|
Name |
Accession |
Description |
Interval |
E-value |
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
19-554 |
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: 985.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 19 LNEPMDNFEPGSaSAKGTLEA-CKAARGEVRECPIMIGGKPYTSSNI-IKGIMPSDHQVQIAKAYNATPELARKAVEAAV 96
Cdd:TIGR01236 1 ANEPVLPFRPGS-PERDLLRKsLKELKSSSLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 97 EASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQQPrsVSN 176
Cdd:TIGR01236 80 DAKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQP--ISA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 177 SGVWNTTDYRPLEGFVSAITPFNFTAIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAV 256
Cdd:TIGR01236 158 PGEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 257 MDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKC 336
Cdd:TIGR01236 238 VSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 337 SACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSNYEVVVGGKCDKTRGYF 416
Cdd:TIGR01236 318 SAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEALTILYGGKYDDSQGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 417 VEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSKpgyWKEVCELVDSTTKYGLTGAVFSRERAPIREADKYLRYAAGNYY 496
Cdd:TIGR01236 398 VEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDK---YKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFY 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009572 497 VNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSIKESFDVTPTISYPHQL 554
Cdd:TIGR01236 475 INDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
20-542 |
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: 891.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 20 NEPMDNFEPGSASAKGTLEACKAARGEVRECPIMIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEAS 99
Cdd:cd07123 3 NEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 100 KEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQQPRSvSNSGV 179
Cdd:cd07123 83 KEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLS-SPAGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 180 WNTTDYRPLEGFVSAITPFNFTAIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDS 259
Cdd:cd07123 162 WNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 260 AVNADPRLAAVVFTGSTRVFTEINKNVFSRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSAC 339
Cdd:cd07123 242 TVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 340 SRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADsSNYEVVVGGKCDKTRGYFVEP 419
Cdd:cd07123 322 SRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSD-PEAEIIAGGKCDDSVGYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 420 TIIETKDPRAQLMREEIFGPVLTVFVYDDSKpgyWKEVCELVDSTTKYGLTGAVFSRERAPIREADKYLRYAAGNYYVND 499
Cdd:cd07123 401 TVIETTDPKHKLMTEEIFGPVLTVYVYPDSD---FEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYIND 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 398009572 500 KCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSIKESF 542
Cdd:cd07123 478 KPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
38-542 |
5.84e-160 |
|
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: 465.52 E-value: 5.84e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 38 EACKAARGE-VRECPIMIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYK 116
Cdd:cd07083 6 EALRRVKEEfGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 117 AAHLLSTKYRHEMRAATMLGqSKNpWQAEIDCVAEACDFIRWNIHFAEELYAQQPRSVSNSGVWNTTDYRPLeGFVSAIT 196
Cdd:cd07083 86 AADLLRRRRRELIATLTYEV-GKN-WVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGL-GAGVVIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 197 PFNFT-AIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGS 275
Cdd:cd07083 163 PWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 276 TRVFTEINKNVFSRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKAL 355
Cdd:cd07083 243 LETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 356 LIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKadsSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREE 435
Cdd:cd07083 323 LLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGK---NEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 436 IFGPVLTVFVYDDSKpgyWKEVCELVDSTTkYGLTGAVFSRERAPIREADKYLryAAGNYYVNDKCTGAVVGQQPFGGSR 515
Cdd:cd07083 400 IFGPVLSVIRYKDDD---FAEALEVANSTP-YGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGFK 473
|
490 500
....*....|....*....|....*..
gi 398009572 516 LSGSNDKPGAGQFVTRFVSARSIKESF 542
Cdd:cd07083 474 LSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-542 |
2.59e-140 |
|
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: 415.85 E-value: 2.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 20 NEPMDNFEPGSASAKGTlEACKAARGEV-RECPIMIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEA 98
Cdd:cd07124 3 NEPFTDFADEENRAAFR-AALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 99 SKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPWQAEIDcVAEACDFIRWnihFAEELYA-QQPRSVSNS 177
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADAD-VAEAIDFLEY---YAREMLRlRGFPVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 178 GVWNTTDYRPLeGFVSAITPFNF-TAIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAV 256
Cdd:cd07124 157 GEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 257 MDSAVNADPRLAAVVFTGSTRVFTEINKnVFSRLETYHNFP-RISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQK 335
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYE-RAAKVQPGQKWLkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 336 CSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyeVVVGGKCD--KTR 413
Cdd:cd07124 315 CSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGR---LLLGGEVLelAAE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 414 GYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAG 493
Cdd:cd07124 392 GYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD-----FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VG 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 398009572 494 NYYVNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSIKESF 542
Cdd:cd07124 464 NLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
54-542 |
1.31e-139 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 412.98 E-value: 1.31e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRA 131
Cdd:COG1012 10 IGGEwvAAASGETFDVINPATGEV-LARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL-EERREELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATMLGQSKNPWQAEIDcVAEACDFIRWNIHFAEELYAQQPRSVSnSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTP 211
Cdd:COG1012 88 LLTLETGKPLAEARGE-VDRAADFLRYYAGEARRLYGETIPSDA-PGTRAYVRREPL-GVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 212 AL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRL 290
Cdd:COG1012 165 ALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 291 etyhnfPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDD 370
Cdd:COG1012 245 ------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 371 FQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKC-DKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDs 449
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGA--ELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDD- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 450 kpgyWKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAvVGQQPFGGSRLSGSNDKpGAGQFV 529
Cdd:COG1012 396 ----EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGL 466
|
490
....*....|...
gi 398009572 530 TRFVSARSIKESF 542
Cdd:COG1012 467 EEYTETKTVTIRL 479
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
17-542 |
2.28e-129 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 387.75 E-value: 2.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 17 PVLNEPMDNFEPgSASAKGTLEACKAARGEV-RECPIMIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAA 95
Cdd:PRK03137 4 PYKHEPFTDFSV-EENVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 96 VEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMrAATMLGQSKNPW-QAEIDcVAEACDFIRWnihFAEEL--YAQQPR 172
Cdd:PRK03137 83 LEAFETWKKWSPEDRARILLRAAAIIRRR-KHEF-SAWLVKEAGKPWaEADAD-TAEAIDFLEY---YARQMlkLADGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 173 SVSNSGVWNTTDYRPLeGFVSAITPFNF-TAIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVP 251
Cdd:PRK03137 157 VESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 252 CEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKnVFSRLETYHNF-PRISGETGGKDFHLVHPSADMKHVAAGTVRGAFE 330
Cdd:PRK03137 236 GSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE-RAAKVQPGQIWlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 331 FQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDfQSFMCAVIDETSFNKNKKYIEIAKADSsnyEVVVGGKCD 410
Cdd:PRK03137 315 FSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG---RLVLGGEGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 411 KTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERAPIREADKylRY 490
Cdd:PRK03137 391 DSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD-----FDHALEIANN-TEYGLTGAVISNNREHLEKARR--EF 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 398009572 491 AAGNYYVNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSIKESF 542
Cdd:PRK03137 463 HVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-518 |
4.15e-118 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 356.84 E-value: 4.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 61 SSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATMLGQSKN 140
Cdd:pfam00171 5 ESETIEVINPATGEV-IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLL-EERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 141 PWQAEIDcVAEACDFIRWnihFAEELYAQQPRSVSNS-GVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTV 218
Cdd:pfam00171 83 LAEARGE-VDRAIDVLRY---YAGLARRLDGETLPSDpGRLAYTRREPL-GVVGAITPWNFPLLLPAWKIAPALAaGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 219 VWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSrletyhNFPR 298
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ------NLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 299 ISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAV 378
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 IDETSFNKNKKYIEIAKADssNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVC 458
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEE--GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE-----EEAI 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009572 459 ELVDStTKYGLTGAVFSReraPIREADKYLRYA-AGNYYVNDKCTGAVVGqQPFGGSRLSG 518
Cdd:pfam00171 385 EIAND-TEYGLAAGVFTS---DLERALRVARRLeAGMVWINDYTTGDADG-LPFGGFKQSG 440
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
20-542 |
8.38e-111 |
|
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: 339.92 E-value: 8.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 20 NEPMDNFepgsaSAKGTLEACKAARGEVREC-----PIMIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEA 94
Cdd:TIGR01237 3 HEPFTDF-----ADEENRQAFFKALATVKEQlgktyPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 95 AVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPWQAEIDcVAEACDFIRWNIHFAEELYAQQPrSV 174
Cdd:TIGR01237 78 AAKAFEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAE-VAEAIDFMEYYARQMIELAKGKP-VN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 175 SNSGVWNTTDYRPLeGFVSAITPFNFT-AIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCE 253
Cdd:TIGR01237 155 SREGETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 254 PAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQG 333
Cdd:TIGR01237 234 GSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 334 QKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSsnyEVVVGGKCDKTR 413
Cdd:TIGR01237 314 QKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG---RLVSGGCGDDSK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 414 GYFVEPTIIETKDPRAQLMREEIFGPVLTVfvyddSKPGYWKEVCELVDSTtKYGLTGAVFSRERAPIREADKylRYAAG 493
Cdd:TIGR01237 391 GYFIGPTIFADVDRKARLAQEEIFGPVVAF-----IRASDFDEALEIANNT-EYGLTGGVISNNRDHINRAKA--EFEVG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 398009572 494 NYYVNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSIKESF 542
Cdd:TIGR01237 463 NLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
90-518 |
2.72e-105 |
|
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: 323.01 E-value: 2.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 90 KAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATM-LGQsknPWQAEIDCVAEACDFIRWNIHFAEELYA 168
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLeTGK---PIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 169 QQPRSVSNSGVwNTTDYRPLeGFVSAITPFNFT-AIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVI 247
Cdd:cd07078 79 EVIPSPDPGEL-AIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 248 NFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLetyhnfPRISGETGGKDFHLVHPSADMKHVAAGTVRG 327
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 328 AFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGG 407
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGA--KLLCGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 408 KCDKT-RGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTkYGLTGAVFSRERAPIREADK 486
Cdd:cd07078 309 KRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE-----EEAIELANDTE-YGLAAGVFTRDLERALRVAE 382
|
410 420 430
....*....|....*....|....*....|..
gi 398009572 487 YLRyaAGNYYVNDKcTGAVVGQQPFGGSRLSG 518
Cdd:cd07078 383 RLE--AGTVWINDY-SVGAEPSAPFGGVKQSG 411
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
27-536 |
8.89e-92 |
|
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: 291.02 E-value: 8.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 27 EPGSASAKGTLEACKAARGEVRecPImIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVP 106
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAI--PI-INGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 107 FRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAeIDCVAEACDFIRWNIHFAEELYAQqPRSVSNSGVWNTTDYR 186
Cdd:cd07125 90 VEERAEILEKAADLLE-ANRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSD-PELPGPTGELNGLELH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 187 PLeGFVSAITPFNF-TAI-----AANLAGtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSA 260
Cdd:cd07125 167 GR-GVFVCISPWNFpLAIftgqiAAALAA-----GNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 261 VNADPRLAAVVFTGSTRVFTEINKnvfSRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACS 340
Cdd:cd07125 241 LVAHPRIDGVIFTGSTETAKLINR---ALAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 341 RLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSsnyEVVVGGKCDKTRGYFVEPT 420
Cdd:cd07125 318 LLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEA---WLIAPAPLDDGNGYFVAPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 421 IIEtkDPRAQLMREEIFGPVLTVFVYddsKPGYWKEVCELVDStTKYGLTGAVFSRErapIREADKYLRYA-AGNYYVND 499
Cdd:cd07125 395 IIE--IVGIFDLTTEVFGPILHVIRF---KAEDLDEAIEDINA-TGYGLTLGIHSRD---EREIEYWRERVeAGNLYINR 465
|
490 500 510
....*....|....*....|....*....|....*..
gi 398009572 500 KCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSAR 536
Cdd:cd07125 466 NITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEK 502
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-524 |
8.23e-75 |
|
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: 242.13 E-value: 8.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 93 EAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATM-LGQsknPWQAEIDCVAEACDFIRWNIHFAEELYAQQP 171
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLeTGK---PIEEALGEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 172 RSVSNSGVwNTTDYRPLeGFVSAITPFNF-TAIAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFV 250
Cdd:cd06534 78 PSPDPGGE-AYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 251 PCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLetyhnfPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFE 330
Cdd:cd06534 156 PGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 331 FQGQKCSACSRLYAPKTCWKELKALLIkgqkqikmgqpddfqsfmcavidetsfnknkkyieiakadssnyevvvggkcd 410
Cdd:cd06534 230 NAGQICTAASRLLVHESIYDEFVEKLV----------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 411 ktrgyfvepTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTkYGLTGAVFSRERAPIREADKYLRy 490
Cdd:cd06534 257 ---------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE-----EEAIALANDTE-YGLTAGVFTRDLNRALRVAERLR- 320
|
410 420 430
....*....|....*....|....*....|....
gi 398009572 491 aAGNYYVNDKCTGaVVGQQPFGGSRLSGSNDKPG 524
Cdd:cd06534 321 -AGTVYINDSSIG-VGPEAPFGGVKNSGIGREGG 352
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
54-519 |
1.83e-72 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 239.07 E-value: 1.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAAT 133
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDEL--EARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 134 MLGQSKNPWQAEIDCVAEACDFIRwniHFAEELYAQQPRSVSNS--GVWNTTDYRPLeGFVSAITPFNF-TAIAA-NLAg 209
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFR---YYAGEALRLSGETLPSTrpGVEVETTREPL-GVVGLITPWNFpIAIPAwKIA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 210 tPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFS 288
Cdd:cd07097 158 -PALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 289 RletyhnFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQP 368
Cdd:cd07097 237 R------GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 369 DDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKC--DKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVY 446
Cdd:cd07097 311 LDEGVDIGPVVSERQLEKDLRYIEIARSEGA--KLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 447 DDskpgyWKEVCELVDStTKYGLTGAVFSRErapIREADKYLRYA-AGNYYVNDKCTGaVVGQQPFGGSRLSGS 519
Cdd:cd07097 389 RD-----YDEALAIAND-TEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSSY 452
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
70-518 |
5.58e-71 |
|
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: 234.77 E-value: 5.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATMLGQSKNPWQA---EI 146
Cdd:cd07093 4 PATGEV-LAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLI-EARADELALLESLDTGKPITLArtrDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 147 DCVAEacdfirwNIHF--------AEELYAQQPrsvsnsGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNT 217
Cdd:cd07093 82 PRAAA-------NFRFfadyilqlDGESYPQDG------GALNYVLRQPV-GVAGLITPWNLPLMLLTWKIAPALaFGNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 218 VVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfp 297
Cdd:cd07093 148 VVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLK------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 298 RISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCA 377
Cdd:cd07093 222 PVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 378 VIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKT----RGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgy 453
Cdd:cd07093 302 LISKEHLEKVLGYVELARAEGA--TILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE---- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009572 454 wKEVCELVDStTKYGLTGAVFSR--ERApIREADKyLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07093 376 -EEAIELAND-TPYGLAAYVWTRdlGRA-HRVARR-LE--AGTVWVN--CWLVRDLRTPFGGVKASG 434
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
55-518 |
1.20e-69 |
|
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: 231.68 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 55 GGKPYTSSNiikgimPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEmraatm 134
Cdd:cd07086 11 GGETFTSRN------PANGEP-IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL-RKKKEA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 135 LGQS------KNPWQAEIDcVAEA---CDFI---------------RWNiHFAEElyaqqprsvsnsgVWNttdyrPLeG 190
Cdd:cd07086 77 LGRLvslemgKILPEGLGE-VQEMidiCDYAvglsrmlygltipseRPG-HRLME-------------QWN-----PL-G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 191 FVSAITPFNF-TAIAA-NLAgtPALM-GNTVVWKPSPTAVLSNYLMYKIMEEA----GLPAGVINFVpCEPAVMDSAVNA 263
Cdd:cd07086 136 VVGVITAFNFpVAVPGwNAA--IALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLV-TGGGDGGELLVH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 264 DPRLAAVVFTGSTRVFTEINKNVFSRletyhnFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLY 343
Cdd:cd07086 213 DPRVPLVSFTGSTEVGRRVGETVARR------FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 344 APKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKC--DKTRGYFVEPTI 421
Cdd:cd07086 287 VHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGG--TVLTGGKRidGGEPGNYVEPTI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 422 IETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRErapIREADKYLRYA---AGNYYVN 498
Cdd:cd07086 365 VTGVTDDARIVQEETFAPILYVIKFDS-----LEEAIAINND-VPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVN 435
|
490 500
....*....|....*....|
gi 398009572 499 DKCTGAVVGqQPFGGSRLSG 518
Cdd:cd07086 436 IPTSGAEIG-GAFGGEKETG 454
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
53-536 |
8.12e-68 |
|
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: 227.87 E-value: 8.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 53 MIGGKPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTkyrhEMRAA 132
Cdd:TIGR01238 41 IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLEL----HMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 133 TMLG--QSKNPWQAEIDCVAEACDFIRWnihfaeelYAQQPRSVsnsgvWNTTDYRPLEGFVsAITPFNFT------AIA 204
Cdd:TIGR01238 117 MALCvrEAGKTIHNAIAEVREAVDFCRY--------YAKQVRDV-----LGEFSVESRGVFV-CISPWNFPlaiftgQIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 205 ANLAGtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINK 284
Cdd:TIGR01238 183 AALAA-----GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 285 NVFSRLETyhNFPRISgETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIK 364
Cdd:TIGR01238 258 TLAQREDA--PVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 365 MGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADS-SNYEVVVGGKCDKTRGYFVEPTIIETKDPRAqlMREEIFGPVLTV 443
Cdd:TIGR01238 335 VGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkKIAQLTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 444 FVYDDskpgywKEVCELVD--STTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAVVGQQPFGGSRLSGSND 521
Cdd:TIGR01238 413 VRYKA------RELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGP 484
|
490
....*....|....*
gi 398009572 522 KPGAGQFVTRFVSAR 536
Cdd:TIGR01238 485 KAGGPHYLYRLTQVQ 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-536 |
2.24e-65 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 230.98 E-value: 2.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 53 MIGGKPYTSSNIIKgIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstkyrhEMRAA 132
Cdd:COG4230 561 LIAGEAASGEARPV-RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLL------EAHRA 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 133 TML-------GQSknpWQAEIDCVAEACDFIRWnihfaeelYAQQPRSVSNsgvwNTTDYRPLeGFVSAITPFNFT-AI- 203
Cdd:COG4230 634 ELMallvreaGKT---LPDAIAEVREAVDFCRY--------YAAQARRLFA----APTVLRGR-GVFVCISPWNFPlAIf 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 204 ----AANLAgtpalMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVF 279
Cdd:COG4230 698 tgqvAAALA-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 TEINKNVFSRLETYHnfPRISgETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:COG4230 773 RLINRTLAARDGPIV--PLIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGA 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIE-IAKADSSNYEVVVGGKCDKtrGYFVEPTIIETKDPrAQLMReEIFG 438
Cdd:COG4230 850 MAELRVGDPADLSTDVGPVIDAEARANLEAHIErMRAEGRLVHQLPLPEECAN--GTFVAPTLIEIDSI-SDLER-EVFG 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 439 PVLTVFVYDDSKPGywkevcELVDS--TTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAVVGQQPFGGSRL 516
Cdd:COG4230 926 PVLHVVRYKADELD------KVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGL 997
|
490 500
....*....|....*....|
gi 398009572 517 SGSNDKPGAGQFVTRFVSAR 536
Cdd:COG4230 998 SGTGPKAGGPHYLLRFATER 1017
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
22-535 |
6.71e-65 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 229.75 E-value: 6.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 22 PMDNFEPGSASAKG-------TLEACKAARGEVREC-----PIMIGGKPYTSSNIIKGimPSDHQVQIAKAYNATPELAR 89
Cdd:PRK11905 516 PRDLYGPERRNSKGldlsdeaTLAALDEALNAFAAKtwhaaPLLAGGDVDGGTRPVLN--PADHDDVVGTVTEASAEDVE 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 90 KAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYrHEMRAATMLGQSKNPWQAeIDCVAEACDFIRWnihfaeelYAQ 169
Cdd:PRK11905 594 RALAAAQAAFPEWSATPAAERAAILERAADLMEAHM-PELFALAVREAGKTLANA-IAEVREAVDFLRY--------YAA 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 170 QPRSVsnsgvWNTTDYRPLeGFVSAITPFNFT-AI-----AANLAgtpalMGNTVVWKPSPTAVLSNYLMYKIMEEAGLP 243
Cdd:PRK11905 664 QARRL-----LNGPGHKPL-GPVVCISPWNFPlAIftgqiAAALV-----AGNTVLAKPAEQTPLIAARAVRLLHEAGVP 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 244 AGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyHNFPRISgETGGKDFHLVHPSADMKHVAAG 323
Cdd:PRK11905 733 KDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSG--PPVPLIA-ETGGQNAMIVDSSALPEQVVAD 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 324 TVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADS-SNYE 402
Cdd:PRK11905 810 VIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGrLVHQ 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 403 VVVGGKCDKtrGYFVEPTIIETKDPRAqlMREEIFGPVLTVFVYDDSkpgywkEVCELVDS--TTKYGLTGAVFSR--ER 478
Cdd:PRK11905 890 LPLPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRFKAD------ELDRVIDDinATGYGLTFGLHSRidET 959
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 398009572 479 ApireADKYLRYAAGNYYVNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSA 535
Cdd:PRK11905 960 I----AHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
37-538 |
7.46e-65 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 228.93 E-value: 7.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 37 LEACKAARGEVRECPIMIGGkpytSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYK 116
Cdd:PRK11904 540 AAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILER 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 117 AAHLLstkyrhEMRAATML-------GQSknpWQAEIDCVAEACDFIRWNIHFAEELYAQQPRSVSNSGVWNTTDYRPLE 189
Cdd:PRK11904 616 AADLL------EANRAELIalcvreaGKT---LQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRG 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 190 GFVsAITPFNFT-AI-----AAnlagtpALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVN 262
Cdd:PRK11904 687 VFV-CISPWNFPlAIflgqvAA------ALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALT 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 263 ADPRLAAVVFTGSTRVFTEINKNVFSRletyhnfpriSG-------ETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQK 335
Cdd:PRK11904 760 ADPRIAGVAFTGSTETARIINRTLAAR----------DGpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQR 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 336 CSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADS-SNYEVVVGGKCDKtrG 414
Cdd:PRK11904 830 CSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArLLAQLPLPAGTEN--G 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 415 YFVEPTIIETKDPrAQLmREEIFGPVLTVFVYddsKPGYWKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGN 494
Cdd:PRK11904 908 HFVAPTAFEIDSI-SQL-EREVFGPILHVIRY---KASDLDKVIDAINA-TGYGLTLGIHSRIEETADRIADRVR--VGN 979
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 398009572 495 YYVNDKCTGAVVGQQPFGGSRLSGSNDKPGAGQFVTRFVSARSI 538
Cdd:PRK11904 980 VYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
83-536 |
7.52e-65 |
|
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: 219.14 E-value: 7.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 83 ATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQ-SKNPWQAEIDcVAEACDFIRWNIH 161
Cdd:cd07131 34 STASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELL--KKRKEELARLVTREmGKPLAEGRGD-VQEAIDMAQYAAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 162 FAEELYAQQ-PRSVSNSgvWNTTDYRPLeGFVSAITPFNF-TAIAANLAGtPALM-GNTVVWKPSPTAVLSNYLMYKIME 238
Cdd:cd07131 111 EGRRLFGETvPSELPNK--DAMTRRQPI-GVVALITPWNFpVAIPSWKIF-PALVcGNTVVFKPAEDTPACALKLVELFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 239 EAGLPAGVINFV--PCEPAvmDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhnFPRISGETGGKDFHLVHPSAD 316
Cdd:cd07131 187 EAGLPPGVVNVVhgRGEEV--GEALVEHPDVDVVSFTGSTEVGERIGETCARP------NKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 317 MKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKA 396
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 397 DSSnyEVVVGG----KCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGA 472
Cdd:cd07131 339 EGA--TLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS-----LEEAIEIAND-TEYGLSSA 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009572 473 VFSRErapIREADKYLRYA-AGNYYVNDKCTGAVVgQQPFGGSRLSGsNDKPGAGQFVTRFVSAR 536
Cdd:cd07131 411 IYTED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSG-NGHREAGTTALDAFTEW 470
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
70-518 |
1.92e-63 |
|
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: 214.60 E-value: 1.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATMLGQSKnPW---QAEI 146
Cdd:cd07103 4 PATGEV-IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI-RERAEDLARLLTLEQGK-PLaeaRGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 147 DcvaEACDFIRWnihFAEE---LYAQQPRSvSNSGVWNTTDYRPLeGFVSAITPFNFTA--IAANLAgtPAL-MGNTVVW 220
Cdd:cd07103 81 D---YAASFLEW---FAEEarrIYGRTIPS-PAPGKRILVIKQPV-GVVAAITPWNFPAamITRKIA--PALaAGCTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 221 KPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpRIS 300
Cdd:cd07103 151 KPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 301 GETGGkdfH---LVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCA 377
Cdd:cd07103 225 LELGG---NapfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 378 VIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEV 457
Cdd:cd07103 302 LINERAVEKVEALVEDAVAKGA--KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE-----DEV 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009572 458 CELVDStTKYGLTGAVFSRERAPIREADKYLRYaaGNYYVNdkcTGAVVG-QQPFGGSRLSG 518
Cdd:cd07103 375 IARAND-TPYGLAAYVFTRDLARAWRVAEALEA--GMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
70-518 |
3.84e-63 |
|
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: 213.73 E-value: 3.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQSKNPWQAEIDCV 149
Cdd:cd07150 6 PADGSV-YARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM--ERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 150 AEACDFIRWNIHFAEELYAQQPRSVSNsGVWNTTDYRPLeGFVSAITPFNF-TAIAANLAGTPALMGNTVVWKPSPTAVL 228
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSP-GTVSMSVRRPL-GVVAGITPFNYpLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 229 SNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINknvfsrLETYHNFPRISGETGGKDF 308
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIA------EKAGRHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 309 HLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNK 388
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 389 KYIEIAKADSSNyeVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYG 468
Cdd:cd07150 315 RQVEDAVAKGAK--LLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDA-----EEALELAND-TEYG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398009572 469 LTGAVFSRErapIREADKY-LRYAAGNYYVNDKC--TGAVVgqqPFGGSRLSG 518
Cdd:cd07150 384 LSAAILTND---LQRAFKLaERLESGMVHINDPTilDEAHV---PFGGVKASG 430
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
88-518 |
2.33e-62 |
|
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: 211.24 E-value: 2.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 88 ARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstkyrhEMRAATMlgqsknpwqaeIDCVAEACDFIR----WNIHFA 163
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEIL------EERRDEI-----------ADWLIRESGSTRpkaaFEVGAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 164 EELY---AQQPRSV------SNS-GVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSP-TAVLSNY 231
Cdd:cd07104 65 IAILreaAGLPRRPegeilpSDVpGKESMVRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSrTPVTGGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 232 LMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKnVFSRletyhNFPRISGETGGKDFHLV 311
Cdd:cd07104 144 LIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGR-----HLKKVALELGGNNPLIV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 312 HPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYI 391
Cdd:cd07104 218 LDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 392 EIAKADSSnyEVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTG 471
Cdd:cd07104 298 EDAVAAGA--RLLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD-----EEAVELAND-TEYGLSA 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398009572 472 AVFSR--ERApIREADKyLRyaAGNYYVNDKcT---GAVVgqqPFGGSRLSG 518
Cdd:cd07104 367 AVFTRdlERA-MAFAER-LE--TGMVHINDQ-TvndEPHV---PFGGVKASG 410
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
70-518 |
9.92e-62 |
|
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: 210.10 E-value: 9.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLSTkyRHEMRAATMLGQSKNPWQaeiD 147
Cdd:cd07114 4 PATGEP-WARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEA--NAEELAELETRDNGKLIR---E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 148 CVAEACDFIRWNIHFAEELYAQQPRS--VSNSGVWNTTDYRPLeGFVSAITPFN--FTAIAANLAgtPAL-MGNTVVWKP 222
Cdd:cd07114 78 TRAQVRYLAEWYRYYAGLADKIEGAVipVDKGDYLNFTRREPL-GVVAAITPWNspLLLLAKKLA--PALaAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 223 SPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNvfsrleTYHNFPRISGE 302
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARA------AAENLAPVTLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 303 TGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDET 382
Cdd:cd07114 229 LGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 383 SFNKNKKYIEIAKADSSnyEVVVGGK----CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVC 458
Cdd:cd07114 309 QLEKVERYVARAREEGA--RVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE-----EEAI 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009572 459 ELVDStTKYGLTGAVFSRE--RApIREADKyLRyaAGNYYVND-KCTGAVVgqqPFGGSRLSG 518
Cdd:cd07114 382 ALAND-SEYGLAAGIWTRDlaRA-HRVARA-IE--AGTVWVNTyRALSPSS---PFGGFKDSG 436
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
54-518 |
5.07e-61 |
|
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: 208.51 E-value: 5.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKY------ 125
Cdd:cd07138 3 IDGAwvAPAGTETIDVINPATEEV-IGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARAdelaqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 126 -RHEMRAATMLGQSknpWQAE--IDCVAEACDFIRwNIHFAEElyaqqprsVSNSGVwnttDYRPLeGFVSAITPFNFTA 202
Cdd:cd07138 82 iTLEMGAPITLARA---AQVGlgIGHLRAAADALK-DFEFEER--------RGNSLV----VREPI-GVCGLITPWNWPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 203 --IAANLAgtPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVF 279
Cdd:cd07138 145 nqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 TEINKNVFSRLEtyhnfpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:cd07138 223 KRVAEAAADTVK------RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGG-----KCDktRGYFVEPTIIETKDPRAQLMRE 434
Cdd:cd07138 297 AEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGA--RLVAGGpgrpeGLE--RGYFVKPTVFADVTPDMTIARE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 435 EIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDkctGAVVGQQPFGGS 514
Cdd:cd07138 373 EIFGPVLSIIPYDDE-----DEAIAIAND-TPYGLAGYVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGY 441
|
....
gi 398009572 515 RLSG 518
Cdd:cd07138 442 KQSG 445
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
52-518 |
4.64e-60 |
|
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: 206.29 E-value: 4.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 52 IMIGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLStKYRH 127
Cdd:cd07091 6 LFINNEfvDSVSGKTFPTINPATEEV-ICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIE-RDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 128 EMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELyaqQPRSVSNSG-VWNTTDYRPLeGFVSAITPFNFTAIAAN 206
Cdd:cd07091 84 ELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKI---QGKTIPIDGnFLAYTRREPI-GVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 207 LAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKn 285
Cdd:cd07091 160 WKLAPALaAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIME- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 286 vfSRLETyhNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKM 365
Cdd:cd07091 239 --AAAKS--NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 366 GQPDDFQSFMCAVIDETSFNKNKKYIEIAKadSSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFV 445
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGK--KEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILK 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 446 YDDSkpgywKEVCELVDSTTkYGLTGAVFSRErapIREADKYLRY-AAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07091 393 FKTE-----DEVIERANDTE-YGLAAGVFTKD---INKALRVSRAlKAGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
53-536 |
5.98e-60 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 215.61 E-value: 5.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 53 MIGGkPYTSSNIIKGIMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEM--- 129
Cdd:PRK11809 650 MLED-PVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMgll 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 130 -RAAtmlGQSKNPWQAEidcVAEACDFIRWnihfaeelYAQQPRSVSNsgvwNTTdYRPLeGFVSAITPFNFT------A 202
Cdd:PRK11809 729 vREA---GKTFSNAIAE---VREAVDFLRY--------YAGQVRDDFD----NDT-HRPL-GPVVCISPWNFPlaiftgQ 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 203 IAANLAGtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEI 282
Cdd:PRK11809 789 VAAALAA-----GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLL 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 283 NKNVFSRLETY-HNFPRISgETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLyapktCWKELKA----LLI 357
Cdd:PRK11809 864 QRNLAGRLDPQgRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVL-----CLQDDVAdrtlKML 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 358 KG-QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADS-SNYEVVVGGKCDKTRGYFVEPTIIETkDPRAQLMREe 435
Cdd:PRK11809 938 RGaMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGrPVFQAARENSEDWQSGTFVPPTLIEL-DSFDELKRE- 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 436 IFGPVLTVFVYDDSkpgywkEVCELVDS--TTKYGLTGAVFSRerapIRE--ADKYLRYAAGNYYVNDKCTGAVVGQQPF 511
Cdd:PRK11809 1016 VFGPVLHVVRYNRN------QLDELIEQinASGYGLTLGVHTR----IDEtiAQVTGSAHVGNLYVNRNMVGAVVGVQPF 1085
|
490 500
....*....|....*....|....*
gi 398009572 512 GGSRLSGSNDKPGAGQFVTRFVSAR 536
Cdd:PRK11809 1086 GGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
68-518 |
1.57e-59 |
|
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: 204.37 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQV--QIAKAYNATPELARKAVEAAVEaSKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAE 145
Cdd:cd07112 7 INPATGRVlaEVAACDAADVDRAVAAARRAFE-SGVWSRLSPAERKAVLLRLADLIE-AHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 146 IDCVAEACDFIRWNIHFAEELYAQQPRSvsNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSP 224
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYGEVAPT--GPDALALITREPL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 225 TAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVfteinKNVFSRLETYHNFPRISGETG 304
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEV-----GRRFLEYSGQSNLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 305 GKDFHLVHPSA-DMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETS 383
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 384 FNKNKKYIEIAKADSSNyeVVVGGKCD--KTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELV 461
Cdd:cd07112 317 FDKVLGYIESGKAEGAR--LVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE-----EEAVALA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009572 462 dSTTKYGLTGAVFSRE--RApIREADKyLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07112 390 -NDSVYGLAASVWTSDlsRA-HRVARR-LR--AGTVWVN--CFDEGDITTPFGGFKQSG 441
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
68-518 |
4.42e-59 |
|
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: 204.08 E-value: 4.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATM-----LGQSKn 140
Cdd:cd07119 18 INPANGEV-IATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLntgktLRESE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 141 pwqAEIDCVAEACDFirwnihFAEELYAQQPRSVS-NSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTV 218
Cdd:cd07119 96 ---IDIDDVANCFRY------YAGLATKETGEVYDvPPHVISRTVREPV-GVCGLITPWNYPLLQAAWKLAPALAaGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 219 VWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSrletyhNFPR 298
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG------NVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 299 ISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAV 378
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 IDETSFNKNKKYIEIAKADSSnyEVVVGGK------CDKtrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpg 452
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGA--RLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--- 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 453 ywKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDkcTGAVVGQQPFGGSRLSG 518
Cdd:cd07119 393 --EEAIRLAND-TPYGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
70-518 |
4.91e-59 |
|
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: 203.05 E-value: 4.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEIDCV 149
Cdd:cd07115 4 PATGEL-IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 150 AEACDFIRWNIHFAEELYAQQ-PRSvsnSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSPTAV 227
Cdd:cd07115 82 PRAADTFRYYAGWADKIEGEViPVR---GPFLNYTVREPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 228 LSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNvfsrleTYHNFPRISGETGGKD 307
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQG------AAGNLKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 308 FHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKN 387
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 388 KKYIEIAKADSSNyeVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTkY 467
Cdd:cd07115 312 LDYVDVGREEGAR--LLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE-----EEALRIANGTE-Y 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398009572 468 GLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07115 384 GLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
77-518 |
5.94e-59 |
|
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: 202.83 E-value: 5.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 77 IAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQSKNPW---QAEIDCVAEAC 153
Cdd:cd07149 12 IGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIALEAGKPIkdaRKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 154 DFIrwnihfAEE---LYAQQPRSVSNSGVWNTTDY---RPLeGFVSAITPFNF----------TAIAAnlagtpalmGNT 217
Cdd:cd07149 90 RLS------AEEakrLAGETIPFDASPGGEGRIGFtirEPI-GVVAAITPFNFplnlvahkvgPAIAA---------GNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 218 VVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhnfp 297
Cdd:cd07149 154 VVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 298 RISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCA 377
Cdd:cd07149 226 KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 378 VIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEV 457
Cdd:cd07149 306 MISEAEAERIEEWVEEAVEGGA--RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDT-----LDEA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009572 458 CELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTgAVVGQQPFGGSRLSG 518
Cdd:cd07149 376 IAMAND-SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSST-FRVDHMPYGGVKESG 432
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
68-518 |
3.29e-58 |
|
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: 201.05 E-value: 3.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVQIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTkyRHEMRAATMLGQSKNPW--QAE 145
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALETGNALrtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 146 IDcVAEACDFIRWNIHFAEELYAQQ-PrsvSNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPS 223
Cdd:cd07108 79 PE-AAVLADLFRYFGGLAGELKGETlP---FGPDVLTYTVREPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 224 PTAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLetyhnFPrISGET 303
Cdd:cd07108 154 EDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL-----IP-VSLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 304 GGKDFHLVHPSADMKHVAAGTVRGA-FEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDET 382
Cdd:cd07108 227 GGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 383 SFNKNKKYIEIAKAdSSNYEVVVGGK----CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVC 458
Cdd:cd07108 307 QFAKVCGYIDLGLS-TSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD-----EDEVI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009572 459 ELVDSTTkYGLTGAVFSRE-RAPIREADkylRYAAGNYYVNdKCTGAVVGQQpFGGSRLSG 518
Cdd:cd07108 381 AMANDSH-YGLAAYVWTRDlGRALRAAH---ALEAGWVQVN-QGGGQQPGQS-YGGFKQSG 435
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
54-518 |
2.35e-57 |
|
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: 198.95 E-value: 2.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLSTKyRHEM 129
Cdd:cd07139 3 IGGRwvAPSGSETIDVVSPATEEV-VGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEAR-ADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 130 RAATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQQPRSVSNSGVWNTTdYRPLeGFVSAITPFNFTAIAANLAG 209
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVR-REPV-GVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 210 TPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVnADPRLAAVVFTGSTRVFTEINKNVFS 288
Cdd:cd07139 159 APALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLV-RHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 289 RLEtyhnfpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQP 368
Cdd:cd07139 238 RLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 369 DDFQSFMCAVIDETSFNKNKKYIEIAKADSsnYEVVVGGK--CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVY 446
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIAKGRAEG--ARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009572 447 DDskpgywkeVCELV----DSttKYGLTGAVFSRERApiREADKYLRYAAGNYYVNdkctGAVVG-QQPFGGSRLSG 518
Cdd:cd07139 390 DD--------EDDAVrianDS--DYGLSGSVWTADVE--RGLAVARRIRTGTVGVN----GFRLDfGAPFGGFKQSG 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
67-518 |
2.45e-57 |
|
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: 198.14 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 67 GIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEI 146
Cdd:cd07106 1 VINPATGEV-FASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIE-ANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 147 DcVAEACDFIRwniHFAEelYAQQPRSVS-NSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSP 224
Cdd:cd07106 79 E-VGGAVAWLR---YTAS--LDLPDEVIEdDDTRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 225 TAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpRISGETG 304
Cdd:cd07106 152 FTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 305 GKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSF 384
Cdd:cd07106 224 GNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 385 NKNKKYIEIAKAdsSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSt 464
Cdd:cd07106 304 DKVKELVEDAKA--KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE-----DEVIARAND- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 465 TKYGLTGAVFS--RERApIREADkylRYAAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07106 376 SEYGLGASVWSsdLERA-EAVAR---RLEAGTVWIN--THGALDPDAPFGGHKQSG 425
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
54-518 |
3.46e-57 |
|
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: 198.26 E-value: 3.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRA 131
Cdd:cd07088 2 INGEfvPSSSGETIDVLNPATGEV-VATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI-RENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATMLGQSKNPWQAEIDcVAEACDFIRWnihfaeelYAQQPRSVSNSGVWNTtdyRPLE---------GFVSAITPFNFTA 202
Cdd:cd07088 80 LIVEEQGKTLSLARVE-VEFTADYIDY--------MAEWARRIEGEIIPSD---RPNEnififkvpiGVVAGILPWNFPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 203 --IAANLAgtPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVF 279
Cdd:cd07088 148 flIARKLA--PALVtGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 TEINKNVFSrletyhNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:cd07088 226 QKIMEAAAE------NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTR-GYFVEPTIIETKDPRAQLMREEIFG 438
Cdd:cd07088 300 MKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGA--TLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 439 PVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRYaaGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07088 378 PVLPVVKFSS-----LDEAIELAND-SEYGLTSYIYTENLNTAMRATNELEF--GETYIN--RENFEAMQGFHAGWKKSG 447
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
77-518 |
4.31e-57 |
|
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: 197.96 E-value: 4.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 77 IAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTkyRHEMRAATMLGQSKNPWQaeiDCVAEACDFI 156
Cdd:cd07145 12 IDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIER--RKEELAKLLTIEVGKPIK---QSRVEVERTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 157 RWNIHFAEE---LYAQQPRS---VSNSGVWNTTDYRPLeGFVSAITPFNFTA------IAANLAgtpalMGNTVVWKPSP 224
Cdd:cd07145 87 RLFKLAAEEakvLRGETIPVdayEYNERRIAFTVREPI-GVVGAITPFNFPAnlfahkIAPAIA-----VGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 225 TAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhnFPRISGETG 304
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 305 GKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSF 384
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 385 NKNKKYieIAKADSSNYEVVVGGKcdKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDSt 464
Cdd:cd07145 315 ERMENL--VNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD-----DEEAVEIANS- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009572 465 TKYGLTGAVFSRErapIREAdkyLRYA----AGNYYVNDKcTGAVVGQQPFGGSRLSG 518
Cdd:cd07145 385 TEYGLQASVFTND---INRA---LKVAreleAGGVVINDS-TRFRWDNLPFGGFKKSG 435
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
51-518 |
2.16e-56 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 196.25 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 51 PIMIGGKPYTSSNIIKGIM-PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQ-VPFRDRAAIFYKAAHLLStKYRHE 128
Cdd:cd07082 3 KYLINGEWKESSGKTIEVYsPIDGEV-IGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLK-ENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 129 MRAATML--GQSKNPWQAEIDcvaEACDFIRWNIHFAEELYAQQPRSVSNSGVWNTTD--YR-PLeGFVSAITPFNFtai 203
Cdd:cd07082 81 VANLLMWeiGKTLKDALKEVD---RTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAqvRRePL-GVVLAIGPFNY--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 204 AANLAGT---PAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVF 279
Cdd:cd07082 154 PLNLTVSkliPALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 TEINKNvfsrletyHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:cd07082 234 NRLKKQ--------HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKcdKTRGYFVEPTIIETKDPRAQLMREEIFGP 439
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGA--TVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 440 VLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCtgavvgQQ-----PFGGS 514
Cdd:cd07082 382 VLPIIRVNDI-----EEAIELANK-SNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGR 447
|
....
gi 398009572 515 RLSG 518
Cdd:cd07082 448 KDSG 451
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
68-518 |
3.08e-56 |
|
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: 195.67 E-value: 3.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQSKNPWQAEID 147
Cdd:cd07107 2 INPATGQV-LARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRL--REHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 148 CVAEACDFIRWNIHFAEELYAQQPRSVSNSgvWNTTDYRPLeGFVSAITPFNFTAI-AANLAGTPALMGNTVVWKPSPTA 226
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRN--LHYTLREPY-GVVARIVAFNHPLMfAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 227 VLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpRISGETGGK 306
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 307 DFHLVHPSADMKHVAAGTVRGA-FEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFN 385
Cdd:cd07107 229 NALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 386 KNKKYIEIAKADSSnyEVVVGGKCDKT----RGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELV 461
Cdd:cd07107 309 RVMHYIDSAKREGA--RLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE-----AEMVAQA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009572 462 DStTKYGLTGAVFSRE-RAPIREADkylRYAAGNYYVNDKCT---GAvvgqqPFGGSRLSG 518
Cdd:cd07107 382 NG-VEYGLTAAIWTNDiSQAHRTAR---RVEAGYVWINGSSRhflGA-----PFGGVKNSG 433
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
83-524 |
7.30e-54 |
|
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: 189.04 E-value: 7.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 83 ATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStkyRHEMRAATML----GQSKNPWQAEIDCVAEACdfirw 158
Cdd:cd07152 10 ADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE---EHADEIADWIvresGSIRPKAGFEVGAAIGEL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 159 niHFAEELyAQQPRSV---SNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSP-TAVLSNYLM 233
Cdd:cd07152 82 --HEAAGL-PTQPQGEilpSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDPrTPVSGGVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 234 YKIMEEAGLPAGVINFVPCEPAVMDsAVNADPRLAAVVFTGSTRVFTEINKNVfSRletyhNFPRISGETGGKDFHLVHP 313
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGE-ALVEDPNVAMISFTGSTAVGRKVGEAA-GR-----HLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 314 SADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEI 393
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 394 AKADSSnyEVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAV 473
Cdd:cd07152 311 SVAAGA--RLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD-----EEAVALAND-TEYGLSAGI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398009572 474 FSR--ERApIREADKyLRyaAGNYYVNDKcTGAVVGQQPFGGSRLSGSNDKPG 524
Cdd:cd07152 380 ISRdvGRA-MALADR-LR--TGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
73-518 |
1.54e-53 |
|
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: 188.32 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 73 HQVQIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPWQA--EIDc 148
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 149 vaEACDFIRWNIHFAEELYAQQPRSVSnSGVWNTTDYRPLeGFVSAITPFNFT----------AIAAnlagtpalmGNTV 218
Cdd:cd07118 84 --GAADLWRYAASLARTLHGDSYNNLG-DDMLGLVLREPI-GVVGIITPWNFPflilsqklpfALAA---------GCTV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 219 VWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpR 298
Cdd:cd07118 151 VVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK------K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 299 ISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAV 378
Cdd:cd07118 225 VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 IDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTR-GYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEV 457
Cdd:cd07118 305 INEAQLAKITDYVDAGRAEGA--TLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTV-----DEA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009572 458 CELVDSTTkYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAVvgQQPFGGSRLSG 518
Cdd:cd07118 378 IALANDTV-YGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-518 |
3.98e-53 |
|
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: 187.45 E-value: 3.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWS-QVPFRDRAAIFYKAAHLLsTKYRHEMRAATMlgqsknpwqAEI 146
Cdd:cd07089 2 INPATEEV-IGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEAL-EARKEELRALLV---------AEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 147 DC---------VAEACDFIRWNIHFAEELYAQQPRSVSNSGVWNTT---DYRPLeGFVSAITPFNFtAIAANLAGT-PAL 213
Cdd:cd07089 71 GApvmtaramqVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvRREPV-GVVAAITPWNF-PFFLNLAKLaPAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 214 -MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEt 292
Cdd:cd07089 149 aAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 293 yhnfpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQ 372
Cdd:cd07089 228 -----RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 373 SFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGK----CDKtrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDD 448
Cdd:cd07089 303 TVMGPLISAAQRDRVEGYIARGRDEGA--RLVTGGGrpagLDK--GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDD 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009572 449 SkpgywKEVCELVDStTKYGLTGAVFSR--ERApIREAdkyLRYAAGNYYVNdkcTGAVVG-QQPFGGSRLSG 518
Cdd:cd07089 379 D-----DEAVRIAND-SDYGLSGGVWSAdvDRA-YRVA---RRIRTGSVGIN---GGGGYGpDAPFGGYKQSG 438
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-518 |
3.87e-52 |
|
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: 184.43 E-value: 3.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPWQAEID 147
Cdd:cd07090 2 IEPATGEV-LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 148 CVAEACDFirwnihfaeELYAQQPRSVSNS------GVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVW 220
Cdd:cd07090 80 IDSSADCL---------EYYAGLAPTLSGEhvplpgGSFAYTRREPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 221 KPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpRIS 300
Cdd:cd07090 150 KPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 301 GETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVID 380
Cdd:cd07090 223 LELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 381 ETSFNKNKKYIEIAKADSSnyEVVVGG-----KCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywK 455
Cdd:cd07090 303 EEHLEKVLGYIESAKQEGA--KVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTE-----E 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 456 EVCELVDSTTkYGLTGAVFSRErapIREADKYL-RYAAGNYYVNDKCTGAVvgQQPFGGSRLSG 518
Cdd:cd07090 376 EVIRRANDTT-YGLAAGVFTRD---LQRAHRVIaQLQAGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
54-518 |
4.59e-52 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 184.95 E-value: 4.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYT--SSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASK-EWSQVPFRDRAAIFYKAAHLLStKYRHEMR 130
Cdd:cd07113 4 IDGRPVAgqSEKRLDITNPATEQV-IASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIE-QHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 131 AATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQ--QPRSVSNSGVWNT--TDYRPLeGFVSAITPFNFTAIAAN 206
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGEtlAPSIPSMQGERYTafTRREPV-GVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 207 LAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEINKN 285
Cdd:cd07113 161 WKIGAALAtGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 286 VFSRLEtyhnfpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKM 365
Cdd:cd07113 240 AASDLT------RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 366 GQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFV 445
Cdd:cd07113 314 GSPMDESVMFGPLANQPHFDKVCSYLDDARAEGD--EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 446 YDDSKpgywkevcELVD--STTKYGLTGAVFSRERApireadKYLRYA----AGNYYVNDKC--TGAVvgqqPFGGSRLS 517
Cdd:cd07113 392 YEDEE--------ELIQliNDTPFGLTASVWTNNLS------KALRYIprieAGTVWVNMHTflDPAV----PFGGMKQS 453
|
.
gi 398009572 518 G 518
Cdd:cd07113 454 G 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
91-525 |
6.04e-51 |
|
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: 180.55 E-value: 6.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 91 AVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPW--QAEIDCVAEACDFirwnihfaeELYA 168
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKAN-KEELARLISRETGKPLWeaQTEVAAMAGKIDI---------SIKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 169 QQ----PRSVSNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLP 243
Cdd:cd07095 75 YHertgERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 244 AGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEINKnvfsrlETYHNFPRISG-ETGGKDFHLVHPSADMKHVAA 322
Cdd:cd07095 154 PGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHR------QFAGRPGKILAlEMGGNNPLVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 323 GTVRGAFEFQGQKCSACSRLYAPKTCW-KELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSny 401
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGG-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 402 EVVVGGKCDKTRGYFVEPTIIETKDPrAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERAPI 481
Cdd:cd07095 305 EPLLAMERLVAGTAFLSPGIIDVTDA-ADVPDEEIFGPLLQVYRYDD-----FDEAIALANA-TRFGLSAGLLSDDEALF 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 398009572 482 REAdkYLRYAAGNYYVNDKCTGAvVGQQPFGGSRLSGsNDKPGA 525
Cdd:cd07095 378 ERF--LARIRAGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
70-518 |
8.93e-51 |
|
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: 180.90 E-value: 8.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEIDcV 149
Cdd:cd07147 6 PYTGEV-VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE-ERFEELAETIVLEAGKPIKDARGE-V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 150 AEACDFIRWNIHFAEELYAQQPR---SVSNSGVWNTTDYRPLeGFVSAITPFNFtaiAANLAG---TPAL-MGNTVVWKP 222
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQGLVRRFPI-GPVSAITPFNF---PLNLVAhkvAPAIaAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 223 SPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNaDPRLAAVVFTGSTRVFTEINKNVFSRletyhnfpRISGE 302
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVT-DERIKLLSFTGSPAVGWDLKARAGKK--------KVVLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 303 TGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDET 382
Cdd:cd07147 230 LGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 383 SFNKNKKYIEiaKADSSNYEVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVD 462
Cdd:cd07147 310 EAERVEGWVN--EAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDD-----FDEALAAVN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 463 StTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAvVGQQPFGGSRLSG 518
Cdd:cd07147 380 D-SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
70-518 |
2.04e-50 |
|
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: 179.74 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKE-WSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEIDC 148
Cdd:cd07109 4 PSTGEV-FARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIR-EHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 149 VAEACDFirwnihfaeELYAQQPRSVS------NSGVWNTTDYRPLeGFVSAITPFNFTA-IAANLAGtPAL-MGNTVVW 220
Cdd:cd07109 82 EAAARYF---------EYYGGAADKLHgetiplGPGYFVYTVREPH-GVTGHIIPWNYPLqITGRSVA-PALaAGNAVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 221 KPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKnvfsrlETYHNFPRIS 300
Cdd:cd07109 151 KPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMR------AAAENVVPVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 301 GETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMG----QPDdfqsfMC 376
Cdd:cd07109 225 LELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpgleDPD-----LG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 377 AVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTR---GYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgy 453
Cdd:cd07109 300 PLISAKQLDRVEGFVARARARGA--RIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398009572 454 wKEVCELVDStTKYGLTGAVFSrerapiREADKYLRYA----AGNYYVNDKCTGAVVgQQPFGGSRLSG 518
Cdd:cd07109 374 -AEAIALANG-TDYGLVAGVWT------RDGDRALRVArrlrAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
68-518 |
3.20e-50 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 179.47 E-value: 3.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATMLGQSKNPWQAEID 147
Cdd:cd07110 2 INPATEAT-IGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGV-RERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 148 cVAEACDFIRWNIHFAEELYAQQPRSVS--NSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSP 224
Cdd:cd07110 80 -VDDVAGCFEYYADLAEQLDAKAERAVPlpSEDFKARVRREPV-GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 225 TAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKnvfsrlETYHNFPRISGETG 304
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQ------AAAQDIKPVSLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 305 GKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSF 384
Cdd:cd07110 232 GKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 385 NKNKKYIEIAKADSSnyEVVVGGK--CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVD 462
Cdd:cd07110 312 EKVLSFIARGKEEGA--RLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE-----DEAIALAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 463 StTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07110 385 D-SEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
58-518 |
5.60e-50 |
|
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: 179.53 E-value: 5.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 58 PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKE-WSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLG 136
Cdd:cd07144 18 KSSDGETIKTVNPSTGEV-IASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVE-KNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 137 QSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQQPRSVSNSGVWntTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-G 215
Cdd:cd07144 96 SGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAY--TLHEPY-GVCGQIIPWNYPLAMAAWKLAPALAaG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 216 NTVVWKPSPTAVLSnyLMY--KIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSrlety 293
Cdd:cd07144 173 NTVVIKPAENTPLS--LLYfaNLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 294 hNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQI-KMGQPDDFQ 372
Cdd:cd07144 246 -NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 373 SFMCAVIDETSFNKNKKYIEIAKadSSNYEVVVGG---KCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVfvyddS 449
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGK--KEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVI-----S 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009572 450 KPGYWKEVCELVDSTTkYGLTGAVFSRErapIREADKYLR-YAAGNYYVN---DKCTGAvvgqqPFGGSRLSG 518
Cdd:cd07144 398 KFKTYEEAIKKANDTT-YGLAAAVFTKD---IRRAHRVAReLEAGMVWINssnDSDVGV-----PFGGFKMSG 461
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
82-518 |
1.39e-49 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 177.41 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 82 NATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstkYRHEMRAATML----GQSKNPWQAEIDCVAEACDFIR 157
Cdd:cd07099 14 VTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRAL---ADHADELAELLhaetGKPRADAGLEVLLALEAIDWAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 158 WNihfAEELYAQQPRSVSN--SGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMY 234
Cdd:cd07099 91 RN---APRVLAPRKVPTGLlmPNKKATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 235 KIMEEAGLPAGVINFVpcepaVMDSAVNA---DPRLAAVVFTGSTRVFTEINKNVFSRLetyhnFPrISGETGGKDFHLV 311
Cdd:cd07099 167 EAWAAAGPPQGVLQVV-----TGDGATGAaliDAGVDKVAFTGSVATGRKVMAAAAERL-----IP-VVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 312 HPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDEtsfnknkKYI 391
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTA-------RQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 392 EIAK-----ADSSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTK 466
Cdd:cd07099 309 DIVRrhvddAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE-----DEAIALAND-SR 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398009572 467 YGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07099 383 YGLSASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
77-518 |
2.47e-49 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 176.85 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 77 IAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQSKNPWQAEIDCVAEACDFI 156
Cdd:cd07094 12 IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLL--KKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 157 RWNIHFAEELYAQQ---PRSVSNSGVWNTTDYRPLeGFVSAITPFNF--TAIAANLAgtPAL-MGNTVVWKPSPTAVLSN 230
Cdd:cd07094 90 RLAAEEAERIRGEEiplDATQGSDNRLAWTIREPV-GVVLAITPFNFplNLVAHKLA--PAIaTGCPVVLKPASKTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 231 YLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVfsrletyhNFPRISGETGGKDFHL 310
Cdd:cd07094 167 LELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA--------GGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 311 VHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKY 390
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 391 IEiaKADSSNYEVVVGGKCDKTrgyFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLT 470
Cdd:cd07094 319 VE--EAVEAGARLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDD-----FEEAIRIANS-TDYGLQ 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 398009572 471 GAVFSRERAPIREADKYLRyaAGNYYVNDKcTGAVVGQQPFGGSRLSG 518
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLE--VGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
63-518 |
2.73e-49 |
|
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: 177.34 E-value: 2.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 63 NIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEA-SKEWS-QVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKN 140
Cdd:cd07143 22 GTVKVYNPSTGKL-ITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLME-RNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 141 -PWQAEIDcVAEACDFIRWNIHFAEELYAQQPRSvsNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTV 218
Cdd:cd07143 100 fGTAKRVD-VQASADTFRYYGGWADKIHGQVIET--DIKKLTYTRHEPI-GVCGQIIPWNFPLLMCAWKIAPALAaGNTI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 219 VWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhNFPR 298
Cdd:cd07143 176 VLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 299 ISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAV 378
Cdd:cd07143 251 VTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 IDETSFNKNKKYIEIAKADSSNyeVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVC 458
Cdd:cd07143 331 VSQIQYERIMSYIESGKAEGAT--VETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE-----EEAI 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009572 459 ELVDSTTkYGLTGAVFSRE--RApIREADKylrYAAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07143 404 KRANDST-YGLAAAVFTNNinNA-IRVANA---LKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
52-518 |
3.97e-48 |
|
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: 174.18 E-value: 3.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 52 IMIGGKPYTSSN--IIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEM 129
Cdd:cd07117 3 LFINGEWVKGSSgeTIDSYNPANGET-LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 130 RAATM-----LGQSKNpwqaeIDcVAEACDFIRWnihFAEELYAQQPRSVS-NSGVWNTTDYRPLeGFVSAITPFNFTAI 203
Cdd:cd07117 82 MVETLdngkpIRETRA-----VD-IPLAADHFRY---FAGVIRAEEGSANMiDEDTLSIVLREPI-GVVGQIIPWNFPFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 204 AANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEI 282
Cdd:cd07117 152 MAAWKLAPALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 283 NKNVFSRLetyhnFPRiSGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQ 362
Cdd:cd07117 231 AIAAAKKL-----IPA-TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 363 IKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGK------CDKtrGYFVEPTIIETKDPRAQLMREEI 436
Cdd:cd07117 305 VKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGA--KILTGGHrltengLDK--GFFIEPTLIVNVTNDMRVAQEEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 437 FGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSrerapiREADKYLRYA----AGNYYVNdkCTGAVVGQQPFG 512
Cdd:cd07117 381 FGPVATVIKFKTE-----DEVIDMAND-SEYGLGGGVFT------KDINRALRVAraveTGRVWVN--TYNQIPAGAPFG 446
|
....*.
gi 398009572 513 GSRLSG 518
Cdd:cd07117 447 GYKKSG 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
84-540 |
1.55e-47 |
|
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: 172.11 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 84 TPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAaHLLSTKYRHEMRAATMLGQSKNPWQA--EIDCVAEACdfiRWNIH 161
Cdd:cd07101 16 TPADVEAAFARARAAQRAWAARPFAERAAVFLRF-HDLVLERRDELLDLIQLETGKARRHAfeEVLDVAIVA---RYYAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 162 FAEELYAQQPRSVSNSGVWNTTDYRPLEGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEA 240
Cdd:cd07101 92 RAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLaGNAVVLKPDSQTALTALWAVELLIEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 241 GLPAGVINFVPCEPAVMDSAV--NADprlaAVVFTGSTRVFTEINKNVFSRLETYhnfpriSGETGGKDFHLVHPSADMK 318
Cdd:cd07101 172 GLPRDLWQVVTGPGSEVGGAIvdNAD----YVMFTGSTATGRVVAERAGRRLIGC------SLELGGKNPMIVLEDADLD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 319 HVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADS 398
Cdd:cd07101 242 KAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 399 SnyEVVVGGKCDKTRG-YFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSRE 477
Cdd:cd07101 322 A--TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD-----DEAIELAND-TDYGLNASVWTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 478 RAPIREADKYLRyaAGNYYVNDKCTGAVVG-QQPFGGSRLSGSNDKPGAgQFVTRFVSARSIKE 540
Cdd:cd07101 394 GARGRRIAARLR--AGTVNVNEGYAAAWASiDAPMGGMKDSGLGRRHGA-EGLLKYTETQTVAV 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
60-518 |
7.49e-47 |
|
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: 170.56 E-value: 7.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 60 TSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTkyRHE---MRAATMLG 136
Cdd:cd07151 7 TSERTIDVLNPYTGET-LAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEE--RRDeivEWLIRESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 137 QSKNPWQAEIDCVAEacdFIRWNIHFAEELYAQqprsVSNSGVWNTTD--YRPLEGFVSAITPFNFTAIAANLAGTPAL- 213
Cdd:cd07151 84 STRIKANIEWGAAMA---ITREAATFPLRMEGR----ILPSDVPGKENrvYREPLGVVGVISPWNFPLHLSMRSVAPALa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 214 MGNTVVWKP-SPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPA-VMDSAV-NADPRLaaVVFTGSTRVFTEInknvfSRL 290
Cdd:cd07151 157 LGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSeIGDAFVeHPVPRL--ISFTGSTPVGRHI-----GEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 291 ETYHnFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDD 370
Cdd:cd07151 230 AGRH-LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 371 FQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDktrGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSk 450
Cdd:cd07151 309 PDTVVGPLINESQVDGLLDKIEQAVEEGA--TLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009572 451 pgywKEVCELVDStTKYGLTGAVFSR--ERApIREADkylRYAAGNYYVNDKctgaVVGQQP---FGGSRLSG 518
Cdd:cd07151 383 ----EEALELAND-TEYGLSGAVFTSdlERG-VQFAR---RIDAGMTHINDQ----PVNDEPhvpFGGEKNSG 442
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
54-518 |
1.24e-46 |
|
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: 170.22 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYTSSN--IIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRA 131
Cdd:cd07559 5 INGEWVAPSKgeYFDNYNPVNGKV-LCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATM-----LGQSKNpwqaeIDcVAEACDFIRWnihFAEELYAQqprsvsnSGVWNTTD--------YRPLeGFVSAITPF 198
Cdd:cd07559 84 ETLdngkpIRETLA-----AD-IPLAIDHFRY---FAGVIRAQ-------EGSLSEIDedtlsyhfHEPL-GVVGQIIPW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 199 NFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTR 277
Cdd:cd07559 147 NFPLLMAAWKLAPALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 278 VFTEINKNVFSRLetyhnFPrISGETGGKDFHLVHPSADMKHV----AAGTVRGAFEF-QGQKCSACSRLYAPKTCWKEL 352
Cdd:cd07559 226 VGRLIMQYAAENL-----IP-VTLELGGKSPNIFFDDAMDADDdfddKAEEGQLGFAFnQGEVCTCPSRALVQESIYDEF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 353 KALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGK------CDKtrGYFVEPTIIETKD 426
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGA--EVLTGGErltlggLDK--GYFYEPTLIKGGN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 427 PRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSrerapiREADKYLRYA----AGNYYVNdkCT 502
Cdd:cd07559 376 NDMRIFQEEIFGPVLAVITFKDE-----EEAIAIAND-TEYGLGGGVWT------RDINRALRVArgiqTGRVWVN--CY 441
|
490
....*....|....*.
gi 398009572 503 GAVVGQQPFGGSRLSG 518
Cdd:cd07559 442 HQYPAHAPFGGYKKSG 457
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
85-525 |
2.31e-46 |
|
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: 168.69 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 85 PELARKAVEAAVEASKEWSQVPFR-DRAAIFYKAAHLLsTKYRHEMraATML----GQSKNPWQAEIDcvaEACDFIRWN 159
Cdd:cd07146 16 PAGTEEALREALALAASYRSTLTRyQRSAILNKAAALL-EARREEF--ARLItlesGLCLKDTRYEVG---RAADVLRFA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 160 ihfAEELYAQQPRSVSnSGVWNTTDYR-------PLeGFVSAITPFNF--TAIAANLAgtPALM-GNTVVWKPSPTAVLS 229
Cdd:cd07146 90 ---AAEALRDDGESFS-CDLTANGKARkiftlrePL-GVVLAITPFNHplNQVAHKIA--PAIAaNNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 230 NYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhnfpRISGETGGKDFH 309
Cdd:cd07146 163 AIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 310 LVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKK 389
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 390 YIEIAKADSSnyEVVVGGkcdKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGL 469
Cdd:cd07146 315 RVEEAIAQGA--RVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL-----DEAIAISNS-TAYGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 470 TGAVFSRERAPIREADKYLRYAAGNyyVNDKcTGAVVGQQPFGGSRLSGSNDKPGA 525
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVN--VNEV-PGFRSELSPFGGVKDSGLGGKEGV 436
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
83-518 |
4.99e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 169.29 E-value: 4.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 83 ATPELARKAVEAAVEASKEWSQVPFRDRAAIFyKAAHLLSTKYRHEMRAATMLGQSKNPWQA--EIDCVAEACdfiRWNI 160
Cdd:PRK09407 51 STAADVEAAFARARAAQRAWAATPVRERAAVL-LRFHDLVLENREELLDLVQLETGKARRHAfeEVLDVALTA---RYYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 161 HFAEELYAQQPRSVSNSGVWNTTDYRPLEGFVSAITPFNF---TAIAANLagtPALM-GNTVVWKP-SPTAvLSNYLMYK 235
Cdd:PRK09407 127 RRAPKLLAPRRRAGALPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTP-LTALAAVE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 236 IMEEAGLPAGVINFVPCEPAVMDSAV--NADprlaAVVFTGSTRVFTEINKNVFSRLETYhnfpriSGETGGKDFHLVHP 313
Cdd:PRK09407 203 LLYEAGLPRDLWQVVTGPGPVVGTALvdNAD----YLMFTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 314 SADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEI 393
Cdd:PRK09407 273 DADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 394 AKADSSnyEVVVGGKCDKTRG-YFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTkYGLTGA 472
Cdd:PRK09407 353 AVAKGA--TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV-----DEAVERANDTP-YGLNAS 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398009572 473 VFSRERAPIREADKYLRyaAGNYYVNDKCT---GAVvgQQPFGGSRLSG 518
Cdd:PRK09407 425 VWTGDTARGRAIAARIR--AGTVNVNEGYAaawGSV--DAPMGGMKDSG 469
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
55-519 |
4.05e-45 |
|
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: 165.84 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 55 GGKPYTSSNiikgimPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATM 134
Cdd:cd07130 10 GGGVVTSIS------PANGEP-IARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDAL-RKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 135 L--GQSKNPWQAEIDCVAEACDFirwnihfAEELYAQQPRSVSNS--------GVWNttdyrPLeGFVSAITPFNF---- 200
Cdd:cd07130 82 LemGKILPEGLGEVQEMIDICDF-------AVGLSRQLYGLTIPSerpghrmmEQWN-----PL-GVVGVITAFNFpvav 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 201 ----TAIAAnlagtpaLMGNTVVWKPSPTAVLSNYLMYKIMEEA----GLPAGVINFVpCEPAVMDSAVNADPRLAAVVF 272
Cdd:cd07130 149 wgwnAAIAL-------VCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLV-CGGADVGEALVKDPRVPLVSF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 273 TGSTRVFTEINKNVFSRletyhnFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKEL 352
Cdd:cd07130 221 TGSTAVGRQVGQAVAAR------FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 353 KALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKdPRAQLM 432
Cdd:cd07130 295 LERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGG--TVLFGGKVIDGPGNYVEPTIVEGL-SDAPIV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 433 REEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRErapIREADKYLRyAAG------NyyVNDKCTGAVV 506
Cdd:cd07130 372 KEETFAPILYVLKFDT-----LEEAIAWNNE-VPQGLSSSIFTTD---LRNAFRWLG-PKGsdcgivN--VNIGTSGAEI 439
|
490
....*....|....*...
gi 398009572 507 -----GQQPFGGSRLSGS 519
Cdd:cd07130 440 ggafgGEKETGGGRESGS 457
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
50-443 |
6.80e-45 |
|
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: 165.38 E-value: 6.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 50 CPIMIGGKPYTSSN--IIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRH 127
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEV-IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL-EENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 128 EMRAATMLGQSKNPWQAE------IDCVAEACDfirwnihfAEELYAQQPRSVSNSGVWNTTDYRPLeGFVSAITPFNF- 200
Cdd:cd07085 79 ELARLITLEHGKTLADARgdvlrgLEVVEFACS--------IPHLLKGEYLENVARGIDTYSYRQPL-GVVAGITPFNFp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 201 ---------TAIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDsAVNADPRLAAVV 271
Cdd:cd07085 150 amiplwmfpMAIAC---------GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 272 FTGSTRVFTEInknvfsrletYH----NFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKT 347
Cdd:cd07085 220 FVGSTPVGEYI----------YEraaaNGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 348 CWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKT----RGYFVEPTIIE 423
Cdd:cd07085 290 EADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGA--KLVLDGRGVKVpgyeNGNFVGPTILD 367
|
410 420
....*....|....*....|
gi 398009572 424 TKDPRAQLMREEIFGPVLTV 443
Cdd:cd07085 368 NVTPDMKIYKEEIFGPVLSI 387
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
68-479 |
7.90e-45 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 164.34 E-value: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVQIAKAYnATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKA-AHLLSTKYRHEMRAATMLG----QSKNpw 142
Cdd:cd07102 1 ISPIDGSVIAERPL-ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAANTDEIAEELTWQMGrpiaQAGG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 143 qaEIDCVAEACDFIrwnIHFAEELYAQQPrsVSNS-GVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVW 220
Cdd:cd07102 78 --EIRGMLERARYM---ISIAEEALADIR--VPEKdGFERYIRREPL-GVVLIIAPWNYPYLTAVNAVIPALLaGNAVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 221 KPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMdSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhnFPRIS 300
Cdd:cd07102 150 KHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETS-AALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 301 GETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVID 380
Cdd:cd07102 223 LELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 381 ETSFNKNKKYIEIAKADSSnyEVVVGGK---CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVF-VYDDSkpgywkE 456
Cdd:cd07102 303 ARAADFVRAQIADAIAKGA--RALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMkVKSDA------E 374
|
410 420
....*....|....*....|....
gi 398009572 457 VCELV-DSttKYGLTGAVFSRERA 479
Cdd:cd07102 375 AIALMnDS--EYGLTASVWTKDIA 396
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
90-518 |
1.07e-44 |
|
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: 163.79 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 90 KAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATM-----LGQSKnpwqAEIDCVAEACDFIRWNihfAE 164
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLemgkpIAEAR----AEVEKCAWICRYYAEN---AE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 165 ELYAQQPRSVSNSGVWNTtdYRPLeGFVSAITPFNFTA-----IAAnlagtPALM-GNTVVWKPSPTAVLSNYLMYKIME 238
Cdd:cd07100 76 AFLADEPIETDAGKAYVR--YEPL-GVVLGIMPWNFPFwqvfrFAA-----PNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 239 EAGLPAGVINFVPCEPAVMDSAVnADPRLAAVVFTGSTRVFT--------EINKNVFsrletyhnfprisgETGGKDFHL 310
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRavaaeagkNLKKSVL--------------ELGGSDPFI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 311 VHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKY 390
Cdd:cd07100 213 VLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 391 IEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTkYGLT 470
Cdd:cd07100 293 VEEAVAAGA--TLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE-----EEAIALANDSP-FGLG 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398009572 471 GAVFSRERAPIREADKYLRyaAGNYYVNDkctgaVVGQQ---PFGGSRLSG 518
Cdd:cd07100 365 GSVFTTDLERAERVARRLE--AGMVFING-----MVKSDprlPFGGVKRSG 408
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
68-518 |
1.57e-44 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 164.91 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEA-----SKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATM-LGQSKNP 141
Cdd:PLN02467 28 VNPATEET-IGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLdCGKPLDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 142 WQAEIDCVAEACDFIrwnIHFAEELYAQQ--PRSVSNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTV 218
Cdd:PLN02467 107 AAWDMDDVAGCFEYY---ADLAEALDAKQkaPVSLPMETFKGYVLKEPL-GVVGLITPWNYPLLMATWKVAPALAaGCTA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 219 VWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGST----RVFTEINKNVfsrletyh 294
Cdd:PLN02467 183 VLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTatgrKIMTAAAQMV-------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 295 nfPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSF 374
Cdd:PLN02467 255 --KPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 375 MCAVIDETSFNKNKKYIEIAKadSSNYEVVVGGKCDK--TRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpg 452
Cdd:PLN02467 333 LGPVVSEGQYEKVLKFISTAK--SEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 453 ywKEVCELVDSTTkYGLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:PLN02467 408 --DEAIELANDSH-YGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
76-518 |
1.59e-44 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 163.65 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 76 QIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAatmlgQSKN---PWQAEI-DCVAE 151
Cdd:cd07092 9 EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAAL-----ESRNtgkPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 152 ACDFIRWnihFAEELYAQQPRSvSNSGVWNTTDY---RPLeGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSPTAV 227
Cdd:cd07092 84 AVDNFRF---FAGAARTLEGPA-AGEYLPGHTSMirrEPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 228 LSNYLMYKIMEEaGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLETYHNfprisgETGGKD 307
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL------ELGGKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 308 FHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKN 387
Cdd:cd07092 232 PVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 388 KKYIEIAKADSsnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKY 467
Cdd:cd07092 312 AGFVERAPAHA---RVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE-----DEAIELAND-VEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398009572 468 GLTGAVFSRERAPIREADKYLRYaaGNYYVNDKctGAVVGQQPFGGSRLSG 518
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDF--GTVWVNTH--IPLAAEMPHGGFKQSG 429
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
70-518 |
1.61e-44 |
|
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: 163.67 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 70 PSDHQVqIAKAYNATPELARKAVEAAVEASKE--WSQVPfRDRAAIFYKAAHLLStkyRHEMRAATML----GQSKNPWQ 143
Cdd:cd07120 4 PATGEV-IGTYADGGVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE---ANAERLARLLalenGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 144 AEID-CVAEacdfIRWNIHFAEELY--AQQPRSvsnsGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVV 219
Cdd:cd07120 79 FEISgAISE----LRYYAGLARTEAgrMIEPEP----GSFSLVLREPM-GVAGIIVPWNSPVVLLVRSLAPALAaGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 220 WKPSPTAVLSNYLMYKIMEEA-GLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpR 298
Cdd:cd07120 150 VKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK------R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 299 ISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAV 378
Cdd:cd07120 224 LGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 IDETSFNKNKKYIEIAKADSSnyEVVV-GGKCDK--TRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywK 455
Cdd:cd07120 304 IDRANVDRVDRMVERAIAAGA--EVVLrGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDE-----A 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009572 456 EVCELVDStTKYGLTGAVFSrerapiREADKYLRYA----AGNYYVNDKctGAVVGQQPFGGSRLSG 518
Cdd:cd07120 377 EAVALAND-TDYGLAASVWT------RDLARAMRVArairAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
54-518 |
1.70e-43 |
|
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: 161.36 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYTSSNiikgimPSDHQV--QIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStkyRHEMRA 131
Cdd:cd07141 19 VSGKTFPTIN------PATGEKicEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIE---RDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATM--LGQSKnPWQ--AEIDcVAEACDFIRWNIHFAEELYAqqpRSVSNSG-VWNTTDYRPLeGFVSAITPFNFTAIAAN 206
Cdd:cd07141 90 ASLetLDNGK-PFSksYLVD-LPGAIKVLRYYAGWADKIHG---KTIPMDGdFFTYTRHEPV-GVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 207 LAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKN 285
Cdd:cd07141 164 WKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 286 VFSRletyhNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKM 365
Cdd:cd07141 244 AGKS-----NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 366 GQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIE--TKDPRaqLMREEIFGPVLTV 443
Cdd:cd07141 319 GNPFDPKTEQGPQIDEEQFKKILELIESGKKEGA--KLECGGKRHGDKGYFIQPTVFSdvTDDMR--IAKEEIFGPVQQI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 444 FVYddskpgywKEVCELVD--STTKYGLTGAVFSRErapIREADKY---LRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:cd07141 395 FKF--------KTIDEVIEraNNTTYGLAAAVFTKD---IDKAITFsnaLR--AGTVWVN--CYNVVSPQAPFGGYKMSG 459
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
55-519 |
1.02e-42 |
|
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: 159.48 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 55 GGKPYTSSNiikgimPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStkyRHEMRAATM 134
Cdd:cd07111 35 NRKSFPTIN------PATGEV-LASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQ---KHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 135 --LGQSKnPWQAEIDC-VAEAcdfIRWNIHFA-------EELYAQQPrsvsnsgvwnttdyrplEGFVSAITPFNFTAIA 204
Cdd:cd07111 105 esLDNGK-PIRESRDCdIPLV---ARHFYHHAgwaqlldTELAGWKP-----------------VGVVGQIVPWNFPLLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 205 ANLAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEIn 283
Cdd:cd07111 164 LAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRAL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 284 knvfsRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQI 363
Cdd:cd07111 242 -----RRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 364 KMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTV 443
Cdd:cd07111 317 RVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGA--DVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009572 444 FVYDDSkpgywKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSGS 519
Cdd:cd07111 395 LTFRTA-----KEAVALANN-TPYGLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGF 460
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
88-550 |
1.84e-42 |
|
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: 157.35 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 88 ARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMlgqsknpwqAEIDCVAEacdFIRWNIHFAEEL- 166
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLE-SRRDEFIEAMM---------EETGATAA---WAGFNVDLAAGMl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 167 --YAQQPRSV-------SNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKI 236
Cdd:cd07105 69 reAASLITQIiggsipsDKPGTLAMVVKEPV-GVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 237 MEEAGLPAGVINFVPCEPAVMDSAVN---ADPRLAAVVFTGSTRVFTEInknvfSRLETYHNFPRISgETGGKDFHLVHP 313
Cdd:cd07105 148 FHEAGLPKGVLNVVTHSPEDAPEVVEaliAHPAVRKVNFTGSTRVGRII-----AETAAKHLKPVLL-ELGGKAPAIVLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 314 SADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGqPDDFQSfmcaVIDETSFNKNKKYIEi 393
Cdd:cd07105 222 DADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-PVVLGS----LVSAAAADRVKELVD- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 394 aKADSSNYEVVVGGKCDKT-RGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGA 472
Cdd:cd07105 296 -DALSKGAKLVVGGLADESpSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE-----EEAVRIAND-SEYGLSAA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 473 VFSR--ERApIREADkylRYAAGNYYVNdkctGAVVG---QQPFGGSRLSGSNdkpgagqfvtRFVSARSIKEsFDVTPT 547
Cdd:cd07105 369 VFTRdlARA-LAVAK---RIESGAVHIN----GMTVHdepTLPHGGVKSSGYG----------RFNGKWGIDE-FTETKW 429
|
...
gi 398009572 548 ISY 550
Cdd:cd07105 430 ITI 432
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
68-525 |
5.45e-40 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 151.49 E-value: 5.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVqIAKAYNATPELARKAVEAAVEASKE--WSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAE 145
Cdd:cd07142 24 IDPRNGEV-IAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 146 IDCVAEACDFIRWNIHFAEELYAQQPRSVSNSGVWntTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSP 224
Cdd:cd07142 102 YAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVY--TLHEPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 225 TAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEInknvfSRLETYHNFPRISGETG 304
Cdd:cd07142 179 QTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKII-----MQLAAKSNLKPVTLELG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 305 GKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSF 384
Cdd:cd07142 254 GKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 385 NKNKKYIEIAKADSSNyeVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYddskpgywKEVCELVD-- 462
Cdd:cd07142 334 EKILSYIEHGKEEGAT--LITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKF--------KTVDEVIKra 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009572 463 STTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSGSNDKPGA 525
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKGI 462
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
84-518 |
1.05e-38 |
|
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: 147.83 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 84 TPELARKAVEAAVEASKEWSQVPFRDRAAIFYkaaHLLSTKYRH--EMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIH 161
Cdd:cd07098 16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLR---SLLKYILENqeEICRVACRDTGKTMVDASLGEILVTCEKIRWTLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 162 FAEELYAQQPRSvSNSGVW---NTTDYRPLeGFVSAITPFNFT-------AIAANLAGtpalmgNTVVWKPSPTAVLSNY 231
Cdd:cd07098 93 HGEKALRPESRP-GGLLMFykrARVEYEPL-GVVGAIVSWNYPfhnllgpIIAALFAG------NAIVVKVSEQVAWSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 232 LMYKIMEEA----GLPAGVINFVPCEPAVMDSAVNAdPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfPRISgETGGKD 307
Cdd:cd07098 165 FFLSIIREClaacGHDPDLVQLVTCLPETAEALTSH-PVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 308 FHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKN 387
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 388 KKyiEIAKADSSNYEVVVGGK----CDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDS 463
Cdd:cd07098 318 EE--LVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD-----EEAVEIANS 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 398009572 464 tTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07098 391 -TEYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSG 442
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
76-519 |
1.18e-38 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 148.12 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 76 QIAKAYNATPELARKAVEAAVEaSKEWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEIDCVAEACDF 155
Cdd:PRK09847 50 KIARGKSVDIDRAVSAARGVFE-RGDWSLSSPAKRKAVLNKLADLME-AHAEELALLETLDTGKPIRHSLRDDIPGAARA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 156 IRWNIHFAEELYAQQprSVSNSGVWNTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMY 234
Cdd:PRK09847 128 IRWYAEAIDKVYGEV--ATTSSHELAMIVREPV-GVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 235 KIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhNFPRISGETGGKDFHLVHPS 314
Cdd:PRK09847 205 GLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 315 A-DMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEI 393
Cdd:PRK09847 280 CpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIRE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 394 AKADSsnyEVVVGGKCDKTRGYfVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgywKEVCELVDSTTKYGLTGAV 473
Cdd:PRK09847 360 GESKG---QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTS------EEQALQLANDSQYGLGAAV 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 398009572 474 FSRERAPIREADKYLRyaAGNYYVNDKCTGAVVgqQPFGGSRLSGS 519
Cdd:PRK09847 430 WTRDLSRAHRMSRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSGN 471
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
54-555 |
4.77e-37 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 143.82 E-value: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAAT 133
Cdd:PLN02315 25 VGGEWRANGPLVSSVNPANNQP-IAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 134 M-LGQSKNPWQAEIDCVAEACDFirwnihfAEELYAQQPRSVSNSG--------VWNttdyrPLeGFVSAITPFNFTAIA 204
Cdd:PLN02315 104 LeMGKILAEGIGEVQEIIDMCDF-------AVGLSRQLNGSIIPSErpnhmmmeVWN-----PL-GIVGVITAFNFPCAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 205 ANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKI----MEEAGLPAGVINFVpCEPAVMDSAVNADPRLAAVVFTGSTRVF 279
Cdd:PLN02315 171 LGWNACIALVcGNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 TEINKNVFSRletyhnFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:PLN02315 250 LMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSNyeVVVGGKCDKTRGYFVEPTIIETKdPRAQLMREEIFGP 439
Cdd:PLN02315 324 YKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGK--ILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 440 VLTVFVYDDskpgyWKEVCELVDSTTKyGLTGAVFSRERAPIREADKYLRYAAGNYYVNDKCTGAVVGQQpFGGSRLSGS 519
Cdd:PLN02315 401 VLYVMKFKT-----LEEAIEINNSVPQ-GLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGG 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 398009572 520 NDKPGAG---QFVTRfvsarsikesfdVTPTISYPHQLP 555
Cdd:PLN02315 474 GREAGSDswkQYMRR------------STCTINYGNELP 500
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
54-518 |
1.05e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 142.71 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPY--TSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRA 131
Cdd:PRK13252 11 IDGAYVeaTSGETFEVINPATGEV-LATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRER-NDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATMLGQSKnPWQaEIDCV--AEACDFIrwnihfaeELYA---------QQPRsvsNSGVWNTTDYRPLeGFVSAITPFNF 200
Cdd:PRK13252 89 LETLDTGK-PIQ-ETSVVdiVTGADVL--------EYYAglapalegeQIPL---RGGSFVYTRREPL-GVCAGIGAWNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 201 TAIAANLAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTrvf 279
Cdd:PRK13252 155 PIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGV--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 280 tEINKNVFSRLETyhNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:PRK13252 231 -PTGKKVMAAAAA--SLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLER 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKC----DKTRGYFVEPTIIE--TKDPRaqLMR 433
Cdd:PRK13252 308 VERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGA--RLLCGGERltegGFANGAFVAPTVFTdcTDDMT--IVR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 434 EEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSRErapIREADKYL-RYAAGNYYVNdkCTGAVVGQQPFG 512
Cdd:PRK13252 384 EEIFGPVMSVLTFDDE-----DEVIARAND-TEYGLAAGVFTAD---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVG 452
|
....*.
gi 398009572 513 GSRLSG 518
Cdd:PRK13252 453 GYKQSG 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
76-518 |
1.55e-36 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 141.97 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 76 QIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstkyrhEMRAATMLG-QSKN---PWQAEI-DCVA 150
Cdd:PRK13473 29 VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAI------EENADEFARlESLNcgkPLHLALnDEIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 151 EACDFIRWnihfaeelYAQQPRSVSNSGvwnTTDY---------RPLEGFVSAITPFNFTAIAANLAGTPALM-GNTVVW 220
Cdd:PRK13473 103 AIVDVFRF--------FAGAARCLEGKA---AGEYleghtsmirRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 221 KPSPTAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVfteiNKNVFSRleTYHNFPRIS 300
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT----GKHVLSA--AADSVKRTH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 301 GETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVID 380
Cdd:PRK13473 245 LELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 381 ETSFNKNKKYIEIAKAdSSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCEL 460
Cdd:PRK13473 325 AAHRDRVAGFVERAKA-LGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE-----DQAVRW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 461 VDsTTKYGLTGAVFSRE--RApIREADkylRYAAGNYYVNDKCTgaVVGQQPFGGSRLSG 518
Cdd:PRK13473 399 AN-DSDYGLASSVWTRDvgRA-HRVSA---RLQYGCTWVNTHFM--LVSEMPHGGQKQSG 451
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-525 |
3.19e-36 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 141.25 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 56 GKPYTSSNiikgimPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMraATML 135
Cdd:PRK09457 14 GEAFESRN------PVSGEV-LWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL-EENKEEL--AEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 136 GQ--SKNPWQA--EIDCVAEacdfirwNIHFAEELYAQQPRSVSNSGVWNTT--DYRPLeGFVSAITPFNFTAIAANLAG 209
Cdd:PRK09457 84 ARetGKPLWEAatEVTAMIN-------KIAISIQAYHERTGEKRSEMADGAAvlRHRPH-GVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 210 TPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVmDSAVNADPRLAAVVFTGSTRVFTEINKNVFS 288
Cdd:PRK09457 156 VPALLaGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 289 RLEtyhnfpRISG-ETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCW-KELKALLIKGQKQIKMG 366
Cdd:PRK09457 235 QPE------KILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 367 QPD-DFQSFMCAVIDETSfnknkkyieiAKA--DSSNYEVVVGGKC-------DKTRGyFVEPTIIETKDPrAQLMREEI 436
Cdd:PRK09457 309 RWDaEPQPFMGAVISEQA----------AQGlvAAQAQLLALGGKSllemtqlQAGTG-LLTPGIIDVTGV-AELPDEEY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 437 FGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERApirEADKYLRYA-AGNYYVNDKCTGAvVGQQPFGGSR 515
Cdd:PRK09457 377 FGPLLQVVRYDD-----FDEAIRLANN-TRFGLSAGLLSDDRE---DYDQFLLEIrAGIVNWNKPLTGA-SSAAPFGGVG 446
|
490
....*....|
gi 398009572 516 LSGsNDKPGA 525
Cdd:PRK09457 447 ASG-NHRPSA 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
77-518 |
6.39e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 140.73 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 77 IAKAYNATPELARKAVEAAVEASKeWSQVPFRDRAAIFYKAAHLLStKYRHEMRAATMLGQSKNPWQAEIDCVAEACDFI 156
Cdd:PLN02766 52 IAEGDKEDVDLAVKAAREAFDHGP-WPRMSGFERGRIMMKFADLIE-EHIEELAALDTIDAGKLFALGKAVDIPAAAGLL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 157 RWNIHFAEELYAQqprSVSNSGVWNTTDYRPLEGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYK 235
Cdd:PLN02766 130 RYYAGAADKIHGE---TLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 236 IMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRletyhNFPRISGETGGKDFHLVHPSA 315
Cdd:PLN02766 207 LAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS-----NLKQVSLELGGKSPLLIFDDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 316 DMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAK 395
Cdd:PLN02766 282 DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 396 ADSSNyeVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSKPGYWKEVCelvdstTKYGLTGAVFS 475
Cdd:PLN02766 362 REGAT--LLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANN------TKYGLAAGIVT 433
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 398009572 476 RERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:PLN02766 434 KDLDVANTVSRSIR--AGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
88-518 |
1.67e-35 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 139.44 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 88 ARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLsTKYRHEMRAATMLGQSKnPWQAEIDCVAEACDFIRWnihFAEEly 167
Cdd:PLN02278 64 TNDAIASAHDAFPSWSKLTASERSKILRRWYDLI-IANKEDLAQLMTLEQGK-PLKEAIGEVAYGASFLEY---FAEE-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 168 AQQPrsvsNSGVWNTTDYR--------PLeGFVSAITPFNFT-AIAANLAGtPALM-GNTVVWKPSPTAVLSNYLMYKIM 237
Cdd:PLN02278 137 AKRV----YGDIIPSPFPDrrllvlkqPV-GVVGAITPWNFPlAMITRKVG-PALAaGCTVVVKPSELTPLTALAAAELA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 238 EEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfpRISGETGGKDFHLVHPSADM 317
Cdd:PLN02278 211 LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 318 KHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEiaKAD 397
Cdd:PLN02278 285 DVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ--DAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 398 SSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPV--LTVFVYDDskpgywkEVCELVDSTTkYGLTGAVFS 475
Cdd:PLN02278 363 SKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVapLTRFKTEE-------EAIAIANDTE-AGLAAYIFT 434
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 398009572 476 RERAPIREADKYLRYaaGNYYVNDKCTGAVVGqqPFGGSRLSG 518
Cdd:PLN02278 435 RDLQRAWRVSEALEY--GIVGVNEGLISTEVA--PFGGVKQSG 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
186-498 |
3.31e-34 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 134.09 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 186 RPLeGFVSAITPFNFT--AIAANLAgtPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVN 262
Cdd:PRK10090 70 RAL-GVTTGILPWNFPffLIARKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 263 ADPRLAAVVFTGST----RVFTEINKNVfsrletyhnfPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSA 338
Cdd:PRK10090 147 GNPKVAMVSMTGSVsageKIMAAAAKNI----------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNC 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 339 CSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSF-MCAVIDETSFNKNKKyiEIAKADSSNYEVVVGGKCDKTRGYFV 417
Cdd:PRK10090 217 AERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQ--KVARAVEEGARVALGGKAVEGKGYYY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 418 EPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDStTKYGLTGAVFSRERAPIREADKYLRYaaGNYYV 497
Cdd:PRK10090 295 PPTLLLDVRQEMSIMHEETFGPVLPVVAFDT-----LEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLKF--GETYI 366
|
.
gi 398009572 498 N 498
Cdd:PRK10090 367 N 367
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
89-518 |
1.77e-33 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 133.11 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 89 RKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYRHEMRAATmLGQSKNPWQAEIDcVAEACDFIRWnihFAEElya 168
Cdd:PRK11241 51 RAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT-LEQGKPLAEAKGE-ISYAASFIEW---FAEE--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 169 qQPRSVSNSGVWNTTDYR------PLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAG 241
Cdd:PRK11241 123 -GKRIYGDTIPGHQADKRlivikqPI-GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 242 LPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTrvftEINKNVFSrlETYHNFPRISGETGGKDFHLVHPSADMKHVA 321
Cdd:PRK11241 201 IPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGST----EIGRQLME--QCAKDIKKVSLELGGNAPFIVFDDADLDKAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 322 AGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIeiAKADSSNY 401
Cdd:PRK11241 275 EGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHI--ADALEKGA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 402 EVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGLTGAVFSRERAPI 481
Cdd:PRK11241 353 RVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE-----ADVIAQAND-TEFGLAAYFYARDLSRV 426
|
410 420 430
....*....|....*....|....*....|....*...
gi 398009572 482 READKYLRYaaGNYYVNdkcTGAVVGQ-QPFGGSRLSG 518
Cdd:PRK11241 427 FRVGEALEY--GIVGIN---TGIISNEvAPFGGIKASG 459
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
83-518 |
1.17e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 130.63 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 83 ATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMrAATM---LGQSKNPWQAEIDCVAEACdfiRWN 159
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAE-ADQV-AALMtleMGKTLASAKAEALKCAKGF---RYY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 160 IHFAEELYAQQPRSVSNSGVWNT-TDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPS---PTAVLsnYLMy 234
Cdd:PRK09406 95 AEHAEALLADEPADAAAVGASRAyVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHAsnvPQTAL--YLA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 235 KIMEEAGLPAGVINFVpcepAVMDSAVNA---DPRLAAVVFTGSTRVF--------TEINKNVFsrletyhnfprisgET 303
Cdd:PRK09406 171 DLFRRAGFPDGCFQTL----LVGSGAVEAilrDPRVAAATLTGSEPAGravaaiagDEIKKTVL--------------EL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 304 GGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETS 383
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 384 FNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDS 463
Cdd:PRK09406 313 RDEVEKQVDDAVAAGA--TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD-----IDEAIEIANA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009572 464 TTkYGLTGAVFSRERApirEADKYLR-YAAGNYYVNdkctGAVVG--QQPFGGSRLSG 518
Cdd:PRK09406 386 TT-FGLGSNAWTRDEA---EQERFIDdLEAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
54-518 |
2.56e-32 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 129.92 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGKPYTSSNiikgimPSDHQVqIAKAYNATPELARKAVEAAVEA--SKEWSQVPFRDRAAIFYKAAHLLStkyRHEMRA 131
Cdd:cd07140 18 EGGKTYNTIN------PTDGSV-ICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME---EHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 ATM----------------LGQSKNPWQAeidcVAEACDFIRwnihfAEELYAQQPRSVSNsgvWNTTDYRPLeGFVSAI 195
Cdd:cd07140 88 ATIesldsgavytlalkthVGMSIQTFRY----FAGWCDKIQ-----GKTIPINQARPNRN---LTLTKREPI-GVCGIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 196 TPFNFT------AIAANLAGtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAA 269
Cdd:cd07140 155 IPWNYPlmmlawKMAACLAA-----GNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 270 VVFTGSTRVFTEINKNVfsrleTYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCW 349
Cdd:cd07140 230 LGFTGSTPIGKHIMKSC-----AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 350 KELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGYFVEPTIIETKDPRA 429
Cdd:cd07140 305 DEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGA--TLVYGGKQVDRPGFFFEPTVFTDVEDHM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 430 QLMREEIFGPVLTVFVYDDSKpgywkevcelVDS------TTKYGLTGAVFSrerapiREADKYLRYA----AGNYYVND 499
Cdd:cd07140 383 FIAKEESFGPIMIISKFDDGD----------VDGvlqranDTEYGLASGVFT------KDINKALYVSdkleAGTVFVNT 446
|
490
....*....|....*....
gi 398009572 500 KCTGAVVGqqPFGGSRLSG 518
Cdd:cd07140 447 YNKTDVAA--PFGGFKQSG 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
68-518 |
1.96e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 121.12 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 68 IMPSDHQVQIAKAYN--------ATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATM---LG 136
Cdd:PRK13968 3 ITPATHAISVNPATGeqlsvlpwAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKAL--RARSEEMAQMItreMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 137 QSKNPWQAEIDCVAEACDfirWNIHFAEELYAQQPRSVSNSGVwnTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-G 215
Cdd:PRK13968 81 KPINQARAEVAKSANLCD---WYAEHGPAMLKAEPTLVENQQA--VIEYRPL-GTILAIMPWNFPLWQVMRGAVPILLaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 216 NTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNaDPRLAAVVFTGSTRVFTEINKNVFSRLEtyhn 295
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAALK---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 296 fpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFM 375
Cdd:PRK13968 230 --KCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 376 CAVideTSFN-KNKKYIEIAKADSSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgyw 454
Cdd:PRK13968 308 GPM---ARFDlRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDA----- 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 455 KEVCELVDStTKYGLTGAVFSRERApiREADKYLRYAAGNYYVNDKCtgAVVGQQPFGGSRLSG 518
Cdd:PRK13968 380 EHALELAND-SEFGLSATIFTTDET--QARQMAARLECGGVFINGYC--ASDARVAFGGVKKSG 438
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
54-518 |
6.62e-29 |
|
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: 119.86 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 54 IGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKYrhEMRA 131
Cdd:cd07116 5 IGGEwvAPVKGEYFDNITPVTGKV-FCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL--EMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 132 -ATMLGQSKNPWQAEIDCVAEACDFIRWnihFAEELYAQQPrsvSNSGVWNTTD----YRPLeGFVSAITPFNFTAIAAN 206
Cdd:cd07116 82 vAETWDNGKPVRETLAADIPLAIDHFRY---FAGCIRAQEG---SISEIDENTVayhfHEPL-GVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 207 LAGTPALM-GNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKn 285
Cdd:cd07116 155 WKLAPALAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQ- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 286 vfsrlETYHNFPRISGETGGKDFHLVHPSADMKHVA------AGTVRGAFEfQGQKCSACSRLYAPKTCWKELKALLIKG 359
Cdd:cd07116 233 -----YASENIIPVTLELGGKSPNIFFADVMDADDAffdkalEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 360 QKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGK----CDKTRGYFVEPTIIETKDpRAQLMREE 435
Cdd:cd07116 307 VKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGA--EVLTGGErnelGGLLGGGYYVPTTFKGGN-KMRIFQEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 436 IFGPVLTVFVYDDSkpgywKEVCELVDSTTkYGLTGAVFSRErapIREADKYLR-YAAGNYYVNdkCTGAVVGQQPFGGS 514
Cdd:cd07116 384 IFGPVLAVTTFKDE-----EEALEIANDTL-YGLGAGVWTRD---GNTAYRMGRgIQAGRVWTN--CYHLYPAHAAFGGY 452
|
....
gi 398009572 515 RLSG 518
Cdd:cd07116 453 KQSG 456
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
77-518 |
2.29e-28 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 119.14 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 77 IAKAYNATPELARKAVEAAVEASKE--WSQVPFRDRAAIFYKAAHLLStKYRHEMrAATMLGQSKNPWQ----AEIDCVA 150
Cdd:PLN02466 86 IAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDEL-AALETWDNGKPYEqsakAELPMFA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 151 EacdFIRWNIHFAEELYAQQPRSVSNSGVwnTTDYRPLeGFVSAITPFNFTAIAANLAGTPALM-GNTVVWKPSPTAVLS 229
Cdd:PLN02466 164 R---LFRYYAGWADKIHGLTVPADGPHHV--QTLHEPI-GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 230 NYLMYKIMEEAGLPAGVINFV----PCEPAVMDSAVNADprlaAVVFTGSTrvftEINKNVFSrLETYHNFPRISGETGG 305
Cdd:PLN02466 238 ALYAAKLLHEAGLPPGVLNVVsgfgPTAGAALASHMDVD----KLAFTGST----DTGKIVLE-LAAKSNLKPVTLELGG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 306 KDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKEL----KALLIKGQkqikMGQPddfqsFMCAV--- 378
Cdd:PLN02466 309 KSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARALKRV----VGDP-----FKKGVeqg 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 379 --IDETSFNKNKKYIEiaKADSSNYEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYddskpgywKE 456
Cdd:PLN02466 380 pqIDSEQFEKILRYIK--SGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKF--------KD 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 457 VCELVD--STTKYGLTGAVFSRERAPIREADKYLRyaAGNYYVNdkCTGAVVGQQPFGGSRLSG 518
Cdd:PLN02466 450 LDEVIRraNNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVN--CFDVFDAAIPFGGYKMSG 509
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
197-518 |
5.98e-28 |
|
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: 116.56 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 197 PFNFT------AIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAglpagvinFVPCEPAVMDSAVNADPRLAA- 269
Cdd:cd07134 113 PFNLAfgplvsAIAA---------GNTAILKPSELTPHTSAVIAKIIREA--------FDEDEVAVFEGDAEVAQALLEl 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 270 ----VVFTGSTR----VFTEINKNVFSrletyhnfprISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSR 341
Cdd:cd07134 176 pfdhIFFTGSPAvgkiVMAAAAKHLAS----------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 342 LYAPKTCWKELKALLIK------GQKQIKMGQPDdfqsfMCAVIDETSFNKNKKYIEIAKADSSnyEVVVGGKCDKTRGY 415
Cdd:cd07134 246 VFVHESVKDAFVEHLKAeiekfyGKDAARKASPD-----LARIVNDRHFDRLKGLLDDAVAKGA--KVEFGGQFDAAQRY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 416 fVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTKyGLTGAVFSRERAPIreaDKYL-RYAAGN 494
Cdd:cd07134 319 -IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDL-----DEVIEYINAKPK-PLALYVFSKDKANV---NKVLaRTSSGG 388
|
330 340
....*....|....*....|....
gi 398009572 495 YYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07134 389 VVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
90-520 |
1.78e-26 |
|
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: 112.51 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 90 KAVEAAVEASKEWSQ-VPFRDRAAIFYKAAHLLSTkyRHEMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIhfaEELYA 168
Cdd:cd07148 25 KALDTAHALFLDRNNwLPAHERIAILERLADLMEE--RADELALLIAREGGKPLVDAKVEVTRAIDGVELAA---DELGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 169 QQPRSV------SNSGVWNTTDYRPLeGFVSAITPFNF----------TAIAAnlaGTPalmgntVVWKPSPTAVLSNYL 232
Cdd:cd07148 100 LGGREIpmgltpASAGRIAFTTREPI-GVVVAISAFNHplnlivhqvaPAIAA---GCP------VIVKPALATPLSCLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 233 MYKIMEEAGLPAGVINFVPCEPAVMDSAVnADPRLAAVVFTGSTRVFTEINKNVFsrletyhnfP--RISGETGGKDFHL 310
Cdd:cd07148 170 FVDLLHEAGLPEGWCQAVPCENAVAEKLV-TDPRVAFFSFIGSARVGWMLRSKLA---------PgtRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 311 VHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKY 390
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 391 IEIAKADSSnyEVVVGGK-CDKTrgyFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDStTKYGL 469
Cdd:cd07148 320 VNEAVAAGA--RLLCGGKrLSDT---TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDL-----DEAIAQANS-LPVAF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398009572 470 TGAVFSRERAPIREADKYLryAAGNYYVNDKcTGAVVGQQPFGGSRLSGSN 520
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
60-477 |
3.95e-26 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 111.77 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 60 TSSNIIKGIMPSDHQVQIaKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLstKYRHEMRAATMLGQSK 139
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQY-KVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAIL--KEHKAPIAECLVKEIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 140 NPWQAEIDCVAEACDFIRWNihfAEE---LYAQQPRSVSNSGVWNT------TDYRPLeGFVSAITPFNFtaiAANLAGT 210
Cdd:PLN00412 105 KPAKDAVTEVVRSGDLISYT---AEEgvrILGEGKFLVSDSFPGNErnkyclTSKIPL-GVVLAIPPFNY---PVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 211 ---PALM-GNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNV 286
Cdd:PLN00412 178 kiaPALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 287 FSRLETyhnfprisgETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMG 366
Cdd:PLN00412 258 MVPLQM---------ELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 367 QPDDfQSFMCAVIDETSFNKNKKYIEIAKADSSNYevvvggkCDKTR--GYFVEPTIIETKDPRAQLMREEIFGPVLTVF 444
Cdd:PLN00412 329 PPED-DCDITPVVSESSANFIEGLVMDAKEKGATF-------CQEWKreGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430
....*....|....*....|....*....|...
gi 398009572 445 VYDDSKPGYwkEVCelvdSTTKYGLTGAVFSRE 477
Cdd:PLN00412 401 RINSVEEGI--HHC----NASNFGLQGCVFTRD 427
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
185-518 |
7.55e-23 |
|
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: 101.06 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 185 YRPLeGFVSAITPFNF----------TAIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAglpagvinFVPCEP 254
Cdd:cd07087 98 PEPL-GVVLIIGPWNYplqlalapliGAIAA---------GNTVVLKPSELAPATSALLAKLIPKY--------FDPEAV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 255 AVmdsaVNADPRLAA---------VVFTGSTRVFTEINKNVFSRLeTyhnfPrISGETGGKDFHLVHPSADMKHVAAGTV 325
Cdd:cd07087 160 AV----VEGGVEVATallaepfdhIFFTGSPAVGKIVMEAAAKHL-T----P-VTLELGGKSPCIVDKDANLEVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 326 RGAFEFQGQKCSACSRLYAPKTCWKELKALLikgQKQIKMGQPDDFQSFMC--AVIDETSFNKNKKYIEIAKadssnyeV 403
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEEL---KKAIKEFYGEDPKESPDygRIINERHFDRLASLLDDGK-------V 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 404 VVGGKCDKTRGYfVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDSTTKyGLTGAVFSRERApirE 483
Cdd:cd07087 300 VIGGQVDKEERY-IAPTILDDVSPDSPLMQEEIFGPILPILTYDD-----LDEAIEFINSRPK-PLALYLFSEDKA---V 369
|
330 340 350
....*....|....*....|....*....|....*.
gi 398009572 484 ADKYL-RYAAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07087 370 QERVLaETSSGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
51-483 |
3.22e-22 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 100.59 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 51 PIMIGGK--PYTSSNIIKGIMPSDHQVqIAKAYNATPELARKAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKY-RH 127
Cdd:PLN02419 115 PNLIGGSfvESQSSSFIDVINPATQEV-VSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMdKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 128 EMRAATMLGQSKNPWQAEI----DCVAEACDFIrwNIHFAEELyaqqpRSVSNsGVWNTTDYRPLeGFVSAITPFNFTA- 202
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIfrglEVVEHACGMA--TLQMGEYL-----PNVSN-GVDTYSIREPL-GVCAGICPFNFPAm 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 203 IAANLAGTPALMGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDsAVNADPRLAAVVFTGSTRVFTEI 282
Cdd:PLN02419 265 IPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 283 NKNVFSRLEtyhnfpRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLY--APKTCWKELkalLIKGQ 360
Cdd:PLN02419 344 YARAAAKGK------RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVfvGDAKSWEDK---LVERA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 361 KQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSSNY-----EVVVGGKcdkTRGYFVEPTIIETKDPRAQLMREE 435
Cdd:PLN02419 415 KALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLlldgrDIVVPGY---EKGNFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 398009572 436 IFGPVLTVFvyddsKPGYWKEVCELVDStTKYGLTGAVFSRERAPIRE 483
Cdd:PLN02419 492 IFGPVLVCM-----QANSFDEAISIINK-NKYGNGAAIFTSSGAAARK 533
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
140-551 |
2.75e-21 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 97.02 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 140 NPWQAEIDCVAEacDFIRWNihfaeelyaqQPRSVSNSGVWNTTD----YRPLeGFVSAITPFNFTA--IAANLAGTPAl 213
Cdd:PTZ00381 70 LLTVAEIEHLLK--HLDEYL----------KPEKVDTVGVFGPGKsyiiPEPL-GVVLVIGAWNYPLnlTLIPLAGAIA- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 214 MGNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFvpCEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLety 293
Cdd:PTZ00381 136 AGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRV--IEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENL--- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 294 hnFPRISgETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTcwkeLKALLIKGQKQ--IKMGQPD-- 369
Cdd:PTZ00381 210 --TPCTL-ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS----IKDKFIEALKEaiKEFFGEDpk 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 370 ---DFQsfmcAVIDETSFNKNKKYIEIAKADssnyeVVVGGKCDKTRGYfVEPTIIETKDPRAQLMREEIFGPVLTVFVY 446
Cdd:PTZ00381 283 kseDYS----RIVNEFHTKRLAELIKDHGGK-----VVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 447 DDSkpgywKEVCELVDSTTKyGLTGAVFSRERAPIREADKylRYAAGNYYVNDkCTGAVVGQQ-PFGGSRLSGSNDKPGA 525
Cdd:PTZ00381 353 ENI-----DEVLEFINSRPK-PLALYYFGEDKRHKELVLE--NTSSGAVVIND-CVFHLLNPNlPFGGVGNSGMGAYHGK 423
|
410 420 430
....*....|....*....|....*....|
gi 398009572 526 GQFVT----RFVSARSIKESFDvtPTISYP 551
Cdd:PTZ00381 424 YGFDTfshpKPVLNKSTGNSFD--LSLRYP 451
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
170-518 |
2.00e-19 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 90.74 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 170 QPRSVSNSGVWN-----TTDYRPLeGFVSAITPFNF----------TAIAAnlagtpalmGNTVVWKPSPTAVLSNYLMY 234
Cdd:cd07135 86 KDEKVKDGPLAFmfgkpRIRKEPL-GVVLIIGPWNYpvllalsplvGAIAA---------GCTVVLKPSELTPHTAALLA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 235 KIMEEAgLPAGVINFVPCEPAVMDSAVnaDPRLAAVVFTGSTRVFTEINKNVFSRLEtyhnfPrISGETGGKDFHLVHPS 314
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQGGVPETTALL--EQKFDKIFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 315 ADMKHVAAGTVRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDfQSFMCAVIDETSFNKNKKYIEIA 394
Cdd:cd07135 227 ADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 395 KADssnyeVVVGGKCDK-TRgyFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDS--TTkygLTG 471
Cdd:cd07135 306 KGK-----VVIGGEMDEaTR--FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDL-----DEAIKVINSrdTP---LAL 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398009572 472 AVFSRERApirEADKYL-RYAAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07135 371 YIFTDDKS---EIDHILtRTRSGGVVINDTLIHVGVDNAPFGGVGDSG 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
185-518 |
8.44e-17 |
|
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: 82.94 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 185 YRPLeGFVSAITPFNFT----------AIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAglpagvinFVPCEP 254
Cdd:cd07136 98 YEPY-GVVLIIAPWNYPfqlalapligAIAA---------GNTAVLKPSELTPNTSKVIAKIIEET--------FDEEYV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 255 AVMDSAVNADPRLAA-----VVFTGSTRVFTEINKNVFSRLeTyhnfPrISGETGGKDFHLVHPSADMKHVAAGTVRGAF 329
Cdd:cd07136 160 AVVEGGVEENQELLDqkfdyIFFTGSVRVGKIVMEAAAKHL-T----P-VTLELGGKSPCIVDEDANLKLAAKRIVWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 330 EFQGQKCSACSRLYAPKTCWKELKALLikgQKQI-KMGQPDDFQS-FMCAVIDETSFNKNKKYIEIAKadssnyeVVVGG 407
Cdd:cd07136 234 LNAGQTCVAPDYVLVHESVKEKFIKEL---KEEIkKFYGEDPLESpDYGRIINEKHFDRLAGLLDNGK-------IVFGG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 408 KCDKTRGYfVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDskpgyWKEVCELVDSTTKyGLTGAVFSRERAPIREADKY 487
Cdd:cd07136 304 NTDRETLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTYDT-----LDEAIEIIKSRPK-PLALYLFSEDKKVEKKVLEN 376
|
330 340 350
....*....|....*....|....*....|.
gi 398009572 488 LRYAAGnyYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07136 377 LSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
90-533 |
1.68e-16 |
|
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: 81.90 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 90 KAVEAAVEASKEWSQVPFRDRAAIFYKAAHLLSTKyRHEMRAATMLGQSKNPWQAEIDCVAEACDFIRWNIHFAEELYAQ 169
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 170 QPRSVSNSGVWNTTDYRPLEGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAG-LPAGVI 247
Cdd:cd07084 82 PGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 248 NFVPCEPAVMdSAVNADPRLAAVVFTGSTRVFteinknvfSRLETYHNFPRISGETGGKDFHLVHPSAD-MKHVAAGTVR 326
Cdd:cd07084 162 TLINGDGKTM-QALLLHPNPKMVLFTGSSRVA--------EKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 327 GAFEFQGQKCSACSRLYAPKTCWKE-----LKALLIK---GQKQIKMGQPDDFQsfmcAVIDETSFNKNKKYIEIAKADS 398
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPENWSKTplvekLKALLARrklEDLLLGPVQTFTTL----AMIAHMENLLGSVLLFSGKELK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 399 SNYEVVVGGKCDKTRGYFVeptiIETKDPRAQLMREEIFGPVLTVFVYDDSKPGYWKEVCELVDSTtkygLTGAVFSRER 478
Cdd:cd07084 309 NHSIPSIYGACVASALFVP----IDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS----LTAAIYSNDP 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009572 479 APIREADKYLRYAAGNYYVNDKCTGAVVGQQPFGGSRLSGSNDKPG---AGQFVTRFV 533
Cdd:cd07084 381 IFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGgpeAIKLVWRCH 438
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
185-518 |
1.02e-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: 79.45 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 185 YRPLeGFVSAITPFNF----------TAIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAglpagvinFVPCEP 254
Cdd:cd07133 99 YQPL-GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAELLAEY--------FDEDEV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 255 AVmdsaVNADPRLAA---------VVFTGSTRVFTEINKNVfSRletyhNFPRISGETGGKDFHLVHPSADMKHVAAGTV 325
Cdd:cd07133 161 AV----VTGGADVAAafsslpfdhLLFTGSTAVGRHVMRAA-AE-----NLTPVTLELGGKSPAIIAPDADLAKAAERIA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 326 RGAFEFQGQKCSACSRLYAPKTCWKELKALLikgQKQIKMGQPD-----DFqsfmCAVIDETSFNKNKKYIEIAKADSSN 400
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAA---KAAVAKMYPTladnpDY----TSIINERHYARLQGLLEDARAKGAR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 401 YEVVVGGKCDKTRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTK----YgltgaVFSR 476
Cdd:cd07133 304 VIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSL-----DEAIDYINARPRplalY-----YFGE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398009572 477 ERApirEADKYL-RYAAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07133 374 DKA---EQDRVLrRTHSGGVTINDTLLHVAQDDLPFGGVGASG 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
172-475 |
8.15e-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: 70.60 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 172 RSVSNSGVW---NTTDYRPLEGFVSAITPFNFTAIAANLAGTPAL-MGNTVVWKPSPTAVLSNYLMYKIMEEAGLPAGVI 247
Cdd:cd07126 123 RSFNVPGDHqgqQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 248 NFVPCEPAVMDSAV-NADPRLaaVVFTGSTRVFTEINKNVFSRLETyhnfprisgETGGKDFHLVHPS-ADMKHVAAGTV 325
Cdd:cd07126 203 DLIHSDGPTMNKILlEANPRM--TLFTGSSKVAERLALELHGKVKL---------EDAGFDWKILGPDvSDVDYVAWQCD 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 326 RGAFEFQGQKCSACSRLYAPKTcW------KELKALliKGQKQIkmgqpDDFQsfMCAVI---DETSFNKNKKYIEIAKA 396
Cdd:cd07126 272 QDAYACSGQKCSAQSILFAHEN-WvqagilDKLKAL--AEQRKL-----EDLT--IGPVLtwtTERILDHVDKLLAIPGA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 397 dssnyEVVVGGKCDKTRGY-----FVEPTII-----ETKDPRA-QLMREEIFGPVLTVFVYDDSKPGYWKEVCELVDSTt 465
Cdd:cd07126 342 -----KVLFGGKPLTNHSIpsiygAYEPTAVfvpleEIAIEENfELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH- 415
|
330
....*....|
gi 398009572 466 kygLTGAVFS 475
Cdd:cd07126 416 ---LTAAVVS 422
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
197-518 |
3.08e-12 |
|
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: 68.79 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 197 PFNFT------AIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKImeeagLPAGVINfvPCEPaVMDSAVNADPRLAA- 269
Cdd:cd07132 113 PLQLTlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAEL-----IPKYLDK--ECYP-VVLGGVEETTELLKq 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 270 ----VVFTGSTRVfteiNKNVfsRLETYHNFPRISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSA-----CS 340
Cdd:cd07132 176 rfdyIFYTGSTSV----GKIV--MQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 341 RLYAPKTCwKELKALLikgqKQIKMGQPDDFQSFmCAVIDETSFNKNKKYIEiakadssNYEVVVGGKCD-KTRgyFVEP 419
Cdd:cd07132 250 PEVQEKFV-EALKKTL----KEFYGEDPKESPDY-GRIINDRHFQRLKKLLS-------GGKVAIGGQTDeKER--YIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 420 TIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTKyGLTGAVFSRERAPIreaDKYL-RYAAGNYYVN 498
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNL-----DEAIEFINSREK-PLALYVFSNNKKVI---NKILsNTSSGGVCVN 385
|
330 340
....*....|....*....|
gi 398009572 499 DKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07132 386 DTIMHYTLDSLPFGGVGNSG 405
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
187-448 |
4.45e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 68.58 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 187 PLEGFVSAITPFNF-------TAIAANLAGTPalmgntVVWKP-SPTAVLSnYLMYKIMEEAG-LPAGVINFVPCEPA-V 256
Cdd:PRK11903 147 PTRGVALFINAFNFpawglweKAAPALLAGVP------VIVKPaTATAWLT-QRMVKDVVAAGiLPAGALSVVCGSSAgL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 257 MDSAVNADprlaAVVFTGSTRVFTEI--NKNVFSRletyhnFPRISGETGGKDFHLVHPSAdmkhvAAGT---------- 324
Cdd:PRK11903 220 LDHLQPFD----VVSFTGSAETAAVLrsHPAVVQR------SVRVNVEADSLNSALLGPDA-----APGSeafdlfvkev 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 325 VRGAFEFQGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKADSsnyEVV 404
Cdd:PRK11903 285 VREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQA---EVL 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 398009572 405 VGGK------CDKTRGYFVEPTIIETKDPR-AQLMRE-EIFGPVLTVFVYDD 448
Cdd:PRK11903 362 FDGGgfalvdADPAVAACVGPTLLGASDPDaATAVHDvEVFGPVATLLPYRD 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
187-448 |
9.79e-11 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 64.21 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 187 PLEGFVSAITPFNFTA------IA-ANLAGTPALMgntvvwKP-SPTAVLSnYLMYKIMEEAG-LPAGVINFVpCEPA-- 255
Cdd:cd07128 143 PRRGVAVHINAFNFPVwgmlekFApALLAGVPVIV------KPaTATAYLT-EAVVKDIVESGlLPEGALQLI-CGSVgd 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 256 VMDSAVNADprlaAVVFTGStrvfteinKNVFSRLETYHNFPR---------------ISGET---GGKDFHLVhpsadM 317
Cdd:cd07128 215 LLDHLGEQD----VVAFTGS--------AATAAKLRAHPNIVArsirfnaeadslnaaILGPDatpGTPEFDLF-----V 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 318 KHVAAGTVRGAfefqGQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSFMCAVIDETSFNKNKKYIEIAKAD 397
Cdd:cd07128 278 KEVAREMTVKA----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 398 SsnyEVVVGGK-------CDKTRGYFVEPTIIETKDP-RAQLMRE-EIFGPVLTVFVYDD 448
Cdd:cd07128 354 A---EVVFGGPdrfevvgADAEKGAFFPPTLLLCDDPdAATAVHDvEAFGPVATLMPYDS 410
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
215-518 |
7.97e-08 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 55.05 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 215 GNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFVpcEPAVMDSAVNADPRLAAVVFTGSTRVFTEINKNVFSRLETyh 294
Cdd:PLN02174 140 GNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 295 nfprISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQ-GQKCSA-----CSRLYAPKTCwKELKALLIKGQKQIKMGQP 368
Cdd:PLN02174 215 ----VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNnGQACISpdyilTTKEYAPKVI-DAMKKELETFYGKNPMESK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 369 DdfqsfMCAVIDETSFNKNKKYIEIAKADSsnyEVVVGGKCDKtRGYFVEPTIIETKDPRAQLMREEIFGPVLTVFVYDD 448
Cdd:PLN02174 290 D-----MSRIVNSTHFDRLSKLLDEKEVSD---KIVYGGEKDR-ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNN 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009572 449 SKPGYwkevcELVDSTTKyGLTGAVFSRERApIREadkylRYA----AGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:PLN02174 361 LEESF-----DVIRSRPK-PLAAYLFTHNKK-LKE-----RFAatvsAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
187-518 |
1.71e-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: 53.57 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 187 PLeGFVSAITPFNFT----------AIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEEAgLPAGVINFVpcEPAV 256
Cdd:cd07137 101 PL-GVVLVISAWNFPfllslepvigAIAA---------GNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVI--EGGV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 257 MDSAVNADPRLAAVVFTGSTRVfteinKNVFSRLETYHNFPrISGETGGKDFHLVHPSADMKHVAAGTVRGAFEF-QGQK 335
Cdd:cd07137 168 PETTALLEQKWDKIFFTGSPRV-----GRIIMAAAAKHLTP-VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 336 CSACSRLYAPKTCWKELKALLIKGQKqiKMGQPDDFQS-FMCAVIDETSFNKNKKYIEIAKADSSnyeVVVGGKCDKTRG 414
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLE--KFFGENPKESkDLSRIVNSHHFQRLSRLLDDPSVADK---IVHGGERDEKNL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 415 YfVEPTIIETKDPRAQLMREEIFGPVLTVFVYDDSkpgywKEVCELVDSTTKyGLTGAVFSR----ERAPIREAdkylry 490
Cdd:cd07137 317 Y-IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKI-----EESIEIINSRPK-PLAAYVFTKnkelKRRIVAET------ 383
|
330 340
....*....|....*....|....*...
gi 398009572 491 AAGNYYVNDKCTGAVVGQQPFGGSRLSG 518
Cdd:cd07137 384 SSGGVTFNDTVVQYAIDTLPFGGVGESG 411
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
187-441 |
4.99e-06 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 49.34 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 187 PLeGFVSAITPFNFT----------AIAAnlagtpalmGNTVVWKPSPTAVLSNYLMYKIMEeAGLPAGVINFVPCEPAV 256
Cdd:PLN02203 108 PL-GVVLIFSSWNFPiglslepligAIAA---------GNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEGGPAV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 257 MDSAVnaDPRLAAVVFTGSTRVfteinKNVFSRLETYHNFPrISGETGGKD---FHLVHPSADMKHVAAGTVRGAF-EFQ 332
Cdd:PLN02203 177 GEQLL--QHKWDKIFFTGSPRV-----GRIIMTAAAKHLTP-VALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWgSCA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 333 GQKCSACSRLYAPKTCWKELKALLIKGQKQIKMGQPDDFQSfMCAVIDETSFNKNKKYIEIAKADSSnyeVVVGGKCDKt 412
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAAS---IVHGGSIDE- 323
|
250 260
....*....|....*....|....*....
gi 398009572 413 RGYFVEPTIIETKDPRAQLMREEIFGPVL 441
Cdd:PLN02203 324 KKLFIEPTILLNPPLDSDIMTEEIFGPLL 352
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
202-278 |
6.01e-05 |
|
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: 45.61 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 202 AIAAnlagtpalmGNTVVWKPSP----TAVLSNYLMYKIMEEAGLPAGVINFVPCEPAVMDSAVNADPRLAAVVFTGSTR 277
Cdd:cd07129 131 ALAA---------GCPVVVKAHPahpgTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRR 201
|
.
gi 398009572 278 V 278
Cdd:cd07129 202 G 202
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
215-346 |
3.47e-03 |
|
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: 40.15 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009572 215 GNTVVWKPSPTAVLSNYLMYKI----MEEAGLPAGVINFV---PCEPAVMDSAVnaDPRLAAVVFTGSTRVFTEINKNVF 287
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAadtPEEPIAQTLAT--RPEVRIIDFTGSNAFGDWLEANAR 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009572 288 SRLetyhnfprISGETGGKDFHLVHPSADMKHVAAGTVRGAFEFQGQKCSACSRLYAPK 346
Cdd:cd07127 299 QAQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPR 349
|
|
| |
