|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
2-493 |
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: 990.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 2 EAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRA 81
Cdd:cd07123 31 VEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 82 EILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPST-NSTVYRGLEGFVAAISPFNFTAIGGNLA 160
Cdd:cd07123 111 ELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAGVwNRLEYRPLEGFVYAVSPFNFTAIGGNLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 161 GAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ 240
Cdd:cd07123 191 GAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 241 NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP 320
Cdd:cd07123 271 NLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 321 aEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 400
Cdd:cd07123 351 -DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 401 DKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 480
Cdd:cd07123 430 SDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR 509
|
490
....*....|...
gi 238859541 481 WTSPQVIKETHKP 493
Cdd:cd07123 510 WVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
1-503 |
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: 951.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 1 MEAIPCVVGDEEVWTSDV-QYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPR 79
Cdd:TIGR01236 29 SLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSGPY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 80 RAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNL 159
Cdd:TIGR01236 109 RYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGEWNRTEYRPLEGFVYAISPFNFTAIAGNL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 160 AGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVA 239
Cdd:TIGR01236 189 AGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 240 QNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGD 319
Cdd:TIGR01236 269 QNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 320 PaEDFGTFFSAVIDAKSFARIKKWLEHARSSPS-LTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVY 398
Cdd:TIGR01236 349 P-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVY 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 399 PDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYI 478
Cdd:TIGR01236 428 PDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCTGAVVGQQPFGGARMSGTNDKAGGPNNL 507
|
490 500
....*....|....*....|....*
gi 238859541 479 LRWTSPQVIKETHKPLGDWSYAYMQ 503
Cdd:TIGR01236 508 LRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-491 |
0e+00 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 809.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 1 MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRR 80
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 81 AEILAKTMVGqGKTVIQaEIDAAAELIDFFRFNAKYAVELEGQQPI--SVPPSTNSTVYRGLeGFVAAISPFNFT-AIGG 157
Cdd:cd07083 96 ELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GAGVVISPWNFPvAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 158 NLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQ 237
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 238 VAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKV 317
Cdd:cd07083 253 AARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 318 GDPAEDfGTFFSAVIDAKSFARIKKWLEHARSspSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYV 397
Cdd:cd07083 333 GPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 398 YPDDKYKETLQLVDSTTSYGLTGAVFSQdKDVVQEATKVLrnAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHY 477
Cdd:cd07083 410 YKDDDFAEALEVANSTPYGLTGGVYSRK-REHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
490
....*....|....
gi 238859541 478 ILRWTSPQVIKETH 491
Cdd:cd07083 487 LRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
43-487 |
1.10e-142 |
|
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: 416.99 E-value: 1.10e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQAEIDAAaELIDFFRFNAKYAVELEG 122
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLET-GKPIEEALGEVA-RAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 123 QQ-PISVPPSTNSTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 200
Cdd:cd07078 79 EViPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 201 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSA 280
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 281 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK 360
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAKAEGA-KLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 361 CDDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRn 439
Cdd:cd07078 310 RLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDTE-YGLAAGVFTRDLERALRVAERLE- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 238859541 440 aAGNFYINDKSTGsIVGQQPFGGARASGTNdKPGGPHYILRWTSPQVI 487
Cdd:cd07078 386 -AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
4-491 |
8.16e-140 |
|
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: 411.06 E-value: 8.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 4 IPCVVGDEEVWTSDVQYQ--VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRA 81
Cdd:COG1012 6 YPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE--ERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 82 EILAKTMV-GQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQ-PISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNL 159
Cdd:COG1012 83 EELAALLTlETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETiPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 160 AGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQV 238
Cdd:COG1012 161 KLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 239 AQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG 318
Cdd:COG1012 241 AENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 319 DPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC-DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYV 397
Cdd:COG1012 315 DPL-DPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 398 YPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGTNDKpGGPHY 477
Cdd:COG1012 393 FDD--EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREG 465
|
490
....*....|....
gi 238859541 478 ILRWTSPQVIKETH 491
Cdd:COG1012 466 LEEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-489 |
1.35e-131 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 391.59 E-value: 1.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 5 PCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEiL 84
Cdd:cd07124 34 PLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLR-RRRFE-L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 85 AKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF-TAIGGNLAGA 162
Cdd:cd07124 112 AAWMVLEvGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 163 PALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNL 242
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 243 DRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaE 322
Cdd:cd07124 270 PGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP-E 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 323 DFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSV--GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 400
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 401 dkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 480
Cdd:cd07124 427 --FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQ 501
|
....*....
gi 238859541 481 WTSPQVIKE 489
Cdd:cd07124 502 FMQPKTVTE 510
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
22-487 |
1.02e-125 |
|
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: 374.56 E-value: 1.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQAEI 100
Cdd:pfam00171 12 INPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELETlENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 101 DAAaELIDFFRFNAKYAVELEGQqPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSD 176
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 177 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECG 256
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 257 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKS 336
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsY 416
Cdd:pfam00171 317 LERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEIANDTE-Y 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238859541 417 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGqQPFGGARASGTNDKpGGPHYILRWTSPQVI 487
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
4-490 |
4.88e-113 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 343.84 E-value: 4.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 4 IPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEI 83
Cdd:PRK03137 37 YPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIR-RRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 84 LAkTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVEL-EGQQPISVPPSTNSTVYRGLeGFVAAISPFNF-TAIGGNLA 160
Cdd:PRK03137 116 SA-WLVKEaGKPWAEADADTA-EAIDFLEYYARQMLKLaDGKPVESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 161 GAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ 240
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 241 NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP 320
Cdd:PRK03137 273 VQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 321 AEDfgTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 400
Cdd:PRK03137 353 EDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 401 dkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 480
Cdd:PRK03137 429 --FDHALEIANN-TEYGLTGAVISNNREHLEKARREFH--VGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLL 503
|
490
....*....|
gi 238859541 481 WTSPQVIKET 490
Cdd:PRK03137 504 FLQAKTVSEM 513
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
47-487 |
5.05e-105 |
|
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: 318.02 E-value: 5.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 47 EAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTvIQAEIDAAAELIDFFRFNAKYAVELEGQQPI 126
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLET-GKP-IEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 127 SVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPAD 205
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 206 GPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGG 285
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 286 QKCSACSRLYVPHSLWPQIKGRLLeehsrikvgdpaedfgtffsavidaksfarikkwleharsspsltilaggkcddsv 365
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 366 gyfvepCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFY 445
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDTE-YGLTAGVFTRDLNRALRVAERLR--AGTVY 325
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 238859541 446 INDKSTGSiVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 487
Cdd:cd06534 326 INDSSIGV-GPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-489 |
2.52e-101 |
|
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: 313.73 E-value: 2.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 5 PCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEIL 84
Cdd:TIGR01237 34 PLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVR-RRRHEFS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 85 AKTMVGQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPI-SVPPSTNSTVYRGLeGFVAAISPFNFT-AIGGNLAGA 162
Cdd:TIGR01237 113 ALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVnSREGETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 163 PALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNL 242
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 243 DRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaE 322
Cdd:TIGR01237 271 PGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPP-D 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 323 DFGTFFSAVIDAKSFARIKKWLEHARSSPSLTIlaGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdk 402
Cdd:TIGR01237 350 SADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVS--GGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASD-- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 403 YKETLQLVDSTtSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWT 482
Cdd:TIGR01237 426 FDEALEIANNT-EYGLTGGVISNNRDHINRAKAEFE--VGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFM 502
|
....*..
gi 238859541 483 SPQVIKE 489
Cdd:TIGR01237 503 QAKTVTE 509
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-480 |
3.03e-97 |
|
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: 303.35 E-value: 3.03e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 2 EAIPCVVGDEEVWTsDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRA 81
Cdd:cd07125 32 EAIPIINGEETETG-EGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEA-NRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 82 EILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQPISVPPS-TNSTVYRGLeGFVAAISPFNF---TAIGG 157
Cdd:cd07125 110 ELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGeLNGLELHGR-GVFVCISPWNFplaIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 158 NLAgapALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWK 236
Cdd:cd07125 188 IAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 237 QVAQnldRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWP----QIKGRLLEeh 312
Cdd:cd07125 265 ALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAErfieMLKGAMAS-- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 313 srIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSVGYFVEPCIVESKDPQEpiMKEEIFGPV 392
Cdd:cd07125 340 --LKVGDPW-DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYFVAPGIIEIVGIFD--LTTEVFGPI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 393 LSVYVYPDDKYKETLQLVDStTSYGLTGAVFSQDKDvvqEATKVLRNA-AGNFYINDKSTGSIVGQQPFGGARASGTNDK 471
Cdd:cd07125 413 LHVIRFKAEDLDEAIEDINA-TGYGLTLGIHSRDER---EIEYWRERVeAGNLYINRNITGAIVGRQPFGGWGLSGTGPK 488
|
....*....
gi 238859541 472 PGGPHYILR 480
Cdd:cd07125 489 AGGPNYLLR 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-487 |
5.01e-79 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 266.68 E-value: 5.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAeID 101
Cdd:PRK11904 567 VSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IA 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 102 AAAELIDFFRFnakYAVELEGQ--QPISVPPSTNSTVYRGLEG---FVAaISPFNFT-AIggnLAG--APALM-GNVVLW 172
Cdd:PRK11904 645 EVREAVDFCRY---YAAQARRLfgAPEKLPGPTGESNELRLHGrgvFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIA 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 173 KPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVptfkhlwkQVAQNLDRfhtfpRL 251
Cdd:PRK11904 718 KPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGST--------ETARIINR-----TL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 AG----------ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ----IKGRLLEehsrIKV 317
Cdd:PRK11904 784 AArdgpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRviemLKGAMAE----LKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 318 GDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGGKCDDS--VGYFVEPCIVESKDPQEpiMKEEIFGPVLSV 395
Cdd:PRK11904 860 GDPR-LLSTDVGPVIDAEAKANLDAHIERMKREA--RLLAQLPLPAGteNGHFVAPTAFEIDSISQ--LEREVFGPILHV 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 396 YVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPG 473
Cdd:PRK11904 935 IRY---KASDLDKVIDAinATGYGLTLGIHSRIEETADRIADRVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAG 1009
|
490
....*....|....
gi 238859541 474 GPHYILRWTSPQVI 487
Cdd:PRK11904 1010 GPHYLLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
22-487 |
1.50e-77 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 263.72 E-value: 1.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTvIQaeiD 101
Cdd:COG4230 575 RNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA-HRAELMALLVREAGKT-LP---D 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 102 AAAEL---IDFFRFnakYAVELEGQQpisvppsTNSTVYRGLeGFVAAISPFNFTaiggnLAG-----APALM-GNVVLW 172
Cdd:COG4230 650 AIAEVreaVDFCRY---YAAQARRLF-------AAPTVLRGR-GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 173 KPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprL 251
Cdd:COG4230 714 KPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--I 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 AgECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ----IKGRLLEehsrIKVGDPAE---DF 324
Cdd:COG4230 791 A-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRvlemLKGAMAE----LRVGDPADlstDV 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 325 GtffsAVIDAKSFARIKKWLEHARSSPslTILAGGKCDDSV--GYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddK 402
Cdd:COG4230 866 G----PVIDAEARANLEAHIERMRAEG--RLVHQLPLPEECanGTFVAPTLIEIDSISD--LEREVFGPVLHVVRY---K 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 403 YKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 480
Cdd:COG4230 935 ADELDKVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
....*..
gi 238859541 481 WTSPQVI 487
Cdd:COG4230 1013 FATERTV 1019
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
17-476 |
8.81e-74 |
|
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: 241.00 E-value: 8.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 17 DVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTV 95
Cdd:cd07097 14 DGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELARLLTrEEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 96 IQA--EIDAAaelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAgAPALM-GNVVL 171
Cdd:cd07097 92 PEArgEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-APALAyGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 172 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprl 251
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 agECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 331
Cdd:cd07097 244 --EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE-GVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 IDAKSFARIKKWLEHARSSPSlTILAGG---KCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQ 408
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGA-KLVYGGerlKRPDE-GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD--YDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 409 LVDStTSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINDKSTGsiVGQQ-PFGGARASGTNDKPGGPH 476
Cdd:cd07097 397 IAND-TEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEA 460
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
22-484 |
1.57e-70 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 244.00 E-value: 1.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIqaeiD 101
Cdd:PRK11905 572 LNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEA-HMPELFALAVREAGKTLA----N 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 102 AAAEL---IDFFRFNAKYAVELEGQQPIsvppstnstvyRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD 176
Cdd:PRK11905 647 AIAEVreaVDFLRYYAAQARRLLNGPGH-----------KPL-GPVVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAE 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 177 -TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtFPRLAGEC 255
Cdd:PRK11905 714 qTPLIAARAV-RLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGP---PVPLIAET 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 256 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQI----KGRLLEehsrIKVGDPAE---DFGtff 328
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVltmlKGAMDE----LRIGDPWRlstDVG--- 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 329 sAVIDAKSFARIKKWLEHARSSPSL--TILAGGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKET 406
Cdd:PRK11905 863 -PVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRF---KADEL 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 407 LQLVDS--TTSYGLTGAVFSQDKDVVQEATKvlRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSP 484
Cdd:PRK11905 935 DRVIDDinATGYGLTFGLHSRIDETIAHVTS--RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-468 |
5.64e-69 |
|
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: 227.86 E-value: 5.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 23 SPFnHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--E 99
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 100 IDAAaelIDFFRFNAKYAVELEGQQ-PISVPPSTNSTV---YRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVL 171
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFDASPGGEGRIgftIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 172 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRL 251
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 331
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 IDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVD 411
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 412 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGT 468
Cdd:cd07149 381 D-SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
42-483 |
8.59e-68 |
|
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: 223.95 E-value: 8.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 42 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAElIDFFRFNAKYAVEL 120
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAAFEVGAA-IAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 121 EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILREAGLPPNI 198
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 199 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTLR 278
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKK------VALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 279 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAG 358
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERQVDRVHAIVEDAVAA-GARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 359 GKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLR 438
Cdd:cd07104 311 GTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVELAND-TEYGLSAAVFTRD---LERAMAFAE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 238859541 439 NA-AGNFYINDKST--GSIVgqqPFGGARASGTnDKPGGPHYI-----LRWTS 483
Cdd:cd07104 382 RLeTGMVHINDQTVndEPHV---PFGGVKASGG-GRFGGPASLeefteWQWIT 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
45-468 |
3.61e-67 |
|
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: 222.99 E-value: 3.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 45 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELidfFRFNAKYAVELE 121
Cdd:cd07145 26 AIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLTIEvGKPIKQSrvEVERTIRL---FKLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 122 GQqpisVPPSTNstvYRGLE-----------GFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVY 186
Cdd:cd07145 101 GE----TIPVDA---YEYNErriaftvrepiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 187 RILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRS 266
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 267 ADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEH 346
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE-STDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 347 ARSSPSlTILAGGKCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQD 426
Cdd:cd07145 324 AVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTND 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 238859541 427 kdvVQEATKVLRN-AAGNFYINDKSTGSIvGQQPFGGARASGT 468
Cdd:cd07145 398 ---INRALKVARElEAGGVVINDSTRFRW-DNLPFGGFKKSGI 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
28-447 |
7.39e-66 |
|
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: 219.83 E-value: 7.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAA 104
Cdd:cd07088 23 GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLIVEeQGKTLSLArvEVEFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 105 eliDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAML 180
Cdd:cd07088 101 ---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 181 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNF 260
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----TKVSL--ELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 261 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARI 340
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 341 KKWLEHARSSPSlTILAGGKCDDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLT 419
Cdd:cd07088 328 EEMVERAVEAGA-TLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAND-SEYGLT 403
|
410 420
....*....|....*....|....*...
gi 238859541 420 GAVFSQDKDVVQEATKVLRnaAGNFYIN 447
Cdd:cd07088 404 SYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
37-487 |
8.87e-66 |
|
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: 218.94 E-value: 8.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 37 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLS--GPRRAEILAKTmvgQGKTVIQA--EIDAAAeliDFFRF 112
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEanAEELARLLTLE---QGKPLAEAqfEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 113 NAKYAVELEGQQpiSVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAMLASYAVYRI 188
Cdd:cd07106 90 TASLDLPDEVIE--DDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAgLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 268
Cdd:cd07106 164 AQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 269 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHAR 348
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 349 SSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkd 428
Cdd:cd07106 315 AK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE--DEVIARAND-SEYGLGASVWSSD-- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238859541 429 vVQEATKV-LRNAAGNFYINdkSTGSIVGQQPFGGARASGTndkpG---GPHYILRWTSPQVI 487
Cdd:cd07106 389 -LERAEAVaRRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGLKEYTQTQVI 444
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
2-485 |
3.46e-65 |
|
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: 219.01 E-value: 3.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 2 EAIPcVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRA 81
Cdd:TIGR01238 37 QAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 82 EILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQpiSVPPstnstvyrglEGFVAAISPFNFT-AI-GGNL 159
Cdd:TIGR01238 115 ELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEF--SVES----------RGVFVCISPWNFPlAIfTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 160 AGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQV 238
Cdd:TIGR01238 182 SAALA-AGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 239 AQNLDrfHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG 318
Cdd:TIGR01238 260 AQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 319 DPAEdFGTFFSAVIDAKSFARIKKWLEH----ARSSPSLTILAGGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLS 394
Cdd:TIGR01238 337 VPHL-LTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDDSRACQH--GTFVAPTLFELDDIAE--LSEEVFGPVLH 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 395 VYVYpddKYKETLQLVD--STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKP 472
Cdd:TIGR01238 412 VVRY---KARELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKA 486
|
490
....*....|...
gi 238859541 473 GGPHYILRWTSPQ 485
Cdd:TIGR01238 487 GGPHYLYRLTQVQ 499
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
43-483 |
9.95e-65 |
|
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: 216.43 E-value: 9.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEG 122
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 123 QQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 201
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 202 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAF 281
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 282 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKC 361
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 362 DdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA- 440
Cdd:cd07150 334 D---GNFYQPTVLTDVTPDMRIFREETFGPVTS--VIPAKDAEEALELAND-TEYGLSAAILTND---LQRAFKLAERLe 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 238859541 441 AGNFYINDkSTGSIVGQQPFGGARASGTNdKPGGPHYI-----LRWTS 483
Cdd:cd07150 405 SGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-467 |
1.73e-64 |
|
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: 215.76 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAA 104
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLTLeQGKPLAEArgEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 105 eliDFFRFNAKYAVELEGQqpiSVPPSTNST---VYRGLEGFVAAISPFNFTAigGNLA--GAPAL-MGNVVLWKPSDTA 178
Cdd:cd07103 85 ---SFLEWFAEEARRIYGR---TIPSPAPGKrilVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 179 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGk 258
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 259 NFHF-VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 337
Cdd:cd07103 230 NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 338 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 417
Cdd:cd07103 309 EKVEALVEDAVAKGA-KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE--DEVIARAND-TPYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 238859541 418 LTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVG-QQPFGGARASG 467
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALE--AGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-467 |
3.90e-64 |
|
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: 215.51 E-value: 3.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 7 VVGDEEVWTSdvqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK 86
Cdd:cd07086 8 VGSGGETFTS-----RNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 87 TM---VGQGKTVIQAEIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNS-----TVYRGLeGFVAAISPFNF-TAIGG 157
Cdd:cd07086 80 LVsleMGKILPEGLGEVQ---EMIDI----CDYAVGLSRMLYGLTIPSERPghrlmEQWNPL-GVVGVITAFNFpVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 158 -NLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREA----GLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTF 231
Cdd:cd07086 152 wNAA--IALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 232 KHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE 311
Cdd:cd07086 229 RRVGETVAR------RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 312 HSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC--DDSVGYFVEPCIVESKDPQEPIMKEEIF 389
Cdd:cd07086 303 YKQVRIGDPLDE-GTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 390 GPVLsvYVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA---AGNFYINDKSTGSIVGqQPFGGARAS 466
Cdd:cd07086 381 APIL--YVIKFDSLEEAIAINND-VPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEIG-GAFGGEKET 453
|
.
gi 238859541 467 G 467
Cdd:cd07086 454 G 454
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
31-482 |
4.91e-64 |
|
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: 215.29 E-value: 4.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 31 VAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAaELIDF 109
Cdd:cd07131 28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGDVQ-EAIDM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 110 FRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI 188
Cdd:cd07131 105 AQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSAD 268
Cdd:cd07131 185 FAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR------PNKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 269 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHAR 348
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE-ETDMGPLINEAQLEKVLNYNEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 349 SSpSLTILAGG----KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFS 424
Cdd:cd07131 338 EE-GATLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVA--LIEVSSLEEAIEIAND-TEYGLSSAIYT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238859541 425 QDkdvVQEATKVLRNA-AGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGPHYILRWT 482
Cdd:cd07131 414 ED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
22-468 |
1.53e-63 |
|
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: 213.58 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--- 98
Cdd:cd07093 2 FNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEA-RADELALLESLDTGKPITLArtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAAElidFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APAL-MGNVVLWKP 174
Cdd:cd07093 80 DIPRAAA---NFRFFADYILQLDGESYPQDGGALNYVLRQPV-GVAGLITPWNLPLM---LLTwkiAPALaFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 175 SDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagE 254
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL------E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 255 CGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDA 334
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 335 KSFARIKKWLEHARSSPSlTILAGGKCDDSV----GYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLV 410
Cdd:cd07093 306 EHLEKVLGYVELARAEGA-TILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIELA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238859541 411 DSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASGT 468
Cdd:cd07093 383 NDTP-YGLAAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-467 |
5.15e-63 |
|
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: 212.94 E-value: 5.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA 98
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR--EDAEELARlETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAaELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 177
Cdd:cd07119 95 EIDID-DVANCFRYYAGLATKETGEV-YDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 178 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGG 257
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 258 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSF 337
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG-LDADTEMGPLVSAEHR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 338 ARIKKWLEHARSSPSlTILAGGK------CDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVD 411
Cdd:cd07119 326 EKVLSYIQLGKEEGA-RLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--EEAIRLAN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 238859541 412 STTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDksTGSIVGQQPFGGARASG 467
Cdd:cd07119 401 DTP-YGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
22-467 |
1.45e-62 |
|
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: 210.75 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 98
Cdd:cd07094 4 HNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIACEgGKPIKDArv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAaelIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APAL-MGNV 169
Cdd:cd07094 81 EVDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 170 VLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFP 249
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 250 RLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS 329
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 330 AVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQL 409
Cdd:cd07094 305 PLISEEAAERVERWVEEAVEAGA-RLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 238859541 410 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDkSTGSIVGQQPFGGARASG 467
Cdd:cd07094 379 ANS-TDYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
28-467 |
4.15e-62 |
|
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: 209.60 E-value: 4.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAELI 107
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 108 DFFRFNAKYAVELEGQQ-PISvPPSTNSTVyRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 185
Cdd:cd07115 86 DTFRYYAGWADKIEGEViPVR-GPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 186 YRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHR 265
Cdd:cd07115 164 AELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR------VSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 266 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLE 345
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 346 HARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQ 425
Cdd:cd07115 317 VGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE-YGLAAGVWTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 238859541 426 DKDVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:cd07115 393 DLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
14-467 |
4.21e-62 |
|
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: 209.85 E-value: 4.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 14 WTSDVQyqvSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGK 93
Cdd:cd07151 10 RTIDVL---NPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 94 TVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNV 169
Cdd:cd07151 85 TRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 170 VLWKP-SDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtf 248
Cdd:cd07151 161 VVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 249 pRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF 328
Cdd:cd07151 236 -KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 329 SAVIDAKSFARIKKWLEHARSSpSLTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQ 408
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEE-GATLLVGGEAEGNV---LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238859541 409 LVDStTSYGLTGAVFSQDkdvVQEATKV-LRNAAGNFYINDKStgsiVGQQP---FGGARASG 467
Cdd:cd07151 388 LAND-TEYGLSGAVFTSD---LERGVQFaRRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-467 |
1.66e-61 |
|
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: 208.31 E-value: 1.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTV--IQAEIDAAAE 105
Cdd:cd07090 7 GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIeeARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 106 LIDFFrfnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 182
Cdd:cd07090 86 CLEYY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 183 YAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHF 262
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 263 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKK 342
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 343 WLEHARSSPSlTILAGG-------KCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDSTTs 415
Cdd:cd07090 312 YIESAKQEGA-KVLCGGervvpedGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTT- 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 238859541 416 YGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 467
Cdd:cd07090 386 YGLAAGVFTRD---LQRAHRVIAQlQAGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-467 |
1.73e-61 |
|
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: 208.17 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 27 HGHKVAKFCYADKSLLNKAIEAALAA--RKEW-DLKPIAdRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTViqAEIDA 102
Cdd:cd07114 6 TGEPWARVPEASAADVDRAVAAARAAfeGGAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELETRDnGKLI--RETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 103 -AAELIDFFRFNAKYAVELEGQ-QPISVPPSTNSTVYRGLeGFVAAISPFN----FTAiggnLAGAPAL-MGNVVLWKPS 175
Cdd:cd07114 81 qVRYLAEWYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 176 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGEC 255
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 256 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK 335
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDP-ETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 336 SFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVD 411
Cdd:cd07114 309 QLEKVERYVARAREEGA-RVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALAN 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 238859541 412 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgqQPFGGARASG 467
Cdd:cd07114 386 D-SEYGLAAGIWTRDLARAHRVARAIE--AGTVWVNTYRALSPS--SPFGGFKDSG 436
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
23-489 |
7.10e-60 |
|
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: 203.69 E-value: 7.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 23 SPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQA--EI 100
Cdd:cd07101 2 APFT-GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 101 DAAAELIDFFRFNAKYAVELEGQQPiSVPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKPSD 176
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRG-AIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 177 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTssEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECG 256
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 257 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKS 336
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTS 415
Cdd:cd07101 307 LDRVTAHVDDAVAKGA-TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELAND-TD 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 416 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND---KSTGSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKE 489
Cdd:cd07101 383 YGLNASVWTRDGARGRRIAARLR--AGTVNVNEgyaAAWASI--DAPMGGMKDSGLGRR-HGAEGLLKYTETQTVAV 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
37-467 |
1.97e-59 |
|
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: 202.86 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 37 ADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNA 114
Cdd:cd07089 16 AGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLRYFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 115 KYAVELEGQQPISVPPS----TNSTVYRGLEGFVAAISPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAMLASYAVYRI 188
Cdd:cd07089 94 DLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSAD 268
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLL------ELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 269 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHAR 348
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGYIARGR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 349 SSPSlTILAGGKCDDS--VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQD 426
Cdd:cd07089 326 DEGA-RLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVRIAND-SDYGLSGGVWSAD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 238859541 427 KDVVQEATKVLRnaAGNFYINDKSTGSIVGqqPFGGARASG 467
Cdd:cd07089 402 VDRAYRVARRIR--TGSVGINGGGGYGPDA--PFGGYKQSG 438
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
28-485 |
3.46e-59 |
|
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: 202.67 E-value: 3.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAEL 106
Cdd:cd07113 25 EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 107 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLE-----GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAML 180
Cdd:cd07113 104 ANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 181 ASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNF 260
Cdd:cd07113 184 TLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGGKNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 261 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARI 340
Cdd:cd07113 257 AAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE-SVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 341 KKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTG 420
Cdd:cd07113 336 CSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE--EELIQLIND-TPFGLTA 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238859541 421 AVFSQDkdvvqeATKVLRNA----AGNFYIN-----DKSTgsivgqqPFGGARASGTNdKPGGPHYILRWTSPQ 485
Cdd:cd07113 412 SVWTNN------LSKALRYIprieAGTVWVNmhtflDPAV-------PFGGMKQSGIG-REFGSAFIDDYTELK 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
45-468 |
5.28e-59 |
|
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: 201.45 E-value: 5.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 45 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQA---EIDAAAELIDFFrfnAKYAVELE 121
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIDALDCGNPVSAmlgDVMVAAALLDYF---AGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 122 GQqpiSVPPSTNSTVYRGLE--GFVAAISPFN----FTAigGNLAgAPALMGNVVLWKPSDTAMLASYAVYRILREAgLP 195
Cdd:cd07107 99 GE---TIPVGGRNLHYTLREpyGVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 196 PNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVVSG 275
Cdd:cd07107 172 PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 276 TLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLT 354
Cdd:cd07107 246 AVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQQYDRVMHYIDSAKREGARL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 355 ILAGGKCDDSV---GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQ 431
Cdd:cd07107 325 VTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANG-VEYGLTAAIWTND---IS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 238859541 432 EATKVLRNA-AGNFYINDKST---GSivgqqPFGGARASGT 468
Cdd:cd07107 399 QAHRTARRVeAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
22-467 |
6.66e-59 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 201.44 E-value: 6.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTV-IQAE 99
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALEtGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 100 IDAAAeLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSD 176
Cdd:cd07108 79 PEAAV-LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 177 TAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtfPRLAG--- 253
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 254 ECGGKNFHFVHRSADVESVVSGTLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffs 329
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeATDIG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 330 AVIDAKSFARIKKWLEHARSSPSLTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKE 405
Cdd:cd07108 301 AIISEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238859541 406 TLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKstgsiVGQQP---FGGARASG 467
Cdd:cd07108 379 VIAMANDSH-YGLAAYVWTRDLGRALRAAHALE--AGWVQVNQG-----GGQQPgqsYGGFKQSG 435
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
44-495 |
1.29e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 202.03 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 44 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILaktmvgqgkTVIQAEI-----DAAAELIDFF---RFNAK 115
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 116 YAVELEGQQPIS--VPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAMLASYAVyRI 188
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAGLPPNIIQFVPADGPLFGDTVT-SSEHLCginFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSA 267
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVdNADYLM---FTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 268 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKSFARIKKWLEHA 347
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 348 RSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQD 426
Cdd:PRK09407 354 VAKGA-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERANDTP-YGLNASVWTGD 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238859541 427 KDVVQEATKVLRnaAGNFYINDKST---GSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKETHK-PLG 495
Cdd:PRK09407 430 TARGRAIAARIR--AGTVNVNEGYAaawGSV--DAPMGGMKDSGLGRR-HGAEGLLKYTESQTIATQRVlPLA 497
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
22-467 |
1.95e-58 |
|
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: 199.87 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPfNHGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA 98
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIR--ARRERLALIETLEsGKPISQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 --EIDAAAELidfFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTA--IGGNLAGAPAlMGNVVLWKP 174
Cdd:cd07118 79 rgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 175 SD-----TAMLAsyavyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfp 249
Cdd:cd07118 155 SEftsgtTLMLA-----ELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 250 rLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS 329
Cdd:cd07118 225 -VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDP-ETKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 330 AVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQL 409
Cdd:cd07118 303 AIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIAL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 238859541 410 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASG 467
Cdd:cd07118 381 AND-TVYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-467 |
1.09e-57 |
|
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: 197.85 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEI 100
Cdd:cd07147 4 TNPYT-GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 101 DAAaELIDFFRFNAKYAVELEGQ-QPISVPPSTNStvYRGL-----EGFVAAISPFNFTAiggNLAG---APAL-MGNVV 170
Cdd:cd07147 81 EVA-RAIDTFRIAAEEATRIYGEvLPLDISARGEG--RQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 171 LWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtfpR 250
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 251 LAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSA 330
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD-ATDVGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 331 VIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLV 410
Cdd:cd07147 305 MISESEAERVEGWVNEAVDAGA-KLLTGGKRDGAL---LEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 411 DStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASG 467
Cdd:cd07147 379 ND-SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-467 |
1.95e-56 |
|
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: 194.76 E-value: 1.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPiADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQAEIDAAA 104
Cdd:cd07109 7 GEVFARIARGGAADVDRAVQAARRAfeSGWLRLSP-AERGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 105 eLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAML 180
Cdd:cd07109 84 -AARYFEYYGGAADKLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 181 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNF 260
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 261 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGtfFSAVIDAKSFARI 340
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 341 KKWLEHARSSpSLTILAGG---KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 417
Cdd:cd07109 311 EGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANG-TDYG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 238859541 418 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgQQPFGGARASG 467
Cdd:cd07109 387 LVAGVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
45-480 |
9.74e-56 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 201.36 E-value: 9.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 45 AIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTVIQAeIDAAAELIDFFRFnakYAVELEGQ 123
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEA--QMQTLMGLLVREaGKTFSNA-IAEVREAVDFLRY---YAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 124 qpisvppSTNSTvYRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQ 200
Cdd:PRK11809 761 -------FDNDT-HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEAGVPAGVVQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 201 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLD-RFHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRS 279
Cdd:PRK11809 830 LLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLAS 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 280 AFEYGGQKCSACSRLYVP-----HSLwPQIKGRLLEehsrIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSS--PS 352
Cdd:PRK11809 909 AFDSAGQRCSALRVLCLQddvadRTL-KMLRGAMAE----CRMGNP-DRLSTDIGPVIDAEAKANIERHIQAMRAKgrPV 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 353 LTILAGGKCDDSVGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVV 430
Cdd:PRK11809 983 FQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRY---NRNQLDELIEQinASGYGLTLGVHTRIDETI 1057
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 238859541 431 QEATKvlRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 480
Cdd:PRK11809 1058 AQVTG--SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
28-467 |
1.60e-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: 192.81 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPI--ADRAQIFLKAADMLSgpRRAEILAK--TMVGqGKTV-IQAEIDA 102
Cdd:cd07091 29 EEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIE--RDRDELAAleSLDN-GKPLeESAKGDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 103 AaELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 179
Cdd:cd07091 106 A-LSIKCLRYYAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 180 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFhTFprlagECGGK 258
Cdd:cd07091 182 LSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV-TL-----ELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 259 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFA 338
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP-DTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 339 RIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLVD--STTSY 416
Cdd:cd07091 335 KILSYIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTIL-----KFKTEDEVIEraNDTEY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 238859541 417 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVGQQ-PFGGARASG 467
Cdd:cd07091 409 GLAAGVFTKDINKALRVSRALK--AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-474 |
1.24e-54 |
|
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: 189.40 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 45 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFfrfNAKYAVELE 121
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARLIsreTGKPLWEAQTEVAAMAGKIDI---SIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 122 GQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 200
Cdd:cd07095 80 GERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 201 FVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSA 280
Cdd:cd07095 159 LVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 281 FEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGG 359
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 360 KCDDSvGYFVEPCIVESKDPQEPiMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRn 439
Cdd:cd07095 312 RLVAG-TAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRY--DDFDEAIALANA-TRFGLSAGLLSDDEALFERFLARIR- 385
|
410 420 430
....*....|....*....|....*....|....*
gi 238859541 440 aAGNFYINDKSTGSiVGQQPFGGARASGtNDKPGG 474
Cdd:cd07095 386 -AGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
43-467 |
2.92e-54 |
|
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: 188.97 E-value: 2.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQAEIDAAAELIDFFRFNAKYAVE 119
Cdd:cd07112 27 DRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSAANTFRWYAEAIDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 120 LEGQQPiSVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNI 198
Cdd:cd07112 105 VYGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 199 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFHTfprlagECGGKNFHFV-HRSADVESVVSGT 276
Cdd:cd07112 184 LNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWL------ECGGKSPNIVfADAPDLDAAAEAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 277 LRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTIL 356
Cdd:cd07112 258 AAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKVLGYIESGKAE-GARLV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 357 AGGKCD--DSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVdSTTSYGLTGAVFSQDKDVVQEAT 434
Cdd:cd07112 336 AGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALA-NDSVYGLAASVWTSDLSRAHRVA 412
|
410 420 430
....*....|....*....|....*....|...
gi 238859541 435 KVLRnaAGNFYINDKSTGSIvgQQPFGGARASG 467
Cdd:cd07112 413 RRLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
35-467 |
2.08e-53 |
|
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: 186.78 E-value: 2.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 35 CYAD--KSLLNKAIEAALAARKE--WDLKPiADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAAaelI 107
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLAlENGKILGEArfEISGA---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 108 DFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP-SDTAMLASyAV 185
Cdd:cd07120 86 SELRYYAGLARTEAGRM-IEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINA-AI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 186 YRILREA-GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVH 264
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRL------GLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 265 RSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDFGtffsAVIDAKSFARIK 341
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASDMG----PLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 342 KWLEHARSSPSLTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLT 419
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDE--AEAVALAND-TDYGLA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 238859541 420 GAVFSQDkdvVQEATKVLRN-AAGNFYINDKstGSIVGQQPFGGARASG 467
Cdd:cd07120 391 ASVWTRD---LARAMRVARAiRAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-475 |
8.10e-53 |
|
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: 184.80 E-value: 8.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 36 YADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVI---QAEIDAAAElidFFRF 112
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE--EHADEIADWIVRESGSIRpkaGFEVGAAIG---ELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 113 NAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILR 190
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 191 EAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVE 270
Cdd:cd07152 163 EAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL------ELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 271 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 350
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 351 PSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 430
Cdd:cd07152 315 GA-RLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALAND-TEYGLSAGIISRDVGRA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 238859541 431 QEATKVLRnaAGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGP 475
Cdd:cd07152 388 MALADRLR--TGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
43-467 |
2.15e-52 |
|
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: 184.24 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTV---IQAE-----IDAAAELIDFFR 111
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAItleMGAPITLaraAQVGlgighLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 112 FnakyaVELEGqqpisvppstNSTVYRGLEGFVAAISPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAMLASYAVYRI 188
Cdd:cd07138 117 F-----EERRG----------NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfkhlWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSAD 268
Cdd:cd07138 180 LDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA----GKRVAEAAAD--TVKRVALELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 269 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWL---- 344
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP-ATTLGPLASAAQFDRVQGYIqkgi 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 345 -EHARsspsltILAGG--KCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTG 420
Cdd:cd07138 333 eEGAR------LVAGGpgRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE--DEAIAIAND-TPYGLAG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 238859541 421 AVFSQDKDVVQEATKVLRnaAGNFYINDkstGSIVGQQPFGGARASG 467
Cdd:cd07138 404 YVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-468 |
6.18e-52 |
|
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: 182.53 E-value: 6.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAEL 106
Cdd:cd07092 7 GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 107 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 185
Cdd:cd07092 85 VDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 186 YRILREaGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHR 265
Cdd:cd07092 165 AELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL------ELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 266 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLE 345
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDE-DTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 346 haRSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQ 425
Cdd:cd07092 317 --RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELAND-VEYGLASSVWTR 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 238859541 426 DKDVVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASGT 468
Cdd:cd07092 392 DVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
43-467 |
9.27e-52 |
|
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: 182.77 E-value: 9.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFFRFNAKyav 118
Cdd:cd07082 41 LEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANLLmweIGKTLKDALKEVDRTIDYIRDTIEELK--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 119 ELEGQ--QPISVPPSTNS--TVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVYRILR 190
Cdd:cd07082 116 RLDGDslPGDWFPGTKGKiaQVRREPLGVVLAIGPFNYPL---NLTVsklIPALiMGNTVVFKPATQGVLLGIPLAEAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 191 EAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQvaqnldrfHTFPRLAGECGGKNFHFVHRSADVE 270
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ--------HPMKRLVLELGGKDPAIVLPDADLE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 271 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 350
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN-GVDITPLIDPKSADFVEGLIDDAVAK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 351 PSlTILAGGKCDdsVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 430
Cdd:cd07082 344 GA-TVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI--EEAIELANK-SNYGLQASIFTKDINKA 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 238859541 431 QEATKVLRnaAGNFYINDKSTGSIvGQQPFGGARASG 467
Cdd:cd07082 418 RKLADALE--VGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
37-467 |
3.09e-51 |
|
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: 180.62 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 37 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKY 116
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 117 AVELEGQQPISVP---PSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 192
Cdd:cd07110 94 AEQLDAKAERAVPlpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 193 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESV 272
Cdd:cd07110 174 GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 273 VSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpS 352
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGKEE-G 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 353 LTILAGGKCDDSV--GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 430
Cdd:cd07110 326 ARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIALAND-SEYGLAAAVISRDAERC 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 238859541 431 QEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:cd07110 403 DRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-467 |
7.53e-51 |
|
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: 180.42 E-value: 7.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA-RKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQA 98
Cdd:cd07143 27 YNPST-GKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAAELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 177
Cdd:cd07143 104 KRVDVQASADTFRYYGGWADKIHGQV-IETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 178 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGECGG 257
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 258 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 337
Cdd:cd07143 258 KSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQIQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 338 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYG 417
Cdd:cd07143 337 ERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE--EEAIKRANDST-YG 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 238859541 418 LTGAVFSQDkdvVQEATKVlRNA--AGNFYINDKSTgsIVGQQPFGGARASG 467
Cdd:cd07143 413 LAAAVFTNN---INNAIRV-ANAlkAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-487 |
9.65e-51 |
|
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: 179.34 E-value: 9.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--EIDAAAE 105
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALAD-HADELAELLHAETGKPRADAglEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 106 LIDFFrfnAKYAVELEGQQPISVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 181
Cdd:cd07099 85 AIDWA---ARNAPRVLAPRKVPTGLLMPnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 182 SYAVYRILREAGLPPNIIQFVPADGPlfgdtvtSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgECG 256
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGA-------TGAALIDagvdkVAFTGSVATGRKVMAAAAERL-----IPVVL-ELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 257 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTfFSAVIDAKS 336
Cdd:cd07099 229 GKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDAD-IGPMTTARQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsY 416
Cdd:cd07099 308 LDIVRRHVDDAVAKGA-KALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIALANDSR-Y 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238859541 417 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 487
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAI 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
28-467 |
3.03e-50 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 178.56 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GK---TVIQAEIDAA 103
Cdd:PRK13473 27 GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 104 aelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 182
Cdd:PRK13473 105 ---VDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 183 YAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHF 262
Cdd:PRK13473 182 LKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 263 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKK 342
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DDEDTELGPLISAAHRDRVAG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 343 WLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDsTTSYGLTGAV 422
Cdd:PRK13473 334 FVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE--DQAVRWAN-DSDYGLASSV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 238859541 423 FSQDKDVVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASG 467
Cdd:PRK13473 411 WTRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
45-467 |
6.57e-50 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 178.39 E-value: 6.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 45 AIEAALAA-----RKEWDLKPIADRAQiFLKA-ADMLSgpRRAEILAKT-MVGQGKTVIQAE--IDAAAELIDFFrfnAK 115
Cdd:PLN02467 50 AVEAARKAfkrnkGKDWARTTGAVRAK-YLRAiAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFEYY---AD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 116 YAVELEGQQ--PISVPPST-NSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILRE 191
Cdd:PLN02467 124 LAEALDAKQkaPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 192 AGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVES 271
Cdd:PLN02467 204 VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 272 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSP 351
Cdd:PLN02467 278 AVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE-GCRLGPVVSEGQYEKVLKFISTAKSEG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 352 SlTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDV 429
Cdd:PLN02467 357 A-TILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLER 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 238859541 430 VQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:PLN02467 433 CERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
43-467 |
1.01e-48 |
|
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: 173.53 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAeLIDFFRFNAKYAVELEG 122
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLES-RRDEFIEAMMEETGATAAWAGFNVDL-AAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 123 QQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 201
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 202 V---PADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHRSADVESVVSGTLR 278
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK-----PVLL-ELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 279 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEdfgtffSAVIDAKSFARIKKWLEHARSSPSlTILAG 358
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDDALSKGA-KLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 359 GKCDDSV-GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVL 437
Cdd:cd07105 308 GLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIAND-SEYGLSAAVFTRD------LARAL 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 238859541 438 RNA----AGNFYINdkstGSIVG---QQPFGGARASG 467
Cdd:cd07105 379 AVAkrieSGAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
22-447 |
1.28e-48 |
|
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: 173.59 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 98
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLA--ANTDEIAEELTWQmGRPIAQAgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAAELIDFFRFNAKYAVelegqQPISVPPSTNST---VYRGLeGFVAAISPFN---FTAIGgnlAGAPALM-GNVVL 171
Cdd:cd07102 78 EIRGMLERARYMISIAEEAL-----ADIRVPEKDGFEryiRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 172 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRL 251
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 331
Cdd:cd07102 222 GLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 IDAKSFARIKKWLEHARSSPSlTILAGGK---CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQ 408
Cdd:cd07102 301 VSARAADFVRAQIADAIAKGA-RALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 238859541 409 LV-DSTtsYGLTGAVFSQDKDVVQE-ATKVlrnAAGNFYIN 447
Cdd:cd07102 378 LMnDSE--YGLTASVWTKDIARAEAlGEQL---ETGTVFMN 413
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
28-467 |
2.06e-48 |
|
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: 173.75 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILA--KTMvGQGKTVIQAEIDAAA 104
Cdd:cd07144 33 GEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 105 ELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTA 178
Cdd:cd07144 110 EIIAVIRYYAGWADKIQGK---TIPTSPNKLAYTLHEpyGVCGQIIPWNYPL---AMAAwklAPALAaGNTVVIKPAENT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 179 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGK 258
Cdd:cd07144 184 PLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK------AVTLECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 259 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE-HSRIKVGDPAEDfGTFFSAVIDAKSF 337
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHvKQNYKVGSPFDD-DTVVGPQVSKTQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 338 ARIKKWLEHARSSPSLTILAGGK--CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDSTTs 415
Cdd:cd07144 337 DRVLSYIEKGKKEGAKLVYGGEKapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT--YEEAIKKANDTT- 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 238859541 416 YGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 467
Cdd:cd07144 414 YGLAAAVFTKD---IRRAHRVARElEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
42-467 |
1.04e-45 |
|
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: 165.33 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 42 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELIDFFrfnAKYAV 118
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 119 ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAMLASYAVYRILR 190
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 191 EAGLPPNIIQFVPADGPLFgDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSADVE 270
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKS------VLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 271 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS--AVIDAKSfaRIKKWLEHAR 348
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE-DTDLGplARKDLRD--ELHEQVEEAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 349 SSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 428
Cdd:cd07100 298 AA-GATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALAND-SPFGLGGSVFTTDLE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 238859541 429 vvqEATKVLRN-AAGNFYIND--KSTGSIvgqqPFGGARASG 467
Cdd:cd07100 374 ---RAERVARRlEAGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-478 |
4.94e-45 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 164.86 E-value: 4.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAAELIDFFrfnAKYAVE 119
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMTLeQGKPLKEAigEVAYGASFLEYF---AEEAKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 120 LEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAMLASYAVYRILREAG 193
Cdd:PLN02278 140 VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 194 LPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVV 273
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 274 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 353
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE-GVTQGPLINEAAVQKVESHVQDAVSKGA- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 354 TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDkdvVQEA 433
Cdd:PLN02278 367 KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRD---LQRA 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 238859541 434 TKVlrNAAGNFYINDKSTGSIVGQQ-PFGGARASGTNdKPGGPHYI 478
Cdd:PLN02278 441 WRV--SEALEYGIVGVNEGLISTEVaPFGGVKQSGLG-REGSKYGI 483
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
44-467 |
5.59e-45 |
|
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: 164.29 E-value: 5.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 44 KAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNAKYAVEL 120
Cdd:cd07139 40 AAVAAARRAfdNGPWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALARDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 121 EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNII 199
Cdd:cd07139 118 PFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 200 QFVPADgplfgdtVTSSEHLCG------INFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVESVV 273
Cdd:cd07139 198 NVVPAD-------REVGEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLDAAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 274 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSL 353
Cdd:cd07139 265 PGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP-ATQIGPLASARQRERVEGYIAKGRAEGAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 354 TILAGGKCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKyketlQLV----DSttSYGLTGAVFSQDkd 428
Cdd:cd07139 344 LVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED-----DAVrianDS--DYGLSGSVWTAD-- 414
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 238859541 429 vVQEATKVLRNA-AGNFYINDKSTGSivgQQPFGGARASG 467
Cdd:cd07139 415 -VERGLAVARRIrTGTVGVNGFRLDF---GAPFGGFKQSG 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
37-467 |
9.01e-45 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 163.90 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 37 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTvIQ----AEIDAAAELIDFFr 111
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALETlDTGKP-IQetsvVDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 112 fnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 188
Cdd:PRK13252 117 --AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 189 LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 268
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE------VTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 269 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHAR 348
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-MDPATNFGPLVSFAHRDKVLGYIEKGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 349 SSPSlTILAGGKC----DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFS 424
Cdd:PRK13252 344 AEGA-RLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE--DEVIARANDTE-YGLAAGVFT 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 238859541 425 QDkdvVQEATKVL-RNAAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:PRK13252 420 AD---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
42-473 |
1.15e-44 |
|
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: 162.91 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 42 LNKAIEAALAARKEwdLKPiADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAaelIDFFRFNAKYAV 118
Cdd:cd07146 23 LREALALAASYRST--LTR-YQRSAILNKAAALLE--ARREEFARLITLEsGLCLKDTryEVGRA---ADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 119 ELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASYAVYRIL 189
Cdd:cd07146 95 RDDGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 190 REAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRLAGECGGKNFHFVHRSADV 269
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 270 ESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARS 349
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDEEAAIQIENRVEEAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 350 SPSLTILAGGKcddsVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDV 429
Cdd:cd07146 322 QGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNS-TAYGLSSGVCTNDLDT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 238859541 430 VQEATKVLRNAAGNfyINDkSTGSIVGQQPFGGARASGTNDKPG 473
Cdd:cd07146 395 IKRLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
80-467 |
4.43e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 160.29 E-value: 4.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 80 RAEILAKTMVG-QGKTVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFT--AIG 156
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 157 GNLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLW 235
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 236 KQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRI 315
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 316 KVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSV 395
Cdd:PRK10090 242 QFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238859541 396 YVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgqQPF-GGARASG 467
Cdd:PRK10090 321 VAF--DTLEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRENFEAM---QGFhAGWRKSG 385
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
22-426 |
9.10e-44 |
|
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: 160.84 E-value: 9.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPiadraqiflkaadmlsGPRRAEIL---------AKTMVGQ- 91
Cdd:cd07130 17 ISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVP----------------APKRGEIVrqigdalrkKKEALGKl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 92 -----GKTVIQA--EIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNSTvYRGLE-----GFVAAISPFNF-TAIGG- 157
Cdd:cd07130 80 vslemGKILPEGlgEVQ---EMIDI----CDFAVGLSRQLYGLTIPSERPG-HRMMEqwnplGVVGVITAFNFpVAVWGw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 158 NLAGApALMGNVVLWKPSDTAMLASYAVYRI----LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkH 233
Cdd:cd07130 152 NAAIA-LVCGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGST----A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 234 LWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHS 313
Cdd:cd07130 226 VGRQVGQAVAA--RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 314 RIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVL 393
Cdd:cd07130 304 QVRIGDPLDD-GTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPIL 380
|
410 420 430
....*....|....*....|....*....|...
gi 238859541 394 svYVYPDDKYKETLQLVDStTSYGLTGAVFSQD 426
Cdd:cd07130 381 --YVLKFDTLEEAIAWNNE-VPQGLSSSIFTTD 410
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
24-467 |
2.49e-43 |
|
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: 159.93 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 24 PFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTVIQ---A 98
Cdd:cd07117 23 PAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAAeliDFFRFNAKyAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 177
Cdd:cd07117 99 DIPLAA---DHFRYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 178 AMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgECGG 257
Cdd:cd07117 175 TSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 258 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 337
Cdd:cd07117 248 KSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP-DTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 338 ARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSt 413
Cdd:cd07117 327 DKILSYVDIAKEEGA-KILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE--DEVIDMAND- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 238859541 414 TSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:cd07117 403 SEYGLGGGVFTKD---INRALRVARAVeTGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
22-468 |
3.53e-43 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 159.44 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARK---EWDLKPIADRAQIFLKAADMLSgpRRAEILA--KTMVGqGKTVI 96
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIE--RDRAYLAslETLDN-GKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 97 QAEIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWK 173
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 174 PSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfKHLWKQVA--QNLDrfhtfpRL 251
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 252 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 331
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP-KTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLVD 411
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIF-----KFKTIDEVIE 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238859541 412 --STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASGT 468
Cdd:cd07141 406 raNNTTYGLAAAVFTKDIDKAITFSNALR--AGTVWVNCYNVVSP--QAPFGGYKMSGN 460
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
28-473 |
6.91e-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: 158.43 E-value: 6.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEIDAAAE 105
Cdd:cd07142 29 GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 106 LIDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 182
Cdd:cd07142 108 AARLFRYYAGWADKIHG---MTLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 183 YAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDrfhtfpRLAGECGGKNFH 261
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK------PVTLELGGKSPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 262 FVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaedfgtFFSAV-----IDAKS 336
Cdd:cd07142 259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDStTSY 416
Cdd:cd07142 333 FEKILSYIEHGKEEGA-TLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT--VDEVIKRANN-SKY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238859541 417 GLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 473
Cdd:cd07142 409 GLAAGVFSKNIDTANTLSRALK--AGTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-467 |
1.41e-42 |
|
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: 157.89 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTV---I 96
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLELLAVaeTL-DNGKPIretL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 97 QAEIDAAaelIDFFRFNAKYAVELEGQqpIS-VPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP 174
Cdd:cd07559 97 AADIPLA---IDHFRYFAGVIRAQEGS--LSeIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 175 SDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPrLAGE 254
Cdd:cd07559 172 ASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-VTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 255 CGGK--NFHFvhrsADVES--------VVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDf 324
Cdd:cd07559 245 LGGKspNIFF----DDAMDadddfddkAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 325 GTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 400
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGA-EVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238859541 401 DkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:cd07559 398 E--EEAIAIAND-TEYGLGGGVWTRD---INRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
27-466 |
2.39e-42 |
|
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: 157.29 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 27 HGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAA 103
Cdd:cd07085 25 TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLITlEHGKTLADArgDVLRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 104 AELIDFfrfNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSD 176
Cdd:cd07085 103 LEVVEF---ACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAM------IPLWMfpmaiacGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 177 TAMLASYAVYRILREAGLPPNIIQFVPADGplfgDTVtssEHLC------GINFTGSVPTFKHLWKQVAQNLDRFHTFpr 250
Cdd:cd07085 174 RVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAV---NALLdhpdikAVSFVGSTPVGEYIYERAAANGKRVQAL-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 251 lageCGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSA 330
Cdd:cd07085 245 ----GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG-AGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 331 VIDAKSFARIKKWLEHArsspsltILAGGKC-----DDSV-----GYFVEPCIVESKDPQEPIMKEEIFGPVLSVyVYPD 400
Cdd:cd07085 320 VISPAAKERIEGLIESG-------VEEGAKLvldgrGVKVpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSI-VRVD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859541 401 DkYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNA-AGNFYINdkstgsI-----VGQQPFGGARAS 466
Cdd:cd07085 392 T-LDEAIAIINA-NPYGNGAAIFTRSGAA---ARKFQREVdAGMVGIN------VpipvpLAFFSFGGWKGS 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
28-476 |
4.34e-42 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 156.40 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQ---AEIDAAA 104
Cdd:cd07111 47 GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 105 ELidfFRFNAKYA----VELEGQQPIsvppstnstvyrgleGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 179
Cdd:cd07111 126 RH---FYHHAGWAqlldTELAGWKPV---------------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 180 LASYAVYRILREAGLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKN 259
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 260 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffsAVIDAKS 336
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkAIDMG----AIVDPAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSPSLTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSY 416
Cdd:cd07111 337 LKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTFRTAKEAVALANN-TPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 417 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASGTNdKPGGPH 476
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
44-475 |
5.15e-40 |
|
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: 150.53 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 44 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA---EIDAAAELIDFFRFNAKYAVe 119
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKIRWTLKHGEKAL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 120 legqQPISVPPSTNsTVYRGLE------GFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVYRIL 189
Cdd:cd07098 99 ----RPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGFFLSII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 190 REA----GLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHR 265
Cdd:cd07098 171 REClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 266 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFGtffsAVIDAKSFARIKK 342
Cdd:cd07098 244 DADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVG----AMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 343 WLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGL 418
Cdd:cd07098 320 LVADAVEKGA-RLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANS-TEYGL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 419 TGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTnDKPGGP 475
Cdd:cd07098 396 GASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
37-472 |
2.88e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 145.87 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 37 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAkTMVGQ--GKTVIQAEIDAAAELidffrfnA 114
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 115 KYAV------ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYR 187
Cdd:PRK09457 104 KIAIsiqayhERTGEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 188 ILREAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSA 267
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 268 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEH 346
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 347 ARSSPSLTILAGGKCDDSVGyFVEPCIVESKDPQEPImKEEIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQD 426
Cdd:PRK09457 337 LLALGGKSLLEMTQLQAGTG-LLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDD--FDEAIRLANN-TRFGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 238859541 427 KDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGtNDKP 472
Cdd:PRK09457 412 REDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG-NHRP 453
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-469 |
1.56e-37 |
|
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: 143.33 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNHGHkVAKFCYADKSLLNKAIEAALAA---RKEWdlKPIADRAQIFLKAADMLSGprRAEILAKTMVGQG-KTVIQ 97
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 98 A--EIDAAaelIDFFRFNAKYAVELEGQQ-PISV-PPSTNSTVYRGLE--GFVAAISPFNFTAiggNLA---GAPAL-MG 167
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGLtPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 168 NVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNldrfht 247
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 248 fPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTF 327
Cdd:cd07148 226 -TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT-DPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 328 FSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETL 407
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSY--DDLDEAI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859541 408 QLVDStTSYGLTGAVFSQDKDVVQEATKVLrnAAGNFYINDKsTGSIVGQQPFGGARASGTN 469
Cdd:cd07148 379 AQANS-LPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
28-473 |
7.33e-37 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 143.02 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAeidAAAE 105
Cdd:PLN02466 83 GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 106 L---IDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAM 179
Cdd:PLN02466 159 LpmfARLFRYYAGWADKIHG---LTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 180 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprlagECGGKN 259
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 260 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQI----KGRLLeehsRIKVGDPaedfgtFFSAV---- 331
Cdd:PLN02466 311 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARAL----KRVVGDP------FKKGVeqgp 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 -IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLV 410
Cdd:PLN02466 381 qIDSEQFEKILRYIKSGVESGA-TLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL-----KFKDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 411 D--STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 473
Cdd:PLN02466 455 RraNNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-467 |
3.03e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 140.73 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-------TMVGQGKTViqa 98
Cdd:PLN02766 46 GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 EIDAAAELidfFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 177
Cdd:PLN02766 121 DIPAAAGL---LRYYAGAADKIHGET-LKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 178 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRfhtfprLAGECG 256
Cdd:PLN02766 197 TPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 257 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKS 336
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 337 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYK---ETLQLVDSt 413
Cdd:PLN02766 350 FEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM-----KFKtveEAIKKANN- 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238859541 414 TSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASG 467
Cdd:PLN02766 423 TKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
44-467 |
3.32e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.04 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 44 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQA--EIDAAAELIDFFRFNAK--YAV 118
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 119 ELEGQQPisvppSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPN 197
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 198 IIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTL 277
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 278 RSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILA 357
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK-GVTIGPLIDEKAVAKVEEHIADALEKGA-RVVC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 358 GGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVL 437
Cdd:PRK11241 357 GGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE--ADVIAQAND-TEFGLAAYFYARD------LSRVF 427
|
410 420 430
....*....|....*....|....*....|..
gi 238859541 438 RNA-AGNFYINDKSTGSIVGQ-QPFGGARASG 467
Cdd:PRK11241 428 RVGeALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
28-467 |
1.24e-34 |
|
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: 135.70 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILA---------------KTMVG 90
Cdd:cd07140 31 GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME--EHQEELAtiesldsgavytlalKTHVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 91 QGktviqaeidaaaelIDFFRFNAKYAVELEGQQ-PIS-VPPSTNSTVYRGLE-GFVAAISPFNFTAIGGNLAGAPALM- 166
Cdd:cd07140 109 MS--------------IQTFRYFAGWCDKIQGKTiPINqARPNRNLTLTKREPiGVCGIVIPWNYPLMMLAWKMAACLAa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 167 GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVA-QNLDRf 245
Cdd:cd07140 175 GNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKK- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 246 htfprLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AE 322
Cdd:cd07140 254 -----VSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPldrST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 323 DFGTffsavidAKSFARIKKWLEHARSS--PSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 400
Cdd:cd07140 329 DHGP-------QNHKAHLDKLVEYCERGvkEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238859541 401 DKYKETLQLVDsTTSYGLTGAVFSQDkdvvqeATKVLRNA----AGNFYINDKSTGSIVGqqPFGGARASG 467
Cdd:cd07140 402 GDVDGVLQRAN-DTEYGLASGVFTKD------INKALYVSdkleAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
42-487 |
2.82e-32 |
|
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: 128.51 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 42 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEiDAAAeliDFFRFNAKYAVELE 121
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICG---DQVQLRARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 122 GQQP------ISVPPSTNSTVYRGLEGFVAAISPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAG 193
Cdd:cd07084 76 YRIPhepgnhLGQGLKQQSHGYRWPYGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 194 -LPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkhlwkQVAQNLDRFHTFPRLAGECGGKNFHFVHRSAD-VES 271
Cdd:cd07084 155 lLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 272 VVSGTLRSAFEYGGQKCSACSRLYVPH--SLWPQIKgRLLEEHSRIKVGDpaedfgTFFSAVIDAKSFARIkkwlEHARS 349
Cdd:cd07084 226 VAWQCVQDMTACSGQKCTAQSMLFVPEnwSKTPLVE-KLKALLARRKLED------LLLGPVQTFTTLAMI----AHMEN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 350 SPSLTILAGGK--CDDSVGYFVEPCI-------VESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYgLTG 420
Cdd:cd07084 295 LLGSVLLFSGKelKNHSIPSIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 421 AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 487
Cdd:cd07084 374 AIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
42-487 |
8.64e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 127.70 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 42 LNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMvGQGKTV---IQAEIDAAAELIdffRFNAKY 116
Cdd:PRK09847 59 IDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAI---RWYAEA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 117 AVELEGQqpisVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 192
Cdd:PRK09847 135 IDKVYGE----VATTSShelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 193 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGECGGKNFHFVHRSA-DVES 271
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 272 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSP 351
Cdd:PRK09847 286 AASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGESKG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 352 SLtiLAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQ 431
Cdd:PRK09847 365 QL--LLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRDLSRAH 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 238859541 432 EATKVLRnaAGNFYINDKSTGSIVgqQPFGGARASGtNDKPGGPHYILRWTSPQVI 487
Cdd:PRK09847 439 RMSRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-467 |
3.66e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 125.24 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 28 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAeiLAKTMVGQ-GKTVIQAEIDAAaEL 106
Cdd:PRK09406 11 GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQ--VAALMTLEmGKTLASAKAEAL-KC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 107 IDFFRFNAKYAVELEGQQPISVPPSTNS---TVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWK-PSDTAMLA 181
Cdd:PRK09406 88 AKGFRYYAEHAEALLADEPADAAAVGASrayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 182 SYaVYRILREAGLPPNIIQ--FVPADGPlfgDTVTSSEHLCGINFTGSVPTfkhlWKQVAQnldrfhtfprLAG------ 253
Cdd:PRK09406 167 LY-LADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikkt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 254 --ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 331
Cdd:PRK09406 229 vlELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP-DTDVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 332 IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVD 411
Cdd:PRK09406 308 ATEQGRDEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 412 STTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSivGQQPFGGARASG 467
Cdd:PRK09406 385 ATT-FGLGSNAWTRD---EAEQERFIDDlEAGQVFINGMTVSY--PELPFGGVKRSG 435
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
44-473 |
1.77e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 124.18 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 44 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFfrfnAKYAVELEGQ 123
Cdd:PLN02315 60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALR--AKLDYLGRLVSLEMGKILAEGIGEVQEIIDM----CDFAVGLSRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 124 QPISVPPSTNST-----VYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI----LREAG 193
Cdd:PLN02315 134 LNGSIIPSERPNhmmmeVWNPL-GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 194 LPPNIIQFVpADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNFHFVHRSADVESVV 273
Cdd:PLN02315 213 LPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 274 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 353
Cdd:PLN02315 286 RSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLGPLHTPESKKNFEKGIEIIKSQGG- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 354 TILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVLsvYVYPDDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQEA 433
Cdd:PLN02315 364 KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQ-GLSSSIFTRNPETIFKW 439
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 238859541 434 TKVLRNAAGNFYINDKSTGSIVGQQpFGGARASGTNDKPG 473
Cdd:PLN02315 440 IGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAG 478
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
94-467 |
2.06e-27 |
|
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: 114.16 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 94 TVIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVV 170
Cdd:cd07087 61 AVVLGEIDHALKHLK------KWMKPRRVSVPLLLQPAKAYVIPEPL-GVVLIIGPWNYplqLALA-PLIGAIA-AGNTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 171 LWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPlfgdtVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLdrfhT 247
Cdd:cd07087 132 VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-----VATallAEPFDHIFFTGSPAVGKIVMEAAAKHL----T 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 248 FPRLagECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSlwpqIKGRLLEEHSR-IKV---GDPAE- 322
Cdd:cd07087 202 PVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES----IKDELIEELKKaIKEfygEDPKEs 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 323 -DFGtffsAVIDAKSFARIKKWLEHArsspslTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDd 401
Cdd:cd07087 276 pDYG----RIINERHFDRLASLLDDG------KVVIGGQVDKE-ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDD- 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 402 kYKETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 467
Cdd:cd07087 344 -LDEAIEFINS-RPKPLALYLFSEDKAVQE---RVLAEtSSGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
14-467 |
3.57e-27 |
|
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: 114.09 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 14 WTSDV--QY--QVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTmV 89
Cdd:cd07116 9 WVAPVkgEYfdNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-W 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 90 GQGKTV---IQAEIDAAaelIDFFRFNAKYAVELEGqqpiSVPPSTNSTV-YRGLE--GFVAAISPFNFTAIGGNLAGAP 163
Cdd:cd07116 87 DNGKPVretLAADIPLA---IDHFRYFAGCIRAQEG----SISEIDENTVaYHFHEplGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 164 ALM-GNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNL 242
Cdd:cd07116 160 ALAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 243 drfhtFPrLAGECGGK--NFHF----VHRSADVESVVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHSRIK 316
Cdd:cd07116 239 -----IP-VTLELGGKspNIFFadvmDADDAFFDKALEGFVMFALNQG-EVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 317 VGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVEsKDPQEPIMKEEIFGPV 392
Cdd:cd07116 312 QGNPL-DTETMIGAQASLEQLEKILSYIDIGKEEGA-EVLTGGErnelGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238859541 393 LSVYVYPDdkYKETLQLVDSTTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 467
Cdd:cd07116 389 LAVTTFKD--EEEALEIANDTL-YGLGAGVWTRD---GNTAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
124-467 |
2.62e-25 |
|
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: 108.08 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 124 QPISVPPS-----TNSTVYRGLEGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAglp 195
Cdd:cd07134 79 KPKRVRTPlllfgTKSKIRYEPKGVCLIISPWNYpfnLAFG-PLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 196 pniiqFVPADGPLF-GDTVTSSE-------HlcgINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSA 267
Cdd:cd07134 154 -----FDEDEVAVFeGDAEVAQAllelpfdH---IFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 268 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHA 347
Cdd:cd07134 220 DLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 348 RSSPSlTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD-DkyketlQLVDSTTSYG--LTGAVFS 424
Cdd:cd07134 300 VAKGA-KVEFGGQFDAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDlD------EVIEYINAKPkpLALYVFS 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 238859541 425 QDKDVVQeatKVLRN-AAGNFYINDkstgSIV----GQQPFGGARASG 467
Cdd:cd07134 372 KDKANVN---KVLARtSSGGVVVND----VVLhflnPNLPFGGVNNSG 412
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
22-467 |
4.93e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 104.56 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQiflKAADMLSGPR-RAEILAKTMVGQ-GKTVIQA- 98
Cdd:PRK13968 12 VNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQ---KLRDIGKALRaRSEEMAQMITREmGKPINQAr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 99 -EIDAAAELIDFFrfnAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNLAGA-PALM-GNVVLWKPS 175
Cdd:PRK13968 88 aEVAKSANLCDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 176 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGEC 255
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK------CVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 256 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGtffsaviDAK 335
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN-------ALG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 336 SFARIKKWLE-HARSSPSL----TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYkeTLQLV 410
Cdd:PRK13968 309 PMARFDLRDElHHQVEATLaegaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEH--ALELA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 238859541 411 DStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSivGQQPFGGARASG 467
Cdd:PRK13968 387 ND-SEFGLSATIFTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
142-468 |
6.03e-24 |
|
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: 104.22 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 142 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSS-E 217
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 218 HlcgINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP 297
Cdd:cd07135 187 K---IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 298 HSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVgYFVEPCIVESK 377
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANAS--PDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 378 DPQEPIMKEEIFGPVLSVYVYPD-DKYKETLQLVDSTtsygLTGAVFSQDKDVVQeatKVL-RNAAGNFYINDKSTGSIV 455
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDlDEAIKVINSRDTP----LALYIFTDDKSEID---HILtRTRSGGVVINDTLIHVGV 403
|
330
....*....|...
gi 238859541 456 GQQPFGGARASGT 468
Cdd:cd07135 404 DNAPFGGVGDSGY 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
15-428 |
7.61e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 101.37 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 15 TSDVQYQVSPfnhghkvakfCYADKslLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRR--AEILAKTMVGQG 92
Cdd:PLN00412 40 TRKTQYKVQA----------CTQEE--VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 93 KTVIqAEIDAAAELIDffrfnakYAVElEGQQPISVPPSTNSTVYRGLE------------GFVAAISPFNFTAiggNLA 160
Cdd:PLN00412 108 KDAV-TEVVRSGDLIS-------YTAE-EGVRILGEGKFLVSDSFPGNErnkycltskiplGVVLAIPPFNYPV---NLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 161 G---APALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSvptfkhlwk 236
Cdd:PLN00412 176 VskiAPALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG--------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 237 qvaqnlDRFHTFPRLAG------ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLE 310
Cdd:PLN00412 247 ------DTGIAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 311 EHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFG 390
Cdd:PLN00412 321 KVAKLTVGPPEDD--CDITPVVSESSANFIEGLVMDAKEKGA-TFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFG 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 238859541 391 PVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 428
Cdd:PLN00412 395 PVLPVIRINSV--EEGIHHCNA-SNFGLQGCVFTRDIN 429
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
95-467 |
2.50e-22 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 99.72 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 95 VIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVL 171
Cdd:PTZ00381 71 LTVAEIEHLLKHLD------EYLKPEKVDTVGVFGPGKSYIIPEPL-GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 172 WKPSDTAMLASYAVYRILREAgLPPNIIQFVPADgplfgdtVTSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfh 246
Cdd:PTZ00381 142 LKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG-------VEVTTELLKepfdhIFFTGSPRVGKLVMQAAAENL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 247 TFPRLagECGGKNFHFVHRSADV----ESVVSGTLRSAfeygGQKCSACSRLYVPHSlwpqIKGRLLEE--HSRIKV--G 318
Cdd:PTZ00381 210 TPCTL--ELGGKSPVIVDKSCNLkvaaRRIAWGKFLNA----GQTCVAPDYVLVHRS----IKDKFIEAlkEAIKEFfgE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 319 DP--AEDFgtffSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVY 396
Cdd:PTZ00381 280 DPkkSEDY----SRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPIL 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859541 397 VYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 467
Cdd:PTZ00381 351 TYEN--IDEVLEFINS-RPKPLALYYFGEDKRHKE---LVLENtSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
142-467 |
2.01e-21 |
|
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: 96.80 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 142 GFVAAISPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPadgplfGDTVTSSEHL 219
Cdd:cd07136 102 GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 220 CG----INFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVE----SVVSGTLRSAfeygGQKCSAC 291
Cdd:cd07136 174 DQkfdyIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKlaakRIVWGKFLNA----GQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 292 SRLYVPHSlwpqIKGRLLEE---HSRIKVGDPA---EDFGTffsaVIDAKSFARIKKWLEHArsspslTILAGGKCDDSV 365
Cdd:cd07136 244 DYVLVHES----VKEKFIKElkeEIKKFYGEDPlesPDYGR----IINEKHFDRLAGLLDNG------KIVFGGNTDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 366 GYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNAA-GNF 444
Cdd:cd07136 310 LY-IEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKS-RPKPLALYLFSEDKKV---EKKVLENLSfGGG 382
|
330 340
....*....|....*....|...
gi 238859541 445 YINDKSTGSIVGQQPFGGARASG 467
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
130-467 |
1.48e-19 |
|
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: 91.01 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 130 PSTNSTVYRGLeGFVAAISPFNF---TAIGGnLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFV---P 203
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVtggA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 204 ADGPLFgdtvtSS---EHLCginFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVESVVSGTLRSA 280
Cdd:cd07133 168 DVAAAF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 281 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIkvgdpaedFGTF-----FSAVIDAKSFARIKKWLEHARSSPS-LT 354
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM--------YPTLadnpdYTSIINERHYARLQGLLEDARAKGArVI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 355 ILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDSTTS----YgltgaVFSQDKdvv 430
Cdd:cd07133 306 ELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTY--DSLDEAIDYINARPRplalY-----YFGEDK--- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 238859541 431 QEATKVLRN-AAGNFYINDksTGSIVGQ--QPFGGARASG 467
Cdd:cd07133 376 AEQDRVLRRtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-424 |
1.66e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 88.65 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 43 NKAIEAALAARKE----WDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQAEIDAAAELiDFFRFNAKYA 117
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLKDSHGDIFRGL-EVVEHACGMA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 118 VELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAMLASYAVYRILR 190
Cdd:PLN02419 227 TLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAELAM 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 191 EAGLPPNIIQFVPADGplfgDTVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSA 267
Cdd:PLN02419 301 EAGLPDGVLNIVHGTN----DTVNAicdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 268 DVESVVSGTLRSAFEYGGQKCSACSRL-YVPHSL-WpqiKGRLLEEHSRIKV---GDPAEDFGtffsAVIDAKSFARIKK 342
Cdd:PLN02419 371 NIDATLNALLAAGFGAAGQRCMALSTVvFVGDAKsW---EDKLVERAKALKVtcgSEPDADLG----PVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 343 WLEHARSSPSLTILAGgkcDDSV------GYFVEPCIVESKDPQEPIMKEEIFGPVLsvYVYPDDKYKETLQLVDStTSY 416
Cdd:PLN02419 444 LIQSGVDDGAKLLLDG---RDIVvpgyekGNFIGPTILSGVTPDMECYKEEIFGPVL--VCMQANSFDEAISIINK-NKY 517
|
....*...
gi 238859541 417 GLTGAVFS 424
Cdd:PLN02419 518 GNGAAIFT 525
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
254-467 |
1.11e-16 |
|
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: 82.27 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 254 ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA-----CSrlyvphslwPQIKGRLLEE-HSRIKV---GDPAE-- 322
Cdd:cd07132 206 ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCT---------PEVQEKFVEAlKKTLKEfygEDPKEsp 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 323 DFGTffsaVIDAKSFARIKKWLEharsspSLTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdk 402
Cdd:cd07132 277 DYGR----IINDRHFQRLKKLLS------GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNN-- 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238859541 403 YKETLQLVDSTTSyGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 467
Cdd:cd07132 344 LDEAIEFINSREK-PLALYVFSNNKKVIN---KILSNtSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
140-452 |
1.61e-12 |
|
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: 69.61 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 140 LEGFVAAISPFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLAsYAVYRILREAG-LPPNIIQFVPAD-GPLFgDTVTS 215
Cdd:cd07128 144 RRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-DHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 216 SEHlcgINFTGSVPTFKHLwkQVAQNLDRFHTfpRLAGECGGKNFHFVhrSADVES-------VVSGTLRSAFEYGGQKC 288
Cdd:cd07128 222 QDV---VAFTGSAATAAKL--RAHPNIVARSI--RFNAEADSLNAAIL--GPDATPgtpefdlFVKEVAREMTVKAGQKC 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 289 SACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGGK-------C 361
Cdd:cd07128 293 TAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLE-GVRMGPLVSREQREDVRAAVATLLAEA--EVVFGGPdrfevvgA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 362 DDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLSVYVYpdDKYKETLQLVdsttSYG---LTGAVFSQDKDvvqEATKV 436
Cdd:cd07128 370 DAEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPY--DSLAEAIELA----ARGrgsLVASVVTNDPA---FAREL 440
|
330 340
....*....|....*....|....
gi 238859541 437 LRNAA---GNFYINDK-----STG 452
Cdd:cd07128 441 VLGAApyhGRLLVLNRdsakeSTG 464
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
125-468 |
1.16e-11 |
|
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: 66.67 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 125 PISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAMLASYAVYRILrEAGLPPNIIQF 201
Cdd:cd07137 87 PLTTFPAKAEIVSEPL-GVVLVISAWNF-PFLLSLepvIGAIA-AGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 202 VPAdgplfgdTVTSSEHLC-----GINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVESVVSGT 276
Cdd:cd07137 163 IEG-------GVPETTALLeqkwdKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 277 LrsAFEYG---GQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSl 353
Cdd:cd07137 230 A--GGKWGcnnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKES--KDLSRIVNSHHFQRLSRLLDDPSVADK- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 354 tILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVdSTTSYGLTGAVFSQDKDVvqEA 433
Cdd:cd07137 305 -IVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPIITV--KKIEESIEII-NSRPKPLAAYVFTKNKEL--KR 377
|
330 340 350
....*....|....*....|....*....|....*
gi 238859541 434 TKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGT 468
Cdd:cd07137 378 RIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
22-483 |
7.59e-11 |
|
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: 64.05 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 22 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIA--DRAQ----IFLKAADMLSGPRRAEILAK-TMVGQGKT 94
Cdd:cd07126 17 LDPLN-GDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLlygdVSHRVAHELRKPEVEDFFARlIQRVAPKS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 95 VIQA--EIDAAAELIDFF-----RFNAK-YAV--ELEGQQpisvppstnSTVYRGLEGFVAAISPFNFT----AIggNLA 160
Cdd:cd07126 96 DAQAlgEVVVTRKFLENFagdqvRFLARsFNVpgDHQGQQ---------SSGYRWPYGPVAIITPFNFPleipAL--QLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 161 GApALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCgINFTGSvptfkhlwKQVAQ 240
Cdd:cd07126 165 GA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM-TLFTGS--------SKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 241 NLDRfHTFPRLAGECGGKNFHFVHRS-ADVESVVSGTLRSAFEYGGQKCSACSRLYVpHSLWPQ--IKGRLLEEHSRIKV 317
Cdd:cd07126 235 RLAL-ELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA-HENWVQagILDKLKALAEQRKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 318 GD----PAEDFGTffsavidaksfARIKKWLEHARSSPSLTILAGGK-----CDDSVGYFVEPC-----IVESKDPQE-P 382
Cdd:cd07126 313 EDltigPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGKpltnhSIPSIYGAYEPTavfvpLEEIAIEENfE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 383 IMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYgLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQ--QPF 460
Cdd:cd07126 382 LVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHwfGPA 460
|
490 500
....*....|....*....|....
gi 238859541 461 GGARASGTndkpGGPHYI-LRWTS 483
Cdd:cd07126 461 GDPRGAGI----GTPEAIrLVWSC 480
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
138-400 |
1.57e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 63.18 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 138 RGLEGFVAAispFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLASYAVyRILREAG-LPPNIIQFV---PAD-----G 206
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPaTATAWLTQRMV-KDVVAAGiLPAGALSVVcgsSAGlldhlQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 207 PlfGDTVTssehlcginFTGSVPTFKHLwkqvaqnldRFHtfPRLAGecggknfHFVHRSADVESVVSGTL-------RS 279
Cdd:PRK11903 225 P--FDVVS---------FTGSAETAAVL---------RSH--PAVVQ-------RSVRVNVEADSLNSALLgpdaapgSE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 280 AFEY------------GGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAED---FGTFFSAVIDAKSFARIKKWL 344
Cdd:PRK11903 276 AFDLfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDgvrMGPLVSRAQLAAVRAGLAALR 355
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238859541 345 EHArsspslTILAGGK------CDDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLSVYVYPD 400
Cdd:PRK11903 356 AQA------EVLFDGGgfalvdADPAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRD 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
167-467 |
7.50e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.50 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 167 GNVVLWKPSDTAMlASYAVYRILREAGLPPNIIQFVpaDGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfh 246
Cdd:PLN02174 140 GNAVVLKPSELAP-ASSALLAKLLEQYLDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 247 tfprLAGECGGKNFHFVHRSADVESVVSGTLrsAFEYG---GQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAED 323
Cdd:PLN02174 215 ----VVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGcnnGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 324 fgTFFSAVIDAKSFARIKKWLEHARSSPSltILAGGKcDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKY 403
Cdd:PLN02174 289 --KDMSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTL--NNL 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238859541 404 KETLQLVDSTTSyGLTGAVFSQDKDVVQE-ATKVlrnAAGNFYINDKSTGSIVGQQPFGGARASG 467
Cdd:PLN02174 362 EESFDVIRSRPK-PLAAYLFTHNKKLKERfAATV---SAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
115-467 |
2.35e-05 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 46.64 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 115 KYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDtamlasyavyrilre 191
Cdd:PLN02203 84 KWMAPKKAKLPLVAFPATAEVVPEPL-GVVLIFSSWNF-PIGLSLeplIGAIA-AGNAVVLKPSE--------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 192 agLPPNIIQFVPADGPLFGDT---------VTSSEHLC-----GINFTGSVPTFKHLWKQVAQnldrfHTFPrLAGECGG 257
Cdd:PLN02203 146 --LAPATSAFLAANIPKYLDSkavkvieggPAVGEQLLqhkwdKIFFTGSPRVGRIIMTAAAK-----HLTP-VALELGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 258 KN---FHFVHRSADVESVVSGTLRSAFEY-GGQKCSACSRLYVPHSLWPqIKGRLLEEHSRIKVGDPAEDFGTFfSAVID 333
Cdd:PLN02203 218 KCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAP-ILIELLKSTIKKFFGENPRESKSM-ARILN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 334 AKSFARIKKWLEHARSSPSltILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDST 413
Cdd:PLN02203 296 KKHFQRLSNLLKDPRVAAS--IVHGGSIDEK-KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSIAFINSK 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 238859541 414 TSyGLTGAVFSQDKDVVQEAtkVLRNAAGNFYINDKSTGSIVGQQPFGGARASG 467
Cdd:PLN02203 371 PK-PLAIYAFTNNEKLKRRI--LSETSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
167-447 |
2.77e-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: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 167 GNVVLWKPSDTAMLASYAVYRILR----EAGLPPNIIQFV--PADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQ 240
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTLATRPE-VRIIDFTGSNAFGDWLEANARQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 241 NLdrfhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP---------HSLWPQIKGRLLEE 311
Cdd:cd07127 300 AQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgiqtddgRKSFDEVAADLAAA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859541 312 HSRIkVGDPAEDFGtFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGP 391
Cdd:cd07127 372 IDGL-LADPARAAA-LLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGP 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 238859541 392 VLsvYVYPDDKYKETLQLV-DSTTSYG-LTGAVFSQDKDVVQEATKVLRNAAGNFYIN 447
Cdd:cd07127 448 IA--FVVATDSTDHSIELArESVREHGaMTVGVYSTDPEVVERVQEAALDAGVALSIN 503
|
|
| |
