|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
14-534 |
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: 963.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 14 VSNEPMLSYAPGSPERAGLQAALAEMQSqLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGAL 93
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKS-LTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 94 QAKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFGVSYVEELYAQQPPKNAP 173
Cdd:cd07123 80 EARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 174 GCWNRTEYRPLEGFVLAVSPFNFTAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEI 252
Cdd:cd07123 160 GVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 253 VQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCS 332
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 333 ALSRLYVSRSVWeNGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGG-EVLIGGSGDDSKGFFI 411
Cdd:cd07123 320 AASRAYVPESLW-PEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 412 QPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSIYGLTGAIFASERQALLTATNRSRNAAGNIYYNEK 491
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDK 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2494072 492 CTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENFV 534
Cdd:cd07123 479 PTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFV 521
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
16-545 |
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: 755.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 16 NEPMLSYAPGSPERAGLQAALAEMQSQlPFEVPCIINGQEVRTNNI-QKQPMPHDHARHLCTFHEGSPELVEKATCGALQ 94
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSS-SLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 95 AKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFGVSYVEELYAQQPpKNAPG 174
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQP-ISAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 175 CWNRTEYRPLEGFVLAVSPFNFTAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIV 253
Cdd:TIGR01236 160 EWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGdGVQVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 254 QAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSA 333
Cdd:TIGR01236 240 DQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 334 LSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKE--EGGEVLIGGSGDDSKGFFI 411
Cdd:TIGR01236 320 ASRLYVPHSKWPE-FKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKdpEALTILYGGKYDDSQGYFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 412 QPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSIYGLTGAIFASERQALLTATNRSRNAAGNIYYNEK 491
Cdd:TIGR01236 399 EPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDK 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2494072 492 CTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENFVGLEDFHYPSNL 545
Cdd:TIGR01236 479 CTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
29-533 |
2.41e-144 |
|
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: 425.45 E-value: 2.41e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 29 RAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRA 108
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 109 AIFLKAADLASGKYRYKLMAATMLGqGKNtWQAEIDAAAELADFFRFGVSYVEELYAQQP-PKNAPGCWNRTEYRPLeGF 187
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKN-WVEAIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 188 VLAVSPFNFT-AIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSL 265
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 266 HFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWE 345
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 346 NgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEgGEVLIGGSGDDSKGFFIQPTVILTKVPRSTT 425
Cdd:cd07083 318 P-VLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 426 MVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIFASERQALLTATNRSrnAAGNIYYNEKCTGAVVGQQPFGGA 505
Cdd:cd07083 396 AQEEIFGPVLSVIRYKDDDFAEALEVANSTP-YGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGGF 472
|
490 500
....*....|....*....|....*...
gi 2494072 506 RGSGTNDKAGSISIFYRFVSARSIKENF 533
Cdd:cd07083 473 KLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
45-533 |
1.49e-130 |
|
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: 389.10 E-value: 1.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 45 FEVPCIINGQEVRTNNIQKQP--MPHDhARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKY 122
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDviNPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE-ER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 123 RYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGN 202
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 203 LPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKD 280
Cdd:COG1012 160 WKLAPALAaGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 281 ISSNLdkykvyPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIK 360
Cdd:COG1012 240 AAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD-EFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 361 VGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSG-DDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYV 439
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 440 FEdsDYEKTLELIDTTsIYGLTGAIFASERQALLTATNRSRnaAGNIYYNEKCTGAvVGQQPFGGARGSGTNDKAGSISI 519
Cdd:COG1012 393 FD--DEEEAIALANDT-EYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGREGL 466
|
490
....*....|....
gi 2494072 520 fYRFVSARSIKENF 533
Cdd:COG1012 467 -EEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
16-533 |
6.06e-129 |
|
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: 386.19 E-value: 6.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 16 NEPMLSYAPGSpERAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQA 95
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 96 KDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNtWqAEIDA-AAELADFFRFgvsYVEEL--YAQQPPKNA 172
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKN-W-AEADAdVAEAIDFLEY---YAREMlrLRGFPVEMV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 173 PGCWNRTEYRPLeGFVLAVSPFNF-TAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GA 250
Cdd:cd07124 156 PGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGpGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 251 EIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQK 330
Cdd:cd07124 235 EVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 331 CSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEgGEVLIGGSGDD--SKG 408
Cdd:cd07124 315 CSACSRVIVHESVYDE-FLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSE-GRLLLGGEVLElaAEG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 409 FFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiYGLTGAIFASERQALLTATNRSRnaAGNIYY 488
Cdd:cd07124 393 YFVQPTIFADVPPDHRLAQEEIFGPVLA--VIKAKDFDEALEIANDTE-YGLTGGVFSRSPEHLERARREFE--VGNLYA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2494072 489 NEKCTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENF 533
Cdd:cd07124 468 NRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-533 |
1.96e-111 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 341.14 E-value: 1.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 10 KIPPVSNEPMLSYApgSPE-RAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKA 88
Cdd:PRK03137 1 MVVPYKHEPFTDFS--VEEnVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 89 TCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATM-LGQGKNtWqAEIDA-AAELADFFrfgvsyveELYAQ 166
Cdd:PRK03137 79 MQAALEAFETWKKWSPEDRARILLRAAAII--RRRKHEFSAWLvKEAGKP-W-AEADAdTAEAIDFL--------EYYAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 167 Q--------PPKNAPGCWNRTEYRPLeGFVLAVSPFNF-TAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAG 237
Cdd:PRK03137 147 QmlkladgkPVESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 238 VPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVfkslwkdissNLDKY----KVYP------RIVGETGGKNWHVI 306
Cdd:PRK03137 226 LPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREV----------GLRIYeraaKVQPgqiwlkRVIAEMGGKDAIVV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEngfktQYLE---EIAK-IKVGPCLDwNNYMGPVIGRRAYDN 382
Cdd:PRK03137 296 DEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYD-----EVLEkvvELTKeLTVGNPED-NAYMGPVINQASFDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 383 ITGFIKKAKEEGgEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiYGLTG 462
Cdd:PRK03137 370 IMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA--FIKAKDFDHALEIANNTE-YGLTG 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494072 463 AIFASERQALLTAtnRSRNAAGNIYYNEKCTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENF 533
Cdd:PRK03137 446 AVISNNREHLEKA--RREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
74-519 |
8.26e-108 |
|
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: 329.88 E-value: 8.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAaELADFF 153
Cdd:pfam00171 20 IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE-ERKDELAELETLENGKPLAEARGEVD-RAIDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPkNAPGCWNRTEYRPLeGFVLAVSPFNFTAiggNLPG---SPALV-GNVVVWKPAPAATYSNYLV 229
Cdd:pfam00171 98 RYYAGLARRLDGETLP-SDPGRLAYTRREPL-GVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKPSELTPLTALLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 230 FKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNWHVIHK 308
Cdd:pfam00171 173 AELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 309 SAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIK 388
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDE-FVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 389 KAKEEGGEVLIGGSGDDSKGFFIQPTvILTKVPR-STTMVGEIFGPVVTAYVFEDSDyektlELID--TTSIYGLTGAIF 465
Cdd:pfam00171 326 DAKEEGAKLLTGGEAGLDNGYFVEPT-VLANVTPdMRIAQEEIFGPVLSVIRFKDEE-----EAIEiaNDTEYGLAAGVF 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2494072 466 ASERQALLTATNRSRnaAGNIYYNEKCTGAVVGqQPFGGARGSGTNDKAGSISI 519
Cdd:pfam00171 400 TSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGREGGPYGL 450
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
16-533 |
1.43e-104 |
|
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: 323.36 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 16 NEPMLSYAPgSPERAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQA 95
Cdd:TIGR01237 3 HEPFTDFAD-EENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 96 KDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSYVEELYAQQPPKNAPGC 175
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVRRR-RHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVNSREGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 176 WNRTEYRPLeGFVLAVSPFNFT-AIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIV 253
Cdd:TIGR01237 160 TNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGsGSEVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 254 QAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSA 333
Cdd:TIGR01237 239 DYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 334 LSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGgEVLIGGSGDDSKGFFIQP 413
Cdd:TIGR01237 319 GSRAVVHEKVYDE-VVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 414 TVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiYGLTGAIFASERQALltatNRSRNA--AGNIYYNEK 491
Cdd:TIGR01237 397 TIFADVDRKARLAQEEIFGPVVA--FIRASDFDEALEIANNTE-YGLTGGVISNNRDHI----NRAKAEfeVGNLYFNRN 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2494072 492 CTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENF 533
Cdd:TIGR01237 470 ITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
92-529 |
2.84e-100 |
|
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: 309.91 E-value: 2.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 92 ALQAKDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSYVEELYAQQPPKN 171
Cdd:cd07078 7 ARAAFKAWAALPPAERAAILRKLADLLEER-REELAALETLETGKPIEEALGEVA-RAADTFRYYAGLARRLHGEVIPSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 172 APGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-G 249
Cdd:cd07078 85 DPGELAIVRREPL-GVVGAITPWNFPLLLAAWKLAPALaAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGdG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 250 AEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQ 329
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 330 KCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDS-KG 408
Cdd:cd07078 238 VCTAASRLLVHESIYDE-FVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 409 FFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEdsDYEKTLELIDTTsIYGLTGAIFASERQALLTATNRSRnaAGNIYY 488
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDT-EYGLAAGVFTRDLERALRVAERLE--AGTVWI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2494072 489 NEKcTGAVVGQQPFGGARGSGTNdKAGSISIFYRFVSARSI 529
Cdd:cd07078 392 NDY-SVGAEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
27-532 |
4.35e-78 |
|
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: 254.81 E-value: 4.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 27 PERAGLQAALAEMQSQLPFEVPcIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWND 106
Cdd:cd07125 14 VPLEALADALKAFDEKEWEAIP-IINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 107 RAAIFLKAADLASgKYRYKLMAATMLGQGKnTWQAEIDAAAELADFFRFgvsYVEELYAQQPPKNAPGCW---NRTEYRP 183
Cdd:cd07125 93 RAEILEKAADLLE-ANRGELIALAAAEAGK-TLADADAEVREAIDFCRY---YAAQARELFSDPELPGPTgelNGLELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 184 LeGFVLAVSPFNF---TAIGGNlpgSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQ 258
Cdd:cd07125 168 R-GVFVCISPWNFplaIFTGQI---AAALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGdGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 259 SPNFRSLHFTGSTNVFKSlwkdISSNLDKYKVY-PRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRL 337
Cdd:cd07125 244 HPRIDGVIFTGSTETAKL----INRALAERDGPiLPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 338 YVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEgGEVLIGGSGDDSKGFFIQPTVIl 417
Cdd:cd07125 320 YLQEEIAER-FIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGII- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 418 tKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIfaserQALLTATNR--SRNA-AGNIYYNEKCTG 494
Cdd:cd07125 397 -EIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDINATG-YGLTLGI-----HSRDEREIEywRERVeAGNLYINRNITG 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 2494072 495 AVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKEN 532
Cdd:cd07125 470 AIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLN 507
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
92-529 |
1.94e-68 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 224.80 E-value: 1.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 92 ALQAKDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSYVEELYAQQPPKN 171
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGEVA-RAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 172 APGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-G 249
Cdd:cd06534 81 DPGGEAYVRREPL-GVVGVITPWNFPLLLAAWKLAPALAaGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 250 AEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQ 329
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 330 KCSALSRLYVSRSVWEngfktQYLEEIAKIKVGPCLDWnnymgpvigrraydnitgfiKKAKEeggevliggsgddskgf 409
Cdd:cd06534 234 ICTAASRLLVHESIYD-----EFVEKLVTVLVDVDPDM--------------------PIAQE----------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 410 fiqptviltkvprsttmvgEIFGPVVTAYVFEdsDYEKTLELIDTTsIYGLTGAIFASERQALLTATNRSRnaAGNIYYN 489
Cdd:cd06534 272 -------------------EIFGPVLPVIRFK--DEEEAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGTVYIN 327
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2494072 490 EKCTGaVVGQQPFGGARGSGTNDKAGSISIfYRFVSARSI 529
Cdd:cd06534 328 DSSIG-VGPEAPFGGVKNSGIGREGGPYGL-EEYTRTKTV 365
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
81-510 |
2.04e-63 |
|
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: 214.52 E-value: 2.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 81 SPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYR--YKLMAATMlGQGKNTWQAEIDAAAELadfFRFGVS 158
Cdd:cd07145 19 SREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEelAKLLTIEV-GKPIKQSRVEVERTIRL---FKLAAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 159 YVEELYAQQPP-KNAPGCWNR---TEYRPLeGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPAATYSNYLVF 230
Cdd:cd07145 95 EAKVLRGETIPvDAYEYNERRiafTVREPI-GVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEAGVPPGVIQFIPGGAEIVQAAI-QSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHKS 309
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYGSEVGDEIvTNPKVNMISFTGSTAVGLLIASKAGGTGK------KVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 310 AEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKK 389
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDK-FLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 390 AKEEGGEVLIGGSGDDskGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFASE- 468
Cdd:cd07145 324 AVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANSTE-YGLQASVFTNDi 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2494072 469 RQALLTATNRSrnaAGNIYYNeKCTGAVVGQQPFGGARGSGT 510
Cdd:cd07145 399 NRALKVARELE---AGGVVIN-DSTRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
72-510 |
1.28e-62 |
|
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: 212.04 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 72 RHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQA---EIDAAAE 148
Cdd:cd07093 8 EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE-ARADELALLESLDTGKPITLArtrDIPRAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 149 ladFFRFGVSYVEELYAQQPPkNAPGCWNRTEYRPLeGFVLAVSPFNftaiggnLP-------GSPALV-GNVVVWKPAP 220
Cdd:cd07093 87 ---NFRFFADYILQLDGESYP-QDGGALNYVLRQPV-GVAGLITPWN-------LPlmlltwkIAPALAfGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 221 AATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETG 299
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL------ELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 300 GKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRA 379
Cdd:cd07093 229 GKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDE-FLERFVERAKALKVGDPLDPDTEVGPLISKEH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 380 YDNITGFIKKAKEEGGEVLIGGSGDDS----KGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEdsDYEKTLELIDTT 455
Cdd:cd07093 308 LEKVLGYVELARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFD--DEEEAIELANDT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 456 sIYGLTGAIFASE-RQALLTAtnrSRNAAGNIYYNekCTGAVVGQQPFGGARGSGT 510
Cdd:cd07093 386 -PYGLAAYVWTRDlGRAHRVA---RRLEAGTVWVN--CWLVRDLRTPFGGVKASGI 435
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
67-510 |
6.13e-62 |
|
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: 211.05 E-value: 6.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 67 PHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAAD-LASGKYRY-KLMAATMlgqGKNTWQ--AE 142
Cdd:cd07131 21 PADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAElLKKRKEELaRLVTREM---GKPLAEgrGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 143 IDAAAELADFFrFGVSyvEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNF-TAIggnlPG---SPALV-GNVVVWK 217
Cdd:cd07131 98 VQEAIDMAQYA-AGEG--RRLFGETVPSELPNKDAMTRRQPI-GVVALITPWNFpVAI----PSwkiFPALVcGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 218 PAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIV-QAAIQSPNFRSLHFTGSTNVFKSLwKDISSNLDKykvypRIVG 296
Cdd:cd07131 170 PAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERI-GETCARPNK-----RVAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 297 ETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIG 376
Cdd:cd07131 244 EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE-FLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 377 RRAYDNITGFIKKAKEEGGEVLIGGS----GDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELI 452
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGATLLLGGErltgGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVA--LIEVSSLEEAIEIA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494072 453 DTTSiYGLTGAIFA-SERQAlltatNRSRNA--AGNIYYNEKCTGAVVgQQPFGGARGSGT 510
Cdd:cd07131 401 NDTE-YGLSSAIYTeDVNKA-----FRARRDleAGITYVNAPTIGAEV-HLPFGGVKKSGN 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
74-529 |
1.49e-61 |
|
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: 209.22 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELADFF 153
Cdd:cd07115 10 IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARRLDVPRAADTF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGCwNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKI 232
Cdd:cd07115 89 RYYAGWADKIEGEVIPVRGPFL-NYTVREPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 233 LSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAE 311
Cdd:cd07115 167 MAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSL------ELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 312 VRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAK 391
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDE-FLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 392 EEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFASERQA 471
Cdd:cd07115 320 EEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE-YGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2494072 472 LLTATNRSRnaAGNIYYNekCTGAVVGQQPFGGARGSGTNDKAGSISIfYRFVSARSI 529
Cdd:cd07115 397 AHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSGFGREMGREAL-DEYTEVKSV 449
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
51-509 |
8.31e-61 |
|
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: 207.87 E-value: 8.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 51 INGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAAT 130
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDEL--EARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 131 M-------LGQGKntwqAEIDAAAelaDFFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNF-TAIggn 202
Cdd:cd07097 83 LtreegktLPEAR----GEVTRAG---QIFRYYAGEALRLSGETLPSTRPGVEVETTREPL-GVVGLITPWNFpIAI--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 203 lPG---SPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSL 277
Cdd:cd07097 152 -PAwkiAPALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 278 WKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIA 357
Cdd:cd07097 231 AAAAAARGARVQL------EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDR-FVEALVERTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 358 KIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGG---SGDDsKGFFIQPTVILTKVPRSTTMVGEIFGPV 434
Cdd:cd07097 304 ALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGerlKRPD-EGYYLAPALFAGVTNDMRIAREEIFGPV 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 435 vtAYVFEDSDYEKTLELIDTTSiYGLTGAIFAserQALLTATNRSRNA-AGNIYYNEKCTGaVVGQQPFGGARGSG 509
Cdd:cd07097 383 --AAVIRVRDYDEALAIANDTE-FGLSAGIVT---TSLKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSS 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
85-509 |
9.00e-61 |
|
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: 206.61 E-value: 9.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 85 VEKATCGALQAKDGWETMPWNDRAAIFLKAADLA---SGKYRYKLMAATMLGQGKNTWqaEIDAAAEladFFRFGVSYVE 161
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILeerRDEIADWLIRESGSTRPKAAF--EVGAAIA---ILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 162 ELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVF-KILSEAGVP 239
Cdd:cd07104 77 RPEGEILPSDVPGKESMVRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSRTPVTGGLLIaEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 240 PGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRNAVLQ 318
Cdd:cd07104 156 KGVLNVVPGgGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAL------ELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 319 SVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVL 398
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYD-EFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 399 IGGSGDdskGFFIQPTViLTKV-PRSTTMVGEIFGPVVTAYVFedSDYEKTLELIDTTSiYGLTGAIFASErqalltaTN 477
Cdd:cd07104 309 TGGTYE---GLFYQPTV-LSDVtPDMPIFREEIFGPVAPVIPF--DDDEEAVELANDTE-YGLSAAVFTRD-------LE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2494072 478 RSRNAAGNIYynekcTGAV-VGQQ--------PFGGARGSG 509
Cdd:cd07104 375 RAMAFAERLE-----TGMVhINDQtvndephvPFGGVKASG 410
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
78-509 |
3.39e-60 |
|
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: 205.64 E-value: 3.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 78 HEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATMlgqgkntwQAEIDAAAELADF-FRFG 156
Cdd:cd07150 16 AVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM--ERRADDLIDLL--------IDEGGSTYGKAWFeTTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYVEE-------LYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYL 228
Cdd:cd07150 86 PELLRAaagecrrVRGETLPSDSPGTVSMSVRRPL-GVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIH 307
Cdd:cd07150 165 IAEIMEEAGLPKGVFNVVTGgGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITL------ELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 308 KSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFI 387
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE-FVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 388 KKAKEEGGEVLIGGSGDdskGFFIQPTViLTKVPRS-TTMVGEIFGPVVTAYVFEdsDYEKTLELIDTTSiYGLTGAIFA 466
Cdd:cd07150 318 EDAVAKGAKLLTGGKYD---GNFYQPTV-LTDVTPDmRIFREETFGPVTSVIPAK--DAEEALELANDTE-YGLSAAILT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 467 SERQallTATNRSRNA-AGNIYYNEKC--TGAVVgqqPFGGARGSG 509
Cdd:cd07150 391 NDLQ---RAFKLAERLeSGMVHINDPTilDEAHV---PFGGVKASG 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-526 |
5.23e-59 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 212.03 E-value: 5.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 15 SNEPMLsyapgsperAGLQAALAEMQSQlPFEVPCIINGQEVRTNniqKQPM--PHDHARHLCTFHEGSPELVEKATCGA 92
Cdd:PRK11905 533 SDEATL---------AALDEALNAFAAK-TWHAAPLLAGGDVDGG---TRPVlnPADHDDVVGTVTEASAEDVERALAAA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 93 LQAKDGWETMPWNDRAAIFLKAADLasgkyrY-----KLMAATMLGQGKnTWQaeiDAAAEL---ADFFRFgvsyveelY 164
Cdd:PRK11905 600 QAAFPEWSATPAAERAAILERAADL------MeahmpELFALAVREAGK-TLA---NAIAEVreaVDFLRY--------Y 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 165 AQQPPKNAPGcwnrTEYRPLeGFVLAVSPFNFT-AI-GGNLpgSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPG 241
Cdd:PRK11905 662 AAQARRLLNG----PGHKPL-GPVVCISPWNFPlAIfTGQI--AAALVaGNTVLAKPAEQTPLIAARAVRLLHEAGVPKD 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 242 VIQFIPGGAEIVQAAI-QSPNFRSLHFTGSTNVFKSLWKDISSNLDKYkvyPRIVGETGGKNWHVIHKSAEVRNAVLQSV 320
Cdd:PRK11905 735 ALQLLPGDGRTVGAALvADPRIAGVMFTGSTEVARLIQRTLAKRSGPP---VPLIAETGGQNAMIVDSSALPEQVVADVI 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 321 RGAFEYQGQKCSALSRLYVSRSVWENgfktqYLEEI----AKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGE 396
Cdd:PRK11905 812 ASAFDSAGQRCSALRVLCLQEDVADR-----VLTMLkgamDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 397 VL-IGGSGDDSKGFFIQPTVIltKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIFA--SERQALL 473
Cdd:PRK11905 887 VHqLPLPAETEKGTFVAPTLI--EIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATG-YGLTFGLHSriDETIAHV 963
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2494072 474 TatnrSRNAAGNIYYNEKCTGAVVGQQPFGGaRG-SGTNDKAGSISIFYRFVSA 526
Cdd:PRK11905 964 T----SRIRAGNIYVNRNIIGAVVGVQPFGG-EGlSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
73-509 |
1.09e-57 |
|
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: 198.81 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 73 HLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATM-LGQGKnTW---QAEIDAAAe 148
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLI--RERAEDLARLLtLEQGK-PLaeaRGEVDYAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 149 laDFFRFgvsYVEE---LYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPA 221
Cdd:cd07103 85 --SFLEW---FAEEarrIYGRTIPSPAPGKRILVIKQPV-GVVAAITPWNFPA---AMITrkiAPALaAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 222 ATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkyKvypRIVGETGG 300
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV---K---RVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 301 knwH---VIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGR 377
Cdd:cd07103 230 ---NapfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDE-FVEKLVERVKKLKVGNGLDEGTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 378 RAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTViLTKVPRSTT-MVGEIFGPVVTAYVFEDSDyektlELI---- 452
Cdd:cd07103 306 RAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTV-LTDVTDDMLiMNEETFGPVAPIIPFDTED-----EVIaran 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 453 DTtsIYGLTGAIFaserqalltaTNRSRNA--------AGNIYYNekcTGAVVG-QQPFGGARGSG 509
Cdd:cd07103 380 DT--PYGLAAYVF----------TRDLARAwrvaealeAGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
74-516 |
1.89e-57 |
|
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: 198.94 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRY--KLMAATMlgqGKNTWQA--EIDAAAEL 149
Cdd:cd07086 26 IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEAlgRLVSLEM---GKILPEGlgEVQEMIDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 150 ADFFrFGVSyvEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNF-TAIGG-NLpgSPALV-GNVVVWKPAPAATYSN 226
Cdd:cd07086 103 CDYA-VGLS--RMLYGLTIPSERPGHRLMEQWNPL-GVVGVITAFNFpVAVPGwNA--AIALVcGNTVVWKPSETTPLTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 227 YLVFKILSEA----GVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVfkslWKDISSNLDKYkvYPRIVGETGGKN 302
Cdd:cd07086 177 IAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEV----GRRVGETVARR--FGRVLLELGGNN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 303 WHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDN 382
Cdd:cd07086 251 AIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDE-FLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 383 ITGFIKKAKEEGGEVLIGGSG--DDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVtaYVFEDSDYEKTLELIDTTSiYGL 460
Cdd:cd07086 330 YLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YVIKFDSLEEAIAINNDVP-QGL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 461 TGAIFASERQALLTATNRSRNAAGNIYYNEKCTGAVVGqQPFGGARGSGTNDKAGS 516
Cdd:cd07086 407 SSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGS 461
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
79-510 |
3.17e-56 |
|
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: 195.12 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATMLGQGKNTW---QAEIDAAAELadfFRF 155
Cdd:cd07149 17 VASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIALEAGKPIkdaRKEVDRAIET---LRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 156 GVSYVEELYAQQPPKNA-PGCWNRTEY---RPLeGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPAATYSNY 227
Cdd:cd07149 92 SAEEAKRLAGETIPFDAsPGGEGRIGFtirEPI-GVVAAITPFNFPL---NLVAhkvGPAIaAGNAVVLKPASQTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAGVPPGVIQFIPGGAEIV-QAAIQSPNFRSLHFTGSTNVFKSLWKdiSSNLDKykvyprIVGETGGKNWHVI 306
Cdd:cd07149 168 KLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIAR--KAGLKK------VTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDE-FLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLIGGSGDdskGFFIQPTViLTKVPRSTTMV-GEIFGPVVTAYVFEdsDYEKTLELIDtTSIYGLTGAIF 465
Cdd:cd07149 319 VEEAVEGGARLLTGGKRD---GAILEPTV-LTDVPPDMKVVcEEVFAPVVSLNPFD--TLDEAIAMAN-DSPYGLQAGVF 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2494072 466 ASERQALLTATNRSRnaAGNIYYNEKCTgAVVGQQPFGGARGSGT 510
Cdd:cd07149 392 TNDLQKALKAARELE--VGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
75-509 |
1.10e-55 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 193.92 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 75 CTFHEGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADL--------------ASGKyryklMAATMLGQgknt 138
Cdd:cd07114 11 ARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLieanaeelaeletrDNGK-----LIRETRAQ---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 139 wqaeidaAAELADFFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFN----FTA--IGgnlpgsPAL-VG 211
Cdd:cd07114 82 -------VRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLAkkLA------PALaAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 212 NVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAI-QSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKV 290
Cdd:cd07114 148 NTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALvEHPLVAKIAFTGGTETGRHIARAAAENLAPVTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 291 yprivgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNY 370
Cdd:cd07114 228 ------ELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYD-EFVERLVARARAIRVGDPLDPETQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 371 MGPVIGRRAYDNITGFIKKAKEEGGEVLIGG----SGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDye 446
Cdd:cd07114 301 MGPLATERQLEKVERYVARAREEGARVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-- 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 447 ktlELID--TTSIYGLTGAIFASE-RQALLTAtnrSRNAAG----NIYYnekctgAVVGQQPFGGARGSG 509
Cdd:cd07114 379 ---EAIAlaNDSEYGLAAGIWTRDlARAHRVA---RAIEAGtvwvNTYR------ALSPSSPFGGFKDSG 436
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
74-509 |
9.81e-55 |
|
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: 191.65 E-value: 9.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWE--TMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELAD 151
Cdd:cd07091 32 ICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIE-RDRDELAALESLDNGKPLEESAKGDVALSIK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 152 FFRFGVSYVEELYAQQPPKNAPG-CWNRTEyrPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLV 229
Cdd:cd07091 111 CLRYYAGWADKIQGKTIPIDGNFlAYTRRE--PI-GVCGQIIPWNFPLLMLAWKLAPALAaGNTVVLKPAEQTPLSALYL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 230 FKILSEAGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDIS-SNLDKykvyprIVGETGGKNWHVIH 307
Cdd:cd07091 188 AELIKEAGFPPGVVNIVPGFGPTAGAAISShMDVDKIAFTGSTAVGRTIMEAAAkSNLKK------VTLELGGKSPNIVF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 308 KSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFI 387
Cdd:cd07091 262 DDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDE-FVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 388 KKAKEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELID--TTSIYGLTGAIF 465
Cdd:cd07091 341 ESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED-----EVIEraNDTEYGLAAGVF 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2494072 466 AserQALLTATNRSRN-AAGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07091 416 T---KDINKALRVSRAlKAGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
22-527 |
9.83e-55 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 192.43 E-value: 9.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 22 YAPGSPERAGLQAA----LAEMQSQL------PFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCG 91
Cdd:TIGR01238 3 YGEGRKNSLGIDLDneseLKPLEAQIhawadkTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 92 ALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKnTWQAEIDAAAELADFFRFGVSYVEELYAQQppkn 171
Cdd:TIGR01238 83 AQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGK-TIHNAIAEVREAVDFCRYYAKQVRDVLGEF---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 172 apgcwnrtEYRPLeGFVLAVSPFNFT-AIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGA 250
Cdd:TIGR01238 157 --------SVESR-GVFVCISPWNFPlAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 251 EIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDISSNLDKYKvypRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQ 329
Cdd:TIGR01238 228 ADVGAALTSdPRIAGVAFTGSTEVAQLINQTLAQREDAPV---PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 330 KCSALSRLYVSRSVWENGFkTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEG---GEVLIGGSGDDS 406
Cdd:TIGR01238 305 RCSALRVLCVQEDVADRVL-TMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 407 KGFFIQPTVIltKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIFAseRQALLTATNRSRNAAGNI 486
Cdd:TIGR01238 384 HGTFVAPTLF--ELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTG-YGLTMGVHS--RIETTYRWIEKHARVGNC 458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2494072 487 YYNEKCTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSAR 527
Cdd:TIGR01238 459 YVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-532 |
1.33e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 199.01 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 28 ERAGLQAALAEMQSQlPFEVPCIINGqEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDR 107
Cdd:COG4230 540 VLAALSAALAAAAEK-QWQAAPLIAG-EAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 108 AAIFLKAADLasgkY---RYKLMAATMLGQGKnTWQaeiDAAAEL---ADFFRFgvsyveelYAQQPPKNapgCWNRTEY 181
Cdd:COG4230 618 AAILERAADL----LeahRAELMALLVREAGK-TLP---DAIAEVreaVDFCRY--------YAAQARRL---FAAPTVL 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 182 RPLeGFVLAVSPFNF---------TAiggnlpgspALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GA 250
Cdd:COG4230 679 RGR-GVFVCISPWNFplaiftgqvAA---------ALAaGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGdGE 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 251 EIVQAAIQSPNFRSLHFTGSTNVFKSlwkdISSNL-DKYKVYPRIVGETGGKNWHVIHKSA--E--VRNaVLQSvrgAFE 325
Cdd:COG4230 749 TVGAALVADPRIAGVAFTGSTETARL----INRTLaARDGPIVPLIAETGGQNAMIVDSSAlpEqvVDD-VLAS---AFD 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 326 YQGQKCSALSRLYVsrsvwengfktQylEEIAK------------IKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEE 393
Cdd:COG4230 821 SAGQRCSALRVLCV-----------Q--EDIADrvlemlkgamaeLRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 394 GGEVLIGGSGDDS-KGFFIQPTVIltKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAI------FA 466
Cdd:COG4230 888 GRLVHQLPLPEECaNGTFVAPTLI--EIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATG-YGLTLGVhsrideTI 964
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2494072 467 SErqalltATNRSRnaAGNIYYNEKCTGAVVGQQPFGGaRG-SGTNDKAGSISIFYRFVSARSIKEN 532
Cdd:COG4230 965 DR------VAARAR--VGNVYVNRNIIGAVVGVQPFGG-EGlSGTGPKAGGPHYLLRFATERTVTVN 1022
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
70-509 |
2.69e-54 |
|
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: 189.86 E-value: 2.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 70 HARHLCTFHEGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQA--EIDA 145
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 146 AAELadfFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTA--IGGNLPGSPAlVGNVVVWKPAPAAT 223
Cdd:cd07118 85 AADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPI-GVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 224 YSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKN 302
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSL------ELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 303 WHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVwENGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDN 382
Cdd:cd07118 234 PQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESI-ADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 383 ITGFIKKAKEEGGEVLIGGSGDDS-KGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLT 461
Cdd:cd07118 313 ITDYVDAGRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD--EAIALANDTV-YGLS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2494072 462 GAIFASERQALLTATNRSRnaAGNIYYNEKCTGAVvgQQPFGGARGSG 509
Cdd:cd07118 390 AGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
74-509 |
1.33e-52 |
|
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: 186.07 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQA-KDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELADF 152
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVE-KNRDLLAAIEALDSGKPYHSNALGDLDEIIAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 153 FRFGVSYVEELYAQQPPkNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFK 231
Cdd:cd07144 115 IRYYAGWADKIQGKTIP-TSPNKLAYTLHEPY-GVCGQIIPWNYPLAMAAWKLAPALAaGNTVVIKPAENTPLSLLYFAN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 232 ILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSA 310
Cdd:cd07144 193 LVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA------VTLECGGKSPALVFEDA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 311 EVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWeNGFKTQYLEEIAKI-KVGPCLDWNNYMGPVIGRRAYDNITGFIKK 389
Cdd:cd07144 267 DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIY-DKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 390 AKEEGGEVLIGGSG---DDSKGFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFedSDYEKTLELIDTTSiYGLTGAIF 465
Cdd:cd07144 346 GKKEGAKLVYGGEKapeGLGKGYFIPPT-IFTDVPQDMRIVKeEIFGPVVVISKF--KTYEEAIKKANDTT-YGLAAAVF 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 466 ASErqalLTATNR--SRNAAGNIYYNEKCTGAVvgQQPFGGARGSG 509
Cdd:cd07144 422 TKD----IRRAHRvaRELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
74-531 |
1.43e-52 |
|
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: 185.21 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAeIDAAAELADFF 153
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHA-FEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNA-PGCWNRTEYRPLEGFVLAVSPFNF---TAIGGNLPgspALV-GNVVVWKPAPAATYSNYL 228
Cdd:cd07101 87 RYYARRAERLLKPRRRRGAiPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAIP---ALLaGNAVVLKPDSQTALTALW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFrsLHFTGSTNVFKSLWKDISSNLdkykvypriVG---ETGGKNWH 304
Cdd:cd07101 164 AVELLIEAGLPRDLWQVVTGpGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRL---------IGcslELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 305 VIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNIT 384
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDE-FVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 385 GFIKKAKEEGGEVLIGGSGDDSKG-FFIQPTViLTKVPRSTTM-VGEIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLTG 462
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDLGpYFYEPTV-LTGVTEDMELfAEETFGPVVSIYRVADDD--EAIELANDTD-YGLNA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494072 463 AIFA-SERQALLTAtnrSRNAAGNIYYNEKCTGAVVG-QQPFGGARGSGTNDKAGSISIfYRFVSARSIKE 531
Cdd:cd07101 388 SVWTrDGARGRRIA---ARLRAGTVNVNEGYAAAWASiDAPMGGMKDSGLGRRHGAEGL-LKYTETQTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
74-509 |
1.77e-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: 185.20 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAAElADFF 153
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRER-NDEIARLETIDNGKPIEEARVDIDSS-ADCL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNApGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKI 232
Cdd:cd07090 88 EYYAGLAPTLSGEHVPLPG-GSFAYTRREPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALLLAEI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 233 LSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHKSAEV 312
Cdd:cd07090 166 LTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 313 RNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKE 392
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDE-FTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 393 EGGEVLIGGSGDDSK-----GFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFEDSDyektlELI----DTTsiYGLTG 462
Cdd:cd07090 319 EGAKVLCGGERVVPEdglenGFYVSPC-VLTDCTDDMTIVReEIFGPVMSILPFDTEE-----EVIrranDTT--YGLAA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2494072 463 AIFASE-RQALLTAtnrSRNAAGNIY---YNEKCTgavvgQQPFGGARGSG 509
Cdd:cd07090 391 GVFTRDlQRAHRVI---AQLQAGTCWintYNISPV-----EVPFGGYKQSG 433
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
79-509 |
1.43e-51 |
|
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: 183.28 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFG 156
Cdd:cd07119 31 EGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIRED-AEELARLETLNTGKTLRESEIDID-DVANCFRYY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYVEELYAQQPPKnAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSE 235
Cdd:cd07119 109 AGLATKETGEVYDV-PPHVISRTVREPV-GVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVTPLTTIALFELIEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 236 AGVPPGVIQFIPGGAEIVQAAI-QSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRN 314
Cdd:cd07119 187 AGLPAGVVNLVTGSGATVGAELaESPDVDLVSFTGGTATGRSIMRAAAGNVKKVAL------ELGGKNPNIVFADADFET 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 315 AVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEG 394
Cdd:cd07119 261 AVDQALNGVFFNAGQVCSAGSRLLVEESIHDK-FVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 395 GEVLIGG---SGDD-SKGFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFEDSdyEKTLELIDTTsIYGLTGAIFASER 469
Cdd:cd07119 340 ARLVCGGkrpTGDElAKGYFVEPT-IFDDVDRTMRIVQeEIFGPVLTVERFDTE--EEAIRLANDT-PYGLAGAVWTKDI 415
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2494072 470 QALLTATNRSRnaAGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07119 416 ARANRVARRLR--AGTVWIN--DYHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
81-509 |
5.93e-51 |
|
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: 181.09 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 81 SPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsGKYRYKLMAATMLGQGKNTWQA--EIDAAAelaDFFRFGVS 158
Cdd:cd07094 19 DRADAEEALATARAGAENRRALPPHERMAILERAADLL-KKRAEEFAKIIACEGGKPIKDArvEVDRAI---DTLRLAAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 159 YVEELYAQQPP------KNAPGCWNRTEyrPLeGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPAATYSNYL 228
Cdd:cd07094 95 EAERIRGEEIPldatqgSDNRLAWTIRE--PV-GVVLAITPFNFPL---NLVAhklAPAIaTGCPVVLKPASKTPLSALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVfkslWKDISSNLDKykvyPRIVGETGGKNWHVIH 307
Cdd:cd07094 169 LAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAV----GEALRANAGG----KRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 308 KSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFI 387
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDE-FIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 388 KKAKEEGGEVLIGGSGDDSkgfFIQPTViLTKVPRSTTMVG-EIFGPVVTAYVFedSDYEKTLELIDTTSiYGLTGAIFA 466
Cdd:cd07094 320 EEAVEAGARLLCGGERDGA---LFKPTV-LEDVPRDTKLSTeETFGPVVPIIRY--DDFEEAIRIANSTD-YGLQAGIFT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2494072 467 SERQALLTATNRSRnaAGNIYYNEKcTGAVVGQQPFGGARGSG 509
Cdd:cd07094 393 RDLNVAFKAAEKLE--VGGVMVNDS-SAFRTDWMPFGGVKESG 432
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
80-509 |
1.24e-50 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 180.25 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 80 GSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAAD-LASGKYRYKLMAATMLGQGKNTwQAEIDAAAeLADFFRFGVS 158
Cdd:cd07108 16 SRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADaLEARSEELARLLALETGNALRT-QARPEAAV-LADLFRYFGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 159 YVEELYAQQPPKNaPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAg 237
Cdd:cd07108 94 LAGELKGETLPFG-PDVLTYTVREPL-GVVGAILPWNAPLMLAALKIAPALVaGNTVVLKAAEDAPLAVLLLAEILAQV- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 238 VPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKdissnldkyKVYPRIVG---ETGGKNWHVIHKSAEVR 313
Cdd:cd07108 171 LPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYR---------AAADRLIPvslELGGKSPMIVFPDADLD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 314 NAVLQSVRGA-FEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKE 392
Cdd:cd07108 242 DAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDA-FLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 393 E-GGEVLIGGS----GDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFedSDYEKTLELIDTTSiYGLTGAIFAS 467
Cdd:cd07108 321 TsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPW--KDEDEVIAMANDSH-YGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2494072 468 ERQALLTATNRSRnaAGNIYYNEkCTGAVVGQQpFGGARGSG 509
Cdd:cd07108 398 DLGRALRAAHALE--AGWVQVNQ-GGGQQPGQS-YGGFKQSG 435
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
26-532 |
1.62e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 186.94 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 26 SPERAGLQAALAEMQSQlPFEVPCIING----QEVRtnniqkqpMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWET 101
Cdd:PRK11904 533 RSELEPLAAAIAAFLEK-QWQAGPIINGegeaRPVV--------SPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSR 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 102 MPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKnTWQAEIDAAAELADFFRFgvsyveelYAQQP------PKNAPG- 174
Cdd:PRK11904 604 TPVEERAAILERAADLLE-ANRAELIALCVREAGK-TLQDAIAEVREAVDFCRY--------YAAQArrlfgaPEKLPGp 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 175 CWNRTEYRpLEG---FVlAVSPFNFT-AI--GgnlPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIP 247
Cdd:PRK11904 674 TGESNELR-LHGrgvFV-CISPWNFPlAIflG---QVAAALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLP 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 248 G-GAEIVQAAIQSPNFRSLHFTGSTNVFKSlwkdISSNL---DKYKVYprIVGETGGKNWHVIHKSA---EVRNAVLQSv 320
Cdd:PRK11904 749 GdGATVGAALTADPRIAGVAFTGSTETARI----INRTLaarDGPIVP--LIAETGGQNAMIVDSTAlpeQVVDDVVTS- 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 321 rgAFEYQGQKCSALSRLYVSRSVWEngfktQYLEEI----AKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGE 396
Cdd:PRK11904 822 --AFRSAGQRCSALRVLFVQEDIAD-----RVIEMLkgamAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARL 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 397 VLIGGSGDDS-KGFFIQPTVIltKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIfASERQAllTA 475
Cdd:PRK11904 895 LAQLPLPAGTeNGHFVAPTAF--EIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATG-YGLTLGI-HSRIEE--TA 968
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2494072 476 TNRSRNA-AGNIYYNEKCTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKEN 532
Cdd:PRK11904 969 DRIADRVrVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVN 1026
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
50-527 |
2.73e-50 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 179.69 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 50 IINGQEVRTN-NIQKQPMPHDHARhLCTFHEGSPELVEKATCGALQAKDGWE-TMPWNDRAAIFLKAADLASgKYRYKLM 127
Cdd:cd07082 5 LINGEWKESSgKTIEVYSPIDGEV-IGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLK-ENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 128 AATML--GQGKNTWQAEIDAAAelaDFFRFGVSYVEELYAQQ-PPKNAPG-----CWNRTEyrPLeGFVLAVSPFNFTAi 199
Cdd:cd07082 83 NLLMWeiGKTLKDALKEVDRTI---DYIRDTIEELKRLDGDSlPGDWFPGtkgkiAQVRRE--PL-GVVLAIGPFNYPL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 200 ggNLPGS---PALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVF 274
Cdd:cd07082 156 --NLTVSkliPALImGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 275 KSLwKDISSNLdkykvypRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLE 354
Cdd:cd07082 234 NRL-KKQHPMK-------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADE-LVELLKE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 355 EIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDdsKGFFIQPTVIltkVPRSTTMV---GEIF 431
Cdd:cd07082 305 EVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE--GGNLIYPTLL---DPVTPDMRlawEEPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 432 GPVVTAYVFedSDYEKTLELIDtTSIYGLTGAIFASErqalltaTNRSRNAA-----GNIYYNEKCtgavvgQQ-----P 501
Cdd:cd07082 380 GPVLPIIRV--NDIEEAIELAN-KSNYGLQASIFTKD-------INKARKLAdalevGTVNINSKC------QRgpdhfP 443
|
490 500
....*....|....*....|....*...
gi 2494072 502 FGGARGSGtndkAGSISIFY--RFVSAR 527
Cdd:cd07082 444 FLGRKDSG----IGTQGIGDalRSMTRR 467
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
72-510 |
2.81e-50 |
|
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: 179.11 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 72 RHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKyryklmaATMLG-----QGKNTWQAEIDAA 146
Cdd:cd07107 8 QVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREH-------AEELAlidalDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 147 AELADFFRFGVSYVEELYAQQPPKnAPGCWNRTEYRPLeGFVLAVSPFN----FTAigGNLpGSPALVGNVVVWKPAPAA 222
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPV-GGRNLHYTLREPY-GVVARIVAFNhplmFAA--AKI-AAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 223 TYSNYLVFKILSEAgVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGK 301
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRhPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 302 NWHVIHKSAEVRNAVLQSVRGA-FEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAY 380
Cdd:cd07107 229 NALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDE-VLARVVERVAAIKVGDPTDPATTMGPLVSRQQY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 381 DNITGFIKKAKEEGGEVLIGG----SGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDTTS 456
Cdd:cd07107 308 DRVMHYIDSAKREGARLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQANGVE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2494072 457 iYGLTGAIFASE-RQALLTAtnrSRNAAGNIYYNEKCT---GAvvgqqPFGGARGSGT 510
Cdd:cd07107 386 -YGLTAAIWTNDiSQAHRTA---RRVEAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
30-527 |
3.01e-50 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 186.33 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 30 AGLQAALAEMQSQLPFEVPCIinGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAA 109
Cdd:PRK11809 631 ASLSSALLASAHQKWQAAPML--EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 110 IFLKAADLASGKYRYkLMAATMLGQGKnTWQAEIDAAAELADFFRFgvsyveelYAQQPpknAPGCWNRTeYRPLeGFVL 189
Cdd:PRK11809 709 ILERAADLMEAQMQT-LMGLLVREAGK-TFSNAIAEVREAVDFLRY--------YAGQV---RDDFDNDT-HRPL-GPVV 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 190 AVSPFNFT-AI-GGNLpgSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAA-IQSPNFRSL 265
Cdd:PRK11809 774 CISPWNFPlAIfTGQV--AAALAaGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAAlVADARVRGV 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 266 HFTGSTNVFKSLWKDISSNLD-KYKVYPRIvGETGGKNWHVIHKSA---EVRNAVLQSvrgAFEYQGQKCSALSRLYVSR 341
Cdd:PRK11809 852 MFTGSTEVARLLQRNLAGRLDpQGRPIPLI-AETGGQNAMIVDSSAlteQVVADVLAS---AFDSAGQRCSALRVLCLQD 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 342 SVWENGFkTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVL---IGGSGDDSKGFFIQPTVI-- 416
Cdd:PRK11809 928 DVADRTL-KMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFqaaRENSEDWQSGTFVPPTLIel 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 417 -----LTKvprsttmvgEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIFASERQALLTATNRSRnaAGNIYYNEK 491
Cdd:PRK11809 1007 dsfdeLKR---------EVFGPVLHVVRYNRNQLDELIEQINASG-YGLTLGVHTRIDETIAQVTGSAH--VGNLYVNRN 1074
|
490 500 510
....*....|....*....|....*....|....*.
gi 2494072 492 CTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSAR 527
Cdd:PRK11809 1075 MVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
79-509 |
5.77e-50 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 178.11 E-value: 5.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADlASGKYRYKLMAATMLGQGKNTWQA--EIDAAAelaDFFRFG 156
Cdd:cd07106 15 VASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIAD-AIEANAEELARLLTLEQGKPLAEAqfEVGGAV---AWLRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYV--EELYAQQPPKNApgcwnRTEYRPLeGFVLAVSPFNFTAI--GGNLPgsPALV-GNVVVWKPAPAATYSNYLVFK 231
Cdd:cd07106 91 ASLDlpDEVIEDDDTRRV-----ELRRKPL-GVVAAIVPWNFPLLlaAWKIA--PALLaGNTVVLKPSPFTPLCTLKLGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 232 ILSEAgVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkyKvypRIVGETGGKNWHVIHKSAE 311
Cdd:cd07106 163 LAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTL---K---RVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 312 VRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAK 391
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYD-EFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 392 EEGGEVLIGGSGDDSKGFFIQPTvILTKVPRSTTMVG-EIFGPV--VTAYvfedSDYEKTLELIDtTSIYGLTGAIFASE 468
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPT-IVDDPPEGSRIVDeEQFGPVlpVLKY----SDEDEVIARAN-DSEYGLGASVWSSD 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2494072 469 R-QALLTAtnrSRNAAGNIYYNEKctGAVVGQQPFGGARGSG 509
Cdd:cd07106 389 LeRAEAVA---RRLEAGTVWINTH--GALDPDAPFGGHKQSG 425
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
74-509 |
8.66e-50 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 178.27 E-value: 8.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAAELAdFF 153
Cdd:cd07151 23 LAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRESGSTRIKANIEWGAAMA-IT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGCWNRTeYRPLEGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPAATYSNYLV 229
Cdd:cd07151 101 REAATFPLRMEGRILPSDVPGKENRV-YREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNAVVLKPASDTPITGGLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 230 F-KILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIH 307
Cdd:cd07151 177 LaKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK------KVALELGGNNPFVVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 308 KSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFI 387
Cdd:cd07151 251 EDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYD-EFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 388 KKAKEEGGEVLIGGsgdDSKGFFIQPTViLTKVPRSTTMV-GEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFA 466
Cdd:cd07151 330 EQAVEEGATLLVGG---EAEGNVLEPTV-LSDVTNDMEIArEEIFGPVAPIIKADDE--EEALELANDTE-YGLSGAVFT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2494072 467 SErqalltaTNRSRNAA-----GNIYYNEKctgaVVGQQP---FGGARGSG 509
Cdd:cd07151 403 SD-------LERGVQFArridaGMTHINDQ----PVNDEPhvpFGGEKNSG 442
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
51-516 |
6.37e-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: 176.18 E-value: 6.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 51 INGQEVRT-NNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDG-W-ETMPWNDRAAIFLKAADLASGKYRYkLM 127
Cdd:cd07143 11 INGEFVDSvHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDY-LA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 128 AATMLGQGKN-TWQAEIDAAAElADFFRFGVSYVEELYAQQPPKNaPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGS 206
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQAS-ADTFRYYGGWADKIHGQVIETD-IKKLTYTRHEPI-GVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 207 PALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDIS-S 283
Cdd:cd07143 167 PALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISShMDIDKVAFTGSTLVGRKVMEAAAkS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 284 NLDKYKVyprivgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGP 363
Cdd:cd07143 247 NLKKVTL------ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDK-FVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 364 CLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDS 443
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2494072 444 dyEKTLElIDTTSIYGLTGAIFASErqalLTATNRSRNA--AGNIYYNekCTGAVVGQQPFGGARGSGTNDKAGS 516
Cdd:cd07143 400 --EEAIK-RANDSTYGLAAAVFTNN----INNAIRVANAlkAGTVWVN--CYNLLHHQVPFGGYKQSGIGRELGE 465
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
78-516 |
8.16e-49 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 175.71 E-value: 8.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 78 HEGSPELVEKATCGALQAKDG-WETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFG 156
Cdd:cd07113 32 ASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIE-QHGEELAQLETLCSGKSIHLSRAFEVGQSANFLRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYVEELYAQQPPKNAPG-------CWNRTEyrPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYL 228
Cdd:cd07113 111 AGWATKINGETLAPSIPSmqgerytAFTRRE--PV-GVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLTLLR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHK 308
Cdd:cd07113 188 VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT------RVTLELGGKNAAAFLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 309 SAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIK 388
Cdd:cd07113 262 DADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDE-LVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 389 KAKEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFASE 468
Cdd:cd07113 341 DARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE--EELIQLINDTP-FGLTASVWTNN 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2494072 469 -RQALLTAtnrSRNAAGNIYYNEKC--TGAVvgqqPFGGARGSGTNDKAGS 516
Cdd:cd07113 418 lSKALRYI---PRIEAGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS 461
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
79-509 |
8.36e-49 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 175.12 E-value: 8.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDGWE-TMPWNDRAAIFLKAAD-LASGKYRYKLMAATMLGQGKNTWQAEIDA--------AAE 148
Cdd:cd07089 15 DAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEaLEARKEELRALLVAEVGAPVMTARAMQVDgpighlryFAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 149 LADFFrfgvSYVEELYAQQPPKNAPGCWNRTEyrPLeGFVLAVSPFNF------TAIGgnlpgsPAL-VGNVVVWKPAPA 221
Cdd:cd07089 95 LADSF----PWEFDLPVPALRGGPGRRVVRRE--PV-GVVAAITPWNFpfflnlAKLA------PALaAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 222 ATYSNYLVFKILSEAGVPPGVIQFIPGGAEIV-QAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGG 300
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK------RVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 301 KNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENGFKTqyLEEIA-KIKVGPCLDWNNYMGPVIGRRA 379
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEA--LAAAFeALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 380 YDNITGFIKKAKEEGGEVLIGGSGDDS--KGFFIQPTViLTKVPRSTTMVG-EIFGPVVTAYVFEDSDyektlELID--T 454
Cdd:cd07089 314 RDRVEGYIARGRDEGARLVTGGGRPAGldKGFYVEPTL-FADVDNDMRIAQeEIFGPVLVVIPYDDDD-----EAVRiaN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 455 TSIYGLTGAIFASERQALLTATNRSRnaAGNIYYNekcTGAVVG-QQPFGGARGSG 509
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIR--TGSVGIN---GGGGYGpDAPFGGYKQSG 438
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
80-515 |
1.53e-48 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 174.02 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 80 GSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLA---SGKYRYKLMAATMLGQGKNTWqaEIDAAAEladFFRFG 156
Cdd:cd07152 10 ADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLeehADEIADWIVRESGSIRPKAGF--EVGAAIG---ELHEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYVEELYAQQPPkNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSN-YLVFKILS 234
Cdd:cd07152 85 AGLPTQPQGEILP-SAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDPRTPVSGgVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 235 EAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRN 314
Cdd:cd07152 163 EAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL------ELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 315 AVLQSVRGAFEYQGQKCSALSRLYVSRSVWEngfktQYLEEIA----KIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKA 390
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVAD-----AYTAKLAakakHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 391 KEEGGEVLIGGSGDdskGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFeDSDyEKTLELIDTTSiYGLTGAIFASERQ 470
Cdd:cd07152 312 VAAGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVF-DSD-EEAVALANDTE-YGLSAGIISRDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2494072 471 ALLTATNRSRnaAGNIYYNEKcTGAVVGQQPFGGARGSGTNDKAG 515
Cdd:cd07152 386 RAMALADRLR--TGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
85-515 |
2.74e-48 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 173.23 E-value: 2.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 85 VEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATM-LGQGKNTWQAEIDAAAELAdffRFGVS---YV 160
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELL--KANKEELARLIsRETGKPLWEAQTEVAAMAG---KIDISikaYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 161 EELYAQQPP-KNAPGCwnrTEYRPLeGfVLAV-SPFNFTaigGNLPGS---PALV-GNVVVWKPAPAATYSNYLVFKILS 234
Cdd:cd07095 77 ERTGERATPmAQGRAV---LRHRPH-G-VMAVfGPFNFP---GHLPNGhivPALLaGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 235 EAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVG-ETGGKNWHVIHKSAEVR 313
Cdd:cd07095 149 EAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGK------ILAlEMGGNNPLVVWDVADID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 314 NAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEE 393
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 394 GGEVLIGGSGDDSKGFFIQPTVILTkvprsTTMVG----EIFGPVVTAYVFEdsDYEKTLELIDTTSiYGLTGAIFASER 469
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPGIIDV-----TDAADvpdeEIFGPLLQVYRYD--DFDEAIALANATR-FGLSAGLLSDDE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 470 QALLTATNRSRnaAGNIYYNEKCTGAvVGQQPFGGARGSGtNDKAG 515
Cdd:cd07095 375 ALFERFLARIR--AGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPS 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
74-510 |
5.03e-48 |
|
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: 173.69 E-value: 5.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQA-KDG--WETMPWNDRAAIFLKAADLASgkyRYKLMAATM--LGQGK---NTWQAEIDA 145
Cdd:cd07141 35 ICEVQEGDKADVDKAVKAARAAfKLGspWRTMDASERGRLLNKLADLIE---RDRAYLASLetLDNGKpfsKSYLVDLPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 146 AAELadfFRFGVSYVEELYAQQPPKNAPG-CWNRTEyrPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAAT 223
Cdd:cd07141 112 AIKV---LRYYAGWADKIHGKTIPMDGDFfTYTRHE--PV-GVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 224 YSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDIS-SNLDkykvypRIVGETGGK 301
Cdd:cd07141 186 LTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISShPDIDKVAFTGSTEVGKLIQQAAGkSNLK------RVTLELGGK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 302 NWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYD 381
Cdd:cd07141 260 SPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDE-FVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 382 NITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTViLTKVPRSTTMVG-EIFGPVVTAYVFEDSDyektlELID--TTSIY 458
Cdd:cd07141 339 KILELIESGKKEGAKLECGGKRHGDKGYFIQPTV-FSDVTDDMRIAKeEIFGPVQQIFKFKTID-----EVIEraNNTTY 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2494072 459 GLTGAIFASERQALLTATNRSRnaAGNIYYNekCTGAVVGQQPFGGARGSGT 510
Cdd:cd07141 413 GLAAAVFTKDIDKAITFSNALR--AGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
74-509 |
7.29e-48 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 172.79 E-value: 7.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQA-KDG-WETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELAD 151
Cdd:cd07112 15 LAEVAACDAADVDRAVAAARRAfESGvWSRLSPAERKAVLLRLADLIE-AHRDELALLETLDMGKPISDALAVDVPSAAN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 152 FFRFGVSYVEELYAQQPP--KNAPGCWNRteyRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYL 228
Cdd:cd07112 94 TFRWYAEAIDKVYGEVAPtgPDALALITR---EPL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPGGAEIVQAAI-QSPNFRSLHFTGSTNVFKSLWKDIS-SNLDkykvypRIVGETGGKNWHVI 306
Cdd:cd07112 170 LAELALEAGLPAGVLNVVPGFGHTAGEALgLHMDVDALAFTGSTEVGRRFLEYSGqSNLK------RVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAE-VRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITG 385
Cdd:cd07112 244 FADAPdLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDE-FLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 386 FIKKAKEEGGEVLIGGSGD--DSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDTTsIYGLTGA 463
Cdd:cd07112 323 YIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE--EAVALANDS-VYGLAAS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 464 IFASERQALLTATNRSRnaAGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07112 400 VWTSDLSRAHRVARRLR--AGTVWVN--CFDEGDITTPFGGFKQSG 441
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
71-509 |
1.33e-47 |
|
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: 172.03 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 71 ARHLCTFHEGSPELVEKATCGALQA-KDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKNTWQAEIDAAAeL 149
Cdd:cd07109 7 GEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREH-ADELARLESLDTGKPLTQARADVEA-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 150 ADFFRFGVSYVEELYAQQPPKNaPGCWNRTEYRPLeGFVLAVSPFNFTA-IGGNLPGsPAL-VGNVVVWKPAPAATYSNY 227
Cdd:cd07109 85 ARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPH-GVTGHIIPWNYPLqITGRSVA-PALaAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNldkykVYPrIVGETGGKNWHVI 306
Cdd:cd07109 162 RLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN-----VVP-VTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEngfktQYLEEIAK----IKVGPCLDwNNYMGPVIGRRAYDN 382
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYD-----EVLERLVErfraLRVGPGLE-DPDLGPLISAKQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 383 ITGFIKKAKEEGGEVLIGG---SGDDSKGFFIQPTvILTKVPRSTTMV-GEIFGPVVTAYVFEDSdyEKTLELIDTTSiY 458
Cdd:cd07109 310 VEGFVARARARGARIVAGGriaEGAPAGGYFVAPT-LLDDVPPDSRLAqEEIFGPVLAVMPFDDE--AEAIALANGTD-Y 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2494072 459 GLTGAIFASE-RQALLTAtnrSRNAAGNIYYNEKCTGAVVgQQPFGGARGSG 509
Cdd:cd07109 386 GLVAGVWTRDgDRALRVA---RRLRAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
74-509 |
1.46e-47 |
|
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: 171.92 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATM---LGQ---GKNTWQAE----- 142
Cdd:cd07138 27 IGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAY--EARADELAQAItleMGApitLARAAQVGlgigh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 143 IDAAAELADFFRFgvsyveelyaQQPPKNApgcwnRTEYRPLeGFVLAVSPFNFTA--IGGNLpgSPAL-VGNVVVWKPA 219
Cdd:cd07138 105 LRAAADALKDFEF----------EERRGNS-----LVVREPI-GVCGLITPWNWPLnqIVLKV--APALaAGCTVVLKPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 220 PAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDISSNLdkyKvypRIVGET 298
Cdd:cd07138 167 EVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAhPDVDMVSFTGSTRAGKRVAEAAADTV---K---RVALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 299 GGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgfktqyLEEIAK-----IKVGPCLDWNNYMGP 373
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAE------AEEIAAaaaeaYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 374 VIGRRAYDNITGFIKKAKEEGGEVLIGGSG---DDSKGFFIQPTViLTKV-PRSTTMVGEIFGPVVTAYVFEDSDyektl 449
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGPGrpeGLERGYFVKPTV-FADVtPDMTIAREEIFGPVLSIIPYDDED----- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2494072 450 ELI----DTtsIYGLTGAIFASERQALLTATNRSRnaAGNIYYNEkctGAVVGQQPFGGARGSG 509
Cdd:cd07138 389 EAIaianDT--PYGLAGYVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
80-509 |
7.72e-47 |
|
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: 169.84 E-value: 7.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 80 GSPELVEKATCGALQAKDGWETMPWNDRAAiFLKAADLASGKYRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSY 159
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAK-YLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 160 VEELYAQQP---PKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSE 235
Cdd:cd07110 94 AEQLDAKAEravPLPSEDFKARVRREPV-GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 236 AGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHKSAEVRN 314
Cdd:cd07110 173 AGLPPGVLNVVTGTGDEAGAPLAAhPGIDKISFTGSTATGSQVMQAAAQDIK------PVSLELGGKSPIIVFDDADLEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 315 AVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEG 394
Cdd:cd07110 247 AVEWAMFGCFWNNGQICSATSRLLVHESIADA-FLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 395 GEVLIGGS--GDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTT--SIYGLTGAIFASErq 470
Cdd:cd07110 326 ARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-----EAIALAndSEYGLAAAVISRD-- 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2494072 471 alLTATNRSRNA--AGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07110 399 --AERCDRVAEAleAGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
99-509 |
1.15e-46 |
|
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: 168.91 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 99 WETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAeLADFFRFGVSYVEELYAQQPPKNAPGCWNR 178
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLE-SRRDEFIEAMMEETGATAAWAGFNVDL-AAGMLREAASLITQIIGGSIPSDKPGTLAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 179 TEYRPLeGFVLAVSPFNFTAI-GGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIP----GGAEIV 253
Cdd:cd07105 94 VVKEPV-GVVLGIAPWNAPVIlGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThspeDAPEVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 254 QAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSA 333
Cdd:cd07105 173 EALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK------PVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 334 LSRLYVSRSVWENgFKTQYLEEIAKIKVGPCldwnnYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSK-GFFIQ 412
Cdd:cd07105 247 TERIIVHESIADE-FVEKLKAAAEKLFAGPV-----VLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPsGTSMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 413 PTvILTKVPRSTTMVG-EIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFAS-ERQALLTAtnrSRNAAGNIYYNe 490
Cdd:cd07105 321 PT-ILDNVTPDMDIYSeESFGPVVSIIRVKDE--EEAVRIANDSE-YGLSAAVFTRdLARALAVA---KRIESGAVHIN- 392
|
410 420
....*....|....*....|..
gi 2494072 491 kctGAVVG---QQPFGGARGSG 509
Cdd:cd07105 393 ---GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
74-489 |
1.50e-46 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 169.37 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQA--EIDAAAelaD 151
Cdd:cd07088 26 VATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR-ENADELAKLIVEEQGKTLSLArvEVEFTA---D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 152 FFRFGVS----YVEELYAQQPPknapgcwNRTEY---RPLeGFVLAVSPFNFTA--IGGNLpgSPALV-GNVVVWKPAPA 221
Cdd:cd07088 102 YIDYMAEwarrIEGEIIPSDRP-------NENIFifkVPI-GVVAGILPWNFPFflIARKL--APALVtGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 222 ATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGG 300
Cdd:cd07088 172 TPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL------ELGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 301 KNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAY 380
Cdd:cd07088 246 KAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDE-FMEKLVEKMKAVKVGDPFDAATDMGPLVNEAAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 381 DNITGFIKKAKEEGGEVLIGGSGDDS-KGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFedSDYEKTLELIDTTSiYG 459
Cdd:cd07088 325 DKVEEMVERAVEAGATLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELANDSE-YG 401
|
410 420 430
....*....|....*....|....*....|
gi 2494072 460 LTGAIFASERQALLTATNRSRnaAGNIYYN 489
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
72-509 |
9.60e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 168.13 E-value: 9.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 72 RHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQA--EIDAAAEL 149
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVL-ENREELLDLVQLETGKARRHAfeEVLDVALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 150 AdffRFGVSYVEELYAQQPPKNA-PGCWNRTEYRPLEGFVLAVSPFNF---TAIGGNLPgspALV-GNVVVWKPAPAATY 224
Cdd:PRK09407 122 A---RYYARRAPKLLAPRRRAGAlPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAIP---ALLaGNAVVLKPDSQTPL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 225 SNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFrsLHFTGSTNVFKSLWKDISSNLdkykvypriVG---ETGG 300
Cdd:PRK09407 196 TALAAVELLYEAGLPRDLWQVVTGpGPVVGTALVDNADY--LMFTGSTATGRVLAEQAGRRL---------IGfslELGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 301 KNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAY 380
Cdd:PRK09407 265 KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDE-FVRAFVAAVRAMRLGAGYDYSADMGSLISEAQL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 381 DNITGFIKKAKEEGGEVLIGGSGDDSKG-FFIQPTViLTKVPRSTTMVG-EIFGPVVTAYVFEDSDyektlELI----DT 454
Cdd:PRK09407 344 ETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTV-LTGVTPDMELAReETFGPVVSVYPVADVD-----EAVeranDT 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2494072 455 TsiYGLTGAIFA-SERQALLTAtnrSRNAAGNIYYNEKCT---GAVvgQQPFGGARGSG 509
Cdd:PRK09407 418 P--YGLNASVWTgDTARGRAIA---ARIRAGTVNVNEGYAaawGSV--DAPMGGMKDSG 469
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
74-509 |
1.37e-45 |
|
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: 167.14 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMlGQGK---NTWQAEIDAAAela 150
Cdd:cd07559 29 LCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL-DNGKpirETLAADIPLAI--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 151 DFFRF--GVSYVEELYAQQPPKNApgcWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNY 227
Cdd:cd07559 105 DHFRYfaGVIRAQEGSLSEIDEDT---LSYHFHEPL-GVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKPASQTPLSIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAgVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvYPRIVgETGGKNWHVI 306
Cdd:cd07559 181 VLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IPVTL-ELGGKSPNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVR-----NAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYD 381
Cdd:cd07559 254 FDDAMDAdddfdDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDE-FIERAVERFEAIKVGNPLDPETMMGAQVSKDQLE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 382 NITGFIKKAKEEGGEVLIGG----SGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTT-- 455
Cdd:cd07559 333 KILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE-----EAIAIAnd 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2494072 456 SIYGLTGAIFAserQALLTATNRSRN-AAGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07559 408 TEYGLGGGVWT---RDINRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
75-489 |
2.81e-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: 165.50 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 75 CTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKA-ADLASGKYRYKLMAATMLGQGKNTWQAEIDAAAELADFF 153
Cdd:cd07102 10 AERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAvELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 rfgVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFN---FTAIGGNLPgspALV-GNVVVWKPAPAATYSNYLV 229
Cdd:cd07102 90 ---ISIAEEALADIRVPEKDGFERYIRREPL-GVVLIIAPWNypyLTAVNAVIP---ALLaGNAVILKHSPQTPLCGERF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 230 FKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISsnldkykvyPRIVG---ETGGKNWHVI 306
Cdd:cd07102 163 AAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAA---------GRFIKvglELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDA-FVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLIGG---SGDDSKGFFIQPTViLTKVPRS-TTMVGEIFGPVVTAYVFEdSDyEKTLELIDTTSiYGLTG 462
Cdd:cd07102 313 IADAIAKGARALIDGalfPEDKAGGAYLAPTV-LTNVDHSmRVMREETFGPVVGIMKVK-SD-AEAIALMNDSE-YGLTA 388
|
410 420 430
....*....|....*....|....*....|
gi 2494072 463 AIFASERQ---ALLTATNrsrnaAGNIYYN 489
Cdd:cd07102 389 SVWTKDIAraeALGEQLE-----TGTVFMN 413
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
80-509 |
1.61e-44 |
|
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: 163.57 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 80 GSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAaELADFFRFGVSY 159
Cdd:cd07147 18 AGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE-ERFEELAETIVLEAGKPIKDARGEVA-RAIDTFRIAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 160 VEELYAQQPP-------KNAPGCWNRTeyrPLeGFVLAVSPFNFTAiggNLPG---SPAL-VGNVVVWKPAPAATYSNYL 228
Cdd:cd07147 96 ATRIYGEVLPldisargEGRQGLVRRF---PI-GPVSAITPFNFPL---NLVAhkvAPAIaAGCPFVLKPASRTPLSALI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVfkslWKDISSNLDKYKVypriVGETGGKNWHVIHK 308
Cdd:cd07147 169 LGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAV----GWDLKARAGKKKV----VLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 309 SAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIK 388
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDE-FKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 389 KAKEEGGEVLIGGSgddSKGFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFEDSDyeKTLELIDtTSIYGLTGAIFAS 467
Cdd:cd07147 320 EAVDAGAKLLTGGK---RDGALLEPT-ILEDVPPDMEVNCeEVFGPVVTVEPYDDFD--EALAAVN-DSKFGLQAGVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2494072 468 ERQALLTATNrsrnaagniyyNEKCTGAVVG--------QQPFGGARGSG 509
Cdd:cd07147 393 DLEKALRAWD-----------ELEVGGVVINdvptfrvdHMPYGGVKDSG 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
74-509 |
6.52e-44 |
|
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: 162.24 E-value: 6.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMlGQGK---NTWQAEIDAAAela 150
Cdd:cd07117 29 LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL-DNGKpirETRAVDIPLAA--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 151 DFFRF--GVSYVEELYAQQPPKNAPGCWNRteyRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNY 227
Cdd:cd07117 105 DHFRYfaGVIRAEEGSANMIDEDTLSIVLR---EPI-GVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAgVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvYPRIVgETGGKNWHVI 306
Cdd:cd07117 181 ELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANII 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:cd07117 254 FDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDE-FVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLIGG----SGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTT--SIYGL 460
Cdd:cd07117 333 VDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED-----EVIDMAndSEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2494072 461 TGAIFASErqalltaTNRSRNAA-----GNIY---YNEKCTGAvvgqqPFGGARGSG 509
Cdd:cd07117 408 GGGVFTKD-------INRALRVAravetGRVWvntYNQIPAGA-----PFGGYKKSG 452
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
79-509 |
1.50e-43 |
|
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: 161.20 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADLASGkyRYKLMAATM------------LGQGKNTWQAeID 144
Cdd:cd07139 32 EATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEA--RADELARLWtaengmpiswsrRAQGPGPAAL-LR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 145 AAAELADFFRFgvsyvEElyAQQPPKNAPGcwnRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAAT 223
Cdd:cd07139 109 YYAALARDFPF-----EE--RRPGSGGGHV---LVRREPV-GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 224 YSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNW 303
Cdd:cd07139 178 LDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL------ARVTLELGGKSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 304 HVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNI 383
Cdd:cd07139 252 AIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYD-EVVEALAAAVAALKVGDPLDPATQIGPLASARQRERV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 384 TGFIKKAKEEGGEVLIGGSG--DDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTT--SIYG 459
Cdd:cd07139 331 EGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED-----DAVRIAndSDYG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2494072 460 LTGAIFASERQALLTATNRSRnaAGNIYYNekctGAVVG-QQPFGGARGSG 509
Cdd:cd07139 406 LSGSVWTADVERGLAVARRIR--TGTVGVN----GFRLDfGAPFGGFKQSG 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
79-519 |
1.91e-43 |
|
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: 161.12 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKD--GWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFG 156
Cdd:cd07142 37 EGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 157 VSYVEELYAQQPPKNAPgCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSE 235
Cdd:cd07142 116 AGWADKIHGMTLPADGP-HHVYTLHEPI-GVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 236 AGVPPGVIQFIPGGAEIVQAAIQSP-NFRSLHFTGSTNVFKSLWKDIS-SNLDKYKVyprivgETGGKNWHVIHKSAEVR 313
Cdd:cd07142 194 AGLPDGVLNIVTGFGPTAGAAIASHmDVDKVAFTGSTEVGKIIMQLAAkSNLKPVTL------ELGGKSPFIVCEDADVD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 314 NAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEE 393
Cdd:cd07142 268 KAVELAHFALFFNQGQCCCAGSRTFVHESIYDE-FVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 394 GGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELID--TTSIYGLTGAIFAserQA 471
Cdd:cd07142 347 GATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD-----EVIKraNNSKYGLAAGVFS---KN 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2494072 472 LLTATNRSRN-AAGNIYYNekCTGAVVGQQPFGGARGSGTNDKAGSISI 519
Cdd:cd07142 419 IDTANTLSRAlKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGIYAL 465
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
76-509 |
3.72e-42 |
|
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: 157.12 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 76 TFHEGSPELVEKATCGALQAkdgWETMPWND----RAAIFLKAADlASGKYRYKLMAATMLGQGKNTWQA--EIDAAAEL 149
Cdd:cd07120 12 TYADGGVAEAEAAIAAARRA---FDETDWAHdprlRARVLLELAD-AFEANAERLARLLALENGKILGEArfEISGAISE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 150 ADFFRfGVSYVEELYAQQPpknAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYL 228
Cdd:cd07120 88 LRYYA-GLARTEAGRMIEP---EPGSFSLVLREPM-GVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPAGQTAQINAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFKILSEA-GVPPGVIQ-FIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVI 306
Cdd:cd07120 163 IIRILAEIpSLPAGVVNlFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGL------ELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE-VRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLI-GGSGDD--SKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDTTsIYGLTGA 463
Cdd:cd07120 316 VERAIAAGAEVVLrGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALANDT-DYGLAAS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 464 IFASERQALLTATNRSRnaAGNIYYNEKctGAVVGQQPFGGARGSG 509
Cdd:cd07120 393 VWTRDLARAMRVARAIR--AGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
106-515 |
1.38e-41 |
|
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: 155.21 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 106 DRAAIFLKAADLASGKyryKLMAATMLgqgknTWQAEI---DAAAEL---ADFFRFGVSYVE---------ELYAQQPPK 170
Cdd:cd07146 41 QRSAILNKAAALLEAR---REEFARLI-----TLESGLclkDTRYEVgraADVLRFAAAEALrddgesfscDLTANGKAR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 171 NAPGCWnrteyRPLeGFVLAVSPFNF------TAIGgnlpgsPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVI 243
Cdd:cd07146 113 KIFTLR-----EPL-GVVLAITPFNHplnqvaHKIA------PAIAaNNRIVLKPSEKTPLSAIYLADLLYEAGLPPDML 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 244 QFIPGG-AEIVQAAIQSPNFRSLHFTGSTNVFKSlwkdISSNLDkykvYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRG 322
Cdd:cd07146 181 SVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKA----IAATAG----YKRQLLELGGNDPLIVMDDADLERAATLAVAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 323 AFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGS 402
Cdd:cd07146 253 SYANSGQRCTAVKRILVHESVADE-FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 403 GDdskGFFIQPTViLTKVPRSTTMV-GEIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLTGAIFaserqalltaTNRSrN 481
Cdd:cd07146 332 RQ---GALYAPTV-LDHVPPDAELVtEETFGPVAPVIRVKDLD--EAIAISNSTA-YGLSSGVC----------TNDL-D 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2494072 482 AAGNIYYNEKCTGAVVGQQ--------PFGGARGSGTNDKAG 515
Cdd:cd07146 394 TIKRLVERLDVGTVNVNEVpgfrselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
85-509 |
6.27e-40 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 150.30 E-value: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 85 VEKATCGALQAKDGWETMPWNDRAAIFLKAAD-LASGKYRY-KLMAATM---LGQGKntwqAEIDAAAELADFF-RFGVS 158
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADlLRERKDELaRLITLEMgkpIAEAR----AEVEKCAWICRYYaENAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 159 YVEELYAQQPPKNApgcwnRTEYRPLeGFVLAVSPFNFtaiggnlP-------GSPAL-VGNVVVWKPAPAATYSNYLVF 230
Cdd:cd07100 77 FLADEPIETDAGKA-----YVRYEPL-GVVLGIMPWNF-------PfwqvfrfAAPNLmAGNTVLLKHASNVPGCALAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSA 310
Cdd:cd07100 144 ELFREAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKK------SVLELGGSDPFIVLDDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 311 EVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKA 390
Cdd:cd07100 218 DLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYD-EFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 391 KEEGGEVLIGGSGDDSKGFFIQPTViLTKVPR-STTMVGEIFGPVvtAYVFEDSDYEKTLELIDTTSiYGLTGAIFAS-E 468
Cdd:cd07100 297 VAAGATLLLGGKRPDGPGAFYPPTV-LTDVTPgMPAYDEELFGPV--AAVIKVKDEEEAIALANDSP-FGLGGSVFTTdL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2494072 469 RQALLTAtnrSRNAAGNIYYNEkctgaVVGQQ---PFGGARGSG 509
Cdd:cd07100 373 ERAERVA---RRLEAGMVFING-----MVKSDprlPFGGVKRSG 408
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
74-509 |
1.17e-37 |
|
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: 144.29 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADlASGKYRYKLMAATMLGQGKntwqAEIDAAAEL---A 150
Cdd:cd07099 9 LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKR-ALADHADELAELLHAETGK----PRADAGLEVllaL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 151 DFFRFGVSYVEELYAQQPPKNAPGCWN---RTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSN 226
Cdd:cd07099 84 EAIDWAARNAPRVLAPRKVPTGLLMPNkkaTVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 227 YLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPnFRSLHFTGSTNVFKSLWKDISSNLdkykvYPrIVGETGGKNWHVI 306
Cdd:cd07099 163 ELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERL-----IP-VVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYD-EFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLIGGSGDDSKGFFIQPTViLTKVPRSTT-MVGEIFGPVVTAYVFEDSDyektlELIDTT--SIYGLTGA 463
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTV-LTDVPHDMDvMREETFGPVLPVMPVADED-----EAIALAndSRYGLSAS 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2494072 464 IFA-SERQALLTAtnrSRNAAGNIYYNEKCTGAVVGQQPFGGARGSG 509
Cdd:cd07099 389 VFSrDLARAEAIA---RRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
81-521 |
3.99e-37 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 143.56 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 81 SPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsGKYRYKLmaATMLGQ--GKNTWQAEIDAAAELAdffRFGVS 158
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL-EENKEEL--AEVIARetGKPLWEAATEVTAMIN---KIAIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 159 ---YVEELYAQQPPknAPGCWNRTEYRPLeGfVLAV-SPFNFTaigGNLPGS---PALV-GNVVVWKPAPAATYSNYLVF 230
Cdd:PRK09457 109 iqaYHERTGEKRSE--MADGAAVLRHRPH-G-VVAVfGPYNFP---GHLPNGhivPALLaGNTVVFKPSELTPWVAELTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVG-ETGGKNWHVIHKS 309
Cdd:PRK09457 182 KLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK------ILAlEMGGNNPLVIDEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 310 AEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENGFKTQYLEEIAKIKVGPcldWNN----YMGPVIGRRAYDNITG 385
Cdd:PRK09457 256 ADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGR---WDAepqpFMGAVISEQAAQGLVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 386 FIKKAKEEGGEVLIGGSGDDSKGFFIQPTVI-LTKVPRSTTMvgEIFGPVVTayVFEDSDYEKTLELIDTTSiYGLTGAI 464
Cdd:PRK09457 333 AQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdVTGVAELPDE--EYFGPLLQ--VVRYDDFDEAIRLANNTR-FGLSAGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2494072 465 FASERQALLTATNRSRnaAGNIYYNEKCTGAvVGQQPFGGARGSGtNDKAgsiSIFY 521
Cdd:PRK09457 408 LSDDREDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG-NHRP---SAYY 457
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
47-467 |
4.58e-37 |
|
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: 143.04 E-value: 4.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 47 VPCIINGQEVRTNNIQKQPMpHDHA--RHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASgKYRY 124
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDV-YNPAtgEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE-ENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 125 KLMAATMLGQGKNTWQAEidaaaelADFFR------FGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTA 198
Cdd:cd07085 79 ELARLITLEHGKTLADAR-------GDVLRglevveFACSIPHLLKGEYLENVARGIDTYSYRQPL-GVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 199 IggnLPG---SPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVF 274
Cdd:cd07085 151 M---IPLwmfPMAIAcGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 275 KSLWkDISSNLDKykvypRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLE 354
Cdd:cd07085 228 EYIY-ERAAANGK-----RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADE-WIPKLVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 355 EIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDD----SKGFFIQPTvILTKV-PRSTTMVGE 429
Cdd:cd07085 301 RAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKvpgyENGNFVGPT-ILDNVtPDMKIYKEE 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 2494072 430 IFGPVVTayVFEDSDYEKTLELIDtTSIYGLTGAIFAS 467
Cdd:cd07085 380 IFGPVLS--IVRVDTLDEAIAIIN-ANPYGNGAAIFTR 414
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
42-509 |
2.47e-36 |
|
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: 141.48 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 42 QLPFEvpCIINGQEV-----RTNNIQKqpmPHDHARhLCTFHEGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKA 114
Cdd:cd07140 3 KMPHQ--LFINGEFVdaeggKTYNTIN---PTDGSV-ICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 115 ADLASgkyRYKLMAATMlgqgkntwqAEIDAAA--ELA---------DFFRFGVSYVEELYAQQPPKNA--PG---CWNR 178
Cdd:cd07140 77 ADLME---EHQEELATI---------ESLDSGAvyTLAlkthvgmsiQTFRYFAGWCDKIQGKTIPINQarPNrnlTLTK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 179 TEyrPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPApAATYSNYLVFKILS-EAGVPPGVIQFIPG-GAEIVQA 255
Cdd:cd07140 145 RE--PI-GVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPA-QVTPLTALKFAELTvKAGFPKGVINILPGsGSLVGQR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 256 AIQSPNFRSLHFTGSTNVFKSLWKDIS-SNLDKYKVyprivgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSAL 334
Cdd:cd07140 221 LSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKKVSL------ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 335 SRLYVSRSVwENGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPT 414
Cdd:cd07140 295 GRLFVEESI-HDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 415 VILTKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSiYGLTGAIFASE-RQALLTAtnrSRNAAGNIY---YNE 490
Cdd:cd07140 374 VFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTE-YGLASGVFTKDiNKALYVS---DKLEAGTVFvntYNK 449
|
490
....*....|....*....
gi 2494072 491 KCTGAvvgqqPFGGARGSG 509
Cdd:cd07140 450 TDVAA-----PFGGFKQSG 463
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
74-510 |
3.05e-36 |
|
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: 140.54 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRyKLMAATMLGQGKNTWQAEIDAAAELADFF 153
Cdd:cd07092 10 IATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAE-ELAALESRNTGKPLHLVRDDELPGAVDNF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKI 232
Cdd:cd07092 89 RFFAGAARTLEGPAAGEYLPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 233 LSEaGVPPGVIQFIPGGAEIV-QAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRIVGETGGKNWHVIHKSAE 311
Cdd:cd07092 168 AAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 312 VRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAK 391
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDE-FVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 392 eEGGEVLIGGSGDDSKGFFIQPTVIlTKVPRSTTMV-GEIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLTGAIFASERQ 470
Cdd:cd07092 320 -AHARVLTGGRRAEGPGYFYEPTVV-AGVAQDDEIVqEEIFGPVVTVQPFDDED--EAIELANDVE-YGLASSVWTRDVG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2494072 471 ALLTATNRSRnaAGNIYYNekCTGAVVGQQPFGGARGSGT 510
Cdd:cd07092 395 RAMRLSARLD--FGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
186-509 |
5.62e-36 |
|
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: 140.22 E-value: 5.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 186 GFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRS 264
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 265 LHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVW 344
Cdd:cd07111 229 VAFTGSTEVGRALRRATAGTG------KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 345 ENGFKtQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTVIlTKVPRST 424
Cdd:cd07111 303 EELIR-KLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLF-TNVPPAS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 425 TMV-GEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFaSER--QALLTAtnrSRNAAGNIYYNekCTGAVVGQQP 501
Cdd:cd07111 381 RIAqEEIFGPVLVVLTFRTA--KEAVALANNTP-YGLAASVW-SENlsLALEVA---LSLKAGVVWIN--GHNLFDAAAG 451
|
....*...
gi 2494072 502 FGGARGSG 509
Cdd:cd07111 452 FGGYRESG 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
79-519 |
8.38e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 137.63 E-value: 8.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAeidAAAEL---ADFF 153
Cdd:PLN02466 91 EGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAELpmfARLF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGcWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKI 232
Cdd:PLN02466 167 RYYAGWADKIHGLTVPADGPH-HVQTLHEPI-GVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 233 LSEAGVPPGVIQFIPGGAEIVQAAIQSP-NFRSLHFTGSTNVFKSLWKDIS-SNLDKYKVyprivgETGGKNWHVIHKSA 310
Cdd:PLN02466 245 LHEAGLPPGVLNVVSGFGPTAGAALASHmDVDKLAFTGSTDTGKIVLELAAkSNLKPVTL------ELGGKSPFIVCEDA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 311 EVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEngfktQYLEEiAKIK-----VGPCLDWNNYMGPVIGRRAYDNITG 385
Cdd:PLN02466 319 DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD-----EFVEK-AKARalkrvVGDPFKKGVEQGPQIDSEQFEKILR 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 386 FIKKAKEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELID--TTSIYGLTGA 463
Cdd:PLN02466 393 YIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD-----EVIRraNNTRYGLAAG 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2494072 464 IFAserQALLTATNRSRN-AAGNIYYNekCTGAVVGQQPFGGARGSGTNDKAGSISI 519
Cdd:PLN02466 468 VFT---QNLDTANTLSRAlRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKGIYSL 519
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
177-509 |
8.71e-35 |
|
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: 136.66 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 177 NRTEYRPLeGFVLAVSPFNF---TAIGgnlPGSPAL-VGNVVVWKPAPAATYSNY----LVFKILSEAGVPPGVIQFIPG 248
Cdd:cd07098 114 ARVEYEPL-GVVGAIVSWNYpfhNLLG---PIIAALfAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTC 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 249 GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvyPRIVgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQG 328
Cdd:cd07098 190 LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLDDADLDQIASIIMRGTFQSSG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 329 QKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGS----GD 404
Cdd:cd07098 264 QNCIGIERVIVHEKIYDK-LLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryphPE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 405 DSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTsIYGLTGAIFASERQAL------LTATNR 478
Cdd:cd07098 343 YPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMV--VMKASDDEEAVEIANST-EYGLGASVFGKDIKRArriasqLETGMV 419
|
330 340 350
....*....|....*....|....*....|.
gi 2494072 479 SRNAAGNIYYNEkctgavvgQQPFGGARGSG 509
Cdd:cd07098 420 AINDFGVNYYVQ--------QLPFGGVKGSG 442
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
74-509 |
1.73e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 136.10 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDG--WETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGK---NTWQAEIDAAAE 148
Cdd:PLN02766 49 IARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIE-EHIEELAALDTIDAGKlfaLGKAVDIPAAAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 149 LadfFRFGVSYVEELYAQQPpKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNY 227
Cdd:PLN02766 128 L---LRYYAGAADKIHGETL-KMSRQLQGYTLKEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSP-NFRSLHFTGSTNVFKSLWKDIS-SNLDKYKVyprivgETGGKNWHV 305
Cdd:PLN02766 203 FYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHmDVDKVSFTGSTEVGRKIMQAAAtSNLKQVSL------ELGGKSPLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 306 IHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITG 385
Cdd:PLN02766 277 IFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDE-FVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 386 FIKKAKEEGGEVLIGGSGDDSKGFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFEdsDYEKTLELIDTTSiYGLTGAI 464
Cdd:PLN02766 356 YIEHGKREGATLLTGGKPCGDKGYYIEPT-IFTDVTEDMKIAQdEIFGPVMSLMKFK--TVEEAIKKANNTK-YGLAAGI 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2494072 465 FAserQALLTATNRSRNA-AGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:PLN02766 432 VT---KDLDVANTVSRSIrAGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
176-465 |
1.78e-34 |
|
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: 135.80 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 176 WNrteyrPLeGFVLAVSPFNF--------TAIggnlpgspALV-GNVVVWKPAPAATYSNYLVFKILSEA----GVPPGV 242
Cdd:cd07130 130 WN-----PL-GVVGVITAFNFpvavwgwnAAI--------ALVcGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 243 IQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVfkslWKDISSNLDKYkvYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRG 322
Cdd:cd07130 196 ASLVCGGADVGEALVKDPRVPLVSFTGSTAV----GRQVGQAVAAR--FGRSLLELGGNNAIIVMEDADLDLAVRAVLFA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 323 AFEYQGQKCSALSRLYVSRSVWE---NGFKTQYleeiAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLI 399
Cdd:cd07130 270 AVGTAGQRCTTTRRLIVHESIYDevlERLKKAY----KQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLF 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 400 GGSGDDSKGFFIQPTVIlTKVPRSTTMVGEIFGPVVtaYVFEDSDYEKTLELIDTTSiYGLTGAIF 465
Cdd:cd07130 346 GGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPIL--YVLKFDTLEEAIAWNNEVP-QGLSSSIF 407
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
86-510 |
2.37e-34 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 135.97 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 86 EKATCGALQAKDGWETMPWNDRAAIFLKAADL--ASGKYRYKLMAatmLGQGKNTWQA--EIDAAAELADFFrfgvsyVE 161
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLiiANKEDLAQLMT---LEQGKPLKEAigEVAYGASFLEYF------AE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 162 E---LYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAG 237
Cdd:PLN02278 136 EakrVYGDIIPSPFPDRRLLVLKQPV-GVVGAITPWNFPLAMITRKVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 238 VPPGVIQFIPGGA-EIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRNAV 316
Cdd:PLN02278 215 IPPGVLNVVMGDApEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSL------ELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 317 LQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGE 396
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDK-FAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 397 VLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSdyEKTLELIDTTSiYGLTGAIFASERQALLTAT 476
Cdd:PLN02278 368 VLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRDLQRAWRVS 444
|
410 420 430
....*....|....*....|....*....|....
gi 2494072 477 NRSRNaaGNIYYNEKCTGAVVGqqPFGGARGSGT 510
Cdd:PLN02278 445 EALEY--GIVGVNEGLISTEVA--PFGGVKQSGL 474
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
74-465 |
9.43e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 133.85 E-value: 9.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRyKLMAATMLGQGKnTWQ----AEIDAAAEL 149
Cdd:PRK13252 35 LATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND-ELAALETLDTGK-PIQetsvVDIVTGADV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 150 ADFFRFGVSYVEElyAQQPPKNAPGCWNRTEyrPLeGFVLAvspfnftaIGG-NLPGSPALvgnvvvWKPAPAATYSNYL 228
Cdd:PRK13252 113 LEYYAGLAPALEG--EQIPLRGGSFVYTRRE--PL-GVCAG--------IGAwNYPIQIAC------WKSAPALAAGNAM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 229 VFK--------------ILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDkykvypRI 294
Cdd:PRK13252 174 IFKpsevtpltalklaeIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 295 VGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPV 374
Cdd:PRK13252 248 TMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAA-FEARLLERVERIRIGDPMDPATNFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 375 IGRRAYDNITGFIKKAKEEGGEVLIGGS----GDDSKGFFIQPTViLTKVPRSTTMV-GEIFGPVVTAYVFEDSDyektl 449
Cdd:PRK13252 327 VSFAHRDKVLGYIEKGKAEGARLLCGGErlteGGFANGAFVAPTV-FTDCTDDMTIVrEEIFGPVMSVLTFDDED----- 400
|
410 420
....*....|....*....|
gi 2494072 450 ELI----DTTsiYGLTGAIF 465
Cdd:PRK13252 401 EVIaranDTE--YGLAAGVF 418
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
76-509 |
1.74e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 129.86 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 76 TFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADL--ASGKYRYKLMAATMlgqGKNTWQAEIDAAaELADFF 153
Cdd:PRK09406 16 TFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLleAEADQVAALMTLEM---GKTLASAKAEAL-KCAKGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGCWNR--TEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVF 230
Cdd:PRK09406 92 RYYAEHAEALLADEPADAAAVGASRayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHASNVPQTALYLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSA 310
Cdd:PRK09406 171 DLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKK------TVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 311 EVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKA 390
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDA-FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 391 KEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYvfEDSDYEKTLELIDTTSiYGLTGAIFASErq 470
Cdd:PRK09406 324 VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLY--RVADIDEAIEIANATT-FGLGSNAWTRD-- 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2494072 471 alltATNRSRNA----AGNIYYNekctGAVVG--QQPFGGARGSG 509
Cdd:PRK09406 399 ----EAEQERFIddleAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
186-509 |
2.34e-31 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 127.16 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 186 GFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFR 263
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 264 SLHFTGSTNVFKSLWKDISSNldkykVYPrIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSV 343
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQM-----VKP-VSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 344 WENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGS--GDDSKGFFIQPTVIlTKVP 421
Cdd:PLN02467 307 ASE-FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTII-TDVT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 422 RSTTM-VGEIFGPVVTAYVFedSDYEKTLELIDTTSiYGLTGAIFAS--ERQALLTATNRsrnaAGNIYYNekCTGAVVG 498
Cdd:PLN02467 385 TSMQIwREEVFGPVLCVKTF--STEDEAIELANDSH-YGLAGAVISNdlERCERVSEAFQ----AGIVWIN--CSQPCFC 455
|
330
....*....|.
gi 2494072 499 QQPFGGARGSG 509
Cdd:PLN02467 456 QAPWGGIKRSG 466
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
74-444 |
9.29e-31 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 125.02 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYkLMAATMLGQGKNTWQAEIDAAAELADFF 153
Cdd:PRK13473 30 LAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE-FARLESLNCGKPLHLALNDEIPAIVDVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPG--CWNRTEyrPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVF 230
Cdd:PRK13473 109 RFFAGAARCLEGKAAGEYLEGhtSMIRRD--PV-GVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEAgVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKslwKDISSNLDKYKvypRIVGETGGKNWHVIHKS 309
Cdd:PRK13473 186 ELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGK---HVLSAAADSVK---RTHLELGGKAPVIVFDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 310 AEVrNAVLQSVR-GAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIK 388
Cdd:PRK13473 259 ADL-DAVVEGIRtFGYYNAGQDCTAACRIYAQRGIYDD-LVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2494072 389 KAKEEG-GEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSD 444
Cdd:PRK13473 337 RAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
180-509 |
1.70e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 124.20 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 180 EYRPLeGFVLAVSPFNF---TAIGGNLPgsPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAA 256
Cdd:PRK13968 123 EYRPL-GTILAIMPWNFplwQVMRGAVP--ILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 257 IQSPNFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSR 336
Cdd:PRK13968 200 INDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 337 LYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTVI 416
Cdd:PRK13968 274 FIIEEGIAS-AFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 417 LTKVPRSTTMVGEIFGPVVTAYVFEDSdyEKTLELIDtTSIYGLTGAIF-ASERQALLTAtnrSRNAAGNIYYNEKCtgA 495
Cdd:PRK13968 353 ANVTPEMTAFREELFGPVAAITVAKDA--EHALELAN-DSEFGLSATIFtTDETQARQMA---ARLECGGVFINGYC--A 424
|
330
....*....|....
gi 2494072 496 VVGQQPFGGARGSG 509
Cdd:PRK13968 425 SDARVAFGGVKKSG 438
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
74-509 |
1.69e-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: 121.41 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 74 LCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYkLMAATMLGQGK---NTWQAEIDAAAela 150
Cdd:cd07116 29 FCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM-LAVAETWDNGKpvrETLAADIPLAI--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 151 DFFRF--GVSYVEELYAQQPPKNAPGcwnRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNY 227
Cdd:cd07116 105 DHFRYfaGCIRAQEGSISEIDENTVA---YHFHEPL-GVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQTPASIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 228 LVFKILSEAgVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLdkykvYPrIVGETGGKNWHVI 306
Cdd:cd07116 181 VLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKSPNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 ------HKSAEVRNAVLQSVRGAFEyQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAY 380
Cdd:cd07116 254 fadvmdADDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDR-FMERALERVKAIKQGNPLDTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 381 DNITGFIKKAKEEGGEVLIGG----SGDDSKGFFIQPTVILTKvPRSTTMVGEIFGPVVTAYVFEdsDYEKTLELIDTTs 456
Cdd:cd07116 332 EKILSYIDIGKEEGAEVLTGGerneLGGLLGGGYYVPTTFKGG-NKMRIFQEEIFGPVLAVTTFK--DEEEALEIANDT- 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2494072 457 IYGLTGAIFASERQallTATNRSRN-AAGNIYYNekCTGAVVGQQPFGGARGSG 509
Cdd:cd07116 408 LYGLGAGVWTRDGN---TAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
79-518 |
2.53e-29 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 121.48 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 79 EGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRY--KLMAATM---LGQGkntwqaeIDAAAELADFF 153
Cdd:PLN02315 52 EASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYlgRLVSLEMgkiLAEG-------IGEVQEIIDMC 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 154 RFGVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNF--TAIGGNlpGSPALV-GNVVVWKPAPAATYSNYLVF 230
Cdd:PLN02315 125 DFAVGLSRQLNGSIIPSERPNHMMMEVWNPL-GIVGVITAFNFpcAVLGWN--ACIALVcGNCVVWKGAPTTPLITIAMT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 231 KILSEA----GVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVI 306
Cdd:PLN02315 202 KLVAEVleknNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLL------ELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 307 HKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGF 386
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDD-VLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 387 IKKAKEEGGEVLIGGSGDDSKGFFIQPTVILTKvPRSTTMVGEIFGPVVtaYVFEDSDYEKTLElIDTTSIYGLTGAIFA 466
Cdd:PLN02315 355 IEIIKSQGGKILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIE-INNSVPQGLSSSIFT 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2494072 467 SERQALLTATNRSRNAAGNIYYNEKCTGAVVGqQPFGGARGSGTNDKAGSIS 518
Cdd:PLN02315 431 RNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSDS 481
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
82-509 |
1.33e-28 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 118.86 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 82 PELVEKATCGALQAKD----GWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQA--EIDAAAELADFFrf 155
Cdd:PRK11241 43 PKMGADETRAAIDAANralpAWRALTAKERANILRRWFNLMM-EHQDDLARLMTLEQGKPLAEAkgEISYAASFIEWF-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 156 gVSYVEELYAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILS 234
Cdd:PRK11241 120 -AEEGKRIYGDTIPGHQADKRLIVIKQPI-GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 235 EAGVPPGVIQFIPGGAEIVQAAIQS-PNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVR 313
Cdd:PRK11241 198 RAGIPAGVFNVVTGSAGAVGGELTSnPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSL------ELGGNAPFIVFDDADLD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 314 NAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEnGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEE 393
Cdd:PRK11241 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYD-RFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 394 GGEVLIGGSGDDSKGFFIQPTvILTKVPRSTTMVG-EIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLTGAIFASErqal 472
Cdd:PRK11241 351 GARVVCGGKAHELGGNFFQPT-ILVDVPANAKVAKeETFGPLAPLFRFKDEA--DVIAQANDTE-FGLAAYFYARD---- 422
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2494072 473 LTATNRSRNAA--GNIYYNekcTGAVVGQ-QPFGGARGSG 509
Cdd:PRK11241 423 LSRVFRVGEALeyGIVGIN---TGIISNEvAPFGGIKASG 459
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
107-529 |
1.66e-27 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 115.76 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 107 RAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFGVSYVEELYAQQPPkNAPGCWNRTEYRPLeG 186
Cdd:PRK09847 83 RKAVLNKLADLME-AHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVAT-TSSHELAMIVREPV-G 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 187 FVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRS 264
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 265 LHFTGSTNVFKSLWKDI-SSNLDkykvypRIVGETGGKNWHVIHKSA-EVRNAVLQSVRGAFEYQGQKCSALSRLYVSRS 342
Cdd:PRK09847 240 IAFTGSTRTGKQLLKDAgDSNMK------RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 343 VwENGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAkEEGGEVLIGGSGDDSKGfFIQPTVILTKVPR 422
Cdd:PRK09847 314 I-ADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREG-ESKGQLLLDGRNAGLAA-AIGPTIFVDVDPN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 423 STTMVGEIFGPVVTAYVFedSDYEKTLELIDtTSIYGLTGAIFASErqaLLTATNRSRN-AAGNIYYNEKCTGAVVgqQP 501
Cdd:PRK09847 391 ASLSREEIFGPVLVVTRF--TSEEQALQLAN-DSQYGLGAAVWTRD---LSRAHRMSRRlKAGSVFVNNYNDGDMT--VP 462
|
410 420
....*....|....*....|....*...
gi 2494072 502 FGGARGSGtNDKAGSISIFYRFVSARSI 529
Cdd:PRK09847 463 FGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
182-465 |
2.15e-27 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 114.45 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 182 RPLeGFVLAVSPFNFT--AIGGNLpgSPALV-GNVVVWKPApAATYSNYLVF-KILSEAGVPPGVIQFIPG-GAEIVQAA 256
Cdd:PRK10090 70 RAL-GVTTGILPWNFPffLIARKM--APALLtGNTIVIKPS-EFTPNNAIAFaKIVDEIGLPKGVFNLVLGrGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 257 IQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSR 336
Cdd:PRK10090 146 AGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCL------ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 337 LYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNY-MGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTV 415
Cdd:PRK10090 220 VYVQKGIYDQ-FVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTL 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2494072 416 ILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDtTSIYGLTGAIF 465
Cdd:PRK10090 299 LLDVRQEMSIMHEETFGPVLPVVAFDTLE--EAIAMAN-DSDYGLTSSIY 345
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
96-511 |
3.58e-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: 111.36 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 96 KDGWetMPWNDRAAIFLKAADLASGkyRYKLMAATMLGQGKNTWqaeIDAAAELA---DFFRFGVSYVEELYAQQPPKN- 171
Cdd:cd07148 37 RNNW--LPAHERIAILERLADLMEE--RADELALLIAREGGKPL---VDAKVEVTraiDGVELAADELGQLGGREIPMGl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 172 APGCWNRTEYRPLE--GFVLAVSPFNFTAiggNL---PGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQF 245
Cdd:cd07148 110 TPASAGRIAFTTREpiGVVVAISAFNHPL---NLivhQVAPAIaAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 246 IPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLwkdissnldKYKVYP--RIVGETGGKNWHVIHKSAEVRNAVLQSVRGA 323
Cdd:cd07148 187 VPCENAVAEKLVTDPRVAFFSFIGSARVGWML---------RSKLAPgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 324 FEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSG 403
Cdd:cd07148 258 FYHAGQVCVSVQRVFVPAEIADD-FAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 404 DDSKGFfiQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTTSI--YGLTGAIFAserQALLTATN--RS 479
Cdd:cd07148 337 LSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLD-----EAIAQANSlpVAFQAAVFT---KDLDVALKavRR 406
|
410 420 430
....*....|....*....|....*....|..
gi 2494072 480 RNAAGnIYYNEKcTGAVVGQQPFGGARGSGTN 511
Cdd:cd07148 407 LDATA-VMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
85-524 |
3.33e-25 |
|
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: 108.48 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 85 VEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKyRYKLMAATMLGQGKnTWQAEIDAAAELADFfRFGVSYVEELY 164
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGK-GWMFAENICGDQVQL-RARAFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 165 AQQPPKNAPGCWNRTE---YRPLEGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAG-VP 239
Cdd:cd07084 78 IPHEPGNHLGQGLKQQshgYRWPYGPVLVIGAFNFPLWIPLLQLAGALAmGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 240 PGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISsnldkykvYPRIVGETGGKNWHVIHKSAEVRNAVL-Q 318
Cdd:cd07084 158 PEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAK--------QARIYLELAGFNWKVLGPDAQAVDYVAwQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 319 SVRGAFEYQGQKCSALSRLYVSrsvwENGFKTQYLEE----IAKIKVGpcldwnnymGPVIGRRAYDNITGFIKKAKEEG 394
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVP----ENWSKTPLVEKlkalLARRKLE---------DLLLGPVQTFTTLAMIAHMENLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 395 GEVLIGG-------SGDDSKGFFIQPTVILTKVP--RSTTMVG-EIFGPVVTAYVFEDSDYEKTLELIDttSIYG-LTGA 463
Cdd:cd07084 297 GSVLLFSgkelknhSIPSIYGACVASALFVPIDEilKTYELVTeEIFGPFAIVVEYKKDQLALVLELLE--RMHGsLTAA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2494072 464 IFASERQALLTATNRSRnAAGNIYYNEKCTGAV-VGQQPFGGARGSGTNDKAG---SISIFYRFV 524
Cdd:cd07084 375 IYSNDPIFLQELIGNLW-VAGRTYAILRGRTGVaPNQNHGGGPAADPRGAGIGgpeAIKLVWRCH 438
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
186-509 |
4.29e-23 |
|
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: 101.92 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 186 GFVLAVSPFNF---TAIGgnlPGSPALV-GNVVVWKPAPAATYSNYLVFKILSEAgVPPGVIQFIPGGAEIVQAAIQSPn 261
Cdd:cd07134 102 GVCLIISPWNYpfnLAFG---PLVSAIAaGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALLELP- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 262 FRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSR 341
Cdd:cd07134 177 FDHIFFTGSPAVGKIVMAAAAKHLAS------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 342 SVwENGFKTQYLEEIAKI-----KVGPCLDwnnyMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSkGFFIQPTVI 416
Cdd:cd07134 251 SV-KDAFVEHLKAEIEKFygkdaARKASPD----LARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA-QRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 417 LTKVPRSTTMVGEIFGPVVTAYVFEDSDyektlELIDTTSIYG--LTGAIFASERQALLTATNRSrnAAGNIYYNEKCTG 494
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLD-----EVIEYINAKPkpLALYVFSKDKANVNKVLART--SSGGVVVNDVVLH 397
|
330
....*....|....*
gi 2494072 495 AVVGQQPFGGARGSG 509
Cdd:cd07134 398 FLNPNLPFGGVNNSG 412
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
21-471 |
5.15e-22 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 99.82 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 21 SYAPGSPERAglqaalaeMQSQLPFEVPCIINGQEVRTNNiqkqpmphdhARHLCTFHEGSPELVEK-----------AT 89
Cdd:PLN02419 96 SWLSTSPEQS--------TQPQMPPRVPNLIGGSFVESQS----------SSFIDVINPATQEVVSKvplttneefkaAV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 90 CGALQAKDGWETMPWNDRAAIFLKAADLASgKYRYKLMAATMLGQGKNTWQAEidaaaelADFFRfGVSYVEEL------ 163
Cdd:PLN02419 158 SAAKQAFPLWRNTPITTRQRVMLKFQELIR-KNMDKLAMNITTEQGKTLKDSH-------GDIFR-GLEVVEHAcgmatl 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 164 -YAQQPPKNAPGCWNRTEYRPLeGFVLAVSPFNFTAIggnLP--GSPALV--GNVVVWKPAPAATYSNYLVFKILSEAGV 238
Cdd:PLN02419 229 qMGEYLPNVSNGVDTYSIREPL-GVCAGICPFNFPAM---IPlwMFPVAVtcGNTFILKPSEKDPGASVILAELAMEAGL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 239 PPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSnldKYKvypRIVGETGGKNWHVIHKSAEVrNAVLQ 318
Cdd:PLN02419 305 PDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAA---KGK---RIQSNMGAKNHGLVLPDANI-DATLN 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 319 SVRGA-FEYQGQKCSALSRLYV--SRSVWENgfktQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGG 395
Cdd:PLN02419 378 ALLAAgFGAAGQRCMALSTVVFvgDAKSWED----KLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 396 EVLIGGSG----DDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAyvFEDSDYEKTLELIDTTSiYGLTGAIFASERQA 471
Cdd:PLN02419 454 KLLLDGRDivvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVC--MQANSFDEAISIINKNK-YGNGAAIFTSSGAA 530
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
178-510 |
1.06e-21 |
|
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: 97.68 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 178 RTEYRPLeGFVLAVSPFNF---TAIGgnlPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAgVPPGVIQFIPGGAEIV 253
Cdd:cd07135 103 RIRKEPL-GVVLIIGPWNYpvlLALS---PLVGAIaAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 254 QAAIQSPnFRSLHFTGSTNVFKSLWKDISSNLDkykvyPrIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSA 333
Cdd:cd07135 178 TALLEQK-FDKIFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 334 LSRLYVSRSVwengfktqYLEEIAKIK------VGPCLDWNNYMGPVIGRRAYDNITGFIKKAKeegGEVLIGGSGDDSK 407
Cdd:cd07135 251 PDYVLVDPSV--------YDEFVEELKkvldefYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGGEMDEAT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 408 gFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSD-YEKTLELIDTTsiygLTGAIFA---SERQALLTATNrsrnaA 483
Cdd:cd07135 320 -RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDeAIKVINSRDTP----LALYIFTddkSEIDHILTRTR-----S 389
|
330 340
....*....|....*....|....*..
gi 2494072 484 GNIYYNEKCTGAVVGQQPFGGARGSGT 510
Cdd:cd07135 390 GGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
158-509 |
1.17e-21 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 98.18 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 158 SYVEELYAQQPPKNAPG-CWNRTEyrPLeGFVLAVSPFNFTAIGGNLPGSPALV-GNVVVWKPAPAATYSNYLVFKILSE 235
Cdd:PTZ00381 85 EYLKPEKVDTVGVFGPGkSYIIPE--PL-GVVLVIGAWNYPLNLTLIPLAGAIAaGNTVVLKPSELSPHTSKLMAKLLTK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 236 AgVPPGVIQFIPGGAEIVQAAIQSPnFRSLHFTGSTNVFKSLWKDISSNLdkykvYPRIVgETGGKNWHVIHKSAEVRNA 315
Cdd:PTZ00381 162 Y-LDPSYVRVIEGGVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENL-----TPCTL-ELGGKSPVIVDKSCNLKVA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 316 VLQSVRGAFEYQGQKCSALSRLYVSRSVwengfKTQYLEEIA-KIK--VGPCLDWNNYMGPVIGRRAYDNITGFIKkakE 392
Cdd:PTZ00381 234 ARRIAWGKFLNAGQTCVAPDYVLVHRSI-----KDKFIEALKeAIKefFGEDPKKSEDYSRIVNEFHTKRLAELIK---D 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 393 EGGEVLIGGSGDDSKGFfIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDyeKTLELIDTTSiYGLTGAIFASER--- 469
Cdd:PTZ00381 306 HGGKVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENID--EVLEFINSRP-KPLALYYFGEDKrhk 381
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2494072 470 QALLTATNrsrnaAGNIYYNEkCTGAVVGQQ-PFGGARGSG 509
Cdd:PTZ00381 382 ELVLENTS-----SGAVVIND-CVFHLLNPNlPFGGVGNSG 416
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
178-509 |
3.79e-21 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 96.06 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 178 RTEYRPLeGFVLAVSPFNF---TAIGgnlPGSPALV-GNVVVWKP---APAAtySNyLVFKILSEAgVPPGVIQFIPGGA 250
Cdd:cd07087 95 YVIPEPL-GVVLIIGPWNYplqLALA---PLIGAIAaGNTVVLKPselAPAT--SA-LLAKLIPKY-FDPEAVAVVEGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 251 EIVQAAIQSPnFRSLHFTGSTNVFKSLWKDISSNLDkykvyPrIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQK 330
Cdd:cd07087 167 EVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 331 CSALSRLYVSRSVwengfKTQYLEEIAK-IK--VGPCLDWNNYMGPVIGRRAYDNITGFIkkakeEGGEVLIGGSGDDSK 407
Cdd:cd07087 240 CIAPDYVLVHESI-----KDELIEELKKaIKefYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 408 gFFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTS----IYgltgaIFAS---ERQALLTATNrsr 480
Cdd:cd07087 310 -RYIAPTILDDVSPDSPLMQEEIFGPILP--ILTYDDLDEAIEFINSRPkplaLY-----LFSEdkaVQERVLAETS--- 378
|
330 340
....*....|....*....|....*....
gi 2494072 481 naAGNIYYNEKCTGAVVGQQPFGGARGSG 509
Cdd:cd07087 379 --SGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
181-444 |
3.82e-20 |
|
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: 92.95 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 181 YRPLeGFVLAVSPFNFTAiggNLPGSPaLV-----GNVVVWKPAPAATYSNYLVFKILSEAgVPPGVIQFIPGGAEIVQA 255
Cdd:cd07136 98 YEPY-GVVLIIAPWNYPF---QLALAP-LIgaiaaGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 256 AIQSPnFRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALS 335
Cdd:cd07136 172 LLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTP------VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 336 RLYVSRSVWENGFKtqYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIkkakeEGGEVLIGGSGDDsKGFFIQPTv 415
Cdd:cd07136 245 YVLVHESVKEKFIK--ELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDR-ETLYIEPT- 315
|
250 260 270
....*....|....*....|....*....|
gi 2494072 416 ILTKVPR-STTMVGEIFGPVVTAYVFEDSD 444
Cdd:cd07136 316 ILDNVTWdDPVMQEEIFGPILPVLTYDTLD 345
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
81-465 |
9.46e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 85.96 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 81 SPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLAsgKYRYKLMAATMLgqgKNTWQAEIDAAAEL---ADFFRF-- 155
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAIL--KEHKAPIAECLV---KEIAKPAKDAVTEVvrsGDLISYta 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 156 --GVSYVEE---LYAQQPPKNApgcwnRTEY-----RPLeGFVLAVSPFNFTAiggNLPGS---PALV-GNVVVWKPAPA 221
Cdd:PLN00412 126 eeGVRILGEgkfLVSDSFPGNE-----RNKYcltskIPL-GVVLAIPPFNYPV---NLAVSkiaPALIaGNAVVLKPPTQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 222 ATYSNYLVFKILSEAGVPPGVIQFIPG-GAEIVQAAIQSPNFRSLHFTG-STNVFKSlwkdissnlDKYKVYPrIVGETG 299
Cdd:PLN00412 197 GAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGgDTGIAIS---------KKAGMVP-LQMELG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 300 GKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENgFKTQYLEEIAKIKVGPCLDwNNYMGPVIGRRA 379
Cdd:PLN00412 267 GKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADA-LVEKVNAKVAKLTVGPPED-DCDITPVVSESS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 380 YDNITGFIKKAKEEGGEVLiggSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiYG 459
Cdd:PLN00412 345 ANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLP--VIRINSVEEGIHHCNASN-FG 418
|
....*.
gi 2494072 460 LTGAIF 465
Cdd:PLN00412 419 LQGCVF 424
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
183-442 |
1.58e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.44 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 183 PLEGFVLAVSPFNFTAIGGNLPGSPALVGNV-VVWKPAPAATYSNYLVFKILSEAGV-PPGVIQFIPGGAEIVQAAIQSp 260
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQP- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 261 nFRSLHFTGSTNVFKSLwkdissnldkyKVYPRIVGEtggkNWHVIHKSAEVRNAVL--QSVRGAFEYQ----------- 327
Cdd:PRK11903 226 -FDVVSFTGSAETAAVL-----------RSHPAVVQR----SVRVNVEADSLNSALLgpDAAPGSEAFDlfvkevvremt 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 328 ---GQKCSALSRLYVSRSVWENgfKTQYL-EEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEgGEVLIGGSG 403
Cdd:PRK11903 290 vksGQKCTAIRRIFVPEALYDA--VAEALaARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGG 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2494072 404 ------DDSKGFFIQPTVILTKVPRSTTMVG--EIFGPVVTAYVFED 442
Cdd:PRK11903 367 falvdaDPAVAACVGPTLLGASDPDAATAVHdvEVFGPVATLLPYRD 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
183-436 |
6.24e-15 |
|
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: 77.31 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 183 PLEGFVLAVSPFNFTAIGGNLPGSPALVGNV-VVWKPAPAATYSNYLVFKILSEAGV-PPGVIQFIPGGAEIVQAAIQSp 260
Cdd:cd07128 143 PRRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGE- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 261 nFRSLHFTGSTNVFKSLwkdissnldkyKVYPRIVGETggknwhvIHKSAE---VRNAVL--QSVRGAFEYQ-------- 327
Cdd:cd07128 222 -QDVVAFTGSAATAAKL-----------RAHPNIVARS-------IRFNAEadsLNAAILgpDATPGTPEFDlfvkevar 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 328 ------GQKCSALSRLYVSRSVwENGFKTQYLEEIAKIKVG-PCLDwNNYMGPVIGRRAYDNITGFIKKAKEEgGEVLIG 400
Cdd:cd07128 283 emtvkaGQKCTAIRRAFVPEAR-VDAVIEALKARLAKVVVGdPRLE-GVRMGPLVSREQREDVRAAVATLLAE-AEVVFG 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2494072 401 G-------SGDDSKGFFIQPTVILTKVPRSTTMVGEI--FGPVVT 436
Cdd:cd07128 360 GpdrfevvGADAEKGAFFPPTLLLCDDPDAATAVHDVeaFGPVAT 404
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
177-438 |
1.67e-12 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 69.44 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 177 NRTEYRPLeGFVLAVSPFNF---TAIGgnlPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAGvPPGVIQFIPGGAEI 252
Cdd:cd07133 95 AEVEYQPL-GVVGIIVPWNYplyLALG---PLIAALaAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 253 VQAaiqspnFRSL---H--FTGSTNVFKSLWKDISSNLdkykvYPrIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQ 327
Cdd:cd07133 170 AAA------FSSLpfdHllFTGSTAVGRHVMRAAAENL-----TP-VTLELGGKSPAIIAPDADLAKAAERIAFGKLLNA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 328 GQKCSALSRLYVSRSvWENGFKTQYLEEIAKIKvgPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEV--LIGGSGDD 405
Cdd:cd07133 238 GQTCVAPDYVLVPED-KLEEFVAAAKAAVAKMY--PTLADNPDYTSIINERHYARLQGLLEDARAKGARVieLNPAGEDF 314
|
250 260 270
....*....|....*....|....*....|....*
gi 2494072 406 SKGFFIQPTVILTKVPRSTTMVGEIFGPV--VTAY 438
Cdd:cd07133 315 AATRKLPPTLVLNVTDDMRVMQEEIFGPIlpILTY 349
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
181-509 |
6.88e-12 |
|
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: 67.91 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 181 YRPLEGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQS 259
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALfMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 260 PNFRSLHFTGSTNVFKSLWKDISSnldkykvypRIVGETGGKNWHVIHKS-AEVRNAVLQSVRGAFEYQGQKCSALSRLY 338
Cdd:cd07126 219 ANPRMTLFTGSSKVAERLALELHG---------KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 339 VSrsvwENGFKTQYLEEIAK---------IKVGPCLDWNNymgpvigRRAYDNITGF--IKKAKEE-GGEVLIGGSGDDS 406
Cdd:cd07126 290 AH----ENWVQAGILDKLKAlaeqrkledLTIGPVLTWTT-------ERILDHVDKLlaIPGAKVLfGGKPLTNHSIPSI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 407 KGfFIQPTVILtkVPRST--------TMVGEIFGP--VVTAYvfEDSDYEKTLELIDTTSIYgLTGAIFASERQALLTAT 476
Cdd:cd07126 359 YG-AYEPTAVF--VPLEEiaieenfeLVTTEVFGPfqVVTEY--KDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVL 432
|
330 340 350
....*....|....*....|....*....|....*
gi 2494072 477 NRSRNAAGNIYYNEKCTGAVVGQ--QPFGGARGSG 509
Cdd:cd07126 433 ANTVNGTTYAGIRARTTGAPQNHwfGPAGDPRGAG 467
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
166-434 |
1.07e-08 |
|
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: 57.62 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 166 QQPPKNAP----GCWNRTEyrPLeGFVLAVSPFNFT----------AIGGnlpgspalvGNVVVWKPAPAATYSNYLVFK 231
Cdd:cd07132 81 EPVKKNLAtlldDVYIYKE--PL-GVVLIIGAWNYPlqltlvplvgAIAA---------GNCVVIKPSEVSPATAKLLAE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 232 ILseagvP----PGVIQFIPGGAEIVQAAIQSpNFRSLHFTGSTNVFKSLWKDISSNLdkykvyPRIVGETGGKNWHVIH 307
Cdd:cd07132 149 LI-----PkyldKECYPVVLGGVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 308 KSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWEngfktQYLEEIAKikvgpCL-DW-------NNYMGPVIGRRA 379
Cdd:cd07132 217 KSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQE-----KFVEALKK-----TLkEFygedpkeSPDYGRIINDRH 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2494072 380 YDNITGFIkkakeEGGEVLIGGSGDDSKGFfIQPTViLTKV-PRSTTMVGEIFGPV 434
Cdd:cd07132 287 FQRLKKLL-----SGGKVAIGGQTDEKERY-IAPTV-LTDVkPSDPVMQEEIFGPI 335
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
183-542 |
8.17e-08 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 54.73 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 183 PLeGFVLAVSPFNFtAIGGNL-PGSPAL-VGNVVVWKP---APAAtySNYLVFKIlsEAGVPPGVIQFIPGGAEIVQAAI 257
Cdd:PLN02203 108 PL-GVVLIFSSWNF-PIGLSLePLIGAIaAGNAVVLKPselAPAT--SAFLAANI--PKYLDSKAVKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 258 QSPnFRSLHFTGSTNVFKSLWKDISSNLDKYKVyprivgETGGK-----NWHVIHKSAEVrnAVLQSVRGAFEY-QGQKC 331
Cdd:PLN02203 182 QHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVAL------ELGGKcpcivDSLSSSRDTKV--AVNRIVGGKWGScAGQAC 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 332 SALSRLYVsrsvwENGFKTQYLEEIAK-IK--VGPCLDWNNYMGPVIGRRAYDNITGFIKKaKEEGGEVLIGGSGDDsKG 408
Cdd:PLN02203 253 IAIDYVLV-----EERFAPILIELLKStIKkfFGENPRESKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDE-KK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 409 FFIQPTVILTKVPRSTTMVGEIFG---PVVTAYVFEDSdyektLELIDTTSiygLTGAIFASERQALLTATNRSRNAAGN 485
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGpllPIITVKKIEDS-----IAFINSKP---KPLAIYAFTNNEKLKRRILSETSSGS 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2494072 486 IYYNEKCTGAVVGQQPFGGARGSGTNDKAGSISiFYRFVSARSIKENFVGLE-DFHYP 542
Cdd:PLN02203 398 VTFNDAIIQYACDSLPFGGVGESGFGRYHGKYS-FDTFSHEKAVLRRSLLTEfEFRYP 454
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
183-518 |
2.01e-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: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 183 PLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKILSEAgVPPGVIQFIPGGAEIVQAAIQSpN 261
Cdd:cd07137 101 PL-GVVLVISAWNFPFLLSLEPVIGAIaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 262 FRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEY-QGQKCSALSRLYVS 340
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTP------VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 341 RSVWENGFKTqyLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKaKEEGGEVLIGGSGDDSKgFFIQPTVILTKV 420
Cdd:cd07137 252 ESFAPTLIDA--LKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERDEKN-LYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 421 PRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiygLTGAIFASERQALLTATNRSRNAAGNIYYNEKCTGAVVGQQ 500
Cdd:cd07137 328 LDSSIMTEEIFGPLLP--IITVKKIEESIEIINSRP---KPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTL 402
|
330
....*....|....*...
gi 2494072 501 PFGGARGSGTNDKAGSIS 518
Cdd:cd07137 403 PFGGVGESGFGAYHGKFS 420
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
183-518 |
2.74e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 50.04 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 183 PLeGFVLAVSPFNFTAIGGNLPGSPAL-VGNVVVWKPAPAATYSNYLVFKILsEAGVPPGVIQFIPGGAEIVQAAIQSpN 261
Cdd:PLN02174 112 PL-GVVLVISAWNYPFLLSIDPVIGAIsAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 262 FRSLHFTGSTNVFKSLWKDISSNLDKykvyprIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFE-YQGQKCSALSRLYVS 340
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 341 RSVWENGFKTQYLEEIAKIKVGPCLDWNnyMGPVIGRRAYDNITGFIKKaKEEGGEVLIGGSgDDSKGFFIQPTVILTKV 420
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKD--MSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGE-KDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 421 PRSTTMVGEIFGPVVTayVFEDSDYEKTLELIDTTSiYGLTGAIFASERQalLTATNRSRNAAGNIYYNEKCTGAVVGQQ 500
Cdd:PLN02174 339 LDSLIMSEEIFGPLLP--ILTLNNLEESFDVIRSRP-KPLAAYLFTHNKK--LKERFAATVSAGGIVVNDIAVHLALHTL 413
|
330
....*....|....*...
gi 2494072 501 PFGGARGSGTNDKAGSIS 518
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFS 431
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
211-341 |
2.84e-05 |
|
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: 46.70 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 211 GNVVVWKPAPAATYSNYLVFKI----LSEAGVPPGVIQFI--PGGAEIVQAAIQSPNFRSLHFTGStNVFKSlWkdISSN 284
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGS-NAFGD-W--LEAN 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2494072 285 LDKYKVYPrivgETGGKNwHVIHKSAEVRNAVLQSVRGAFE-YQGQKCSALSRLYVSR 341
Cdd:cd07127 297 ARQAQVYT----EKAGVN-TVVVDSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVPR 349
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
186-363 |
1.36e-03 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 41.05 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 186 GFVLAVSPFNFTAIGGNLPGSPALVGNVVVWKPAPAATYSNY---LVFKILSEAGVPPGVIQFIPGGA-EIVQAAIQSPN 261
Cdd:cd07077 102 GVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPFTNRalaLLFQAADAAHGPKILVLYVPHPSdELAEELLSHPK 181
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494072 262 FRSLHFTGSTNVFKSLWKdiSSNldkykvYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQgQKCSALSRLYVSR 341
Cdd:cd07077 182 IDLIVATGGRDAVDAAVK--HSP------HIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NACASEQNLYVVD 252
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170 180
....*....|....*....|....*
gi 2494072 342 SVWE---NGFKTQYLEEIAKIKVGP 363
Cdd:cd07077 253 DVLDplyEEFKLKLVVEGLKVPQET 277
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