEQPP---- 165
Cdd:cd07152 32 TPPRERAAVLRRAADLLeehadeIADWivRESGSI-----RPK----AGFEVGAAIGELH---EAAG---LPTQPQgeil 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 166 ANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSP-TQTHSAVLLMRLLEEAGLPKGVINLVT 243
Cdd:cd07152 97 PSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDPrTPVSGGVVIARLFEEAGLPAGVLHVLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 244 GDGiAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVVAHPSADRAVLKTALTRGSFEF 323
Cdd:cd07152 176 GGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKK------VSLELGGKNALIVLDDADLDLAASNGAWGAFLH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 324 QGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSfAKNKAAIDRAKADPTCEIVAGGSYDd 403
Cdd:cd07152 249 QGQICMAAGRHLVHESVADA-YTAKLAAKAKHLPVGDPATGQVALGPLINARQ-LDRVHAIVDDSVAAGARLEAGGTYD- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 404 svGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegyDAMLDQMESVSAYALTGSVIANDRAAAAHTMEKLRya 483
Cdd:cd07152 326 --GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDS------DEEAVALANDTEYGLSAGIISRDVGRAMALADRLR-- 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1717797354 484 AGNFYINDKSTGAVVgQQPFGGGRASGTNDKAGAPQNLMRWT 525
Cdd:cd07152 396 TGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGPANWEEFT 436
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
98-510 |
1.72e-47 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 171.75 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDTPcelVDFWRFNVAYARDLLAEQPPANSPGVWNRL 175
Cdd:cd07118 40 MSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEGA---ADLWRYAASLARTLHGDSYNNLGDDMLGLV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLeGFVYAITPFNFTA--IAGNLPTAPAlMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVA 253
Cdd:cd07118 116 LREPI-GVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsypriVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATS 332
Cdd:cd07118 194 TEHPDVDMVSFTGSTRVGKAIAAAAARNLKK-------VSlELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 333 RAYIPASIwnsgfKEEFAAEV----DGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSVGYF 408
Cdd:cd07118 267 RLLVHESI-----ADAFVAAVvarsRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 409 VRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFY 488
Cdd:cd07118 342 YQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD----EAI--ALANDTVYGLSAGVWSKDIDTALTVARRIR--AGTVW 413
|
410 420
....*....|....*....|..
gi 1717797354 489 INDKSTGAVvgQQPFGGGRASG 510
Cdd:cd07118 414 VNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
58-510 |
2.81e-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: 171.08 E-value: 2.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 58 VDVVQPHNhRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLaGPWRETLAASTMLGQSKTAQQA 137
Cdd:cd07094 1 LDVHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLL-KKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 138 EIDTPcELVDFWRFNVAYARDLLAEQPPAN-SPGVWNRLD---HRPLeGFVYAITPFNFTAiagNLPT---APAL-MGNV 209
Cdd:cd07094 79 RVEVD-RAIDTLRLAAEEAERIRGEEIPLDaTQGSDNRLAwtiREPV-GVVLAITPFNFPL---NLVAhklAPAIaTGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 210 VVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGniekyrsyP 289
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 290 RIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIG 369
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDE-FIEAFVAAVKKLKVGDPLDEDTDVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 370 AVIDDRSFAKNKAAIDRAkADPTCEIVAGGSYDDSVgyfVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAM 449
Cdd:cd07094 305 PLISEEAAERVERWVEEA-VEAGARLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDF-----EEA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717797354 450 LDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDkSTGAVVGQQPFGGGRASG 510
Cdd:cd07094 376 IRIANS-TDYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
98-511 |
5.42e-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: 170.22 E-value: 5.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDTPCELvdfWRFNVAYARDLLAEQPPA-NSPGVWNR 174
Cdd:cd07145 40 LPAYKRYKILMKVAELIERR-KEELAKLLTIEVGKPIKQSrvEVERTIRL---FKLAAEEAKVLRGETIPVdAYEYNERR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 175 L---DHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVS 250
Cdd:cd07145 116 IaftVREPI-GVVGAITPFNFPANLFAHKIAPAIaVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 251 EVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKC 328
Cdd:cd07145 195 DEIVTNPKVNMISFTGSTAVGLLIASKAGGTGK------KVALELGGSDPMIVLKDADleRAV--SIAVRGRFENAGQVC 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 329 SATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTcEIVAGGSYDDsvGYF 408
Cdd:cd07145 267 NAVKRILVEEEVYDK-FLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGG-KILYGGKRDE--GSF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 409 VRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRYaaGNFY 488
Cdd:cd07145 343 FPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD-----EEAVEIANS-TEYGLQASVFTNDINRALKVARELEA--GGVV 414
|
410 420
....*....|....*....|...
gi 1717797354 489 INDkSTGAVVGQQPFGGGRASGT 511
Cdd:cd07145 415 IND-STRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
98-510 |
2.39e-46 |
|
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: 168.39 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGpWRETLAASTMLGQSKTAQQAE-IDTPcELVDFWRFNVAYARDLLAEQPPAnSPGVWNRLD 176
Cdd:cd07115 38 MDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARrLDVP-RAADTFRYYAGWADKIEGEVIPV-RGPFLNYTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALN 255
Cdd:cd07115 115 REPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSAD-RAVLKTALTrGSFEFQGQKCSATSRA 334
Cdd:cd07115 194 HPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFADADlDAAVRAAAT-GIFYNQGQMCTAGSRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTVI 414
Cdd:cd07115 267 LVHESIYDE-FLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE-GARLLTGGKRPGARGFFVEPTIF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 415 VCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDrAAAAHTMEKlRYAAGNFYINdkST 494
Cdd:cd07115 345 AAVPPEMRIAQEEIFGPVVSVMRFRDEE----EAL--RIANGTEYGLAAGVWTRD-LGRAHRVAA-ALKAGTVWIN--TY 414
|
410
....*....|....*.
gi 1717797354 495 GAVVGQQPFGGGRASG 510
Cdd:cd07115 415 NRFDPGSPFGGYKQSG 430
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-510 |
6.78e-46 |
|
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: 167.15 E-value: 6.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 61 VQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAgPWRETLAASTMLGQSK---TAQQA 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALE-ARSEELARLLALETGNalrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 138 EIDTpceLVDFWRFNVAYARDLLAEQPPANsPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSP 216
Cdd:cd07108 80 EAAV---LADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 217 TQTHSAVLLMRLLEEAgLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGniekyrsypRIVG--- 293
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD---------RLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 294 ETGGKDFVVAHPSAD-RAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVI 372
Cdd:cd07108 225 ELGGKSPMIVFPDADlDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDA-FLEKLVAKLSKLKIGDPLDEATDIGAII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 373 DDRSFAKNKAAIDRAKADPTCEIVAGGS----YDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDA 448
Cdd:cd07108 304 SEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDED----EV 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717797354 449 MldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINdKSTGAVVGQQpFGGGRASG 510
Cdd:cd07108 380 I--AMANDSHYGLAAYVWTRDLGRALRAAHALE--AGWVQVN-QGGGQQPGQS-YGGFKQSG 435
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
103-490 |
1.03e-45 |
|
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: 167.06 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 103 RAAIILRAAELLAGPwRETLAASTMLGQSKTAQQA--EIDTPCelvDFWRFNVAYARDLLAEQPPANSPGVWNRLDHRPL 180
Cdd:cd07088 59 RAAYLRKLADLIREN-ADELAKLIVEEQGKTLSLArvEVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 eGFVYAITPFNFTA--IAGNLptAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHP 257
Cdd:cd07088 135 -GVVAGILPWNFPFflIARKL--APALVtGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALAGIHFTGSTRTFQHLWKTVGGNIEKYRSyprivgETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRAY 335
Cdd:cd07088 212 KVGMISLTGSTEAGQKIMEAAAENITKVSL------ELGGKAPAIVMKDADldLAV--KAIVDSRIINCGQVCTCAERVY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 336 IPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDS-VGYFVRPTVI 414
Cdd:cd07088 284 VHEDIYDE-FMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEA-GATLLTGGKRPEGeKGYFYEPTVL 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717797354 415 VCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRYaaGNFYIN 490
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 ... |
98-510 |
2.14e-45 |
|
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: 166.33 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPCELVDFwRFnvaYARDLLAEQPPANS--PGVWNRL 175
Cdd:cd07119 56 LPAQERAALLFRIADKIRED-AEELARLETLNTGKTLRESEIDIDDVANCF-RY---YAGLATKETGEVYDvpPHVISRT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVAL 254
Cdd:cd07119 131 VREPV-GVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 255 NHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSAD-RAVLKTALTrGSFEFQGQKCSATSR 333
Cdd:cd07119 210 ESPDVDLVSFTGGTATGRSIMRAAAGNVK------KVALELGGKNPNIVFADADfETAVDQALN-GVFFNAGQVCSAGSR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGS-YDDSV---GYFV 409
Cdd:cd07119 283 LLVEESIHDK-FVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEE-GARLVCGGKrPTGDElakGYFV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 410 RPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYI 489
Cdd:cd07119 361 EPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE----EAI--RLANDTPYGLAGAVWTKDIARANRVARRLR--AGTVWI 432
|
410 420
....*....|....*....|.
gi 1717797354 490 NDksTGAVVGQQPFGGGRASG 510
Cdd:cd07119 433 ND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
174-525 |
7.16e-45 |
|
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: 165.04 E-value: 7.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 174 RLDHRPLE-----GFVYAITPFNF-TAIAG-NLptAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEA----GLPKGVINL 241
Cdd:cd07086 122 RPGHRLMEqwnplGVVGVITAFNFpVAVPGwNA--AIALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 242 VTGDGiAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGgniekyRSYPRIVGETGGKDFVVAHPSAD-----RAVLktal 316
Cdd:cd07086 200 VTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVA------RRFGRVLLELGGNNAIIVMDDADldlavRAVL---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 317 tRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIV 396
Cdd:cd07086 269 -FAAVGTAGQRCTTTRRLIVHESVYDE-FLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 397 AGGSY--DDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLDQMESVSaYALTGSVIANDRAAAA 474
Cdd:cd07086 346 TGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS-----LEEAIAINNDVP-QGLSSSIFTEDLREAF 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1717797354 475 HTMEKLRYAAGNFYINDKSTGAVVGqQPFGGGRASGTNDKAG--APQNLMRWT 525
Cdd:cd07086 420 RWLGPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGsdAWKQYMRRS 471
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
98-517 |
8.07e-45 |
|
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: 163.60 E-value: 8.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELL---AGPWRETLAASTmlGQSKTAQQAEIDTPCELVDFwrfNVAYARDLLAEQPPANsPGVWNR 174
Cdd:cd07095 19 LSLEERAAILRRFAELLkanKEELARLISRET--GKPLWEAQTEVAAMAGKIDI---SIKAYHERTGERATPM-AQGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 175 LDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEVA 253
Cdd:cd07095 93 LRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGR-ETGEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVG-ETGGKDFVVAHPSAD-RAVLKTALtRGSFEFQGQKCSAT 331
Cdd:cd07095 171 AAHEGIDGLLFTGSAATGLLLHRQFAGRPGK------ILAlEMGGNNPLVVWDVADiDAAAYLIV-QSAFLTAGQRCTCA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAYIPASIWNSGFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPtCEIVAGGSYDDSVGYFVRP 411
Cdd:cd07095 244 RRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALG-GEPLLAMERLVAGTAFLSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 412 TVIVCTDPGnEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYIND 491
Cdd:cd07095 323 GIIDVTDAA-DVPDEEIFGPLLQVYRYDDFD----EAI--ALANATRFGLSAGLLSDDEALFERFLARIR--AGIVNWNR 393
|
410 420
....*....|....*....|....*.
gi 1717797354 492 KSTGAvVGQQPFGGGRASGtNDKAGA 517
Cdd:cd07095 394 PTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
99-490 |
1.04e-44 |
|
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: 163.96 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIDTPCELVDFWrfnVAYARDLLAEQPPANSPGVWNRLD 176
Cdd:cd07102 38 PLEERKAIVTRAVELLAAN-TDEIAEelTWQMGRPIAQAGGEIRGMLERARYM---ISIAEEALADIRVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFN---FTAIAGnlpTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEV 252
Cdd:cd07102 114 REPL-GVVLIIAPWNypyLTAVNA---VIPALLaGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 253 ALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsypriVG-ETGGKDFVVAHPSADravLKTA---LTRGSFEFQGQKC 328
Cdd:cd07102 189 LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIK-------VGlELGGKDPAYVRPDAD---LDAAaesLVDGAFFNSGQSC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 329 SATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDS--VG 406
Cdd:cd07102 259 CSIERIYVHESIYDA-FVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEDkaGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 407 YFVRPTVIVCTDPGNEVFTDEYFGPILAVY-VYEDEspEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLryAAG 485
Cdd:cd07102 338 AYLAPTVLTNVDHSMRVMREETFGPVVGIMkVKSDA--EAIALMND-----SEYGLTASVWTKDIARAEALGEQL--ETG 408
|
....*
gi 1717797354 486 NFYIN 490
Cdd:cd07102 409 TVFMN 413
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
98-510 |
1.19e-44 |
|
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: 163.95 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPW---RETLAASTmlGQSK-TAQQAEIDTPCELVDFWrfnVAYARDLLAEQ--PPANSPGV 171
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKeelRALLVAEV--GAPVmTARAMQVDGPIGHLRYF---ADLADSFPWEFdlPVPALRGG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 172 WNR--LDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIA 248
Cdd:cd07089 114 PGRrvVRREPV-GVVAAITPWNFPFFLNLAKLAPALaAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 249 VSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKC 328
Cdd:cd07089 193 VGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK------RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGC 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 329 SATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDS--VG 406
Cdd:cd07089 267 ALTTRLLVPRSRYDE-VVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDE-GARLVTGGGRPAGldKG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 407 YFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGN 486
Cdd:cd07089 345 FYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD----EAV--RIANDSDYGLSGGVWSADVDRAYRVARRIR--TGS 416
|
410 420
....*....|....*....|....*
gi 1717797354 487 FYINdksTGAVVG-QQPFGGGRASG 510
Cdd:cd07089 417 VGIN---GGGGYGpDAPFGGYKQSG 438
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
101-511 |
3.67e-44 |
|
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: 162.54 E-value: 3.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 101 DDRAAIILRAAELLagpwRETLAASTML-----GQSKTAQQAEIDTPCELVDFWrfnVAYARDLLAEQPPAnSPGVWNRL 175
Cdd:cd07107 41 LERARMLRELATRL----REHAEELALIdaldcGNPVSAMLGDVMVAAALLDYF---AGLVTELKGETIPV-GGRNLHYT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGDGIAVSEVAL 254
Cdd:cd07107 113 LREPY-GVVARIVAFNHPLMFAAAKIAAPLAaGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 255 NHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRG-SFEFQGQKCSATSR 333
Cdd:cd07107 191 RHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSV---GYFVR 410
Cdd:cd07107 265 LFVHESIYDE-VLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPAlegGFYVE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESVSaYALTGSVIANDRAAAAHTMEKLRyaAGNFYIN 490
Cdd:cd07107 344 PTVFADVTPGMRIAREEIFGPVLSVLRWRDE-----AEMVAQANGVE-YGLTAAIWTNDISQAHRTARRVE--AGYVWIN 415
|
410 420
....*....|....*....|....
gi 1717797354 491 DKST---GAvvgqqPFGGGRASGT 511
Cdd:cd07107 416 GSSRhflGA-----PFGGVKNSGI 434
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
24-523 |
1.02e-42 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 163.96 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 24 ERARLEAKLKELAENPIE-LPMTiggERRMGGGERVDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDD 102
Cdd:COG4230 540 VLAALSAALAAAAEKQWQaAPLI---AGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEE 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 103 RAAIILRAAELLAGPwRETLAASTMLGQSKTAQ--QAEIdtpCELVDFWRFNVAYARDLLAeqppanspgvwNRLDHRPL 180
Cdd:COG4230 617 RAAILERAADLLEAH-RAELMALLVREAGKTLPdaIAEV---REAVDFCRYYAAQARRLFA-----------APTVLRGR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 eGFVYAITPFNFT-AI-AGnlPTAPALM-GNVVVWKPSPtQT----HSAVllmRLLEEAGLPKGVINLVTGDGIAVSEVA 253
Cdd:COG4230 682 -GVFVCISPWNFPlAIfTG--QVAAALAaGNTVLAKPAE-QTpliaARAV---RLLHEAGVPADVLQLLPGDGETVGAAL 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRTFQHLWKTV---GGNIekyrsyPRIVGETGGKDfvvahpsadrA--VLKTALT--------RGS 320
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLINRTLaarDGPI------VPLIAETGGQN----------AmiVDSSALPeqvvddvlASA 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 321 FEFQGQKCSATSRAYIPasiwnsgfkEEFAAEVdgIAM----------GDVTDLSNFIGAVIDDRSFAKNKAAIDRAKAD 390
Cdd:COG4230 819 FDSAGQRCSALRVLCVQ---------EDIADRV--LEMlkgamaelrvGDPADLSTDVGPVIDAEARANLEAHIERMRAE 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 391 PTceIVAGGSYDDSV--GYFVRPTVIVCTDPgnEVFTDEYFGPILAVYVYEdesPEGYDAMLDQMESvSAYALTGSV--- 465
Cdd:COG4230 888 GR--LVHQLPLPEECanGTFVAPTLIEIDSI--SDLEREVFGPVLHVVRYK---ADELDKVIDAINA-TGYGLTLGVhsr 959
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717797354 466 IandRAAAAHTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 523
Cdd:COG4230 960 I---DETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
99-530 |
2.36e-42 |
|
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: 157.38 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIDTPCELVDFWRFNvayARDLLAEQ---PPANSPGVWN 173
Cdd:cd07099 38 GVEGRAQRLLRWKRALADH-ADELAEllHAETGKPRADAGLEVLLALEAIDWAARN---APRVLAPRkvpTGLLMPNKKA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 174 RLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEv 252
Cdd:cd07099 114 TVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGA- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 253 ALNHPALAGIHFTGSTRTFQHLWKTVGgniekyRSYPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSA 330
Cdd:cd07099 191 ALIDAGVDKVAFTGSVATGRKVMAAAA------ERLIPVVLELGGKDPMIVLADADleRAA--AAAVWGAMVNAGQTCIS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 331 TSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVR 410
Cdd:cd07099 263 VERVYVHESVYDE-FVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAK-GAKALTGGARSNGGGPFYE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegydamldqmESV-----SAYALTGSVIANDRAAAAHTMEKLRyaAG 485
Cdd:cd07099 341 PTVLTDVPHDMDVMREETFGPVLPVMPVADED-----------EAIalandSRYGLSASVFSRDLARAEAIARRLE--AG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1717797354 486 NFYINDKSTGAVVGQQPFGGGRASGTNDKAGaPQNLMRWTLTRAI 530
Cdd:cd07099 408 AVSINDVLLTAGIPALPFGGVKDSGGGRRHG-AEGLREFCRPKAI 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-517 |
2.91e-42 |
|
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: 157.14 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAAELLAGPWREtlAASTM---LGQSKTAQQAEIDTPCelvDFWRFNVAYARDLLAEQPPA-NSPGVWNRL-- 175
Cdd:cd07146 41 QRSAILNKAAALLEARREE--FARLItleSGLCLKDTRYEVGRAA---DVLRFAAAEALRDDGESFSCdLTANGKARKif 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHR-PLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVA 253
Cdd:cd07146 116 TLRePL-GVVLAITPFNHPLNQVAHKIAPAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRtfqhlwktVGGNIEKYRSYPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSAT 331
Cdd:cd07146 195 ITHPDVDLVTFTGGVA--------VGKAIAATAGYKRQLLELGGNDPLIVMDDADleRAA--TLAVAGSYANSGQRCTAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDdsvGYFVRP 411
Cdd:cd07146 265 KRILVHESVADE-FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQ-GARVLLGNQRQ---GALYAP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 412 TVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRYAAGNfyIND 491
Cdd:cd07146 340 TVLDHVPPDAELVTEETFGPVAPVIRVKDLD----EAI--AISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVN--VNE 411
|
410 420
....*....|....*....|....*.
gi 1717797354 492 kSTGAVVGQQPFGGGRASGTNDKAGA 517
Cdd:cd07146 412 -VPGFRSELSPFGGVKDSGLGGKEGV 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
58-511 |
1.25e-41 |
|
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: 156.06 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 58 VDVVQPHNhRAVIGTFAGATEQDAQDAVDAALAA-APAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQ 136
Cdd:cd07113 17 LDITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQH-GEELAQLETLCSGKSIHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 137 AEIDTPCELVDFWRFNVAYARDLLAE--QPPANSPG--VWNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALM-GNVVV 211
Cdd:cd07113 95 SRAFEVGQSANFLRYFAGWATKINGEtlAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALAtGCTIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 212 WKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRI 291
Cdd:cd07113 175 IKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT------RV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 292 VGETGGKD--FVVAHPSADRAVlkTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIG 369
Cdd:cd07113 248 TLELGGKNaaAFLKDADIDWVV--EGLLTAGFLHQGQVCAAPERFYVHRSKFDE-LVTKLKQALSSFQVGSPMDESVMFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 370 AVIDDRSFAKNKAAIDRAKADPTcEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESPegydam 449
Cdd:cd07113 325 PLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE------ 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717797354 450 LDQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKS--TGAVvgqqPFGGGRASGT 511
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIE--AGTVWVNMHTflDPAV----PFGGMKQSGI 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
165-510 |
3.27e-41 |
|
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: 154.38 E-value: 3.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 165 PANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKP-SPTQTHSAVLLMRLLEEAGLPKGVINLV 242
Cdd:cd07151 116 PSDVPGKENRVYREPL-GVVGVISPWNFPLHLSMRSVAPALaLGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 243 TGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKD-FVV-AHPSADRAVLKTALtrGS 320
Cdd:cd07151 195 VGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK------KVALELGGNNpFVVlEDADIDAAVNAAVF--GK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 321 FEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGS 400
Cdd:cd07151 267 FLHQGQICMAINRIIVHEDVYDE-FVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEE-GATLLVGGE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 401 YDDSVgyfVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKL 480
Cdd:cd07151 345 AEGNV---LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE----EAL--ELANDTEYGLSGAVFTSDLERGVQFARRI 415
|
330 340 350
....*....|....*....|....*....|...
gi 1717797354 481 RyaAGNFYINDKStgavVGQQP---FGGGRASG 510
Cdd:cd07151 416 D--AGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
99-510 |
3.58e-41 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 153.77 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIDTPCELVDFwrfnvaYAR---DLLAEQPpANSPGVWN 173
Cdd:cd07100 19 SFAERAALLRKLADLLRER-KDELARliTLEMGKPIAEARAEVEKCAWICRY------YAEnaeAFLADEP-IETDAGKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 174 RLDHRPLeGFVYAITPFNFtaiagnlP-------TAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGV-INL-VT 243
Cdd:cd07100 91 YVRYEPL-GVVLGIMPWNF-------PfwqvfrfAAPNLMaGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLlID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 244 GDGIavsEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKD-FVVAhPSAD--RAVlKTAlTRGS 320
Cdd:cd07100 163 SDQV---EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKK------SVLELGGSDpFIVL-DDADldKAV-KTA-VKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 321 FEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAViddrsfAKNKAA------IDRAKADpTCE 394
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDE-FLEKFVEAMAALKVGDPMDEDTDLGPL------ARKDLRdelheqVEEAVAA-GAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 395 IVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAA 474
Cdd:cd07100 303 LLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE----EAI--ALANDSPFGLGGSVFTTDLERAE 376
|
410 420 430
....*....|....*....|....*....|....*...
gi 1717797354 475 HTMEKLRyaAGNFYIND--KSTGAVvgqqPFGGGRASG 510
Cdd:cd07100 377 RVARRLE--AGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
60-528 |
3.66e-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: 155.07 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 60 VVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAeI 139
Cdd:TIGR01238 55 VTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELH-MPELMALCVREAGKTIHNA-I 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 140 DTPCELVDFWRFNVAYARDLLAEQPpanspgvwnrldHRPLeGFVYAITPFNFT-AIAGNLPTAPALMGNVVVWKPSPTQ 218
Cdd:TIGR01238 133 AEVREAVDFCRYYAKQVRDVLGEFS------------VESR-GVFVCISPWNFPlAIFTGQISAALAAGNTVIAKPAEQT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 219 THSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGgniEKYRSYPRIVGETGGK 298
Cdd:TIGR01238 200 SLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLA---QREDAPVPLIAETGGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 299 DFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSGFKEEFAAeVDGIAMGDVTDLSNFIGAVIDDRSFA 378
Cdd:TIGR01238 277 NAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGA-MQELKVGVPHLLTTDVGPVIDAEAKQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 379 KNKAAID--RAKADPTCEIVAGGSYDDSVGYFVRPTVIVcTDPGNEVfTDEYFGPILAVYVYEDESpegYDAMLDQMESv 456
Cdd:TIGR01238 356 NLLAHIEhmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE-LDDIAEL-SEEVFGPVLHVVRYKARE---LDQIVDQINQ- 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717797354 457 SAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTR 528
Cdd:TIGR01238 430 TGYGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-523 |
1.73e-40 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 157.33 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 26 ARLEAKLKELAENPIE-LPMTiggERRMGGGERVDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRA 104
Cdd:PRK11905 539 AALDEALNAFAAKTWHaAPLL---AGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERA 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 105 AIILRAAELLagpwrE----TLAASTMLGQSKTAQQAeIDTPCELVDFWRFNVAYARDLLAEQPpanspgvwnrldHRPL 180
Cdd:PRK11905 616 AILERAADLM-----EahmpELFALAVREAGKTLANA-IAEVREAVDFLRYYAAQARRLLNGPG------------HKPL 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 eGFVYAITPFNFT-AI-AGNLptAPALM-GNVVVWKPSPtQT----HSAVllmRLLEEAGLPKGVINLVTGDGIAVSEVA 253
Cdd:PRK11905 678 -GPVVCISPWNFPlAIfTGQI--AAALVaGNTVLAKPAE-QTpliaARAV---RLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 254 LNHPALAGIHFTGSTRTFQHLWKTVggnIEKYRSYPRIVGETGGKDFVVAHPSA-----DRAVLKTAltrgsFEFQGQKC 328
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQRTL---AKRSGPPVPLIAETGGQNAMIVDSSAlpeqvVADVIASA-----FDSAGQRC 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 329 SATSRAYIpasiwnsgfKEEFAAEVdgIAM----------GDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAG 398
Cdd:PRK11905 823 SALRVLCL---------QEDVADRV--LTMlkgamdelriGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLP 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 399 GSYDDSVGYFVRPTVIVCTDPgnEVFTDEYFGPILAVYVYEdesPEGYDAMLDQMESvSAYALTG---SVIaNDRaaAAH 475
Cdd:PRK11905 892 LPAETEKGTFVAPTLIEIDSI--SDLEREVFGPVLHVVRFK---ADELDRVIDDINA-TGYGLTFglhSRI-DET--IAH 962
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1717797354 476 TMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMR 523
Cdd:PRK11905 963 VTSRIR--AGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGR 1008
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
98-510 |
1.78e-40 |
|
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: 152.75 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKT-AQQAEIDTPcELVDFWRFNVAYArDLLAEQPPANSPGVWNRLD 176
Cdd:cd07091 62 MDPRERGRLLNKLADLIERD-RDELAALESLDNGKPlEESAKGDVA-LSIKCLRYYAGWA-DKIQGKTIPIDGNFLAYTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALN 255
Cdd:cd07091 139 REPI-GVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVG-GNIEKyrsyprIVGETGGKDFVVAHPSADravLKTAL---TRGSFEFQGQKCSAT 331
Cdd:cd07091 218 HMDVDKIAFTGSTAVGRTIMEAAAkSNLKK------VTLELGGKSPNIVFDDAD---LDKAVewaAFGIFFNQGQCCCAG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKaDPTCEIVAGGSYDDSVGYFVRP 411
Cdd:cd07091 289 SRIFVQESIYDE-FVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGK-KEGATLLTGGERHGSKGYFIQP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 412 TVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDqMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINd 491
Cdd:cd07091 367 TVFTDVKDDMKIAKEEIFGPVVTILKFKTE-----DEVIE-RANDTEYGLAAGVFTKDINKALRVSRALK--AGTVWVN- 437
|
410 420
....*....|....*....|
gi 1717797354 492 ksTGAVVGQQ-PFGGGRASG 510
Cdd:cd07091 438 --TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
98-510 |
3.75e-40 |
|
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: 151.23 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPcELVDFWRFNVAYARDLLAEQPPANsPGVWNRLDH 177
Cdd:cd07109 39 LSPAERGRLLLRIARLIREH-ADELARLESLDTGKPLTQARADVE-AAARYFEYYGGAADKLHGETIPLG-PGYFVYTVR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:cd07109 116 EPH-GVTGHIIPWNYPLQITGRSVAPALaAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYI 336
Cdd:cd07109 195 PGVDHISFTGSVETGIAVMRAAAENVV------PVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 337 PASIWNSgFKEEFAAEVDGIAMG-DVTDLSnfIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGG---SYDDSVGYFVRPT 412
Cdd:cd07109 269 HRSIYDE-VLERLVERFRALRVGpGLEDPD--LGPLISAKQLDRVEGFVARARAR-GARIVAGGriaEGAPAGGYFVAPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 413 VIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDK 492
Cdd:cd07109 345 LLDDVPPDSRLAQEEIFGPVLAVMPFDDEA----EAI--ALANGTDYGLVAGVWTRDGDRALRVARRLR--AGQVFVNNY 416
|
410
....*....|....*...
gi 1717797354 493 STGAVVgQQPFGGGRASG 510
Cdd:cd07109 417 GAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
99-532 |
4.48e-40 |
|
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: 151.31 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAeIDTPCELVDFWRFNVAYARDLLAEQPPANS-PGVW-NRLD 176
Cdd:cd07101 38 PFAERAAVFLRFHDLVLER-RDELLDLIQLETGKARRHA-FEEVLDVAIVARYYARRAERLLKPRRRRGAiPVLTrTTVN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiavSEVAln 255
Cdd:cd07101 116 RRPK-GVVGVISPWNYPLTLAVSDAIPALLaGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPG---SEVG-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 hPALA----GIHFTGSTRTFQHLWKTVGgniekyrsyPRIVG---ETGGKD--FVVAHPSADRAVlkTALTRGSFEFQGQ 326
Cdd:cd07101 190 -GAIVdnadYVMFTGSTATGRVVAERAG---------RRLIGcslELGGKNpmIVLEDADLDKAA--AGAVRACFSNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 327 KCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVG 406
Cdd:cd07101 258 LCVSIERIYVHESVYDE-FVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK-GATVLAGGRARPDLG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 407 -YFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAG 485
Cdd:cd07101 336 pYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD-EAIELAND-----TDYGLNASVWTRDGARGRRIAARLR--AG 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 486 NFYIND---KSTGAVvgQQPFGGGRASGTNDKAGaPQNLMRWTLTRAIKE 532
Cdd:cd07101 408 TVNVNEgyaAAWASI--DAPMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
98-510 |
5.78e-40 |
|
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: 151.18 E-value: 5.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAgPWRETLAASTML--GQSKTAQQAEIDTPCELVdfwRFNVAYARDLLAEQppanSPGVWNRL 175
Cdd:cd07082 58 MPLEERIDCLHKFADLLK-ENKEEVANLLMWeiGKTLKDALKEVDRTIDYI---RDTIEELKRLDGDS----LPGDWFPG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 176 DHR--------PLeGFVYAITPFN------FTAIAgnlptaPAL-MGNVVVWKPsPTQTH-SAVLLMRLLEEAGLPKGVI 239
Cdd:cd07082 130 TKGkiaqvrrePL-GVVLAIGPFNyplnltVSKLI------PALiMGNTVVFKP-ATQGVlLGIPLAEAFHDAGFPKGVV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 240 NLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKtVGGNIekyrsypRIVGETGGKDFVVAHPSADravLKTALTR- 318
Cdd:cd07082 202 NVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RLVLELGGKDPAIVLPDAD---LELAAKEi 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 319 --GSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIV 396
Cdd:cd07082 271 vkGALSYSGQRCTAIKRVLVHESVADE-LVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAK-GATVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 397 AGGSYDdsVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDqMESVSAYALTGSVIANDRAAAAHT 476
Cdd:cd07082 349 NGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI-----EEAIE-LANKSNYGLQASIFTKDINKARKL 420
|
410 420 430
....*....|....*....|....*....|....*....
gi 1717797354 477 MEKLRyaAGNFYINDKStgavvgQQ-----PFGGGRASG 510
Cdd:cd07082 421 ADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
102-510 |
7.34e-40 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 150.83 E-value: 7.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLlaEQPPAN--SPGVWNRLDHRP 179
Cdd:PRK13473 62 ERAEALLKLADAIEEN-ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCL--EGKAAGeyLEGHTSMIRRDP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 180 LeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGDGIAVSEVALNHPA 258
Cdd:PRK13473 139 V-GVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 259 LAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPA 338
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADSVK------RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 339 SIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSVGYFVRPTVIVCTD 418
Cdd:PRK13473 291 GIYDD-LVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGAR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 419 PGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIAND-----RAAAahtmeklRYAAGNFYINDKS 493
Cdd:PRK13473 370 QDDEIVQREVFGPVVSVTPFDDE-----DQAVRWAND-SDYGLASSVWTRDvgrahRVSA-------RLQYGCTWVNTHF 436
|
410
....*....|....*..
gi 1717797354 494 TgaVVGQQPFGGGRASG 510
Cdd:PRK13473 437 M--LVSEMPHGGQKQSG 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
102-510 |
7.95e-40 |
|
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: 150.96 E-value: 7.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAA-------ELLA--------GPWRETLAAstmlgqsktaqqaeiDTPCElVDFWRFnvaYARDLLAEQppa 166
Cdd:cd07559 61 ERANILNKIAdrieenlELLAvaetldngKPIRETLAA---------------DIPLA-IDHFRY---FAGVIRAQE--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 167 nspGVWNRLD--------HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKG 237
Cdd:cd07559 119 ---GSLSEIDedtlsyhfHEPL-GVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 238 VINLVTGDGIAVSEVALNHPALAGIHFTGSTrtfqhlwkTVGGNIEKYRSyPRIVG---ETGGK-------DFVVAHPSA 307
Cdd:cd07559 194 VVNVVTGFGSEAGKPLASHPRIAKLAFTGST--------TVGRLIMQYAA-ENLIPvtlELGGKspniffdDAMDADDDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 308 DRAVLKTALtrgSFEF-QGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDR 386
Cdd:cd07559 265 DDKAEEGQL---GFAFnQGEVCTCPSRALVQESIYDE-FIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 387 AKADpTCEIVAGG----SYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDqMESVSAYALT 462
Cdd:cd07559 341 GKEE-GAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE-----EEAIA-IANDTEYGLG 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1717797354 463 GSVIANDRAAAAHTMEKLRyaAGNFYINdkSTGAVVGQQPFGGGRASG 510
Cdd:cd07559 414 GGVWTRDINRALRVARGIQ--TGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
154-510 |
9.51e-40 |
|
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: 150.35 E-value: 9.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 154 AYARDLLA----EQPPANSpgvwnRLDHRPLeGFVYAITPFNFTA--IAGNLptAPALM-GNVVVWKPSPTQTHSAVLLM 226
Cdd:cd07138 106 RAAADALKdfefEERRGNS-----LVVREPI-GVCGLITPWNWPLnqIVLKV--APALAaGCTVVLKPSEVAPLSAIILA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 227 RLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPS 306
Cdd:cd07138 178 EILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK------RVALELGGKSANIILDD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 307 ADravLKTALTRG---SFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAA 383
Cdd:cd07138 252 AD---LEKAVPRGvaaCFANSGQSCNAPTRMLVPRSRYAE-AEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 384 IDRAKADPTcEIVAGGSY---DDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYA 460
Cdd:cd07138 328 IQKGIEEGA-RLVAGGPGrpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED----EAI--AIANDTPYG 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 461 LTGSVIANDRAAAAHTMEKLRyaAGNFYINDkstGAVVGQQPFGGGRASG 510
Cdd:cd07138 401 LAGYVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
59-536 |
1.17e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 154.75 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 59 DVVQPHNHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPW--------RETlaastmlGQ 130
Cdd:PRK11809 662 PVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMqtlmgllvREA-------GK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 131 SKTAQQAEIDtpcELVDFWRFNVAYARDLLAEQppanspgvwnrlDHRPLeGFVYAITPFNFT-AI-AGNLPTAPAlMGN 208
Cdd:PRK11809 735 TFSNAIAEVR---EAVDFLRYYAGQVRDDFDND------------THRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGN 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 209 VVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIE-KYRS 287
Cdd:PRK11809 798 SVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRP 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 288 YPRIvGETGGKDFVVAHPSA-------DraVLKTAltrgsFEFQGQKCSATSRAYIpasiwnsgfKEEFAAEV------- 353
Cdd:PRK11809 878 IPLI-AETGGQNAMIVDSSAlteqvvaD--VLASA-----FDSAGQRCSALRVLCL---------QDDVADRTlkmlrga 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 354 -DGIAMGDVTDLSNFIGAVIDdrsfAKNKAAID------RAKADPTCEIVAGGSYDDSVGYFVRPTVIVCTDPGNevFTD 426
Cdd:PRK11809 941 mAECRMGNPDRLSTDIGPVID----AEAKANIErhiqamRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKR 1014
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 427 EYFGPILAVYVYEDespEGYDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAVVGQQPFGGG 506
Cdd:PRK11809 1015 EVFGPVLHVVRYNR---NQLDELIEQINA-SGYGLTLGVHTRIDETIAQVTGSAH--VGNLYVNRNMVGAVVGVQPFGGE 1088
|
490 500 510
....*....|....*....|....*....|...
gi 1717797354 507 RASGTNDKAGAPQNLMRWTLTR---AIKETLVA 536
Cdd:PRK11809 1089 GLSGTGPKAGGPLYLYRLLATRpedALAVTLAR 1121
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
60-510 |
1.81e-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: 149.42 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 60 VVQPHnHRAVIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEI 139
Cdd:cd07110 1 VINPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 140 DtpcelVDfwrfNVA-----YARdlLAEQPPANSP--------GVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM 206
Cdd:cd07110 79 D-----VD----DVAgcfeyYAD--LAEQLDAKAEravplpseDFKARVRREPV-GVVGLITPWNFPLLMAAWKVAPALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 207 -GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEky 285
Cdd:cd07110 147 aGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIK-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 286 rsypRIVGETGGKDFVVAHPSAD--RAVLKTALtrGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTD 363
Cdd:cd07110 225 ----PVSLELGGKSPIIVFDDADleKAVEWAMF--GCFWNNGQICSATSRLLVHESIADA-FLERLATAAEAIRVGDPLE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 364 LSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSV--GYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDE 441
Cdd:cd07110 298 EGVRLGPLVSQAQYEKVLSFIARGKEE-GARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717797354 442 SpEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINdkSTGAVVGQQPFGGGRASG 510
Cdd:cd07110 377 D-EAIALAND-----SEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
146-511 |
5.94e-39 |
|
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: 147.86 E-value: 5.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 146 VDFWRFNVAYARDLlaEQPPANS--PGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSA 222
Cdd:cd07092 85 VDNFRFFAGAARTL--EGPAAGEylPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 223 VLLMRLLEEaGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVV 302
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGKAPVI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 303 AHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKA 382
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDE-FVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 383 AIDRAKADptCEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegydamldqmESV-----S 457
Cdd:cd07092 314 FVERAPAH--ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDED-----------EAIelandV 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1717797354 458 AYALTGSVIANDRAAAAHTMEKLRYaaGNFYINDKstGAVVGQQPFGGGRASGT 511
Cdd:cd07092 381 EYGLASSVWTRDVGRAMRLSARLDF--GTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-510 |
4.42e-38 |
|
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: 145.03 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAAstmlgqsktAQQAEIDTPCELVDfwrFNVAYARDLLAE-----------QPPA 166
Cdd:cd07105 19 TPPSERRDILLKAADLLESR-RDEFIE---------AMMEETGATAAWAG---FNVDLAAGMLREaaslitqiiggSIPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 167 NSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVT-- 243
Cdd:cd07105 86 DKPGTLAMVVKEPV-GVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 244 -GDGIAVSEVALNHPALAGIHFTGSTRtfqhlwktVGgniekyrsypRIVGET------------GGKDFVVAHPSAD-- 308
Cdd:cd07105 165 pEDAPEVVEALIAHPAVRKVNFTGSTR--------VG----------RIIAETaakhlkpvllelGGKAPAIVLEDADld 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 309 RAVLKTALtrGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTdlsnfIGAVIDDRSFAKNKAAIDRAK 388
Cdd:cd07105 227 AAANAALF--GAFLNSGQICMSTERIIVHESIADE-FVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 389 ADpTCEIVAGGSYDDSV-GYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegYDAMldQMESVSAYALTGSVIA 467
Cdd:cd07105 299 SK-GAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE----EEAV--RIANDSEYGLSAAVFT 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1717797354 468 NDRAAAAHTMEKLRYaaGNFYINdkstGAVVG---QQPFGGGRASG 510
Cdd:cd07105 372 RDLARALAVAKRIES--GAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-510 |
1.14e-37 |
|
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: 144.37 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPCElVDFWRFNVAYARDLLAEQPP-ANSPGVWNRld 176
Cdd:cd07090 38 TSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVDIDSS-ADCLEYYAGLAPTLSGEHVPlPGGSFAYTR-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEVALN 255
Cdd:cd07090 114 REPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSAD--RAVlKTALTrGSFEFQGQKCSATSR 333
Cdd:cd07090 192 HPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVTLELGGKSPLIIFDDADleNAV-NGAMM-ANFLSQGQVCSNGTR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSY---DDSV--GYF 408
Cdd:cd07090 264 VFVQRSIKDE-FTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE-GAKVLCGGERvvpEDGLenGFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 409 VRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFY 488
Cdd:cd07090 342 VSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE----EVI--RRANDTTYGLAAGVFTRDLQRAHRVIAQLQ--AGTCW 413
|
410 420
....*....|....*....|..
gi 1717797354 489 INDKSTGAVvgQQPFGGGRASG 510
Cdd:cd07090 414 INTYNISPV--EVPFGGYKQSG 433
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
99-538 |
2.19e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 141.94 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAAELLAGPwRETLAAstmLGQSKT--AQQAEIDTPCELVDFWRFNVAYARDLLAeqpPANSPGVW---- 172
Cdd:PRK09407 74 PVRERAAVLLRFHDLVLEN-REELLD---LVQLETgkARRHAFEEVLDVALTARYYARRAPKLLA---PRRRAGALpvlt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 173 -NRLDHRPLeGFVYAITPFNF---TAIAGNLptaPALM-GNVVVWKPSpTQT-HSAVLLMRLLEEAGLPKGVINLVTGDG 246
Cdd:PRK09407 147 kTTELRQPK-GVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPD-SQTpLTALAAVELLYEAGLPRDLWQVVTGPG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 247 iavSEVAlnhPALA----GIHFTGSTRTFQHLWKTVGGniekyrsypRIVG---ETGGKDFVVAHPSADRAVLKTALTRG 319
Cdd:PRK09407 222 ---PVVG---TALVdnadYLMFTGSTATGRVLAEQAGR---------RLIGfslELGGKNPMIVLDDADLDKAAAGAVRA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 320 SFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGG 399
Cdd:PRK09407 287 CFSNAGQLCISIERIYVHESIYDE-FVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAK-GATVLAGG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 400 SYDDSVG-YFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTME 478
Cdd:PRK09407 365 KARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD-EAVERAND-----TPYGLNASVWTGDTARGRAIAA 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717797354 479 KLRyaAGNFYIND------KSTGAvvgqqPFGGGRASGTNDKAGApQNLMRWTLTRAIKETLVAPV 538
Cdd:PRK09407 439 RIR--AGTVNVNEgyaaawGSVDA-----PMGGMKDSGLGRRHGA-EGLLKYTESQTIATQRVLPL 496
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
177-530 |
5.30e-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: 140.36 E-value: 5.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALN 255
Cdd:cd07143 142 HEPI-GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVG-GNIEKyrsyprIVGETGGKDFVVAHPSAD--RAVLKTAltRGSFEFQGQKCSATS 332
Cdd:cd07143 221 HMDIDKVAFTGSTLVGRKVMEAAAkSNLKK------VTLELGGKSPNIVFDDADleSAVVWTA--YGIFFNHGQVCCAGS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 333 RAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPT 412
Cdd:cd07143 293 RIYVQEGIYDK-FVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAE-GATVETGGKRHGNEGYFIEPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 413 VIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDK 492
Cdd:cd07143 371 IFTDVTEDMKIVKEEIFGPVVAVIKFKTE-----EEAIKRAND-STYGLAAAVFTNNINNAIRVANALK--AGTVWVNCY 442
|
330 340 350
....*....|....*....|....*....|....*...
gi 1717797354 493 STgaVVGQQPFGGGRASGTNDKAGApQNLMRWTLTRAI 530
Cdd:cd07143 443 NL--LHHQVPFGGYKQSGIGRELGE-YALENYTQIKAV 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
119-510 |
1.09e-35 |
|
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: 139.02 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 119 RETLAASTMLGQSKTAQQA--EIDT-PCELvdfwRFNVAYARDLL--AEQPpanSPGVWNRLDHRPLeGFVYAITPFNFT 193
Cdd:cd07120 59 AERLARLLALENGKILGEArfEISGaISEL----RYYAGLARTEAgrMIEP---EPGSFSLVLREPM-GVAGIIVPWNSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 194 AIAGNLPTAPALM-GNVVVWKPSP--TQTHSAVllMRLLEEA-GLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTR 269
Cdd:cd07120 131 VVLLVRSLAPALAaGCTVVVKPAGqtAQINAAI--IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 270 TFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEF 349
Cdd:cd07120 209 TGRAIMAAAAPTLK------RLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE-VRDRL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 350 AAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDD--SVGYFVRPTVIVCTDPGNEVFTDE 427
Cdd:cd07120 282 AARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 428 YFGPILAVYVYEDESpegydamldqmESV-----SAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKstGAVVGQQP 502
Cdd:cd07120 362 IFGPVLTLETFDDEA-----------EAValandTDYGLAASVWTRDLARAMRVARAIR--AGTVWINDW--NKLFAEAE 426
|
....*...
gi 1717797354 503 FGGGRASG 510
Cdd:cd07120 427 EGGYRQSG 434
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
58-510 |
2.03e-35 |
|
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: 138.69 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 58 VDVVQPHNHRaVIGTFAGATEQDAQDAVDAALAAAPAWRAM-SFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQ 136
Cdd:cd07144 25 IKTVNPSTGE-VIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKN-RDLLAAIEALDSGKPYHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 137 AEIDTPCELVDFWRFNVAYArDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPS 215
Cdd:cd07144 103 NALGDLDEIIAVIRYYAGWA-DKIQGKTIPTSPNKLAYTLHEPY-GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 216 PTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGET 295
Cdd:cd07144 181 ENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA------VTLEC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 296 GGKD--FVVAHPSADRAVLKTALtrGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEV-DGIAMGDVTDLSNFIGAVI 372
Cdd:cd07144 255 GGKSpaLVFEDADLDQAVKWAAA--GIMYNSGQNCTATSRIYVQESIYDK-FVEKFVEHVkQNYKVGSPFDDDTVVGPQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 373 DDRSFAKNKAAIDRAKADpTCEIVAGGS---YDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAM 449
Cdd:cd07144 332 SKTQYDRVLSYIEKGKKE-GAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE----EAI 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717797354 450 ldQMESVSAYALTGSVIANDrAAAAHTMEKlRYAAGNFYINDKSTGAVvgQQPFGGGRASG 510
Cdd:cd07144 407 --KKANDTTYGLAAAVFTKD-IRRAHRVAR-ELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
177-510 |
2.20e-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: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGDGIAVSEVALN 255
Cdd:cd07117 134 REPI-GVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVGGNIekyrsYPRIVgETGGKDFVVAHPSA--DRAVLKTALtrGSFEFQGQKCSATSR 333
Cdd:cd07117 212 HPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANIIFDDAnwDKALEGAQL--GILFNQGQVCCAGSR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGG----SYDDSVGYFV 409
Cdd:cd07117 284 IFVQEGIYDE-FVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEE-GAKILTGGhrltENGLDKGFFI 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 410 RPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDqMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYI 489
Cdd:cd07117 362 EPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE-----DEVID-MANDSEYGLGGGVFTKDINRALRVARAVE--TGRVWV 433
|
330 340
....*....|....*....|.
gi 1717797354 490 NdkSTGAVVGQQPFGGGRASG 510
Cdd:cd07117 434 N--TYNQIPAGAPFGGYKKSG 452
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
175-517 |
6.80e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 134.32 E-value: 6.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 175 LDHRPLeGFVYAITPFNFtaiAGNLPTA---PALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGD---GI 247
Cdd:PRK09457 130 LRHRPH-GVVAVFGPYNF---PGHLPNGhivPALLaGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGretGK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 248 AVSevalNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQ 326
Cdd:PRK09457 206 ALA----AHPDIDGLLFTGSANTGYLLHRQFAGQPEK------ILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 327 KCSATSRAYIPASIWNSGFKEEFAAEVDGIAMGDV-TDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSV 405
Cdd:PRK09457 276 RCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 406 GyFVRPTVIVCTDPgNEVFTDEYFGPILAVYVYEDespegYDAMLDQMESvSAYALTGSVIANDRAAAAHTMEKLRyaAG 485
Cdd:PRK09457 356 G-LLTPGIIDVTGV-AELPDEEYFGPLLQVVRYDD-----FDEAIRLANN-TRFGLSAGLLSDDREDYDQFLLEIR--AG 425
|
330 340 350
....*....|....*....|....*....|..
gi 1717797354 486 NFYINDKSTGAvVGQQPFGGGRASGtNDKAGA 517
Cdd:PRK09457 426 IVNWNKPLTGA-SSAAPFGGVGASG-NHRPSA 455
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
102-435 |
1.22e-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: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 102 DRAAIILRAAELLAGPWREtLAASTMLGQSKTAQQA--EIDTPCELVDFwrfNVAYARDLLAEQPPANSPGVWNRLDHRP 179
Cdd:cd07085 61 KRQQVMFKFRQLLEENLDE-LARLITLEHGKTLADArgDVLRGLEVVEF---ACSIPHLLKGEYLENVARGIDTYSYRQP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 180 LeGFVYAITPFNFTAIAGN--LPTAPALmGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVaLNHP 257
Cdd:cd07085 137 L-GVVAGITPFNFPAMIPLwmFPMAIAC-GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNAL-LDHP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALAGIHFTGSTRTFQHLWKTvGGNIEKyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIP 337
Cdd:cd07085 214 DIKAVSFVGSTPVGEYIYER-AAANGK-----RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 338 ASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGG------SYDDsvGYFVRP 411
Cdd:cd07085 288 GDEADE-WIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEE-GAKLVLDGrgvkvpGYEN--GNFVGP 363
|
330 340
....*....|....*....|....
gi 1717797354 412 TVIVCTDPGNEVFTDEYFGPILAV 435
Cdd:cd07085 364 TILDNVTPDMKIYKEEIFGPVLSI 387
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
98-517 |
2.65e-33 |
|
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: 132.62 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPwRETLAASTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLLAEQPPANSPGVWNRLdH 177
Cdd:cd07142 62 MTGYERSRILLRFADLLEKH-ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTL-H 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:cd07142 140 EPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLWKTVG-GNIEKyrsyprIVGETGGKDFVVAHPSA--DRAVLKTALtrGSFEFQGQKCSATSR 333
Cdd:cd07142 219 MDVDKVAFTGSTEVGKIIMQLAAkSNLKP------VTLELGGKSPFIVCEDAdvDKAVELAHF--ALFFNQGQCCCAGSR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKaDPTCEIVAGGSYDDSVGYFVRPTV 413
Cdd:cd07142 291 TFVHESIYDE-FVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGK-EEGATLITGGDRIGSKGYYIQPTI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLdQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYIN--D 491
Cdd:cd07142 369 FSDVKDDMKIARDEIFGPVQSILKFKT-----VDEVI-KRANNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVNcyD 440
|
410 420
....*....|....*....|....*.
gi 1717797354 492 KSTGAVvgqqPFGGGRASGTNDKAGA 517
Cdd:cd07142 441 VFDASI----PFGGYKMSGIGREKGI 462
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
182-510 |
1.86e-32 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 130.62 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALA 260
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 261 GIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVVAHPSAD--RAVLKTALtrGSFEFQGQKCSATSRAYIPA 338
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMVKP------VSLELGGKSPIIVFDDVDldKAVEWAMF--GCFWTNGQICSATSRLLVHE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 339 SIwNSGFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTcEIVAGGSYDD--SVGYFVRPTVIVC 416
Cdd:PLN02467 305 RI-ASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGA-TILCGGKRPEhlKKGFFIEPTIITD 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 417 TDPGNEVFTDEYFGPILAVYVYEDEsPEGYDAMLDqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINdkSTGA 496
Cdd:PLN02467 383 VTTSMQIWREEVFGPVLCVKTFSTE-DEAIELAND-----SHYGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQP 452
|
330
....*....|....
gi 1717797354 497 VVGQQPFGGGRASG 510
Cdd:PLN02467 453 CFCQAPWGGIKRSG 466
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
182-510 |
6.10e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 128.86 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALA 260
Cdd:PRK09847 159 GVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDID 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 261 GIHFTGSTRTFQHLWKTVGGNIEKyrsypRIVGETGGK--DFVVAH-PSADRAVLKTAltRGSFEFQGQKCSATSRAYIP 337
Cdd:PRK09847 239 AIAFTGSTRTGKQLLKDAGDSNMK-----RVWLEAGGKsaNIVFADcPDLQQAASATA--AGIFYNQGQVCIAGTRLLLE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 338 ASIwnsgfKEEFAAEVDGIAM----GDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTceIVAGGSYDDSVGYfVRPTV 413
Cdd:PRK09847 312 ESI-----ADEFLALLKQQAQnwqpGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQ--LLLDGRNAGLAAA-IGPTI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDrAAAAHTMEKlRYAAGNFYINDKS 493
Cdd:PRK09847 384 FVDVDPNASLSREEIFGPVLVVTRFTSEE----QAL--QLANDSQYGLGAAVWTRD-LSRAHRMSR-RLKAGSVFVNNYN 455
|
330
....*....|....*..
gi 1717797354 494 TGAVVgqQPFGGGRASG 510
Cdd:PRK09847 456 DGDMT--VPFGGYKQSG 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
120-510 |
1.62e-31 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 126.00 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 120 ETLAASTMLGQSKTAQQAEIDTPCElVDFWRFNVAYARDLLAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFT--AIAG 197
Cdd:PRK10090 13 SEISALIVEEGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRAL-GVTTGILPWNFPffLIAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 198 NLptAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWK 276
Cdd:PRK10090 91 KM--APALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 277 TVGGNIEKyrsyprIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGI 356
Cdd:PRK10090 169 AAAKNITK------VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ-FVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 357 AMGDVTDLSNF-IGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAV 435
Cdd:PRK10090 242 QFGNPAERNDIaMGPLINAAALERVEQKVARAVEE-GARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717797354 436 YVYE--DESPEgydamldqMESVSAYALTGSVIANDRAAAAHTMEKLRYaaGNFYINDKSTGAVvgqQPFGGG-RASG 510
Cdd:PRK10090 321 VAFDtlEEAIA--------MANDSDYGLTSSIYTQNLNVAMKAIKGLKF--GETYINRENFEAM---QGFHAGwRKSG 385
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
182-510 |
4.39e-31 |
|
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: 125.82 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAiagNL---PTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDgIAVSEVALNHP 257
Cdd:cd07147 125 GPVSAITPFNFPL---NLvahKVAPAIaAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALAGIHFTGStrtfqhlwKTVGGNIEKYRSYPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIP 337
Cdd:cd07147 201 RIKLLSFTGS--------PAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 338 ASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAkADPTCEIVAGGSYDDSVgyfVRPTVIVCT 417
Cdd:cd07147 273 RSVYDE-FKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEA-VDAGAKLLTGGKRDGAL---LEPTILEDV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 418 DPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAv 497
Cdd:cd07147 348 PPDMEVNCEEVFGPVVTVEPYDDFD----EAL--AAVNDSKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR- 418
|
330
....*....|...
gi 1717797354 498 VGQQPFGGGRASG 510
Cdd:cd07147 419 VDHMPYGGVKDSG 431
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
177-511 |
2.87e-30 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 123.61 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALN 255
Cdd:cd07141 143 HEPV-GVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAY 335
Cdd:cd07141 222 HPDIDKVAFTGSTEVGKLIQQAAGKSNLK-----RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTF 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 336 IPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTVIV 415
Cdd:cd07141 297 VQESIYDE-FVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKE-GAKLECGGKRHGDKGYFIQPTVFS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 416 CTDPGNEVFTDEYFGPILAVYVYEDespegydamldqMESV------SAYALTGSVIANDRAAAAHTMEKLRyaAGNFYI 489
Cdd:cd07141 375 DVTDDMRIAKEEIFGPVQQIFKFKT------------IDEVierannTTYGLAAAVFTKDIDKAITFSNALR--AGTVWV 440
|
330 340
....*....|....*....|..
gi 1717797354 490 NdkSTGAVVGQQPFGGGRASGT 511
Cdd:cd07141 441 N--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
174-441 |
4.49e-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: 123.09 E-value: 4.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 174 RLDHRPLE-----GFVYAITPFNF-TAIAG-NlpTAPALM-GNVVVWKPSPTQTHSAVLLMRL----LEEAGLPKGVINL 241
Cdd:cd07130 121 RPGHRMMEqwnplGVVGVITAFNFpVAVWGwN--AAIALVcGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 242 VTGDGiAVSEVALNHPALAGIHFTGSTRTFQHlwktVGGNIEKYrsYPRIVGETGGKDFVVAHPSAD-----RAVLKTAL 316
Cdd:cd07130 199 VCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQ----VGQAVAAR--FGRSLLELGGNNAIIVMEDADldlavRAVLFAAV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 317 trGSfefQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTcEIV 396
Cdd:cd07130 272 --GT---AGQRCTTTRRLIVHESIYDE-VLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVL 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1717797354 397 AGGSYDDSVGYFVRPTvIVCTDPGNEVFTDEYFGPILAVYVYEDE 441
Cdd:cd07130 345 FGGKVIDGPGNYVEPT-IVEGLSDAPIVKEETFAPILYVLKFDTL 388
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
69-510 |
1.27e-29 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 121.38 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 69 VIGTFAGATEQDAQDAVDAALAAAPAWRAMSFDDRAAIILRAAELLAGPwRETLAA--STMLGQSKTAQQAEIdTPCelV 146
Cdd:PRK09406 13 TVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAE-ADQVAAlmTLEMGKTLASAKAEA-LKC--A 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 147 DFWRFNVAYARDLLAEQP--PANSPGVWNRLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAV 223
Cdd:PRK09406 89 KGFRYYAEHAEALLADEPadAAAVGASRAYVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHASNVPQTAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 224 LLMRLLEEAGLPKGVI-NLVTGDGiAVsEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVV 302
Cdd:PRK09406 168 YLADLFRRAGFPDGCFqTLLVGSG-AV-EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKK------TVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 303 AHPSAD--RAVlKTALTrGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKN 380
Cdd:PRK09406 240 VMPSADldRAA-ETAVT-ARVQNNGQSCIAAKRFIVHADVYDA-FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 381 KAAIDRAkADPTCEIVAGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLdQMESVSAYA 460
Cdd:PRK09406 317 EKQVDDA-VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD-----IDEAI-EIANATTFG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 461 LTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGavVGQQPFGGGRASG 510
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLE--AGQVFINGMTVS--YPELPFGGVKRSG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
177-510 |
1.78e-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: 121.35 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVAlN 255
Cdd:cd07111 145 WKPV-GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALA-N 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRTFQHLWKTVGGniekyrSYPRIVGETGGKDFVVAHPSA--DRAVlkTALTRGSFEFQGQKCSATSR 333
Cdd:cd07111 223 HPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKSPFIVFDDAdlDSAV--EGIVDAIWFNQGQVCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSvGYFVRPTV 413
Cdd:cd07111 295 LLVQESVAEE-LIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYE--DESPEgydamldqMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINd 491
Cdd:cd07111 373 FTNVPPASRIAQEEIFGPVLVVLTFRtaKEAVA--------LANNTPYGLAASVWSENLSLALEVALSLK--AGVVWIN- 441
|
330
....*....|....*....
gi 1717797354 492 kSTGAVVGQQPFGGGRASG 510
Cdd:cd07111 442 -GHNLFDAAAGFGGYRESG 459
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
182-511 |
8.49e-29 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 119.80 E-value: 8.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALA 260
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 261 GIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASI 340
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 341 WNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTVIVCTDPG 420
Cdd:PLN02278 316 YDK-FAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSK-GAKVLLGGKRHSLGGTFYEPTVLGDVTED 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 421 NEVFTDEYFGPILAVYVYEDESpegyDAMLdqMESVSAYALTGSVIANDRAAAAHTMEKLRYaaGNFYINDKSTGAVVGq 500
Cdd:PLN02278 394 MLIFREEVFGPVAPLTRFKTEE----EAIA--IANDTEAGLAAYIFTRDLQRAWRVSEALEY--GIVGVNEGLISTEVA- 464
|
330
....*....|.
gi 1717797354 501 qPFGGGRASGT 511
Cdd:PLN02278 465 -PFGGVKQSGL 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
98-516 |
7.74e-28 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 117.22 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPWRETLAASTMLGQSKTAQQAEIDTPCeLVDFWRFNVAYARDLLAEQPPANSPGVWNRLdH 177
Cdd:PLN02466 116 MTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPM-FARLFRYYAGWADKIHGLTVPADGPHHVQTL-H 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 178 RPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:PLN02466 194 EPI-GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTfqhlWKTVGGNIEKYRSYPrIVGETGGKD-FVVAHPS-ADRAV--LKTALtrgsFEFQGQKCSATS 332
Cdd:PLN02466 273 MDVDKLAFTGSTDT----GKIVLELAAKSNLKP-VTLELGGKSpFIVCEDAdVDKAVelAHFAL----FFNQGQCCCAGS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 333 RAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIdRAKADPTCEIVAGGSYDDSVGYFVRPT 412
Cdd:PLN02466 344 RTFVHERVYDE-FVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI-KSGVESGATLECGGDRFGSKGYYIQPT 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 413 VIVCTDPGNEVFTDEYFGPILAVYVYEDespegydamLD---QMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYI 489
Cdd:PLN02466 422 VFSNVQDDMLIAQDEIFGPVQSILKFKD---------LDeviRRANNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWV 490
|
410 420
....*....|....*....|....*....
gi 1717797354 490 N--DKSTGAVvgqqPFGGGRASGTNDKAG 516
Cdd:PLN02466 491 NcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
202-510 |
1.56e-27 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 115.75 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 202 APAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGiAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGG 280
Cdd:PRK13252 164 APALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 281 niekyrSYPRIVGETGGKDFVVAHPSAD--RAVlkTALTRGSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAM 358
Cdd:PRK13252 243 ------SLKEVTMELGGKSPLIVFDDADldRAA--DIAMLANFYSSGQVCTNGTRVFVQKSIKAA-FEARLLERVERIRI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 359 GDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSY----DDSVGYFVRPTVIV-CTDpGNEVFTDEYFGPIL 433
Cdd:PRK13252 314 GDPMDPATNFGPLVSFAHRDKVLGYIEKGKAE-GARLLCGGERltegGFANGAFVAPTVFTdCTD-DMTIVREEIFGPVM 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 434 AVYVYEDEspegydamldqmESV------SAYALTGSVIANDRAAA---AHTMEklryaAGNFYINdkSTGAVVGQQPFG 504
Cdd:PRK13252 392 SVLTFDDE------------DEViarandTEYGLAAGVFTADLSRAhrvIHQLE-----AGICWIN--TWGESPAEMPVG 452
|
....*.
gi 1717797354 505 GGRASG 510
Cdd:PRK13252 453 GYKQSG 458
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
182-510 |
6.67e-27 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 113.85 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALNHPALA 260
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 261 GIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVVAHPSAD-RAVLKTALTrGSFEFQGQKCSATSRAYIPAS 339
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADlDKAVEGALA-SKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 340 IWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAkADPTCEIVAGGSYDDSVGYFVRPTVIVCTDP 419
Cdd:PRK11241 301 VYDR-FAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA-LEKGARVVCGGKAHELGGNFFQPTILVDVPA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 420 GNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRYaaGNFYINdksTGAVVG 499
Cdd:PRK11241 379 NAKVAKEETFGPLAPLFRFKDEA----DVI--AQANDTEFGLAAYFYARDLSRVFRVGEALEY--GIVGIN---TGIISN 447
|
330
....*....|..
gi 1717797354 500 Q-QPFGGGRASG 510
Cdd:PRK11241 448 EvAPFGGIKASG 459
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-530 |
1.04e-26 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 112.72 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 103 RAAIILRAAELLAgPWRETLAASTMLGQSKTAQQA-EIDTPcELVDFWRFNVAYARDLlaEQPPANSPGVWNRLD-HRPL 180
Cdd:cd07084 23 RADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAeNICGD-QVQLRARAFVIYSYRI--PHEPGNHLGQGLKQQsHGYR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 181 --EGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAG-LPKGVINLVTGDGIAVSEVALnH 256
Cdd:cd07084 99 wpYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQALLL-H 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGSTRTFQHLwktvggniekyRSYP---RIVGETGGKDFVVAHPSADR-AVLKTALTRGSFEFQGQKCSATS 332
Cdd:cd07084 178 PNPKMVLFTGSSRVAEKL-----------ALDAkqaRIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 333 RAYIPASIWNSGFKEEFAAEVDGIAMGDVTdlsnfIGAVIDDRSFAK--NKAAIDRAKADPTCEIVAGGSYDDSVGYFVR 410
Cdd:cd07084 247 MLFVPENWSKTPLVEKLKALLARRKLEDLL-----LGPVQTFTTLAMiaHMENLLGSVLLFSGKELKNHSIPSIYGACVA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGN---EVFTDEYFGPILAVYVYEDESPEGYDAMLDQMESvsayALTGSVIANDRAAAAHTMEKLRYAAGNF 487
Cdd:cd07084 322 SALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG----SLTAAIYSNDPIFLQELIGNLWVAGRTY 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1717797354 488 YINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAI 530
Cdd:cd07084 398 AILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
99-441 |
1.49e-25 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 109.85 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 99 SFDDRAAIILRAA-------ELLA--------GPWRETLAAstmlgqsktaqqaeiDTPCElVDFWRFnvaYARDLLAEQ 163
Cdd:cd07116 58 SVAERANILNKIAdrmeanlEMLAvaetwdngKPVRETLAA---------------DIPLA-IDHFRY---FAGCIRAQE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 164 ppanspGVWNRLD--------HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgL 234
Cdd:cd07116 119 ------GSISEIDentvayhfHEPL-GVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQTPASILVLMELIGDL-L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 235 PKGVINLVTGDGIAVSEVALNHPALAGIHFTGSTrtfqhlwkTVGGNIEKYRSYPRI--VGETGGKD---FVVAHPSADR 309
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGET--------TTGRLIMQYASENIIpvTLELGGKSpniFFADVMDADD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 310 AVLKTALtRGSFEF---QGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDR 386
Cdd:cd07116 263 AFFDKAL-EGFVMFalnQGEVCTCPSRALIQESIYDR-FMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDI 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717797354 387 AKADpTCEIVAGG----SYDDSVGYFVRPTVIVctdPGNE--VFTDEYFGPILAVYVYEDE 441
Cdd:cd07116 341 GKEE-GAEVLTGGerneLGGLLGGGYYVPTTFK---GGNKmrIFQEEIFGPVLAVTTFKDE 397
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
120-532 |
2.49e-25 |
|
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: 108.93 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 120 ETLAASTMLGQSKT---AQQAEIDTPCELVdfwRFNVAYARDLLAEQPPANSPGVW---NRLDHRPLeGFVYAITPFN-- 191
Cdd:cd07098 58 EEICRVACRDTGKTmvdASLGEILVTCEKI---RWTLKHGEKALRPESRPGGLLMFykrARVEYEPL-GVVGAIVSWNyp 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 192 FTAIAGnlPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEA----GLPKGVINLVTGDGiAVSEVALNHPALAGIHFTG 266
Cdd:cd07098 134 FHNLLG--PIIAALFaGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 267 StrtfqhlwKTVGGNIEKYRS---YPRIVgETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPASIWNS 343
Cdd:cd07098 211 S--------PPVGKKVMAAAAeslTPVVL-ELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 344 gFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAI-DRAKADPTCeiVAGGSY----DDSVGYFVRPTVIVCTD 418
Cdd:cd07098 282 -LLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVaDAVEKGARL--LAGGKRyphpEYPQGHYFPPTLLVDVT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 419 PGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAVV 498
Cdd:cd07098 359 PDMKIAQEEVFGPVMVVMKASDDE----EAV--EIANSTEYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYV 430
|
410 420 430
....*....|....*....|....*....|....
gi 1717797354 499 GQQPFGGGRASGTnDKAGAPQNLMRWTLTRAIKE 532
Cdd:cd07098 431 QQLPFGGVKGSGF-GRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
162-511 |
4.38e-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: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 162 EQPPANSPGVWN---RLDHRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKG 237
Cdd:cd07135 88 EKVKDGPLAFMFgkpRIRKEPL-GVVLIIGPWNYPVLLALSPLVGAIAaGCTVVLKPSELTPHTAALLAELVPKY-LDPD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 238 VINLVTGdGIAVSEVALNHPaLAGIHFTGSTRtfqhlwktVGgniekyrsypRIVG------------ETGGKDFVVAHP 305
Cdd:cd07135 166 AFQVVQG-GVPETTALLEQK-FDKIFYTGSGR--------VG----------RIIAeaaakhltpvtlELGGKSPVIVTK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 306 SADravLKTALTR---GSFEFQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFiGAVIDDRSFAKNKA 382
Cdd:cd07135 226 NAD---LELAAKRilwGKFGNAGQICVAPDYVLVDPSVYDE-FVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 383 AIDRAKADptceIVAGGSYDDSVgYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESVSaYALT 462
Cdd:cd07135 301 LLDTTKGK----VVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL-----DEAIKVINSRD-TPLA 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1717797354 463 GSVIANDRAAAAHTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASGT 511
Cdd:cd07135 370 LYIFTDDKSEIDHILTRTR--SGGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
175-510 |
4.63e-25 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 108.02 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 175 LDHRPLeGFVYAITPFNF---TAIAGNLPTApaLMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSE 251
Cdd:PRK13968 122 IEYRPL-GTILAIMPWNFplwQVMRGAVPIL--LAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 252 vALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKD--FVVAHPSADRAVlKTALTrGSFEFQGQKCS 329
Cdd:PRK13968 199 -MINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDpfIVLNDADLELAV-KAAVA-GRYQNTGQVCA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 330 ATSRAYIPASIwNSGFKEEFAAEVDGIAMGDVTDLSNFIG--AVIDDRSFAKNKAaidRAKADPTCEIVAGGSYDDSVGY 407
Cdd:PRK13968 270 AAKRFIIEEGI-ASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQV---EATLAEGARLLLGGEKIAGAGN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 408 FVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegyDAMldQMESVSAYALTGSVIANDRAAAAHTMEKLRyaAGNF 487
Cdd:PRK13968 346 YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAE----HAL--ELANDSEFGLSATIFTTDETQARQMAARLE--CGGV 417
|
330 340
....*....|....*....|...
gi 1717797354 488 YINDKStgAVVGQQPFGGGRASG 510
Cdd:PRK13968 418 FINGYC--ASDARVAFGGVKKSG 438
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
98-530 |
3.71e-24 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 105.66 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 98 MSFDDRAAIILRAAELLAGPWRE-------------TLAASTMLGQSktaqqaeidtpcelVDFWRFNVAYARDLLAEQP 164
Cdd:cd07140 64 MNARDRGRLMYRLADLMEEHQEElatiesldsgavyTLALKTHVGMS--------------IQTFRYFAGWCDKIQGKTI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 165 PANsPGVWNR---LDHRPLEGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVIN 240
Cdd:cd07140 130 PIN-QARPNRnltLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVIN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 241 LVTGDGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVG-GNIEKyrsyprIVGETGGKD--FVVAHPSADRAVlKTALT 317
Cdd:cd07140 209 ILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKK------VSLELGGKSplIIFADCDMDKAV-RMGMS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 318 RGSFEfQGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVA 397
Cdd:cd07140 282 SVFFN-KGENCIAAGRLFVEESIHDE-FVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKE-GATLVY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 398 GGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESPEGydamLDQMESVSAYALTGSVIANDRAAAAHTM 477
Cdd:cd07140 359 GGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDG----VLQRANDTEYGLASGVFTKDINKALYVS 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1717797354 478 EKLRyaAGNFYINDKSTGAVVGqqPFGGGRASGTNDKAGApQNLMRWTLTRAI 530
Cdd:cd07140 435 DKLE--AGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLGE-EALNEYLKTKTV 482
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
182-512 |
6.33e-24 |
|
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: 104.81 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAiagNL---PTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDgIAVSEVALNHP 257
Cdd:cd07148 126 GVVVAISAFNHPL---NLivhQVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALAGIHFTGSTRTFQHLwktvggnieKYRSYP--RIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAY 335
Cdd:cd07148 202 RVAFFSFIGSARVGWML---------RSKLAPgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 336 IPASIwNSGFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAkADPTCEIVAGGSYDDSVGYfvRPTVIV 415
Cdd:cd07148 273 VPAEI-ADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEA-VAAGARLLCGGKRLSDTTY--APTVLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 416 CTDPGNEVFTDEYFGPILAVYVYEDespegYDAMLDQMESVSaYALTGSVIANDRAAAAHTMEKLryAAGNFYINDKsTG 495
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDD-----LDEAIAQANSLP-VAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TA 419
|
330
....*....|....*..
gi 1717797354 496 AVVGQQPFGGGRASGTN 512
Cdd:cd07148 420 FRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
177-510 |
5.10e-20 |
|
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: 92.59 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNF---TAIAgnlPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGDGiAVSEV 252
Cdd:cd07087 98 PEPL-GVVLIIGPWNYplqLALA---PLIGAIAaGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGV-EVATA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 253 ALNHPaLAGIHFTGSTRtfqhlwktVGgniekyrsypRIVG------------ETGGKDFVVAHPSADravLKTALTR-- 318
Cdd:cd07087 172 LLAEP-FDHIFFTGSPA--------VG----------KIVMeaaakhltpvtlELGGKSPCIVDKDAN---LEVAARRia 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 319 -GSFEFQGQKCSATSRAYIPASIwnsgfKEEFAAE-VDGIA--MGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKadptce 394
Cdd:cd07087 230 wGKFLNAGQTCIAPDYVLVHESI-----KDELIEElKKAIKefYGEDPKESPDYGRIINERHFDRLASLLDDGK------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 395 IVAGGSYDDSvGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESVSAyALTGSVIANDRAAAA 474
Cdd:cd07087 299 VVIGGQVDKE-ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDL-----DEAIEFINSRPK-PLALYLFSEDKAVQE 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 1717797354 475 HTMEKLRyaAGNFYINDKSTGAVVGQQPFGGGRASG 510
Cdd:cd07087 372 RVLAETS--SGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
177-510 |
2.05e-19 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 91.42 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 177 HRPLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSEVALN 255
Cdd:PLN02766 156 KEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIAS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HPALAGIHFTGSTRtfqhlwktVGGNIEKY--RSYPRIVG-ETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATS 332
Cdd:PLN02766 235 HMDVDKVSFTGSTE--------VGRKIMQAaaTSNLKQVSlELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASS 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 333 RAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPT 412
Cdd:PLN02766 307 RVYVQEGIYDE-FVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKRE-GATLLTGGKPCGDKGYYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 413 VIVCTDPGNEVFTDEYFGPILAVYVYE--DESPEGYDAmldqmesvSAYALTGSVIANDRAAAAHTMEKLRyaAGNFYIN 490
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKFKtvEEAIKKANN--------TKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVN 454
|
330 340
....*....|....*....|
gi 1717797354 491 dkSTGAVVGQQPFGGGRASG 510
Cdd:PLN02766 455 --CYFAFDPDCPFGGYKMSG 472
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-510 |
4.84e-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: 89.59 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 164 PPANSPGVWNRLDHRPlEGFVYAITPFNF---TAIAgnlPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVi 239
Cdd:cd07134 85 TPLLLFGTKSKIRYEP-KGVCLIISPWNYpfnLAFG---PLVSAIAaGNTAILKPSELTPHTSAVIAKIIREAFDEDEV- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 240 NLVTGDgIAVSEVALNHPaLAGIHFTGSTRtfqhlwktVGgniekyrsypRIVG------------ETGGKDFVVAHPSA 307
Cdd:cd07134 160 AVFEGD-AEVAQALLELP-FDHIFFTGSPA--------VG----------KIVMaaaakhlasvtlELGGKSPTIVDETA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 308 DravLKTA---LTRGSFEFQGQKCSATSRAYIPASIwNSGFKEEFAAEVDGIAMGDVTDLSNF-IGAVIDDRSFAKNKAA 383
Cdd:cd07134 220 D---LKKAakkIAWGKFLNAGQTCIAPDYVFVHESV-KDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 384 IDRAKADpTCEIVAGGSYDDSvGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegydamLDQ-MESVSAYA-- 460
Cdd:cd07134 296 LDDAVAK-GAKVEFGGQFDAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYED---------LDEvIEYINAKPkp 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 461 LTGSVIANDRAAAAHTMEklRYAAGNFYINDKSTGAVVGQQPFGGGRASG 510
Cdd:cd07134 365 LALYVFSKDKANVNKVLA--RTSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
179-510 |
2.04e-18 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 88.16 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 179 PLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGdGIAVSEVALNHP 257
Cdd:PTZ00381 109 PL-GVVLVIGAWNYPLNLTLIPLAGAIAaGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 aLAGIHFTGSTRtfqhlwktVGGNIEKYRS---YPRIVgETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRA 334
Cdd:PTZ00381 186 -FDHIFFTGSPR--------VGKLVMQAAAenlTPCTL-ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 335 YIPASIwNSGFKEEFAAEVDGIaMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADptceIVAGGSYDDSVGYfVRPTVI 414
Cdd:PTZ00381 256 LVHRSI-KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK----VVYGGEVDIENKY-VAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 415 VCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLDQMESVSAyALTGSVIANDRAAAAHTMEKLryAAGNFYINDKST 494
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENI-----DEVLEFINSRPK-PLALYYFGEDKRHKELVLENT--SSGAVVINDCVF 400
|
330
....*....|....*.
gi 1717797354 495 GAVVGQQPFGGGRASG 510
Cdd:PTZ00381 401 HLLNPNLPFGGVGNSG 416
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
179-510 |
4.29e-18 |
|
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: 87.33 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 179 PLEGFVYAITPFNFtAIAGNLPT-APALMGNV-VVWKPSPTQTHSAVLLMRLLEEAG-LPKGVINLVTGDGIAVsevaLN 255
Cdd:cd07128 143 PRRGVAVHINAFNF-PVWGMLEKfAPALLAGVpVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDL----LD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 256 HpaLAG---IHFTGSTRTFQHLwktvggniekyRSYPRIVGEtgGKDFVVAHPSADRAVLKTALTRGSFEFQ-------- 324
Cdd:cd07128 218 H--LGEqdvVAFTGSAATAAKL-----------RAHPNIVAR--SIRFNAEADSLNAAILGPDATPGTPEFDlfvkevar 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 325 ------GQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADptCEIVAG 398
Cdd:cd07128 283 emtvkaGQKCTAIRRAFVPEARVDA-VIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE--AEVVFG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 399 G-------SYDDSVGYFVRPTVIVCTDPGNE--VFTDEYFGPILAVYVYEDESpegyDAM-LDQMESVSayaLTGSVIAN 468
Cdd:cd07128 360 GpdrfevvGADAEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLA----EAIeLAARGRGS---LVASVVTN 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1717797354 469 DRAAAAHTMEKLRYAAGNFYINDKST-------GAVVGQQPFGG-GRASG 510
Cdd:cd07128 433 DPAFARELVLGAAPYHGRLLVLNRDSakestghGSPLPQLVHGGpGRAGG 482
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
179-383 |
9.72e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 85.96 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 179 PLeGFVYAITPFNFTAIAGNLPTAPALM-GNVVVWKPsPTQTHSAVLLM-RLLEEAGLPKGVINLVTGDGIAVSEVALNH 256
Cdd:PLN00412 158 PL-GVVLAIPPFNYPVNLAVSKIAPALIaGNAVVLKP-PTQGAVAALHMvHCFHLAGFPKGLISCVTGKGSEIGDFLTMH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 PALAGIHFTGStrtfqhlwkTVGGNIEKYRSYPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYI 336
Cdd:PLN00412 236 PGVNCISFTGG---------DTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLV 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717797354 337 PASIWNSgFKEEFAAEVDGIAMG------DVTDL-----SNFIGAVIDDrsfAKNKAA 383
Cdd:PLN00412 307 MESVADA-LVEKVNAKVAKLTVGppeddcDITPVvsessANFIEGLVMD---AKEKGA 360
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
144-527 |
7.75e-16 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 80.26 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 144 ELVDFWRFNVAYARDLLAEQPPANSPG-----VWNRLdhrpleGFVYAITPFNF-TAIAGNLPTAPALMGNVVVWKPSPT 217
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERPNhmmmeVWNPL------GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 218 QTHSAVLLMRL----LEEAGLPKGVINLVTGdGIAVSEVALNHPALAGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVG 293
Cdd:PLN02315 193 TPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGK------CLL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 294 ETGGKDFVVAHPSAD-----RAVLKTALTRGsfefqGQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFI 368
Cdd:PLN02315 266 ELSGNNAIIVMDDADiqlavRSVLFAAVGTA-----GQRCTTCRRLLLHESIYDD-VLEQLLTVYKQVKIGDPLEKGTLL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 369 GAVIDDRSFAKNKAAIDRAKADpTCEIVAGGSYDDSVGYFVRPTvIVCTDPGNEVFTDEYFGPILavYVYEDESPEgyDA 448
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQ-GGKILTGGSAIESEGNFVQPT-IVEISPDADVVKEELFGPVL--YVMKFKTLE--EA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 449 MldQMESVSAYALTGSVIANDRAAAAHTMEKLRYAAGNFYINDKSTGAVVGqQPFGGGRASGTNDKAGA---PQNLMRWT 525
Cdd:PLN02315 414 I--EINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRRST 490
|
..
gi 1717797354 526 LT 527
Cdd:PLN02315 491 CT 492
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
173-510 |
3.09e-15 |
|
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: 77.91 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 173 NRLDHRPLeGFVYAITPFNF---TAIAgnlPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKgVINLVTGD--- 245
Cdd:cd07133 95 AEVEYQPL-GVVGIIVPWNYplyLALG---PLIAALaAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGadv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 246 GIAVSEVALNHpalagIHFTGSTRTFQHLWKTVGGNIEkyrsyPrIVGETGGKDFVVAHPSADravLKTALTR---GSFE 322
Cdd:cd07133 170 AAAFSSLPFDH-----LLFTGSTAVGRHVMRAAAENLT-----P-VTLELGGKSPAIIAPDAD---LAKAAERiafGKLL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 323 FQGQKCSATSRAYIPASiWNSGFKEEFAAEV-----DGIAMGDVTdlsnfigAVIDDRSFAKNKAAIDRAKAD-PTCEIV 396
Cdd:cd07133 236 NAGQTCVAPDYVLVPED-KLEEFVAAAKAAVakmypTLADNPDYT-------SIINERHYARLQGLLEDARAKgARVIEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 397 AGGSYDDSVGYFVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDespegydamldqMESVSAY--------ALTgsVIAN 468
Cdd:cd07133 308 NPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDS------------LDEAIDYinarprplALY--YFGE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1717797354 469 DRAAAAHTMEklRYAAGNFYINDKSTGAVVGQQPFGGGRASG 510
Cdd:cd07133 374 DKAEQDRVLR--RTHSGGVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
179-510 |
3.85e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.21 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 179 PLEGFVYAITPFNFTAIAGNLPTAPALMGNV-VVWKPSPTQTHSAVLLMRLLEEAG-LPKGVINLVTGDGIAVsevaLNH 256
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGL----LDH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 257 paLAG---IHFTGSTRTFQHLwktvggniekyRSYPRIVGEtgGKDFVVAHPSADRAVLKTALTRGSFEFQ--------- 324
Cdd:PRK11903 223 --LQPfdvVSFTGSAETAAVL-----------RSHPAVVQR--SVRVNVEADSLNSALLGPDAAPGSEAFDlfvkevvre 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 325 -----GQKCSATSRAYIPASIWNSgFKEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADptCEIVAGG 399
Cdd:PRK11903 288 mtvksGQKCTAIRRIFVPEALYDA-VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ--AEVLFDG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 400 S------YDDSVGYFVRPTVIVCTDPGNE--VFTDEYFGPILAVYVYEDESpegydamldqmesvSAYALT----GSVIA 467
Cdd:PRK11903 365 GgfalvdADPAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRDAA--------------HALALArrgqGSLVA 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1717797354 468 ----NDRAAAAHTMEKLRYAAGNFYINDKSTGA-------VVGQQPFGG-GRASG 510
Cdd:PRK11903 431 svysDDAAFLAAAALELADSHGRVHVISPDVAAlhtghgnVMPQSLHGGpGRAGG 485
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
182-510 |
4.76e-15 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 77.54 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFT----------AIAGnlptapalmGNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGdGIAVSE 251
Cdd:cd07136 102 GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 252 VALNHPaLAGIHFTGSTRtfqhlwktVGgniekyrsypRIVG------------ETGGKDFVVAHPSADravLKTALTR- 318
Cdd:cd07136 171 ELLDQK-FDYIFFTGSVR--------VG----------KIVMeaaakhltpvtlELGGKSPCIVDEDAN---LKLAAKRi 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 319 --GSFEFQGQKCSATSRAYIPASIwnsgfKEEFAAEVD---GIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKadptc 393
Cdd:cd07136 229 vwGKFLNAGQTCVAPDYVLVHESV-----KEKFIKELKeeiKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK----- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 394 eIVAGGSYDDSVGYfVRPTVIVCTDPGNEVFTDEYFGPILAVYVYEDESpegydamlDQMESVSAYA--LTGSVIANDRA 471
Cdd:cd07136 299 -IVFGGNTDRETLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLD--------EAIEIIKSRPkpLALYLFSEDKK 368
|
330 340 350
....*....|....*....|....*....|....*....
gi 1717797354 472 AAAHTMEKLRYAAGnfYINDKSTGAVVGQQPFGGGRASG 510
Cdd:cd07136 369 VEKKVLENLSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
160-433 |
2.41e-14 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 75.94 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 160 LAEQPPANSPGVWNRLDHRPLeGFVYAITPFNFTAIAG--NLPTApALMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKG 237
Cdd:PLN02419 230 MGEYLPNVSNGVDTYSIREPL-GVCAGICPFNFPAMIPlwMFPVA-VTCGNTFILKPSEKDPGASVILAELAMEAGLPDG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 238 VINLVTGDGIAVSEVAlNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsypRIVGETGGKDFVVAHPSADRAVLKTALT 317
Cdd:PLN02419 308 VLNIVHGTNDTVNAIC-DDEDIRAVSFVGSNTAGMHIYARAAAKGK------RIQSNMGAKNHGLVLPDANIDATLNALL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 318 RGSFEFQGQKCSATSRAYI--PASIWNSGFKEEfaAEVDGIAMGDVTDLSnfIGAVIDDRsfAKNKAA-IDRAKADPTCE 394
Cdd:PLN02419 381 AAGFGAAGQRCMALSTVVFvgDAKSWEDKLVER--AKALKVTCGSEPDAD--LGPVISKQ--AKERICrLIQSGVDDGAK 454
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1717797354 395 IVAGGSYDDSVGY----FVRPTVIVCTDPGNEVFTDEYFGPIL 433
Cdd:PLN02419 455 LLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVL 497
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
182-530 |
2.22e-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: 72.53 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSptQTHSAVL--LMRLLEEAGLPKGVINLVTGDGIAVSEVALN-HP 257
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVD--SKVSVVMeqFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALagIHFTGSTRTFQHLWKTVGGNIEKyrsyprivgETGGKDFVVAHPS-ADRAVLKTALTRGSFEFQGQKCSATSRAYI 336
Cdd:cd07126 222 RM--TLFTGSSKVAERLALELHGKVKL---------EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 337 PASIWNSGFKEEFAAEVDGIAMGDVTdlsnfIGAVIDDRSfAKNKAAIDRAKADPTCEIVAGG------SYDDSVGYfVR 410
Cdd:cd07126 291 HENWVQAGILDKLKALAEQRKLEDLT-----IGPVLTWTT-ERILDHVDKLLAIPGAKVLFGGkpltnhSIPSIYGA-YE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIV-----CTDPGN-EVFTDEYFGPILAVYVYEDESpegYDAMLDQMESVSAYaLTGSVIAND----RAAAAHTMEKL 480
Cdd:cd07126 364 PTAVFvpleeIAIEENfELVTTEVFGPFQVVTEYKDEQ---LPLVLEALERMHAH-LTAAVVSNDirflQEVLANTVNGT 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1717797354 481 RYAAgnfyINDKSTGAVVGQ--QPFGGGRASGTndkaGAPQNL-MRWTLTRAI 530
Cdd:cd07126 440 TYAG----IRARTTGAPQNHwfGPAGDPRGAGI----GTPEAIrLVWSCHREI 484
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
189-505 |
6.25e-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: 61.40 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 189 PFNFTAIAGNlpTAPAL-MGNVVVWKPSPTQTHSAVLLMRL----LEEAGLPKGVINLVTGDGIAVSEVALNHPALAGIH 263
Cdd:cd07129 118 PLAFSVAGGD--TASALaAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 264 FTGSTRtfqhlwktvGGNIEKYRSYPR-----IVGETGGKDFVVAHPSA--DRAV-----LKTALTRGSfefqGQKCSAT 331
Cdd:cd07129 196 FTGSRR---------GGRALFDAAAARpepipFYAELGSVNPVFILPGAlaERGEaiaqgFVGSLTLGA----GQFCTNP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAYIPASIWNSGFKEEFAAEVDGIAMGdvTDLSNFIGaviddRSFAKNKAAIdraKADPTCEIVAGGSYDDSvGYFVRP 411
Cdd:cd07129 263 GLVLVPAGPAGDAFIAALAEALAAAPAQ--TMLTPGIA-----EAYRQGVEAL---AAAPGVRVLAGGAAAEG-GNQAAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 412 TVIVCTDP---GNEVFTDEYFGPILAVYVYEDEspegydamlDQMESVSAY---ALTGSVIA--NDRAAAAHTMEKLRYA 483
Cdd:cd07129 332 TLFKVDAAaflADPALQEEVFGPASLVVRYDDA---------AELLAVAEAlegQLTATIHGeeDDLALARELLPVLERK 402
|
330 340
....*....|....*....|...
gi 1717797354 484 AGNFYINDKSTG-AVVGQQPFGG 505
Cdd:cd07129 403 AGRLLFNGWPTGvEVCPAMVHGG 425
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
189-469 |
8.17e-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: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 189 PFNFT------AIAGnlptapalmGNVVVWKPSPTQTHSAVLLMRLLeeaglPKGVIN----LVTGdGIAVSEVALNHpA 258
Cdd:cd07132 113 PLQLTlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAELI-----PKYLDKecypVVLG-GVEETTELLKQ-R 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 259 LAGIHFTGSTrtfqhlwkTVGGNIEKY--RSYPRIVGETGGKDFVVAHPSADravLKTALTR---GSFEFQGQKCSATSr 333
Cdd:cd07132 177 FDYIFYTGST--------SVGKIVMQAaaKHLTPVTLELGGKSPCYVDKSCD---IDVAARRiawGKFINAGQTCIAPD- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 aYIpasIWNSGFKEEFAAEVDGIA---MGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKadptceIVAGGSYDDSVGYfVR 410
Cdd:cd07132 245 -YV---LCTPEVQEKFVEALKKTLkefYGEDPKESPDYGRIINDRHFQRLKKLLSGGK------VAIGGQTDEKERY-IA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 411 PTVIVCTDPGNEVFTDEYFGPI----------------------LAVYVYEDESPEgYDAMLDQMESvsayaltGSVIAN 468
Cdd:cd07132 314 PTVLTDVKPSDPVMQEEIFGPIlpivtvnnldeaiefinsrekpLALYVFSNNKKV-INKILSNTSS-------GGVCVN 385
|
.
gi 1717797354 469 D 469
Cdd:cd07132 386 D 386
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
182-510 |
1.15e-08 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 57.36 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 182 GFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGdgiAVSEV-ALNHPAL 259
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG---AVTETtALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 260 AGIHFTGSTRTFQHLWKTVGGNIEKyrsyprIVGETGGKDFVVAHPSADRAVLKTALTRGSFEF-QGQKCSA-----TSR 333
Cdd:PLN02174 190 DKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISpdyilTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPASIwnSGFKEEFAAEVDGIAMgDVTDLSNFIGAVIDDRsfaKNKAAIDRAKADptcEIVAGGSYDDSvGYFVRPTV 413
Cdd:PLN02174 264 EYAPKVI--DAMKKELETFYGKNPM-ESKDMSRIVNSTHFDR---LSKLLDEKEVSD---KIVYGGEKDRE-NLKIAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 414 IVCTDPGNEVFTDEYFGPILAVYVYEDeSPEGYDAMLDQMESVSAYALTGSVIANDRAAAAhtmeklrYAAGNFYINDKS 493
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNN-LEESFDVIRSRPKPLAAYLFTHNKKLKERFAAT-------VSAGGIVVNDIA 405
|
330
....*....|....*..
gi 1717797354 494 TGAVVGQQPFGGGRASG 510
Cdd:PLN02174 406 VHLALHTLPFGGVGESG 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
179-511 |
1.16e-07 |
|
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: 54.34 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 179 PLeGFVYAITPFNFTAIAGNLPTAPAL-MGNVVVWKPSPTQTHSAVLLMRLLEEAgLPKGVINLVTGdGIAVSEVALNHp 257
Cdd:cd07137 101 PL-GVVLVISAWNFPFLLSLEPVIGAIaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 258 ALAGIHFTGSTRtfqhLWKTVGGNIEKYRSyPrIVGETGGKDFVVAHPSADravLKTALTR---GSFEF-QGQKCSATSR 333
Cdd:cd07137 177 KWDKIFFTGSPR----VGRIIMAAAAKHLT-P-VTLELGGKCPVIVDSTVD---LKVAVRRiagGKWGCnNGQACIAPDY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 334 AYIPasiwnsgfkEEFAAEVdgIAMGDVTdLSNFIG---AVIDDRSFAKNKAAIDRAKA---DPTCE--IVAGGSYDDSv 405
Cdd:cd07137 248 VLVE---------ESFAPTL--IDALKNT-LEKFFGenpKESKDLSRIVNSHHFQRLSRlldDPSVAdkIVHGGERDEK- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 406 GYFVRPTvIVCTDP-GNEVFTDEYFGPILAVYVYEDESpEGYDAMLDQMESVSAYALTGSVIANDRAAAAhtmeklrYAA 484
Cdd:cd07137 315 NLYIEPT-ILLDPPlDSSIMTEEIFGPLLPIITVKKIE-ESIEIINSRPKPLAAYVFTKNKELKRRIVAE-------TSS 385
|
330 340
....*....|....*....|....*..
gi 1717797354 485 GNFYINDKSTGAVVGQQPFGGGRASGT 511
Cdd:cd07137 386 GGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
92-517 |
5.30e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 49.01 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 92 APAWRAMSFDDRAAIILRAAELLAGPWREtLAASTML--GQSKT-AQQA----EIDTPCELvdfwrfnVAYARDLLAEQP 164
Cdd:cd07127 97 MPGWRDAGARARAGVCLEILQRLNARSFE-MAHAVMHttGQAFMmAFQAggphAQDRGLEA-------VAYAWREMSRIP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 165 PAnspGVWNRLD--HRPLE-GFVYAITPFNFTAIAG--NLPT---APALM-----GNVVVWKPSPtqthSAVLLMRL--- 228
Cdd:cd07127 169 PT---AEWEKPQgkHDPLAmEKTFTVVPRGVALVIGcsTFPTwngYPGLFaslatGNPVIVKPHP----AAILPLAItvq 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 229 -----LEEAGLPKGVINLVT---GDGIAvSEVALnHPALAGIHFTGSTRTFQHLWKTVGGniekyrsyPRIVGETGGKDF 300
Cdd:cd07127 242 varevLAEAGFDPNLVTLAAdtpEEPIA-QTLAT-RPEVRIIDFTGSNAFGDWLEANARQ--------AQVYTEKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 301 VVAHPSADRAVLKTALTRGSFEFQGQKCSATSRAYIPAS-IWNS----GFKE---EFAAEVDGIAmGDVTDLSNFIGAVI 372
Cdd:cd07127 312 VVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgIQTDdgrkSFDEvaaDLAAAIDGLL-ADPARAAALLGAIQ 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 373 DDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSVgyfVR-PTVIVCTDPGNEVFTDEYFGPILAVYVYEDEspegyDAMLD 451
Cdd:cd07127 391 SPDTLARIAEARQLGEVLLASEAVAHPEFPDAR---VRtPLLLKLDASDEAAYAEERFGPIAFVVATDST-----DHSIE 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 452 QM-ESVSAY-ALTGSVIANDRAAAAHTMEKLRYAAGNFYINdkSTGAVVGQQP--FGGGRASGTNDKAGA 517
Cdd:cd07127 463 LArESVREHgAMTVGVYSTDPEVVERVQEAALDAGVALSIN--LTGGVFVNQSaaFSDFHGTGANPAANA 530
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
12-537 |
2.94e-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: 43.88 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 12 NEPVHSYAPGSPERARLEAKLKELAENPIELPMTIGGERRMGGGERVDVVQPHNHRAVIGTFAGATEQDAQDAVDAALAA 91
Cdd:COG0506 458 RRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAA 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 92 APAWRAMSFDDRAAIILRAAELLAGPWRETLAAsTMLGQSKTAQQAEIDTPCELVDFWRFNVAYARDLLAEQPPANSPGV 171
Cdd:COG0506 538 AAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLA-AAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 172 WNRLDHRPLEGFVYAITPFNFTAIAGNLPTAPALMGNVVVWKPSPTQTHSAVLLMRLLEEAGLPKGVINLVTGDGIAVSE 251
Cdd:COG0506 617 VALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGA 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 252 VALNHPALAGIHFTGSTRTFQHLWKTVGGNIEkyrsyPRIVGETGGKDFVVAHPSADRAVLKTALTRGSFEFQGQKCSAT 331
Cdd:COG0506 697 AALTLAAAAAAATAATAAAAAAAAALAAAAAA-----AAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLL 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 332 SRAyipasiwnsgfkEEFAAEVDGIAMGDVTDLSNFIGAVIDDRSFAKNKAAIDRAKADPTCEIVAGGSYDDSVGYFVRP 411
Cdd:COG0506 772 SLL------------ALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGG 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717797354 412 TVIVCTDPGNEVFTDEYFGPILAVYVYEDESPE------GYDAMLDQMESVSAYALTGSVIANDRAAAAHTMEKLRYAAG 485
Cdd:COG0506 840 GPLVPGLLTAPLLVALILGLIVLVLLEIVLVLAlvlalaLDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGG 919
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1717797354 486 NFYINDKSTGAVVGQQPFGGGRASGTNDKAGAPQNLMRWTLTRAIKETLVAP 537
Cdd:COG0506 920 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAA 971
|
|
| |
