|
Name |
Accession |
Description |
Interval |
E-value |
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
35-581 |
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: 891.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 35 KNEQVKPFTNTDtKDWDLLRASIMKFKSSSLEVPLVINGERIYYNNSNrsvFAQSNPACHKQVLANVTQATELDVKDAIQ 114
Cdd:TIGR01236 1 ANEPVLPFRPGS-PERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNER---IPQVNPHNHQAVLAKATNATEEDAMKAVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 115 AAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNLQPVq 194
Cdd:TIGR01236 77 AALDAKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 195 SAQGVWNKAEYRPLEGFIYAVSPFNFTAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDP 274
Cdd:TIGR01236 156 SAPGEWNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 275 ILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVVNglYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQ 354
Cdd:TIGR01236 236 VQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDR--YHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 355 GQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVntaaspisgGDLHGFMGPVIHEQSYNKLIKVIEEAKTDPE-LEI 433
Cdd:TIGR01236 314 GQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDP---------DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 434 IYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSMYGLTGSVFAKDREAINLADE 513
Cdd:TIGR01236 385 LYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADK 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 514 KLKFSCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIRNTKENFVELTDFKYPSNY 581
Cdd:TIGR01236 465 KLRFAAGNFYINDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
34-570 |
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: 843.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 34 IKNEQVKPFTnTDTKDWDLLRASIMKFKSSSLEVPLVINGERIYYNNSNRsvfaQSNPACHKQVLANVTQATELDVKDAI 113
Cdd:cd07123 1 PVNEPVLSYA-PGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGK----QVMPHDHAHVLATYHYADAALVEKAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 114 QAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNLQPV 193
Cdd:cd07123 76 EAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 194 QSAQGVWNKAEYRPLEGFIYAVSPFNFTAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGD 273
Cdd:cd07123 156 SSPAGVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 274 PILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVVNglYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEF 353
Cdd:cd07123 236 GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDR--YRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 354 QGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNtaaspisggDLHGFMGPVIHEQSYNKLIKVIEEAKTDPELEI 433
Cdd:cd07123 314 QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPD---------DFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 434 IYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSMYGLTGSVFAKDREAINLADE 513
Cdd:cd07123 385 IAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATD 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 366986647 514 KLKFSCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIRNTKENFV 570
Cdd:cd07123 465 ALRNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFV 521
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
51-569 |
5.36e-140 |
|
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: 415.44 E-value: 5.36e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 51 DLLRASIMKFKSSSLE-VPLVINGERIYYNNSNRSVfaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFY 129
Cdd:cd07083 2 RAMREALRRVKEEFGRaYPLVIGGEWVDTKERMVSV----SPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 130 DRAAVFLKAADLISTKYRYDMLAATMLGqGKNVYQaEIDCITELSDFFRFNVKYAHDLYNLQP-VQSAQGVWNKAEYRPL 208
Cdd:cd07083 78 DRARLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVeVVPYPGEDNESFYVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 209 eGFIYAVSPFNFT-AIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEF 287
Cdd:cd07083 156 -GAGVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 288 GGLHFTGSTQVFKQLYGkiQTGVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIP 367
Cdd:cd07083 235 RGINFTGSLETGKKIYE--AAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 368 QSKSEEFFRDLIGTLQQQKVTPvntaasPISGGDlhgFMGPVIHEQSYNKLIKVIEEAKTdpELEIIYGGQYDKGEGWFV 447
Cdd:cd07083 313 QGAYEPVLERLLKRAERLSVGP------PEENGT---DLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 448 GPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSMYGLTGSVFAKDREAINLADEklkFSCGNFYINDK 527
Cdd:cd07083 382 APTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARRE---FHVGNLYINRK 458
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 366986647 528 CTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIRNTKENF 569
Cdd:cd07083 459 ITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
35-569 |
1.15e-124 |
|
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: 376.56 E-value: 1.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 35 KNEqvkPFTNTDTKDW-DLLRASIMKFKSS-SLEVPLVINGERIYynnsNRSVFAQSNPACHKQVLANVTQATELDVKDA 112
Cdd:cd07124 2 RNE---PFTDFADEENrAAFRAALARVREElGREYPLVIGGKEVR----TEEKIESRNPADPSEVLGTVQKATKEEAEAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 113 IQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEIDcITELSDFFRFnvkYAHDLYNLQ- 191
Cdd:cd07124 75 VQAARAAFPTWRRTPPEERARLLLRAAALLRRR-RFELAAWMVLEVGKNWAEADAD-VAEAIDFLEY---YAREMLRLRg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 192 -PVQSAQGVWNKAEYRPLeGFIYAVSPFNF-TAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINF 269
Cdd:cd07124 150 fPVEMVPGEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 270 VPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGkiQTGVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRG 349
Cdd:cd07124 229 LPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE--RAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 350 AFEFQGQKCSATSRLYIPQSKSEEFFRDLIgtlQQQKVTPVNTAASPISggdlhgFMGPVIHEQSYNKLIKVIEEAKTDP 429
Cdd:cd07124 307 AFGFQGQKCSACSRVIVHESVYDEFLERLV---ERTKALKVGDPEDPEV------YMGPVIDKGARDRIRRYIEIGKSEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 430 ELeiIYGGQYDKG--EGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREA 507
Cdd:cd07124 378 RL--LLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIANDTE-YGLTGGVFSRSPEH 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366986647 508 INLADEklKFSCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIRNTKENF 569
Cdd:cd07124 453 LERARR--EFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
63-569 |
7.89e-124 |
|
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: 373.31 E-value: 7.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 63 SSLEVPLVINGERIYYNNSNRsvFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLI 142
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGET--FDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 143 sTKYRYDMLAATMLGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTA 222
Cdd:COG1012 79 -EERREELAALLTLETGKPLAEARGE-VDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPL-GVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 223 IAANLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQ 301
Cdd:COG1012 156 ALAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 302 LYGKIQtgvvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGT 381
Cdd:COG1012 236 IAAAAA--------ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 382 LQQQKVTPVNTAASpisggdlhgFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGE-GWFVGPTIIKCKDPKHK 460
Cdd:COG1012 308 AKALKVGDPLDPGT---------DMGPLISEAQLERVLAYIEDAV-AEGAELLTGGRRPDGEgGYFVEPTVLADVTPDMR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 461 FMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAvVAQQWFGG 540
Cdd:COG1012 378 IAREEIFGPVLSVIPFDD--EEEAIALANDTE-YGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGG 451
|
490 500
....*....|....*....|....*....
gi 366986647 541 ARMSGTDDKSGGPSILnRFVSIRNTKENF 569
Cdd:COG1012 452 VKQSGIGREGGREGLE-EYTETKTVTIRL 479
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
35-569 |
1.12e-110 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 340.37 E-value: 1.12e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 35 KNEqvkPFTN-TDTKDWDLLRASIMKFKSS-SLEVPLVINGERIYYNNSNRSVfaqsNPACHKQVLANVTQATELDVKDA 112
Cdd:PRK03137 6 KHE---PFTDfSVEENVEAFEEALKKVEKElGQDYPLIIGGERITTEDKIVSI----NPANKSEVVGRVSKATKELAEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 113 IQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNLQP 192
Cdd:PRK03137 79 MQAALEAFETWKKWSPEDRARILLRAAAIIRRR-KHEFSAWLVKEAGKPWAEADAD-TAEAIDFLEYYARQMLKLADGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 193 VQSAQGVWNKAEYRPLeGFIYAVSPFNF-TAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVP 271
Cdd:PRK03137 157 VESRPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 272 GDPILVTDQLLASKEFGGLHFTGSTQVFKQLY---GKIQTGvvnglYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIR 348
Cdd:PRK03137 236 GSGSEVGDYLVDHPKTRFITFTGSREVGLRIYeraAKVQPG-----QIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 349 GAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAaspisggdlhgFMGPVIHEQSYNKLIKVIEEAKT 427
Cdd:PRK03137 311 SAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVgNPEDNA-----------YMGPVINQASFDKIMSYIEIGKE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 428 dpELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREA 507
Cdd:PRK03137 380 --EGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANNTE-YGLTGAVISNNREH 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366986647 508 INLADEklKFSCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIRNTKENF 569
Cdd:PRK03137 455 LEKARR--EFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
68-569 |
3.48e-103 |
|
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: 321.04 E-value: 3.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 68 PLVINGERIYYNNSNRSVfaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyR 147
Cdd:TIGR01237 34 PLVINGERVETENKIVSI----NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRR-R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 148 YDMLAATMLGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFT-AIAAN 226
Cdd:TIGR01237 109 HEFSALLVKEVGKPWNEADAE-VAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPT-GVTVVISPWNFPfAIMVG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 227 LIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLY--- 303
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFera 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 304 GKIQTGvvnglYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQ 383
Cdd:TIGR01237 267 AKVQPG-----QKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 384 QQKVTPVNTAASpisggdlhgFMGPVIHEQSYNKLIKVIEEAKTdpELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMT 463
Cdd:TIGR01237 342 SLKVGPPDSADV---------YVGPVIDQKSFNKIMEYIEIGKA--EGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 464 TEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREAINLAdeKLKFSCGNFYINDKCTGAVVAQQWFGGARM 543
Cdd:TIGR01237 411 EEIFGPVVAFIRASD--FDEALEIANNTE-YGLTGGVISNNRDHINRA--KAEFEVGNLYFNRNITGAIVGYQPFGGFKM 485
|
490 500
....*....|....*....|....*.
gi 366986647 544 SGTDDKSGGPSILNRFVSIRNTKENF 569
Cdd:TIGR01237 486 SGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
90-551 |
8.20e-103 |
|
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: 318.32 E-value: 8.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQAEID 168
Cdd:pfam00171 13 NPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLL--EERKDELAELEtLENGKPLAEARGE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 cITELSDFFRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSPFNF-TAIAANLIgAPALM-GNTVIWKPSQSA 246
Cdd:pfam00171 90 -VDRAIDVLRYYAGLARRLDG-ETLPSDPGRLAYTRREPL-GVVGAITPWNFpLLLPAWKI-APALAaGNTVVLKPSELT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 247 ALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYgKIQTgvvnglyRDYPRIVGETG 326
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIA-EAAA-------QNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 327 GKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisGGDLHG-- 404
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKV-----------GDPLDPdt 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 405 FMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYeypdnKFSET 484
Cdd:pfam00171 307 DMGPLISKAQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVI-----RFKDE 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 485 CDLIDQ--TSMYGLTGSVFAKD-REAINLADEklkFSCGNFYINDKCTGAVVAQQwFGGARMSGTDDKSG 551
Cdd:pfam00171 381 EEAIEIanDTEYGLAAGVFTSDlERALRVARR---LEAGMVWINDYTTGDADGLP-FGGFKQSGFGREGG 446
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
112-563 |
1.47e-92 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 291.03 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 112 AIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATM-LGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNL 190
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEE--RREELAALEtLETGKPIEEALGE-VARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 191 QPVQSAQGVWNKAEYRPLeGFIYAVSPFNFT-AIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINF 269
Cdd:cd07078 80 VIPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 270 VPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVVnglyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRG 349
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLK--------RVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 350 AFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisGGDLHG--FMGPVIHEQSYNKLIKVIEEAKt 427
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKV-----------GNPLDPdtDMGPLISAAQLDRVLAYIEDAK- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 428 DPELEIIYGGQYDKGE-GWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDRE 506
Cdd:cd07078 299 AEGAKLLCGGKRLEGGkGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKD--EEEAIELANDTE-YGLAAGVFTRDLE 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 507 -AINLADEklkFSCGNFYINDKcTGAVVAQQWFGGARMSGTdDKSGGPSILNRFVSIR 563
Cdd:cd07078 376 rALRVAER---LEAGTVWINDY-SVGAEPSAPFGGVKQSGI-GREGGPYGLEEYTEPK 428
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
49-563 |
1.17e-84 |
|
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: 272.92 E-value: 1.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 49 DWDLLRASIMKFKSSSLEV-PLVINGEriYYNNSNRSVFaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLP 127
Cdd:cd07125 15 PLEALADALKAFDEKEWEAiPIINGEE--TETGEGAPVI---DPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 128 FYDRAAVFLKAADLIStKYRYDMLAATMLGQGKNVyqaeIDCITELS---DFFRFnvkYAHDLYNLQPVQSAQGVW---N 201
Cdd:cd07125 90 VEERAEILEKAADLLE-ANRGELIALAAAEAGKTL----ADADAEVReaiDFCRY---YAAQARELFSDPELPGPTgelN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 202 KAEYRPLeGFIYAVSPFNF-TAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQ 280
Cdd:cd07125 162 GLELHGR-GVFVCISPWNFpLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 281 LLASKEFGGLHFTGSTQVFKQlygkIQTGVVNGLYRDYPrIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSA 360
Cdd:cd07125 241 LVAHPRIDGVIFTGSTETAKL----INRALAERDGPILP-LIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 361 TSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTdpELEIIYGGQYD 440
Cdd:cd07125 316 LRLLYLQEEIAERFIEMLKGAMASLKV------GDPW---DLSTDVGPLIDKPAGKLLRAHTELMRG--EAWLIAPAPLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 441 KGEGWFVGPTIIkcKDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCG 520
Cdd:cd07125 385 DGNGYFVAPGII--EIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDINATG-YGLTLGIHSRDEREIEYWRERVE--AG 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 366986647 521 NFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIR 563
Cdd:cd07125 460 NLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEK 502
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
114-563 |
2.34e-69 |
|
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: 228.27 E-value: 2.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 114 QAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNLQPV 193
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEER-REELAALETLETGKPIEEALGE-VARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 194 QSAQGVWNKAEYRPLeGFIYAVSPFNF-TAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPG 272
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 273 DPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQtgvvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFE 352
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA--------ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 353 FQGQKCSATSRLYIPQSKSEEFfrdligtlqqqkvtpvntaaspisggdlhgfmgpviheqsynklikvIEEAKtdpele 432
Cdd:cd06534 230 NAGQICTAASRLLVHESIYDEF-----------------------------------------------VEKLV------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 433 iiyggqydkgegwfvgpTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDRE-AINLA 511
Cdd:cd06534 257 -----------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKD--EEEAIALANDTE-YGLTAGVFTRDLNrALRVA 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 366986647 512 DEklkFSCGNFYINDKCTGaVVAQQWFGGARMSGTdDKSGGPSILNRFVSIR 563
Cdd:cd06534 317 ER---LRAGTVYINDSSIG-VGPEAPFGGVKNSGI-GREGGPYGLEEYTRTK 363
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
71-559 |
4.99e-59 |
|
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: 204.12 E-value: 4.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGEriYYNNSNRSVFAQSNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDM 150
Cdd:cd07131 3 IGGE--WVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELL--KKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 151 LAATMLGQ-GKNVYQAEIDcITELSDFFRFNVKYAHDLYNlQPVQSAqgVWNKAEY---RPLeGFIYAVSPFNF-TAIAA 225
Cdd:cd07131 79 LARLVTREmGKPLAEGRGD-VQEAIDMAQYAAGEGRRLFG-ETVPSE--LPNKDAMtrrQPI-GVVALITPWNFpVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 226 NLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYgk 305
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIG-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 306 iQTGVvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQ 385
Cdd:cd07131 232 -ETCA-----RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 386 KVTpvntaaspiSGGDLHGFMGPVIHEQSYNKLIKVIEEAKT-DPEL----EIIYGGQYDKgeGWFVGPTIIKCKDPKHK 460
Cdd:cd07131 306 RVG---------DGLDEETDMGPLINEAQLEKVLNYNEIGKEeGATLllggERLTGGGYEK--GYFVEPTVFTDVTPDMR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 461 FMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLkfSCGNFYINDKCTGAVVaQQWFGG 540
Cdd:cd07131 375 IAQEEIFGPVVALIEVSS--LEEAIEIANDTE-YGLSSAIYTEDVNKAFRARRDL--EAGITYVNAPTIGAEV-HLPFGG 448
|
490
....*....|....*....
gi 366986647 541 ARMSGTDDKSGGPSILNRF 559
Cdd:cd07131 449 VKKSGNGHREAGTTALDAF 467
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
70-504 |
1.34e-58 |
|
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: 202.86 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 70 VINGERIYYNNSNRSVfaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYD 149
Cdd:cd07097 4 YIDGEWVAGGDGEENR----NPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDEL--EARKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 150 MLAATM-LGQGKNVYQAeIDCITELSDFFRFnvkYAHDLYNLQ--PVQSA-QGVWNKAEYRPLeGFIYAVSPFNF-TAIA 224
Cdd:cd07097 78 ELARLLtREEGKTLPEA-RGEVTRAGQIFRY---YAGEALRLSgeTLPSTrPGVEVETTREPL-GVVGLITPWNFpIAIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 225 ANLIgAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLY 303
Cdd:cd07097 153 AWKI-APALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 304 GKIqtgVVNGLyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQ 383
Cdd:cd07097 232 AAA---AARGA-----RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 384 QQKVTpvntaaspisggdlHGF-----MGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKG--EGWFVGPTIIKCKD 456
Cdd:cd07097 304 ALKVG--------------DALdegvdIGPVVSERQLEKDLRYIEIARSE-GAKLVYGGERLKRpdEGYYLAPALFAGVT 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 366986647 457 PKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKD 504
Cdd:cd07097 369 NDMRIAREEIFGPVAAVIRVRD--YDEALAIANDTE-FGLSAGIVTTS 413
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
90-546 |
2.84e-58 |
|
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: 201.42 E-value: 2.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATMLGQ-GKNVYQAEID 168
Cdd:cd07145 5 NPA-NGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIER--RKEELAKLLTIEvGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 cITELSDFFRFNVKYAHDLYN-LQPVQSAQGVWNKAEY---RPLeGFIYAVSPFNFtaiAANLIG---APAL-MGNTVIW 240
Cdd:cd07145 82 -VERTIRLFKLAAEEAKVLRGeTIPVDAYEYNERRIAFtvrEPI-GVVGAITPFNF---PANLFAhkiAPAIaVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 241 KPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGK-IQTGvvnglyrdyP 319
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKaGGTG---------K 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 320 RIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAASpis 398
Cdd:cd07145 228 KVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVgDPLDESTD--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 399 ggdlhgfMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDkgEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07145 305 -------LGPLISPEAVERMENLVNDAVEKGG-KILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 366986647 479 NKfsETCDLIDQTSmYGLTGSVFAKD-REAINLADEkLKFscGNFYINDKCTgavvaQQW----FGGARMSGT 546
Cdd:cd07145 375 DE--EAVEIANSTE-YGLQASVFTNDiNRALKVARE-LEA--GGVVINDSTR-----FRWdnlpFGGFKKSGI 436
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
96-546 |
5.13e-56 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 195.51 E-value: 5.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQA--EID-CIt 171
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLL--EERREEFARTIaLEAGKPIKDArkEVDrAI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 172 elsDFFRFNVKYAHDLYNLQ-PVQSAQGVWNKAEY---RPLeGFIYAVSPFNFtaiAANLIG---APALM-GNTVIWKPS 243
Cdd:cd07149 87 ---ETLRLSAEEAKRLAGETiPFDASPGGEGRIGFtirEPI-GVVAAITPFNF---PLNLVAhkvGPAIAaGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 244 QSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygKIQTGVvnGLyrdyPRIVG 323
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGE----AIARKA--GL----KKVTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggDLH 403
Cdd:cd07149 230 ELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVV------GDPL---DED 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 404 GFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDkgeGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSE 483
Cdd:cd07149 301 TDVGPMISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDT--LDE 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 366986647 484 TCDLIDQtSMYGLTGSVFAKDREAINLADEKLKFscGNFYINDKCTgAVVAQQWFGGARMSGT 546
Cdd:cd07149 375 AIAMAND-SPYGLQAGVFTNDLQKALKAARELEV--GGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
90-563 |
1.78e-55 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 195.13 E-value: 1.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyrydMLAATMLG---QGKNVYQAe 166
Cdd:TIGR01238 57 NPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELH----MPELMALCvreAGKTIHNA- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 167 IDCITELSDFFRFnvkYAHDLYNLQPVQSAQGVwnkaeyrpleGFIYAVSPFNFT-AIAANLIGAPALMGNTVIWKPSQS 245
Cdd:TIGR01238 132 IAEVREAVDFCRY---YAKQVRDVLGEFSVESR----------GVFVCISPWNFPlAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 246 AALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygKIQTGVVNGLYRDYPrIVGET 325
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQ----LINQTLAQREDAPVP-LIAET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 326 GGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPisgGDLHGF 405
Cdd:TIGR01238 274 GGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKV------GVP---HLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 406 MGPVIHEQSYNKLIKVIE--EAKTDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHkfMTTEFFGPILSVYEYPDNKFSE 483
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEhmSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKARELDQ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 484 TCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVSIR 563
Cdd:TIGR01238 423 IVDQINQTG-YGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
71-551 |
1.21e-54 |
|
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: 192.09 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDM 150
Cdd:cd07088 2 INGE--FVPSSSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI--RENADE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 151 LAAT-MLGQGKNVYQA--EIDCITelsDFFRFNVKYAHDlYNLQPVQSAQGVWNKAEYRPLEGFIYAVSPFNFT-AIAAN 226
Cdd:cd07088 77 LAKLiVEEQGKTLSLArvEVEFTA---DYIDYMAEWARR-IEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 227 LIgAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGK 305
Cdd:cd07088 153 KL-APALVtGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 306 IQTGVVnglyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQ 385
Cdd:cd07088 232 AAENIT--------KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 386 KVTPVNTAASpisggdlhgFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGG-QYDKGEGWFVGPTIIKCKDPKHKFMTT 464
Cdd:cd07088 304 KVGDPFDAAT---------DMGPLVNEAALDKVEEMVERAVEAGA-TLLTGGkRPEGEKGYFYEPTVLTNVRQDMEIVQE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 465 EFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKDREAINLADEKLKFscGNFYINdkCTGAVVAQQWFGGAR 542
Cdd:cd07088 374 EIFGPVLPVV-----KFSSLDEAIELAndSEYGLTSYIYTENLNTAMRATNELEF--GETYIN--RENFEAMQGFHAGWK 444
|
490
....*....|..
gi 366986647 543 MSGT---DDKSG 551
Cdd:cd07088 445 KSGLggaDGKHG 456
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
90-561 |
4.84e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 195.47 E-value: 4.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADListkYRYDM---LAATMLGQGKNVYQAe 166
Cdd:PRK11905 573 NPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL----MEAHMpelFALAVREAGKTLANA- 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 167 IDCITELSDFFRFnvkYAhdlynlqpvQSAQGVWNKAEYRPLeGFIYAVSPFNFT-AIaanLIG--APALM-GNTVIWKP 242
Cdd:PRK11905 648 IAEVREAVDFLRY---YA---------AQARRLLNGPGHKPL-GPVVCISPWNFPlAI---FTGqiAAALVaGNTVLAKP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 243 SQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQlygkIQTGVVNGLYRDYPRIv 322
Cdd:PRK11905 712 AEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARL----IQRTLAKRSGPPVPLI- 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 323 GETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTpvNTAaspisggDL 402
Cdd:PRK11905 787 AETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIG--DPW-------RL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 403 HGFMGPVI----------HEQSYNKLIKVIEEAKTDPELEiiyggqydkgEGWFVGPTIIKCKDPKHkfMTTEFFGPILS 472
Cdd:PRK11905 858 STDVGPVIdaeaqanieaHIEAMRAAGRLVHQLPLPAETE----------KGTFVAPTLIEIDSISD--LEREVFGPVLH 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 473 VYEYPDNKFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGG 552
Cdd:PRK11905 926 VVRFKADELDRVIDDINATG-YGLTFGLHSRIDETIAHVTSRIR--AGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGG 1002
|
....*....
gi 366986647 553 PSILNRFVS 561
Cdd:PRK11905 1003 PLYLGRLVR 1011
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
90-545 |
5.89e-53 |
|
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: 186.87 E-value: 5.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHKqVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATM-LGQGKNVYQAEID 168
Cdd:cd07103 3 NPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRE--RAEDLARLLtLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 cITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFtaiAANLIG---APAL-MGNTVIWKPSQ 244
Cdd:cd07103 80 -VDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPV-GVVAAITPWNF---PAAMITrkiAPALaAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 245 SAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVVnglyrdypRIVGE 324
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK--------RVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 325 TGGknfH---LIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisgGD 401
Cdd:cd07103 227 LGG---NapfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKV------------GN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 lhGF-----MGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYey 476
Cdd:cd07103 292 --GLdegtdMGPLINERAVEKVEALVEDAVAK-GAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPII-- 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366986647 477 pdnKFSETCDLI---DQTSmYGLTGSVFAKD-REAINLAdEKLKFscGNFYINdkcTGAV-VAQQWFGGARMSG 545
Cdd:cd07103 367 ---PFDTEDEVIaraNDTP-YGLAAYVFTRDlARAWRVA-EALEA--GMVGIN---TGLIsDAEAPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
70-551 |
1.71e-52 |
|
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: 186.62 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 70 VINGEriyYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYD 149
Cdd:cd07086 2 VIGGE---WVGSGGETFTSRNPA-NGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEAL--RKKKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 150 MLAATM-LGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNL-----QPVQSAQGVWNkaeyrPLeGFIYAVSPFNF-TA 222
Cdd:cd07086 76 ALGRLVsLEMGKILPEGLGE-VQEMIDICDYAVGLSRMLYGLtipseRPGHRLMEQWN-----PL-GVVGVITAFNFpVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 223 IAA-NLigAPALM-GNTVIWKPSQSAALSNY----LLLTVLEEAGLPKGVINFV--PGDpilVTDQLLASKEFGGLHFTG 294
Cdd:cd07086 149 VPGwNA--AIALVcGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVtgGGD---GGELLVHDPRVPLVSFTG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 295 STQVFKQLYGKIQtgvvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEF 374
Cdd:cd07086 224 STEVGRRVGETVA--------RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 375 FRDLIGTLQQQKVtpvntaaspisgGD-LHG--FMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGG-QYDKGE-GWFVGP 449
Cdd:cd07086 296 LERLVKAYKQVRI------------GDpLDEgtLVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGkRIDGGEpGNYVEP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 450 TIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKFSCGNFYINDKCT 529
Cdd:cd07086 363 TIVTGVTDDARIVQEETFAPILYVIKFDS--LEEAIAINNDVP-QGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTS 439
|
490 500
....*....|....*....|..
gi 366986647 530 GAVVaQQWFGGARMSGTDDKSG 551
Cdd:cd07086 440 GAEI-GGAFGGEKETGGGRESG 460
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
108-559 |
4.30e-52 |
|
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: 184.27 E-value: 4.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 108 DVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATMLGQGKNVYQ-AEIDcITELSDFFRFNVKYAHd 186
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEIL--EERRDEIADWLIRESGSTRPkAAFE-VGAAIAILREAAGLPR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 187 LYNLQPVQSAQ-GVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSAALSNYLLLT-VLEEAGLP 263
Cdd:cd07104 77 RPEGEILPSDVpGKESMVRRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDSRTPVTGGLLIAeIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 264 KGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLygkiqtGVVNGlyRDYPRIVGETGGKNFHLIHKSANIPNAV 343
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI------GELAG--RHLKKVALELGGNNPLIVLDDADLDLAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 344 FSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisgGDLHG---FMGPVIHEQSYNKLIK 420
Cdd:cd07104 228 SAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPV------------GDPRDpdtVIGPLINERQVDRVHA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 421 VIEEAKTDpELEIIYGGQYDkgeGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYeypdnKFS---ETCDLIDQTSmYGLT 497
Cdd:cd07104 296 IVEDAVAA-GARLLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVI-----PFDddeEAVELANDTE-YGLS 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 498 GSVFAKDRE-AINLADeklKFSCGNFYINDKcT---GAVVAqqwFGGARMSGTdDKSGGPSILNRF 559
Cdd:cd07104 366 AAVFTRDLErAMAFAE---RLETGMVHINDQ-TvndEPHVP---FGGVKASGG-GRFGGPASLEEF 423
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
71-546 |
4.71e-52 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 185.34 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGERIYYNNSNRsvFAQSNPAChKQVLANVTQATELDVKDAIQAAKEA-KSKWYQLPFYDRAAVFLKAADLIStKYRYD 149
Cdd:cd07113 4 IDGRPVAGQSEKR--LDITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE-QHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 150 MLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLY--NLQP-VQSAQGvwnkAEY-----RPLEGFIYAVSPFNFT 221
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINgeTLAPsIPSMQG----ERYtaftrREPVGVVAGIVPWNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 222 A-IAANLIGAPALMGNTVIWKPSQSAALSnylLLTVLE---EAGLPKGVINFVPGDPiLVTDQLLASKEFGGLHFTGSTQ 297
Cdd:cd07113 156 VmIAVWKIGAALATGCTIVIKPSEFTPLT---LLRVAElakEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 298 VFKqlygKIQTGVVNGLyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRD 377
Cdd:cd07113 232 TGK----KIGRQAASDL----TRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 378 LIGTLQQQKVtpvntaASPISGGdlhGFMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKGEGWFVGPTIIKCKDP 457
Cdd:cd07113 304 LKQALSSFQV------GSPMDES---VMFGPLANQPHFDKVCSYLDDARAE-GDEIVRGGEALAGEGYFVQPTLVLARSA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 458 KHKFMTTEFFGPILSVYEYPDNKfsETCDLIDQTSmYGLTGSVFAKD-REAINLADeklKFSCGNFYINDKCTgaVVAQQ 536
Cdd:cd07113 374 DSRLMREETFGPVVSFVPYEDEE--ELIQLINDTP-FGLTASVWTNNlSKALRYIP---RIEAGTVWVNMHTF--LDPAV 445
|
490
....*....|
gi 366986647 537 WFGGARMSGT 546
Cdd:cd07113 446 PFGGMKQSGI 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
86-553 |
8.08e-52 |
|
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: 184.07 E-value: 8.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 86 FAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATMLGQGKNVYQA 165
Cdd:cd07150 1 FDDLNPA-DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIM--ERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 166 EIDCITELSDFFRFNVKYAHdLYNLQPVQS-AQGVWNKAEYRPLeGFIYAVSPFNF-TAIAANLIGAPALMGNTVIWKPS 243
Cdd:cd07150 78 AWFETTFTPELLRAAAGECR-RVRGETLPSdSPGTVSMSVRRPL-GVVAGITPFNYpLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 244 QSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQtgvvnglyRDYPRIVG 323
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG--------RHLKKITL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisgGDLH 403
Cdd:cd07150 228 ELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKV------------GDPR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 404 G---FMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDkgeGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNK 480
Cdd:cd07150 296 DpdtVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAE 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 481 fsETCDLIDQTSmYGLTGSVFAKDRE-AINLAdekLKFSCGNFYINDKC--TGAVVAqqwFGGARMSGTdDKSGGP 553
Cdd:cd07150 372 --EALELANDTE-YGLSAAILTNDLQrAFKLA---ERLESGMVHINDPTilDEAHVP---FGGVKASGF-GREGGE 437
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
45-561 |
2.40e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 190.53 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 45 TDTKDWDLLRASIMKFKSSSLEVPLVINGERIyyNNSNRSVFaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWY 124
Cdd:COG4230 536 SDEAVLAALSAALAAAAEKQWQAAPLIAGEAA--SGEARPVR---NPADHSDVVGTVVEATAADVEAALAAAQAAFPAWS 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 125 QLPFYDRAAVFLKAADLIsTKYRYDMLAATMLGQGKnVYQAEIDCITELSDFFRFnvkYAhdlynlqpVQSAQGVWNKAE 204
Cdd:COG4230 611 ATPVEERAAILERAADLL-EAHRAELMALLVREAGK-TLPDAIAEVREAVDFCRY---YA--------AQARRLFAAPTV 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 205 YRPLeGFIYAVSPFNFT-AIaanLIG--APALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQ 280
Cdd:COG4230 678 LRGR-GVFVCISPWNFPlAI---FTGqvAAALAaGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAA 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 281 LLASKEFGGLHFTGSTQVFKQlygkIQTGVVNglyRDYPRI--VGETGGKNfhlihksANIpnaVFST----------IR 348
Cdd:COG4230 754 LVADPRIAGVAFTGSTETARL----INRTLAA---RDGPIVplIAETGGQN-------AMI---VDSSalpeqvvddvLA 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 349 GAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPisgGDLHGFMGPVIHEQSYNKLIKVIEEAKTD 428
Cdd:COG4230 817 SAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRV------GDP---ADLSTDVGPVIDAEARANLEAHIERMRAE 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 429 PELeiIYGGQYDKG--EGWFVGPTIIKCKDPKHkfMTTEFFGPILSVYEYPDNKFSETCDLIDQTSmYGLTGSVFAKDRE 506
Cdd:COG4230 888 GRL--VHQLPLPEEcaNGTFVAPTLIEIDSISD--LEREVFGPVLHVVRYKADELDKVIDAINATG-YGLTLGVHSRIDE 962
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 366986647 507 AINLADEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFVS 561
Cdd:COG4230 963 TIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFAT 1015
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
90-545 |
1.66e-50 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 180.42 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAA-TMLGQGKNVYQAEID 168
Cdd:cd07106 3 NPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEA--NAEELARlLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 CITELsDFFRFNVKYAhdlynLQP--VQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQS 245
Cdd:cd07106 80 VGGAV-AWLRYTASLD-----LPDevIEDDDTRRVELRRKPL-GVVAAIVPWNFPLLLAAWKIAPALLaGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 246 AALSNYLLLTVLEEAgLPKGVINFVPGD----PILVtdqllASKEFGGLHFTGSTQVFKqlygKIQTGVVNGLyrdyPRI 321
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSGGdelgPALT-----SHPDIRKISFTGSTATGK----KVMASAAKTL----KRV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VGETGGKNFHLIHKSANIP---NAVFStirGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPvntaaspis 398
Cdd:cd07106 219 TLELGGNDAAIVLPDVDIDavaPKLFW---GAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGD--------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 399 GGDLHGFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07106 287 GLDPGTTLGPVQNKMQYDKVKELVEDAK-AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSD 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 479 nkFSETCDLIDQTSmYGLTGSVFAKDRE-AINLADeklKFSCGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:cd07106 366 --EDEVIARANDSE-YGLGASVWSSDLErAEAVAR---RLEAGTVWIN--THGALDPDAPFGGHKQSG 425
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
69-545 |
4.05e-49 |
|
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: 177.40 E-value: 4.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLISTKY 146
Cdd:cd07091 6 LFINNE--FVDSVSGKTFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 ryDMLAA-TMLGQGKNVYQAEIDCITELSDFFRFNVKYAhDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAA 225
Cdd:cd07091 83 --DELAAlESLDNGKPLEESAKGDVALSIKCLRYYAGWA-DKIQGKTIPIDGNFLAYTRREPI-GVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 226 NLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYg 304
Cdd:cd07091 159 AWKLAPALaAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 305 kiQTGVVNGLyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQ 384
Cdd:cd07091 238 --EAAAKSNL----KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 385 QKVTPVNTAASpisggdlhgFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTT 464
Cdd:cd07091 312 RVVGDPFDPDT---------FQGPQVSKAQFDKILSYIESGK-KEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 465 EFFGPILSVYeypdnKFSETCDLIDQ--TSMYGLTGSVFAKD-REAINLADeKLKfsCGNFYINdkCTGAVVAQQWFGGA 541
Cdd:cd07091 382 EIFGPVVTIL-----KFKTEDEVIERanDTEYGLAAGVFTKDiNKALRVSR-ALK--AGTVWVN--TYNVFDAAVPFGGF 451
|
....
gi 366986647 542 RMSG 545
Cdd:cd07091 452 KQSG 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
71-545 |
6.18e-49 |
|
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: 176.73 E-value: 6.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGERIyyNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLISTKYry 148
Cdd:cd07119 2 IDGEWV--EAASGKTRDIINPA-NGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLAA-TMLGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANL 227
Cdd:cd07119 77 EELARlETLNTGKTLRESEID-IDDVANCFRYYAGLATKETG-EVYDVPPHVISRTVREPV-GVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 228 IGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLygkI 306
Cdd:cd07119 154 KLAPALAaGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSI---M 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 307 QTGVVNglyrdYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQK 386
Cdd:cd07119 231 RAAAGN-----VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 387 VTPvntaaspisGGDLHGFMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKG----EGWFVGPTIIKCKDPKHKFM 462
Cdd:cd07119 306 LGN---------GLDADTEMGPLVSAEHREKVLSYIQLGKEE-GARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 463 TTEFFGPILSVYEYPDNKfsETCDLIDQTsMYGLTGSVFAKDREAINLADEKLKFscGNFYINDkcTGAVVAQQWFGGAR 542
Cdd:cd07119 376 QEEIFGPVLTVERFDTEE--EAIRLANDT-PYGLAGAVWTKDIARANRVARRLRA--GTVWIND--YHPYFAEAPWGGYK 448
|
...
gi 366986647 543 MSG 545
Cdd:cd07119 449 QSG 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
90-545 |
1.10e-48 |
|
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: 175.57 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAA-TMLGQGKNVYQAEID 168
Cdd:cd07090 3 EPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRE--RNDEIARlETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 CITElSDFFRFNVKYAHDLyNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQSAA 247
Cdd:cd07090 80 IDSS-ADCLEYYAGLAPTL-SGEHVPLPGGSFAYTRREPL-GVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 248 LSNYLLLTVLEEAGLPKGVINFVPGDPilVTDQLLASK-EFGGLHFTGSTQVFKqlygKIQTGVVNGLyrdyPRIVGETG 326
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGG--ETGQLLCEHpDVAKVSFTGSVPTGK----KVMSAAAKGI----KHVTLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 327 GKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisgGDL---H 403
Cdd:cd07090 227 GKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRI------------GDPldeD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 404 GFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGE-----GWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07090 295 TQMGALISEEHLEKVLGYIESAKQEGA-KVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDT 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 479 NKfsETCDLIDQTSmYGLTGSVFAKDreaINLAD---EKLKfsCGNFYINDkcTGAVVAQQWFGGARMSG 545
Cdd:cd07090 374 EE--EVIRRANDTT-YGLAAGVFTRD---LQRAHrviAQLQ--AGTCWINT--YNISPVEVPFGGYKQSG 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
45-560 |
1.19e-48 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 182.32 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 45 TDTKDWDLLRASIMKFKSSSLEVPLVINGeriyyNNSNRSVFaqsNPACHKQVLANVTQATELDVKDAIQAAKEAKSKWY 124
Cdd:PRK11904 531 NDRSELEPLAAAIAAFLEKQWQAGPIING-----EGEARPVV---SPADRRRVVGEVAFADAEQVEQALAAARAAFPAWS 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 125 QLPFYDRAAVFLKAADLIstKYRYDMLAAtmLGQ---GKNVyqaeIDCITELS---DFFRFnvkYAH----DLYNLQPVQ 194
Cdd:PRK11904 603 RTPVEERAAILERAADLL--EANRAELIA--LCVreaGKTL----QDAIAEVReavDFCRY---YAAqarrLFGAPEKLP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 195 SAQGVWNkaEYRpLEG---FIyAVSPFNFT-AIAANLIGApALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINF 269
Cdd:PRK11904 672 GPTGESN--ELR-LHGrgvFV-CISPWNFPlAIFLGQVAA-ALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQL 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 270 VPGDPILVTDQLLASKEFGGLHFTGSTQVFKQlygkIQTGVVNglyRDYPRI--VGETGGKNFHLIHKSANIPNAVFSTI 347
Cdd:PRK11904 747 LPGDGATVGAALTADPRIAGVAFTGSTETARI----INRTLAA---RDGPIVplIAETGGQNAMIVDSTALPEQVVDDVV 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 348 RGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisgGD--LHGF-MGPVIHEQSYNKLIKVIEE 424
Cdd:PRK11904 820 TSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKV------------GDprLLSTdVGPVIDAEAKANLDAHIER 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 425 AKTdpELEIIYGGQYDKG--EGWFVGPTIIKCKDPKhkFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSmYGLTGSVFA 502
Cdd:PRK11904 888 MKR--EARLLAQLPLPAGteNGHFVAPTAFEIDSIS--QLEREVFGPILHVIRYKASDLDKVIDAINATG-YGLTLGIHS 962
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 503 KDREAINLADEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRFV 560
Cdd:PRK11904 963 RIEETADRIADRVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFA 1018
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
96-546 |
9.32e-48 |
|
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: 173.13 E-value: 9.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAAT-MLGQGKNVYQAEIDCITELS 174
Cdd:cd07093 8 EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLI--EARADELALLeSLDTGKPITLARTRDIPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 175 DFFRFNVKYAHDLYNLQpVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSAALSNYLL 253
Cdd:cd07093 86 ANFRFFADYILQLDGES-YPQDGGALNYVLRQPV-GVAGLITPWNLPLMLLTWKIAPALaFGNTVVLKPSEWTPLTAWLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 254 LTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygKIQTGVVNGLyrdyPRIVGETGGKNFHLI 333
Cdd:cd07093 164 AELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGR----TIMRAAAPNL----KPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 334 HKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLigtlqqqkvtpVNTAASPISG--GDLHGFMGPVIH 411
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERF-----------VERAKALKVGdpLDPDTEVGPLIS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 412 EQSYNKLIKVIEEAKTDpELEIIYGG----QYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVyeypdNKFSETCDL 487
Cdd:cd07093 305 KEHLEKVLGYVELARAE-GATILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTV-----IPFDDEEEA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 488 IDQT--SMYGLTGSVFAKD-REAINLADeklKFSCGNFYINDkctgavvaqqW--------FGGARMSGT 546
Cdd:cd07093 379 IELAndTPYGLAAYVWTRDlGRAHRVAR---RLEAGTVWVNC----------WlvrdlrtpFGGVKASGI 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
85-550 |
4.09e-47 |
|
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: 171.25 E-value: 4.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 85 VFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLIStKYRyDMLAAT-MLGQGKN 161
Cdd:cd07112 3 TFATINPA-TGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE-AHR-DELALLeTLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 162 VYQAEIDCITELSDFFRFNVKYAHDLY-NLQPVQS-AQGVWNKAeyrPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTV 238
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYgEVAPTGPdALALITRE---PL-GVVGAVVPWNFPLLMAAWKIAPALaAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 239 IWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLlaskefgGLH-------FTGSTQVFKQL--YgkiqTG 309
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEAL-------GLHmdvdalaFTGSTEVGRRFleY----SG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 310 VVNGlyrdyPRIVGETGGKNFHLI-HKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVt 388
Cdd:cd07112 225 QSNL-----KRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKP- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 389 pvntaASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQ--YDKGEGWFVGPTIIKCKDPKHKFMTTEF 466
Cdd:cd07112 299 -----GDPL---DPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 467 FGPILSVYEYpdNKFSETCDLIDQTsMYGLTGSVFAKD-REAINLADEkLKfsCGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:cd07112 370 FGPVLSVITF--DSEEEAVALANDS-VYGLAASVWTSDlSRAHRVARR-LR--AGTVWVN--CFDEGDITTPFGGFKQSG 441
|
....*.
gi 366986647 546 TD-DKS 550
Cdd:cd07112 442 NGrDKS 447
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
90-545 |
7.99e-47 |
|
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: 170.62 E-value: 7.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATM-LGQGKNV-YQAEI 167
Cdd:cd07108 3 NPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLaLETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 168 DCITeLSDFFRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSA 246
Cdd:cd07108 80 EAAV-LADLFRYFGGLAGELKG-ETLPFGPDVLTYTVREPL-GVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 247 ALSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQtgvvnglyrdyPRIVG--- 323
Cdd:cd07108 157 PLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-----------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ETGGKNFHLIHKSANIPNAVFSTIRGA-FEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAASpisggd 401
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIgDPLDEATD------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 lhgfMGPVIHEQSYNKLIKVIEEAKTDPELEIIYGG----QYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYeyp 477
Cdd:cd07108 299 ----IGAIISEKQFAKVCGYIDLGLSTSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAI--- 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366986647 478 dnKFSETCDLIDQT--SMYGLTGSVFAKD-REAINLADEklkFSCGNFYINDkcTGAVVAQQWFGGARMSG 545
Cdd:cd07108 372 --PWKDEDEVIAMAndSHYGLAAYVWTRDlGRALRAAHA---LEAGWVQVNQ--GGGQQPGQSYGGFKQSG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
90-545 |
1.02e-46 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 170.31 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIStKYRYDMLAATMLGQGKNVYQAEIDC 169
Cdd:cd07115 3 NPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELIL-ANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 170 ITELSDFFRFNVKYAHDLY-NLQPVQSaqGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSAA 247
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEgEVIPVRG--PFLNYTVREPV-GVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 248 LSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygkiqtGVVNGLYRDYPRIVGETGG 327
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGR--------KIMQGAAGNLKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 328 KNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLigtlqqqkvtpVNTAASPISGGDLHGF-- 405
Cdd:cd07115 230 KSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERF-----------TSLARSLRPGDPLDPKtq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 406 MGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKfsETC 485
Cdd:cd07115 299 MGPLVSQAQFDRVLDYVDVGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE--EAL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 486 DLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:cd07115 376 RIANGTE-YGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
69-545 |
1.13e-46 |
|
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: 170.67 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA-KSKWYQLPFYDRAAVFLKAADLIStKYR 147
Cdd:cd07144 10 LFINNE--FVKSSDGETIKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVE-KNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 148 yDMLAAT-MLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNlqpvQSAQGVWNKAEY---RPLeGFIYAVSPFNFT-A 222
Cdd:cd07144 86 -DLLAAIeALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQG----KTIPTSPNKLAYtlhEPY-GVCGQIIPWNYPlA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 223 IAANLIgAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVfkq 301
Cdd:cd07144 160 MAAWKL-APALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 302 lyGKIQTGVVNGLYRDyprIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGT 381
Cdd:cd07144 236 --GRLVMKAAAQNLKA---VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 382 lqqqkvtpVNTAASPISGGDLHGFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDK---GEGWFVGPTIIKCKDPK 458
Cdd:cd07144 311 --------VKQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEKAPeglGKGYFIPPTIFTDVPQD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 459 HKFMTTEFFGPILSVyeypdNKFS---ETCDLIDQTSmYGLTGSVFAKD-REAINLADEklkFSCGNFYIN---DKCTGA 531
Cdd:cd07144 382 MRIVKEEIFGPVVVI-----SKFKtyeEAIKKANDTT-YGLAAAVFTKDiRRAHRVARE---LEAGMVWINssnDSDVGV 452
|
490
....*....|....
gi 366986647 532 VvaqqwFGGARMSG 545
Cdd:cd07144 453 P-----FGGFKMSG 461
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
90-563 |
1.48e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 176.32 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRydmlaaTMLG-----QGKNVYQ 164
Cdd:PRK11809 665 NPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQ------TLMGllvreAGKTFSN 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 165 AeIDCITELSDFFRFnvkYAhdlynlqpVQSAQGVWNKAeYRPLeGFIYAVSPFNFT-AIAANLIGAPALMGNTVIWKPS 243
Cdd:PRK11809 739 A-IAEVREAVDFLRY---YA--------GQVRDDFDNDT-HRPL-GPVVCISPWNFPlAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 244 QSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIqTGVVNGLYRDYPRIvG 323
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNL-AGRLDPQGRPIPLI-A 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPisgGDLH 403
Cdd:PRK11809 883 ETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRM------GNP---DRLS 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 404 GFMGPVIHEQSYNKLIKVIE--EAKTDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHkfMTTEFFGPILSVYEYPDNKF 481
Cdd:PRK11809 954 TDIGPVIDAEAKANIERHIQamRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYNRNQL 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 482 SEtcdLIDQ--TSMYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSILNRF 559
Cdd:PRK11809 1032 DE---LIEQinASGYGLTLGVHTRIDETIAQVTGSAH--VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL 1106
|
....
gi 366986647 560 VSIR 563
Cdd:PRK11809 1107 LATR 1110
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
71-528 |
4.28e-46 |
|
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: 168.90 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGERIYYNNSNRSVfaqSNPACHkQVLANVTQATELDVKDAIQAAKEA-KSKWYQLPFYDRAAVFLKAADLIStKYRYD 149
Cdd:cd07082 6 INGEWKESSGKTIEV---YSPIDG-EVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 150 MLAATMLGQGKnvyqAEIDCITELS---DFFRFNVKYAHDLYNlqpvQSAQGVWNK------AEYR--PLeGFIYAVSPF 218
Cdd:cd07082 81 VANLLMWEIGK----TLKDALKEVDrtiDYIRDTIEELKRLDG----DSLPGDWFPgtkgkiAQVRrePL-GVVLAIGPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 219 NFTA-IAANLIgAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGST 296
Cdd:cd07082 152 NYPLnLTVSKL-IPALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 297 QVFKQLygKIQTGVVnglyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFR 376
Cdd:cd07082 231 EVGNRL--KKQHPMK--------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 377 DLIGTLQQQKV-TPVNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEgwFVGPTIIKCK 455
Cdd:cd07082 301 LLKEEVAKLKVgMPWDNGVD----------ITPLIDPKSADFVEGLIDDAVAKGA-TVLNGGGREGGN--LIYPTLLDPV 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366986647 456 DPKHKFMTTEFFGPILSVYEYpdNKFSETCDLIDQtSMYGLTGSVFAKD-REAINLADeklKFSCGNFYINDKC 528
Cdd:cd07082 368 TPDMRLAWEEPFGPVLPIIRV--NDIEEAIELANK-SNYGLQASIFTKDiNKARKLAD---ALEVGTVNINSKC 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
108-545 |
3.92e-45 |
|
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: 165.44 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 108 DVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATMlgqgknvyQAEIDCiTELsdFFRFNVKYAHDL 187
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLL--ESRRDEFIEAM--------MEETGA-TAA--WAGFNVDLAAGM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 188 Y------------NLQPvQSAQGVWNKAEYRPLeGFIYAVSPFNFTAI-AANLIGAPALMGNTVIWKPSQSAALSNYLLL 254
Cdd:cd07105 68 LreaaslitqiigGSIP-SDKPGTLAMVVKEPV-GVVLGIAPWNAPVIlGTRAIAYPLAAGNTVVLKASELSPRTHWLIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 255 TVLEEAGLPKGVINFV---PGDPILVTDQLLASKEFGGLHFTGSTQVfkqlyGkiqtgvvnglyrdypRIVGET------ 325
Cdd:cd07105 146 RVFHEAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRV-----G---------------RIIAETaakhlk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 326 ------GGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQqkvtpvntaaspISG 399
Cdd:cd07105 206 pvllelGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEK------------LFA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 400 GDLHGfmGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGE-GWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07105 274 GPVVL--GSLVSAAAADRVKELVDDA-LSKGAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKD 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366986647 479 NkfSETCDLIDQTSmYGLTGSVFAKD-REAINLADeklKFSCGNFYINdkctGAVV---AQQWFGGARMSG 545
Cdd:cd07105 351 E--EEAVRIANDSE-YGLSAAVFTRDlARALAVAK---RIESGAVHIN----GMTVhdePTLPHGGVKSSG 411
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-559 |
5.92e-45 |
|
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: 165.16 E-value: 5.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIsTKYRYDMLAATMLGQGKNVYQAEIDCITELSD 175
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLL-EEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 176 FFRFNVKYAHDLYNLQPvqSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPS-QSAALSNYLL 253
Cdd:cd07152 81 LHEAAGLPTQPQGEILP--SAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 254 LTVLEEAGLPKGVINFVPGDP----ILVTDQLLASkefggLHFTGSTQVFKQLygkiqtGVVNGlyRDYPRIVGETGGKN 329
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGAdageALVEDPNVAM-----ISFTGSTAVGRKV------GEAAG--RHLKKVSLELGGKN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 330 FHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIgtlQQQKVTPVNTAASpisgGDLHgfMGPV 409
Cdd:cd07152 225 ALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLA---AKAKHLPVGDPAT----GQVA--LGPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 410 IHEQSYNKLIKVIEEAkTDPELEIIYGGQYDkgeGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNkfSETCDLID 489
Cdd:cd07152 296 INARQLDRVHAIVDDS-VAAGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALAN 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366986647 490 QTSmYGLTGSVFAKDRE-AINLADeklKFSCGNFYINDKcTGAVVAQQWFGGARMSGTDDKSGGPSILNRF 559
Cdd:cd07152 370 DTE-YGLSAGIISRDVGrAMALAD---RLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGPANWEEF 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
67-473 |
8.68e-45 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 165.38 E-value: 8.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 67 VPLVINGERIyyNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKY 146
Cdd:cd07085 1 LKLFINGEWV--ESKTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLL--EE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 RYDMLAATM-LGQGKNVYQAEidcitelSDFFRF--NVKYAHDLYNLQP----VQSAQGVWNKAEYRPLeGFIYAVSPFN 219
Cdd:cd07085 76 NLDELARLItLEHGKTLADAR-------GDVLRGleVVEFACSIPHLLKgeylENVARGIDTYSYRQPL-GVVAGITPFN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 220 FTAIAANLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVtDQLLASKEFGGLHFTGSTQV 298
Cdd:cd07085 148 FPAMIPLWMFPMAIaCGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 299 FKQLYgkiQTGVVNGlyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDL 378
Cdd:cd07085 227 GEYIY---ERAAANG-----KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 379 IGTLQQQKVTPvntaaspisgGDLHGF-MGPVIHEQSYNKLIKVIEEAKTD-------------PELEiiyggqydkgEG 444
Cdd:cd07085 299 VERAKKLKVGA----------GDDPGAdMGPVISPAAKERIEGLIESGVEEgaklvldgrgvkvPGYE----------NG 358
|
410 420
....*....|....*....|....*....
gi 366986647 445 WFVGPTIIKCKDPKHKFMTTEFFGPILSV 473
Cdd:cd07085 359 NFVGPTILDNVTPDMKIYKEEIFGPVLSI 387
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
90-504 |
1.82e-44 |
|
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: 163.88 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAAT-----------ML 156
Cdd:cd07114 3 NPA-TGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEA--NAEELAELetrdngklireTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 157 GQgknvyqaeidcITELSDFFRFnvkYAHDLYNLQ----PVQsAQGVWNKAEYRPLeGFIYAVSPFNFT-AIAANLIgAP 231
Cdd:cd07114 80 AQ-----------VRYLAEWYRY---YAGLADKIEgaviPVD-KGDYLNFTRREPL-GVVAAITPWNSPlLLLAKKL-AP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 232 AL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGkiQTGv 310
Cdd:cd07114 143 ALaAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIAR--AAA- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 311 vnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TP 389
Cdd:cd07114 220 -----ENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVgDP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 390 VNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQ----YDKGEGWFVGPTIIKCKDPKHKFMTTE 465
Cdd:cd07114 295 LDPETQ----------MGPLATERQLEKVERYVARAREE-GARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEE 363
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 366986647 466 FFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKD 504
Cdd:cd07114 364 VFGPVLSVI-----PFDDEEEAIALAndSEYGLAAGIWTRD 399
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
89-547 |
2.28e-44 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 163.70 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 89 SNPaCHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATMLGQGKNVYQAEID 168
Cdd:cd07107 2 INP-ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRL--REHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 CITELSDFFRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAI-AANLIGAPALMGNTVIWKPSQSAA 247
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKG-ETIPVGGRNLHYTLREPY-GVVARIVAFNHPLMfAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 248 LSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygKIQTGVVNGLyrdyPRIVGETGG 327
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGR----AIMRAAAEGI----KHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 328 KNFHLIHKSANIPNAVFSTIRGA-FEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNTAASPisggdlhgfM 406
Cdd:cd07107 228 KNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATT---------M 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 407 GPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGE----GWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFS 482
Cdd:cd07107 299 GPLVSRQQYDRVMHYIDSAKREGA-RLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 483 ETCDLIDQTSmYGLTGSVFAKD-REAINLADEklkFSCGNFYINDKCTGAVVAQqwFGGARMSGTD 547
Cdd:cd07107 376 EMVAQANGVE-YGLTAAIWTNDiSQAHRTARR---VEAGYVWINGSSRHFLGAP--FGGVKNSGIG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
90-563 |
2.75e-44 |
|
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: 163.68 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIsTKYRYDMLAATMLGQGKNVYQAEIDc 169
Cdd:cd07110 3 NPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGV-RERREELAELEARDNGKPLDEAAWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 170 ITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLE--GFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQSA 246
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREpvGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 247 ALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQlygkiqtgVVNGLYRDYPRIVGETG 326
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQ--------VMQAAAQDIKPVSLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 327 GKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPISGGDLhgfM 406
Cdd:cd07110 232 GKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRV------GDPLEEGVR---L 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 407 GPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQY--DKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVyeypdNKFSET 484
Cdd:cd07110 303 GPLVSQAQYEKVLSFIARGKEE-GARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCV-----RSFATE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 485 CDLIDQT--SMYGLTGSVFAKDREAINLADEKLKfsCGNFYINdkCTGAVVAQQWFGGARMSGTdDKSGGPSILNRFVSI 562
Cdd:cd07110 377 DEAIALAndSEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSGI-GRELGEWGLDNYLEV 451
|
.
gi 366986647 563 R 563
Cdd:cd07110 452 K 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
69-545 |
4.27e-44 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 163.39 E-value: 4.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRY 148
Cdd:cd07117 3 LFINGE--WVKGSSGETIDSYNPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLAATMlGQGKNVYQAEIDCITELSDFFRfnvkyahdlYNLQPVQSAQGVWNKAEYRPLE-------GFIYAVSPFNFT 221
Cdd:cd07117 80 LAMVETL-DNGKPIRETRAVDIPLAADHFR---------YFAGVIRAEEGSANMIDEDTLSivlrepiGVVGQIIPWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 222 AIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFK 300
Cdd:cd07117 150 FLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 301 QLygkiqtgVVNGLYRDYPRIVgETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIG 380
Cdd:cd07117 229 DV-------AIAAAKKLIPATL-ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 381 TLQQQKV-TPVNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQ------YDKGEgwFVGPTIIK 453
Cdd:cd07117 301 KFENVKVgNPLDPDTQ----------MGAQVNKDQLDKILSYVDIAKEE-GAKILTGGHrltengLDKGF--FIEPTLIV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 454 CKDPKHKFMTTEFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKD-REAINLADEklkFSCGNFYINdkCTG 530
Cdd:cd07117 368 NVTNDMRVAQEEIFGPVATVI-----KFKTEDEVIDMAndSEYGLGGGVFTKDiNRALRVARA---VETGRVWVN--TYN 437
|
490
....*....|....*
gi 366986647 531 AVVAQQWFGGARMSG 545
Cdd:cd07117 438 QIPAGAPFGGYKKSG 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
96-545 |
1.75e-43 |
|
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: 161.06 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQA--EID-CIt 171
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLL--KKRAEEFAKIIaCEGGKPIKDArvEVDrAI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 172 elsDFFRFNVKYAHDLY------NLQPVQSAQGVWNKAEyrPLeGFIYAVSPFNFtaiAANLIG---APAL-MGNTVIWK 241
Cdd:cd07094 87 ---DTLRLAAEEAERIRgeeiplDATQGSDNRLAWTIRE--PV-GVVLAITPFNF---PLNLVAhklAPAIaTGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 242 PSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLygKIQTGVvnglyrdyPRI 321
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGG--------KRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaaspisGGD 401
Cdd:cd07094 228 ALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKV-----------GDP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 LHG--FMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGqydKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDn 479
Cdd:cd07094 297 LDEdtDVGPLISEEAAERVERWVEEAVEAGA-RLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDD- 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 480 kFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKFscGNFYINDkctGAVVAQQW--FGGARMSG 545
Cdd:cd07094 372 -FEEAIRIANSTD-YGLQAGIFTRDLNVAFKAAEKLEV--GGVMVND---SSAFRTDWmpFGGVKESG 432
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
108-551 |
2.78e-42 |
|
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: 157.43 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 108 DVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATM-LGQGKNVYQAEidciTELSDF---FRFNVKY 183
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKA--NKEELARLIsRETGKPLWEAQ----TEVAAMagkIDISIKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 184 AHDLYNLQPVQSAQG---VWnkaeYRPLeGFIYAVSPFNFTAIAANliGA--PALM-GNTVIWKPSQSAALSNYLLLTVL 257
Cdd:cd07095 75 YHERTGERATPMAQGravLR----HRPH-GVMAVFGPFNFPGHLPN--GHivPALLaGNTVVFKPSELTPAVAELMVELW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 258 EEAGLPKGVINFVPGDPIlVTDQLLASKEFGGLHFTGSTQVFKQLYGKI--QTGVVNGLyrdyprivgETGGKNFHLIHK 335
Cdd:cd07095 148 EEAGLPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFagRPGKILAL---------EMGGNNPLVVWD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 336 SANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQS-KSEEFFRDLIGTLQQQKVTPVNtaASPIsggdlhgFMGPVIHEQS 414
Cdd:cd07095 218 VADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPD--AEPP-------FMGPLIIAAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 415 YNKLIKVIEEAKTDPELEIIYGGQYDKGEGwFVGPTII---KCKDPKHKfmttEFFGPILSVYEYPDnkFSETCDLIDQT 491
Cdd:cd07095 289 AARYLLAQQDLLALGGEPLLAMERLVAGTA-FLSPGIIdvtDAADVPDE----EIFGPLLQVYRYDD--FDEAIALANAT 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 492 SmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAVVAQQwFGGARMSGTDDKSG 551
Cdd:cd07095 362 R-FGLSAGLLSDDEALFERFLARIR--AGIVNWNRPTTGASSTAP-FGGVGLSGNHRPSA 417
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
69-557 |
2.80e-42 |
|
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: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLIStKY 146
Cdd:cd07142 6 LFINGQ--FVDAASGKTFPTIDPR-NGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLE-KH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 RYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNLQ-PVQSAQGVWNKAEyrPLeGFIYAVSPFNFTAIAA 225
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTlPADGPHHVYTLHE--PI-GVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 226 NLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFK---Q 301
Cdd:cd07142 159 AWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKiimQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 302 LYGKIQTGVVNglyrdyprivGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGT 381
Cdd:cd07142 239 LAAKSNLKPVT----------LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 382 LQQQKVtpvntaASPISGGDLHgfmGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKF 461
Cdd:cd07142 309 ALKRVV------GDPFRKGVEQ---GPQVDKEQFEKILSYIEHGK-EEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 462 MTTEFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKDREAINLADEKLKfsCGNFYINdkCTGAVVAQQWFG 539
Cdd:cd07142 379 ARDEIFGPVQSIL-----KFKTVDEVIKRAnnSKYGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYDVFDASIPFG 449
|
490
....*....|....*...
gi 366986647 540 GARMSGTDDKSGGPSILN 557
Cdd:cd07142 450 GYKMSGIGREKGIYALNN 467
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
96-545 |
4.96e-42 |
|
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: 157.02 E-value: 4.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQAEIDcITELS 174
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARL--EERFEELAETIvLEAGKPIKDARGE-VARAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 175 DFFRFNVKYAHDLY----NLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFtaiAANLIG---APAL-MGNTVIWKPSQSA 246
Cdd:cd07147 87 DTFRIAAEEATRIYgevlPLDISARGEGRQGLVRRFPI-GPVSAITPFNF---PLNLVAhkvAPAIaAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 247 ALSNYLLLTVLEEAGLPKGVINFVP----GDPILVTDqllasKEFGGLHFTGSTQV---FKQLYGKiqtgvvnglyrdyP 319
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPcsrdDADLLVTD-----ERIKLLSFTGSPAVgwdLKARAGK-------------K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 320 RIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNTAASpisg 399
Cdd:cd07147 225 KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDAT---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 400 gdlhgFMGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGqydKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDn 479
Cdd:cd07147 301 -----DVGPMISESEAERVEGWVNEA-VDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDD- 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 480 kFSETCDLIDQtSMYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAvVAQQWFGGARMSG 545
Cdd:cd07147 371 -FDEALAAVND-SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
91-545 |
7.12e-42 |
|
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: 156.73 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 91 PAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQA--E 166
Cdd:cd07118 4 PA-HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRAR-RERLALIETLESGKPISQArgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 167 IDCITELsdfFRFNVKYAHDLY-----NLQPVQSAQGVwnkaeyRPLEGFIYAVSPFNFT----------AIAAnligap 231
Cdd:cd07118 82 IEGAADL---WRYAASLARTLHgdsynNLGDDMLGLVL------REPIGVVGIITPWNFPflilsqklpfALAA------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 232 almGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVfkqlyGKiqtGVV 311
Cdd:cd07118 147 ---GCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRV-----GK---AIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 312 NGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPV 390
Cdd:cd07118 216 AAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVgDPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 391 NTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPI 470
Cdd:cd07118 296 DPETK----------VGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPV 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 366986647 471 LSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAvvAQQWFGGARMSG 545
Cdd:cd07118 366 LSVLTFDT--VDEAIALANDTV-YGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGS--PELPFGGFKQSG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
96-564 |
2.28e-41 |
|
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: 155.54 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIsTKYRYDMLAATMLGQGKNVYQAeIDCITELSD 175
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLV-LERRDELLDLIQLETGKARRHA-FEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 176 FFRFNVKYAHDLYNLQPVQSAQGVWNKAE--YRPLeGFIYAVSPFNF--TAIAANLIgaPALM-GNTVIWKPSQSAALSN 250
Cdd:cd07101 85 VARYYARRAERLLKPRRRRGAIPVLTRTTvnRRPK-GVVGVISPWNYplTLAVSDAI--PALLaGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 251 YLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFggLHFTGSTQvfkqlygkiqTGVVNGlYRDYPRIVG---ETGG 327
Cdd:cd07101 162 LWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTA----------TGRVVA-ERAGRRLIGcslELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 328 KNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPvntaaspisGGDLHGFMG 407
Cdd:cd07101 229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGA---------ALDYGPDMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 408 PVIHEQSYNKLIKVIEEAKTDPElEIIYGGQY--DKGEgWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNkfSETC 485
Cdd:cd07101 300 SLISQAQLDRVTAHVDDAVAKGA-TVLAGGRArpDLGP-YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 486 DLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAvvaqqW------FGGARMSGTDDKSGGPSILnRF 559
Cdd:cd07101 376 ELANDTD-YGLNASVWTRDGARGRRIAARLR--AGTVNVNEGYAAA-----WasidapMGGMKDSGLGRRHGAEGLL-KY 446
|
....*
gi 366986647 560 VSIRN 564
Cdd:cd07101 447 TETQT 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
61-545 |
4.19e-41 |
|
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: 155.38 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 61 KSSSLEVPLVINGEriYYNNSNRSVFAQSNPACHKqVLANVTQATELDVKDAIQAAKEA-KSKW-YQLPFYDRAAVFLKA 138
Cdd:cd07143 1 GKYEQPTGLFINGE--FVDSVHGGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfETDWgLKVSGSKRGRCLSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 139 ADLISTKYryDMLAAT-MLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSP 217
Cdd:cd07143 78 ADLMERNL--DYLASIeALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHG-QVIETDIKKLTYTRHEPI-GVCGQIIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 218 FNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGST 296
Cdd:cd07143 154 WNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGST 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 297 QVFKQLygkIQTGVVNGLyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFR 376
Cdd:cd07143 234 LVGRKV---MEAAAKSNL----KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 377 DLIGTLQQQKVtpvntaASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVGPTIIKCKD 456
Cdd:cd07143 307 RFKEKAKKLKV------GDPF---AEDTFQGPQVSQIQYERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 457 PKHKFMTTEFFGPILSVyeypdNKFSETCDLIDQ--TSMYGLTGSVFAKD-REAINLADeklKFSCGNFYINdkCTGAVV 533
Cdd:cd07143 377 EDMKIVKEEIFGPVVAV-----IKFKTEEEAIKRanDSTYGLAAAVFTNNiNNAIRVAN---ALKAGTVWVN--CYNLLH 446
|
490
....*....|..
gi 366986647 534 AQQWFGGARMSG 545
Cdd:cd07143 447 HQVPFGGYKQSG 458
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
96-559 |
8.84e-41 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 154.00 E-value: 8.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEID-----CI 170
Cdd:cd07151 21 ETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-RDEIVEWLIRESGSTRIKANIEwgaamAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 171 TELSDFFRFNVKYAHDLYNLQpvqsaqGVWNKAeYRPLEGFIYAVSPFNFT-AIAANLIgAPAL-MGNTVIWKPSQSAAL 248
Cdd:cd07151 100 TREAATFPLRMEGRILPSDVP------GKENRV-YREPLGVVGVISPWNFPlHLSMRSV-APALaLGNAVVLKPASDTPI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 249 SNYLLLT-VLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLyGKIQTGVVNglyrdypRIVGETGG 327
Cdd:cd07151 172 TGGLLLAkIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI-GELAGRHLK-------KVALELGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 328 KNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNTAASPIsggdlhgfmG 407
Cdd:cd07151 244 NNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV---------G 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 408 PVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYdkgEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKfsETCDL 487
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEE-GATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE--EALEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 366986647 488 IDQTSmYGLTGSVFAKDRE-AINLADeklKFSCGNFYINDKCTG--AVVAqqwFGGARMSGTdDKSGGPSILNRF 559
Cdd:cd07151 389 ANDTE-YGLSGAVFTSDLErGVQFAR---RIDAGMTHINDQPVNdePHVP---FGGEKNSGL-GRFNGEWALEEF 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
96-551 |
1.05e-40 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 153.28 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKwyqLPFYDRAAVFLKAADLIsTKYRYDMlaATMLGQGKNVyqAEIDCITELS- 174
Cdd:cd07146 10 EVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALL-EARREEF--ARLITLESGL--CLKDTRYEVGr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 175 --DFFRFNVKYAH---------DLYnlQPVQSAQGVWNKaeyRPLeGFIYAVSPFNFTA-IAANLIgAPALM-GNTVIWK 241
Cdd:cd07146 82 aaDVLRFAAAEALrddgesfscDLT--ANGKARKIFTLR---EPL-GVVLAITPFNHPLnQVAHKI-APAIAaNNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 242 PSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIqtgvvnglyrDYPRI 321
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATA----------GYKRQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEfFRDLIGTLQQQKVTpvntaASPisgGD 401
Cdd:cd07146 225 LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADE-FVDLLVEKSAALVV-----GDP---MD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 LHGFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDkgeGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkF 481
Cdd:cd07146 296 PATDMGTVIDEEAAIQIENRVEEAIAQGA-RVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKD--L 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 482 SETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKcTGAVVAQQWFGGARMSGTDDKSG 551
Cdd:cd07146 370 DEAIAISNSTA-YGLSSGVCTNDLDTIKRLVERLD--VGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
90-545 |
1.39e-40 |
|
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: 153.17 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAChKQVLANVTQATELDVKDAIQAAKEAKSKW-YQLPFYDRAAVFLKAADLISTkyRYDMLAATMlgqgknvyQAEID 168
Cdd:cd07089 3 NPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEA--RKEELRALL--------VAEVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 169 CITELSDFFR-----FNVKYAHDL-------YNLQPVQSAQGVWN-KAEYRPLeGFIYAVSPFNFT-AIAANLIgAPAL- 233
Cdd:cd07089 72 APVMTARAMQvdgpiGHLRYFADLadsfpweFDLPVPALRGGPGRrVVRREPV-GVVAAITPWNFPfFLNLAKL-APALa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 234 MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVvng 313
Cdd:cd07089 150 AGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 314 lyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNTA 393
Cdd:cd07089 227 -----KRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 394 ASpisggdlhgFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQ----YDKgeGWFVGPTIIKCKDPKHKFMTTEFFGP 469
Cdd:cd07089 302 GT---------VMGPLISAAQRDRVEGYIARGR-DEGARLVTGGGrpagLDK--GFYVEPTLFADVDNDMRIAQEEIFGP 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 366986647 470 ILSVYEYPDNkfsETCDLIDQTSMYGLTGSVFAKDRE-AINLAdekLKFSCGNFYINdkctGAVV--AQQWFGGARMSG 545
Cdd:cd07089 370 VLVVIPYDDD---DEAVRIANDSDYGLSGGVWSADVDrAYRVA---RRIRTGSVGIN----GGGGygPDAPFGGYKQSG 438
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
96-545 |
2.30e-40 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 152.39 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEA-KSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQAEIDcITEL 173
Cdd:cd07109 8 EVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLI--REHADELARLEsLDTGKPLTQARAD-VEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 174 SDFFRFnvkYAH--DLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTA-IAANLIgAPAL-MGNTVIWKPSQSAALS 249
Cdd:cd07109 85 ARYFEY---YGGaaDKLHGETIPLGPGYFVYTVREPH-GVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 250 NYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVfkqlyGKiqtGVVNGLYRDYPRIVGETGGKN 329
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET-----GI---AVMRAAAENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 330 FHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPvntaasPISGGDlhgfMGPV 409
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGP------GLEDPD----LGPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 410 IHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKG---EGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNkfSETCD 486
Cdd:cd07109 302 ISAKQLDRVEGFVARAR-ARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 487 LIDQTSmYGLTGSVFAKD-REAINLADeklKFSCGNFYINDKCTGAVVaQQWFGGARMSG 545
Cdd:cd07109 379 LANGTD-YGLVAGVWTRDgDRALRVAR---RLRAGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
71-545 |
1.83e-39 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 150.35 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGERIYYNNSNR-SVFaqsNPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYD 149
Cdd:cd07138 3 IDGAWVAPAGTETiDVI---NPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEA--RAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 150 MLAATM-------LGQGKNVyQAE-----IDCITELSDFFRFNVKYAHDLYNLQPVqsaqGV------WNkaeyrplegf 211
Cdd:cd07138 77 ELAQAItlemgapITLARAA-QVGlgighLRAAADALKDFEFEERRGNSLVVREPI----GVcglitpWN---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 212 iyavSPFNFtaIAANLigAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGL 290
Cdd:cd07138 142 ----WPLNQ--IVLKV--APALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 291 HFTGSTQVFKQLygkIQTGVvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSK 370
Cdd:cd07138 214 SFTGSTRAGKRV---AEAAA-----DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 371 SEEFfrdligtlqqqkVTPVNTAASPISGGD---LHGFMGPVIHEQSYNK---LIKV-IEEAKTdpeleIIYGGQyDKGE 443
Cdd:cd07138 286 YAEA------------EEIAAAAAEAYVVGDprdPATTLGPLASAAQFDRvqgYIQKgIEEGAR-----LVAGGP-GRPE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 444 ----GWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkfsetcdlIDQT------SMYGLTGSVFAKDRE-AINLAd 512
Cdd:cd07138 348 glerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD---------EDEAiaiandTPYGLAGYVWSADPErARAVA- 417
|
490 500 510
....*....|....*....|....*....|...
gi 366986647 513 EKLKfsCGNFYINDkctGAVVAQQWFGGARMSG 545
Cdd:cd07138 418 RRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
69-545 |
7.16e-39 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 149.03 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYry 148
Cdd:cd07559 3 NFINGE--WVAPSKGEYFDNYNPV-NGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLA-ATMLGQGKNVYQAEIDCITELSDFFRfnvkyahdlYNLQPVQSAQGVWNKAE--------YRPLeGFIYAVSPFN 219
Cdd:cd07559 78 ELLAvAETLDNGKPIRETLAADIPLAIDHFR---------YFAGVIRAQEGSLSEIDedtlsyhfHEPL-GVVGQIIPWN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 220 FTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTqv 298
Cdd:cd07559 148 FPLLMAAWKLAPALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGST-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 299 fkqlygkiQTGvvnglyrdypRIVGETGGKN-----FHLIHKSANI--------PNAVFSTIRGAFEF----QGQKCSAT 361
Cdd:cd07559 225 --------TVG----------RLIMQYAAENlipvtLELGGKSPNIffddamdaDDDFDDKAEEGQLGfafnQGEVCTCP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 362 SRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAAspisggdlhgFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQY- 439
Cdd:cd07559 287 SRALVQESIYDEFIERAVERFEAIKVgNPLDPET----------MMGAQVSKDQLEKILSYVDIGK-EEGAEVLTGGERl 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 440 ---DKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVyeypdNKFSETCDLIDQT--SMYGLTGSVFAKDreaINLAdek 514
Cdd:cd07559 356 tlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV-----ITFKDEEEAIAIAndTEYGLGGGVWTRD---INRA--- 424
|
490 500 510
....*....|....*....|....*....|....*
gi 366986647 515 LKFS----CGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:cd07559 425 LRVArgiqTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
59-550 |
1.67e-38 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 148.12 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 59 KFKSSSLEVPLVINGEriYYNNSNRSVFAQSNPAChKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFL 136
Cdd:PRK09847 12 KALSLAIENRLFINGE--YTAAAENETFETVDPVT-QAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 137 KAADLISTKYRYDMLAATmLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLY-NLQPVQSAQGVWNKAEyrPLeGFIYAV 215
Cdd:PRK09847 89 KLADLMEAHAEELALLET-LDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYgEVATTSSHELAMIVRE--PV-GVIAAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 216 SPFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTG 294
Cdd:PRK09847 165 VPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 295 STQVFKQLYgkIQTGVVNglyrdYPRIVGETGGKNFHLIHksANIPN---AVFSTIRGAFEFQGQKCSATSRLYIPQSKS 371
Cdd:PRK09847 245 STRTGKQLL--KDAGDSN-----MKRVWLEAGGKSANIVF--ADCPDlqqAASATAAGIFYNQGQVCIAGTRLLLEESIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 372 EEFFRDLigTLQQQKVTPvntaASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTDPELeIIYGgqydKGEGW--FVGP 449
Cdd:PRK09847 316 DEFLALL--KQQAQNWQP----GHPL---DPATTMGTLIDCAHADSVHSFIREGESKGQL-LLDG----RNAGLaaAIGP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 450 TIIKCKDPKHKFMTTEFFGPILSVYEYpdnKFSETCDLIDQTSMYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCT 529
Cdd:PRK09847 382 TIFVDVDPNASLSREEIFGPVLVVTRF---TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLK--AGSVFVNNYND 456
|
490 500
....*....|....*....|..
gi 366986647 530 GAVVAQqwFGGARMSGTD-DKS 550
Cdd:PRK09847 457 GDMTVP--FGGYKQSGNGrDKS 476
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
69-546 |
1.90e-37 |
|
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: 144.80 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPaCHKQVLANVTQATELDVKDAIQAAKEA---KSKWYQLPFYDRAAVFLKAADLISTK 145
Cdd:cd07141 9 IFINNE--WHDSVSGKTFPTINP-ATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 146 YRYdmlAATM--LGQGK---NVYQAEIDCITELsdfFRFNVKYAHDLY-NLQPVQSAQGVWNKAEyrPLeGFIYAVSPFN 219
Cdd:cd07141 86 RAY---LASLetLDNGKpfsKSYLVDLPGAIKV---LRYYAGWADKIHgKTIPMDGDFFTYTRHE--PV-GVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 220 FTAIAANLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPG-DPIlvTDQLLASK-EFGGLHFTGST 296
Cdd:cd07141 157 FPLLMAAWKLAPALaCGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPT--AGAAISSHpDIDKVAFTGST 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 297 QVfkqlyGKI---QTGVVNglyrdYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEE 373
Cdd:cd07141 235 EV-----GKLiqqAAGKSN-----LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 374 FFRDLIGTLQQQKVtpvntaASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTD-PELEIiyGGQYDKGEGWFVGPTII 452
Cdd:cd07141 305 FVKRSVERAKKRVV------GNPF---DPKTEQGPQIDEEQFKKILELIESGKKEgAKLEC--GGKRHGDKGYFIQPTVF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 453 KCKDPKHKFMTTEFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKDreainlADEKLKFS----CGNFYINd 526
Cdd:cd07141 374 SDVTDDMRIAKEEIFGPVQQIF-----KFKTIDEVIERAnnTTYGLAAAVFTKD------IDKAITFSnalrAGTVWVN- 441
|
490 500
....*....|....*....|
gi 366986647 527 kCTGAVVAQQWFGGARMSGT 546
Cdd:cd07141 442 -CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
96-507 |
2.28e-37 |
|
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: 144.25 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAAtmlgqgknVYQAEIDCITEL 173
Cdd:cd07139 25 EVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEA--RADELAR--------LWTAENGMPISW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 174 SDF---------FRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPS 243
Cdd:cd07139 95 SRRaqgpgpaalLRYYAALARDFPFEERRPGSGGGHVLVRREPV-GVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 244 QSAALSNYLLLTVLEEAGLPKGVINFVPGDpILVTDQLLASKEFGGLHFTGSTQVFKQLygkiqtGVVNGlyRDYPRIVG 323
Cdd:cd07139 174 PETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRI------AAVCG--ERLARVTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggDLH 403
Cdd:cd07139 245 ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKV------GDPL---DPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 404 GFMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKG--EGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKf 481
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAE-GARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED- 393
|
410 420
....*....|....*....|....*...
gi 366986647 482 setcDLID--QTSMYGLTGSVFAKDREA 507
Cdd:cd07139 394 ----DAVRiaNDSDYGLSGSVWTADVER 417
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
104-525 |
2.43e-37 |
|
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: 143.93 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 104 ATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYryDMLAATMLGQ-GKNVYQA--EIDCITELSDFFrfn 180
Cdd:cd07102 15 ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANT--DEIAEELTWQmGRPIAQAggEIRGMLERARYM--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 181 VKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFT-AIAANLIgAPALM-GNTVIWKPSQSAALSNYLLLTVLE 258
Cdd:cd07102 90 ISIAEEALADIRVPEKDGFERYIRREPL-GVVLIIAPWNYPyLTAVNAV-IPALLaGNAVILKHSPQTPLCGERFAAAFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 259 EAGLPKGVI-NFVPGDPilVTDQLLASKEFGGLHFTGST----QVFKQLYGKIqTGVvnGLyrdyprivgETGGKNFHLI 333
Cdd:cd07102 168 EAGLPEGVFqVLHLSHE--TSAALIADPRIDHVSFTGSVaggrAIQRAAAGRF-IKV--GL---------ELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 334 HKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggDLHGFMGPVIHEQ 413
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKL------GDPL---DPSTTLGPVVSAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 414 SYNKLIKVIEEAK-------TDPELEiiyggQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNkfSETCD 486
Cdd:cd07102 305 AADFVRAQIADAIakgaralIDGALF-----PEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 366986647 487 LIDQTSmYGLTGSVFAKDRE-AINLADEklkFSCGNFYIN 525
Cdd:cd07102 378 LMNDSE-YGLTASVWTKDIArAEALGEQ---LETGTVFMN 413
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
69-506 |
2.67e-37 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 144.72 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGERIyynNSNRSVFAQSNPACHkQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRY 148
Cdd:PRK09457 3 LWINGDWI---AGQGEAFESRNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALL--EENK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLAAtMLGQ--GKNVYQA--EIDCIT---ELSdffrfnVKYAHDL--YNLQPVQSAQGVwnkAEYRPLeGFIYAVSPFN 219
Cdd:PRK09457 77 EELAE-VIARetGKPLWEAatEVTAMInkiAIS------IQAYHERtgEKRSEMADGAAV---LRHRPH-GVVAVFGPYN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 220 FTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPilVTDQLLAS-KEFGGLHFTGS-- 295
Cdd:PRK09457 146 FPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR--ETGKALAAhPDIDGLLFTGSan 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 296 --TQVFKQLYGkiQTGVVNGLyrdyprivgETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSK-SE 372
Cdd:PRK09457 224 tgYLLHRQFAG--QPEKILAL---------EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 373 EFFRDLIGTLQQQKVTPVNTAASPisggdlhgFMGPVIHEQSYNKLIKVIEE-----AKTDPELEiiyggQYDKGEGwFV 447
Cdd:PRK09457 293 AFLARLVAVAKRLTVGRWDAEPQP--------FMGAVISEQAAQGLVAAQAQllalgGKSLLEMT-----QLQAGTG-LL 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 448 GPTIIKckdpkhkfMTT-------EFFGPILSVYEYPDnkFSETCDLIDQTSmYGLTGSVFAKDRE 506
Cdd:PRK09457 359 TPGIID--------VTGvaelpdeEYFGPLLQVVRYDD--FDEAIRLANNTR-FGLSAGLLSDDRE 413
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
71-545 |
6.12e-37 |
|
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: 143.31 E-value: 6.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 71 INGEriYYNNSNRSVFAQSNPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRydm 150
Cdd:cd07111 26 INGK--WVKPENRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQR--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 151 LAATM--LGQGKNVYQAEiDC-ITELSDFFRFNVKYAHDL-YNLqpvqsaqgvwnkAEYRPLeGFIYAVSPFNFTAIAAN 226
Cdd:cd07111 100 LFAVLesLDNGKPIRESR-DCdIPLVARHFYHHAGWAQLLdTEL------------AGWKPV-GVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 227 LIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTdQLLASKEFGGLHFTGSTQVfkqlyGK 305
Cdd:cd07111 166 WKICPALaMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGS-ALANHPGVDKVAFTGSTEV-----GR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 306 IQTGVVNGlyrDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDL---IGTL 382
Cdd:cd07111 240 ALRRATAG---TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLkerMSHL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 383 QqqkvtpvntaaspiSGGDLHGF--MGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKGEGWFVGPTIIKCKDPKHK 460
Cdd:cd07111 317 R--------------VGDPLDKAidMGAIVDPAQLKRIRELVEEGRAE-GADVFQPGADLPSKGPFYPPTLFTNVPPASR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 461 FMTTEFFGPILSVYEYPDNKfsETCDLIDQTSmYGLTGSVFAkdrEAINLADE-KLKFSCGNFYINdkCTGAVVAQQWFG 539
Cdd:cd07111 382 IAQEEIFGPVLVVLTFRTAK--EAVALANNTP-YGLAASVWS---ENLSLALEvALSLKAGVVWIN--GHNLFDAAAGFG 453
|
....*.
gi 366986647 540 GARMSG 545
Cdd:cd07111 454 GYRESG 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
90-545 |
3.30e-36 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 141.79 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAChKQVLANVTQATELDVKDAIQAAKEAKSK-----WYQLPFYDRAAvFLKAadlISTKY--RYDMLA-ATMLGQGKN 161
Cdd:PLN02467 29 NPAT-EETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAK-YLRA---IAAKIteRKSELAkLETLDCGKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 162 VYQAEIDcITELSDFFRFnvkYAHDLYNLQPVQSAQGVWNKAEYR------PLeGFIYAVSPFNFTAIAANLIGAPALM- 234
Cdd:PLN02467 104 LDEAAWD-MDDVAGCFEY---YADLAEALDAKQKAPVSLPMETFKgyvlkePL-GVVGLITPWNYPLLMATWKVAPALAa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 235 GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGdpiLVTDQ---LLASKEFGGLHFTGSTQvfkqlygkiqTG-- 309
Cdd:PLN02467 179 GCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTG---LGTEAgapLASHPGVDKIAFTGSTA----------TGrk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 310 VVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtp 389
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 390 vntaASPISGGdlhGFMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKG--EGWFVGPTIIKCKDPKHKFMTTEFF 467
Cdd:PLN02467 324 ----SDPLEEG---CRLGPVVSEGQYEKVLKFISTAKSE-GATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 468 GPILSVYEYPDNkfSETCDLIDQTSmYGLTGSVFAKDREAINLADEklKFSCGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:PLN02467 396 GPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLERCERVSE--AFQAGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
64-563 |
5.09e-35 |
|
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: 138.01 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 64 SLEVP--LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAA 139
Cdd:cd07140 1 TLKMPhqLFINGE--FVDAEGGKTYNTINPT-DGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 140 DLIStKYRYDMLAATMLGQGKnVYQAEIDCITELS-DFFRFNVKYAHDLYNLQ-PVQSAQGVWNKAEYR--PLeGFIYAV 215
Cdd:cd07140 78 DLME-EHQEELATIESLDSGA-VYTLALKTHVGMSiQTFRYFAGWCDKIQGKTiPINQARPNRNLTLTKrePI-GVCGIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 216 SPFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTG 294
Cdd:cd07140 155 IPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 295 STQVFKQLygkIQTGVVNGLyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEF 374
Cdd:cd07140 235 STPIGKHI---MKSCAVSNL----KKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 375 FRDLIGTLQQQKVtpvntaASPISGGDLHgfmGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGEGWFVGPTIIKC 454
Cdd:cd07140 308 VRRVVEEVKKMKI------GDPLDRSTDH---GPQNHKAHLDKLVEYCERG-VKEGATLVYGGKQVDRPGFFFEPTVFTD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 455 KDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQTSmYGLTGSVFAKD-REAINLADeklKFSCGNFYINDKCTGAVV 533
Cdd:cd07140 378 VEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTE-YGLASGVFTKDiNKALYVSD---KLEAGTVFVNTYNKTDVA 453
|
490 500 510
....*....|....*....|....*....|
gi 366986647 534 AQqwFGGARMSGTdDKSGGPSILNRFVSIR 563
Cdd:cd07140 454 AP--FGGFKQSGF-GKDLGEEALNEYLKTK 480
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
90-560 |
5.89e-34 |
|
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: 134.27 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEIDC 169
Cdd:cd07099 2 NPAT-GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADH-ADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 170 ITELsDFFRFNVKYAHDLYNLQPVQSAQGVWNKA---EYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQS 245
Cdd:cd07099 80 LLAL-EAIDWAARNAPRVLAPRKVPTGLLMPNKKatvEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 246 AALSNYLLLTVLEEAGLPKGVINFVPGDPilVTDQLLASKEFGGLHFTGSTQvfkqlygkiqTGvvnglyrdypRIVG-- 323
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDG--ATGAALIDAGVDKVAFTGSVA----------TG----------RKVMaa 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 ----------ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntA 393
Cdd:cd07099 216 aaerlipvvlELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRP-----G 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 394 ASPISGGDLhgfmGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSV 473
Cdd:cd07099 291 ADDIGDADI----GPMTTARQLDIVRRHVDDAV-AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 474 YEYPDNkfSETCDLIDQtSMYGLTGSVFAKDRE-AINLAdEKLKfsCGNFYINDKCTGAVVAQQWFGGARMSGTdDKSGG 552
Cdd:cd07099 366 MPVADE--DEAIALAND-SRYGLSASVFSRDLArAEAIA-RRLE--AGAVSINDVLLTAGIPALPFGGVKDSGG-GRRHG 438
|
....*...
gi 366986647 553 PSILNRFV 560
Cdd:cd07099 439 AEGLREFC 446
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
90-546 |
8.02e-34 |
|
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: 133.99 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRyDMLAATMLGQGKNVYQAEIDC 169
Cdd:cd07092 3 DPAT-GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAE-ELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 170 ITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSAAL 248
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPI-GVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 249 SNYLLLTVLEEaGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQlygkiqtgVVNGLYRDYPRIVGETGGK 328
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKK--------VARAAADTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 329 NFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVntaaspisgGDLHGFMGP 408
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDP---------DDEDTEMGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 409 VIHEQSYNKLIKVIEEAKTDpeLEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNkfSETCDLI 488
Cdd:cd07092 302 LNSAAQRERVAGFVERAPAH--ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 366986647 489 DQTSmYGLTGSVFAKDREAINLADEKLKFSCgnFYINDKctGAVVAQQWFGGARMSGT 546
Cdd:cd07092 378 NDVE-YGLASSVWTRDVGRAMRLSARLDFGT--VWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
96-526 |
8.15e-34 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 135.01 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIsTKYRYDMLAATMLGQGKNVYQAeidcITELSD 175
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLV-LENREELLDLVQLETGKARRHA----FEEVLD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 176 FF---RFNVKYAHDLYNLQPVQSAQGVWNKA-EYRPLEGFIYAVSPFNF---TAIAANLigaPALM-GNTVIWKPSQSAA 247
Cdd:PRK09407 118 VAltaRYYARRAPKLLAPRRRAGALPVLTKTtELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 248 LSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFggLHFTGSTQVfkqlyGKI---QTGvvnglyrdyPRIVG- 323
Cdd:PRK09407 195 LTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTAT-----GRVlaeQAG---------RRLIGf 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 324 --ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTpvntaaspiSGGD 401
Cdd:PRK09407 259 slELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG---------AGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 LHGFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQY--DKGEgWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDN 479
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGA-TVLAGGKArpDLGP-LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 366986647 480 kfSETCDLIDQTSmYGLTGSVFAKDREAINLADEKLKfsCGNFYIND 526
Cdd:PRK09407 408 --DEAVERANDTP-YGLNASVWTGDTARGRAIAARIR--AGTVNVNE 449
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
109-526 |
2.28e-33 |
|
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: 132.20 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 109 VKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRYDMLAATM-------LGQGKnvyqAEID-CitelSDFFRFN 180
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRE--RKDELARLItlemgkpIAEAR----AEVEkC----AWICRYY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 181 VKYAHDLYNLQPVQSAQGvwnKA--EYRPLeGFIYAVSPFNF----TAIAAnligAPALM-GNTVIWKPSQSAALSNYLL 253
Cdd:cd07100 71 AENAEAFLADEPIETDAG---KAyvRYEPL-GVVLGIMPWNFpfwqVFRFA----APNLMaGNTVLLKHASNVPGCALAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 254 LTVLEEAGLPKGVIN--FVPGDpilVTDQLLASKEFGGLHFTGSTQVfkqlyGkiqtgvvnglyrdypRIVGETGGKN-- 329
Cdd:cd07100 143 EELFREAGFPEGVFQnlLIDSD---QVEAIIADPRVRGVTLTGSERA-----G---------------RAVAAEAGKNlk 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 330 -----------FhLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIS 398
Cdd:cd07100 200 ksvlelggsdpF-IVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKV------GDPMD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 399 GGDlhgFMGPVIHEQSYNKLIKVIEEAKtDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07100 273 EDT---DLGPLARKDLRDELHEQVEEAV-AAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKD 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 366986647 479 NKfsETCDLIDQTSmYGLTGSVFAKDRE-AINLADeklKFSCGNFYIND 526
Cdd:cd07100 349 EE--EAIALANDSP-FGLGGSVFTTDLErAERVAR---RLEAGMVFING 391
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
90-545 |
2.30e-32 |
|
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: 129.77 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHkQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPfYDRAAVFLKAADLISTkyRYDMLAATM-LGQGKNVYQA- 165
Cdd:cd07120 3 DPATG-EVIGTYADGGVAEAEAAIAAARRAfdETDWAHDP-RLRARVLLELADAFEA--NAERLARLLaLENGKILGEAr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 166 -EID-CITELsdffRFNVKYAHDLYNlQPVQSAQGVWNKAEYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKP 242
Cdd:cd07120 79 fEISgAISEL----RYYAGLARTEAG-RMIEPEPGSFSLVLREPM-GVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 243 SQSAALSNYLLLTVLEEA-GLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKqlygKIQTGVVNGLYRdypri 321
Cdd:cd07120 153 AGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGR----AIMAAAAPTLKR----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VG-ETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNTAASPisgg 400
Cdd:cd07120 224 LGlELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASD---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 401 dlhgfMGPVIHEQSYNKLIKVIEEAKTDPELEIIYGGQYDKG--EGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07120 300 -----MGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDD 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366986647 479 NKfsETCDLIDQTSmYGLTGSVFAKDreainlADEKLKFS----CGNFYINDKctGAVVAQQWFGGARMSG 545
Cdd:cd07120 375 EA--EAVALANDTD-YGLAASVWTRD------LARAMRVArairAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
86-546 |
3.79e-32 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 129.81 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 86 FAQSNPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRYDMLAATM-LGQGKNVYQ 164
Cdd:PLN02278 42 FPVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI--IANKEDLAQLMtLEQGKPLKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 165 A--EIDCITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKaeyRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWK 241
Cdd:PLN02278 119 AigEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLK---QPV-GVVGAITPWNFPLAMITRKVGPALAaGCTVVVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 242 PSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVvnglyrdyPRI 321
Cdd:PLN02278 195 PSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV--------KRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTpvntaaspisggd 401
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVG------------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 lHGF-----MGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEY 476
Cdd:PLN02278 334 -DGFeegvtQGPLINEAAVQKVESHVQDAVSKGA-KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 477 PDNkfsETCDLIDQTSMYGLTGSVFAKDREAINLADEKLKFscGNFYINDKCTGAVVAQqwFGGARMSGT 546
Cdd:PLN02278 412 KTE---EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEY--GIVGVNEGLISTEVAP--FGGVKQSGL 474
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
77-507 |
4.53e-32 |
|
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: 129.25 E-value: 4.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 77 YYNNSNRS---VFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIsTKYRYDMLAA 153
Cdd:cd07130 2 VYDGEWGGgggVVTSISPA-NGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDAL-RKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 154 TMLGQGKnVYQAEIDCITELSDFFRFNVKYAHDLYNL-----QPVQSAQGVWNkaeyrPLeGFIYAVSPFNF-------- 220
Cdd:cd07130 80 VSLEMGK-ILPEGLGEVQEMIDICDFAVGLSRQLYGLtipseRPGHRMMEQWN-----PL-GVVGVITAFNFpvavwgwn 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 221 TAIAAnligapaLMGNTVIWKPSQSAALSNY----LLLTVLEEAGLPKGVINFVPGDPIlVTDQLLASKEFGGLHFTGST 296
Cdd:cd07130 153 AAIAL-------VCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 297 QVFKQLYGKIQtgvvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFR 376
Cdd:cd07130 225 AVGRQVGQAVA--------ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 377 DLIGTLQQQKVtpvntaASPISGGDLhgfMGPVIHEQSYNKLIKVIEEAKTDpELEIIYGGQYDKGEGWFVGPTIIKCkd 456
Cdd:cd07130 297 RLKKAYKQVRI------GDPLDDGTL---VGPLHTKAAVDNYLAAIEEAKSQ-GGTVLFGGKVIDGPGNYVEPTIVEG-- 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 366986647 457 PKHKFM-TTEFFGPILSVYEYPDnkFSETCDL---IDQtsmyGLTGSVFAKD-REA 507
Cdd:cd07130 365 LSDAPIvKEETFAPILYVLKFDT--LEEAIAWnneVPQ----GLSSSIFTTDlRNA 414
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
61-545 |
7.35e-32 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 129.17 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 61 KSSSLEVP------LVINGEriYYNNSNRSVFAQSNPAChKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRA 132
Cdd:PLN02766 9 GASGVKVPeikftkLFINGE--FVDAASGKTFETRDPRT-GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 133 AVFLKAADLIStKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYN--LQPVQSAQGVWNKaeyRPLeG 210
Cdd:PLN02766 86 RIMMKFADLIE-EHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGetLKMSRQLQGYTLK---EPI-G 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 211 FIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGG 289
Cdd:PLN02766 161 VVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 290 LHFTGSTQVFKQLygkIQTGVVNGLyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQS 369
Cdd:PLN02766 241 VSFTGSTEVGRKI---MQAAATSNL----KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 370 KSEEFFRDLIGTLQQQKV-TPVNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVG 448
Cdd:PLN02766 314 IYDEFVKKLVEKAKDWVVgDPFDPRAR----------QGPQVDKQQFEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 449 PTIIKCKDPKHKFMTTEFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKDREAINLADEKLKfsCGNFYINd 526
Cdd:PLN02766 383 PTIFTDVTEDMKIAQDEIFGPVMSLM-----KFKTVEEAIKKAnnTKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVN- 454
|
490
....*....|....*....
gi 366986647 527 kCTGAVVAQQWFGGARMSG 545
Cdd:PLN02766 455 -CYFAFDPDCPFGGYKMSG 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
69-557 |
8.59e-32 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 129.54 E-value: 8.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAChKQVLANVTQATELDVKDAIQAAKEA--KSKWYQLPFYDRAAVFLKAADLIStKY 146
Cdd:PLN02466 60 LLINGQ--FVDAASGKTFPTLDPRT-GEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLE-KH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 RYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLYNLQ-PVQSAQGVwnKAEYRPLeGFIYAVSPFNFTAIAA 225
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTvPADGPHHV--QTLHEPI-GVAGQIIPWNFPLLMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 226 NLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVfkqlyG 304
Cdd:PLN02466 213 AWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT-----G 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 305 KIQTGVVNGlyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFfrdligtLQQ 384
Cdd:PLN02466 288 KIVLELAAK--SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEF-------VEK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 385 QKVTPVN-TAASPISGGDLHgfmGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMT 463
Cdd:PLN02466 359 AKARALKrVVGDPFKKGVEQ---GPQIDSEQFEKILRYIKSG-VESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 464 TEFFGPILSVYeypdnKFSETCDLIDQ--TSMYGLTGSVFAKDREAINLADEKLKfsCGNFYINdkCTGAVVAQQWFGGA 541
Cdd:PLN02466 435 DEIFGPVQSIL-----KFKDLDEVIRRanNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVN--CFDVFDAAIPFGGY 505
|
490
....*....|....*.
gi 366986647 542 RMSGTDDKSGGPSILN 557
Cdd:PLN02466 506 KMSGIGREKGIYSLNN 521
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
69-545 |
1.60e-31 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 127.72 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriyYNNSNRSVFAQSNPACHKqVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTkyRY 148
Cdd:PRK13473 5 LLINGE---LVAGEGEKQPVYNPATGE-VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEE--NA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLAAT-MLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLynlqPVQSAqgvwnkAEYrpLEGF-----------IYAVS 216
Cdd:PRK13473 79 DEFARLeSLNCGKPLHLALNDEIPAIVDVFRFFAGAARCL----EGKAA------GEY--LEGHtsmirrdpvgvVASIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 217 PFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGS 295
Cdd:PRK13473 147 PWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 296 TQVFKQLygkIQTGVVNGlyrdyPRIVGETGGKNFHLIHKSANIpNAVFSTIR-GAFEFQGQKCSATSRLYIPQSKSEEF 374
Cdd:PRK13473 226 IATGKHV---LSAAADSV-----KRTHLELGGKAPVIVFDDADL-DAVVEGIRtFGYYNAGQDCTAACRIYAQRGIYDDL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 375 frdligtlqqqkVTPVNTAASPISGGDLHGF---MGPVIHEQSYNKLIKVIEEAKTDPELEIIYGGQYDKGEGWFVGPTI 451
Cdd:PRK13473 297 ------------VAKLAAAVATLKVGDPDDEdteLGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 452 IKCKDPKHKFMTTEFFGPILSVYeypdnKFSETCDLIDQ--TSMYGLTGSVFAKD--ReAINLADEkLKFSCgnFYINDK 527
Cdd:PRK13473 365 LAGARQDDEIVQREVFGPVVSVT-----PFDDEDQAVRWanDSDYGLASSVWTRDvgR-AHRVSAR-LQYGC--TWVNTH 435
|
490
....*....|....*...
gi 366986647 528 CTgaVVAQQWFGGARMSG 545
Cdd:PRK13473 436 FM--LVSEMPHGGQKQSG 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
69-578 |
4.54e-30 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 123.45 E-value: 4.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 69 LVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKYRY 148
Cdd:PRK13252 9 LYIDGA--YVEATSGETFEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL--RERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 149 DMLAAT-MLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLY-NLQPVQSAQGVWNKAEyrPLeGFIYAVSPFNF-TAIAA 225
Cdd:PRK13252 84 DELAALeTLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEgEQIPLRGGSFVYTRRE--PL-GVCAGIGAWNYpIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 226 nLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGD----PILVTDQLLASkefggLHFTGSTQVFK 300
Cdd:PRK13252 161 -WKSAPALaAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDgrvgAWLTEHPDIAK-----VSFTGGVPTGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 301 QLYGKIQTGVvnglyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIG 380
Cdd:PRK13252 235 KVMAAAAASL--------KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 381 TLQQQKV-TPVNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKTDPELEIIYGGQYDKG---EGWFVGPTI-IKCK 455
Cdd:PRK13252 307 RVERIRIgDPMDPATN----------FGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfaNGAFVAPTVfTDCT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 456 DPkhkfMT---TEFFGPILSVYEYPDNKfsetcDLIDQT--SMYGLTGSVFAKDreaINLADEKL-KFSCGNFYINdkCT 529
Cdd:PRK13252 377 DD----MTivrEEIFGPVMSVLTFDDED-----EVIARAndTEYGLAAGVFTAD---LSRAHRVIhQLEAGICWIN--TW 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 366986647 530 GAVVAQQWFGGARMSGTdDKSGGPSILNRFVSIrntKENFVELTDFKYP 578
Cdd:PRK13252 443 GESPAEMPVGGYKQSGI-GRENGIATLEHYTQI---KSVQVEMGPFQSP 487
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
67-507 |
7.85e-29 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 121.01 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 67 VPLVINGEriYYNNSNRSVFAQSNPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLIstKY 146
Cdd:PLN02419 114 VPNLIGGS--FVESQSSSFIDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELI--RK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 RYDMLAATMLG-QGKNVYQAEIDCITELSdffrfNVKYAHDLYNLQPVQSAQGVWNKAEY----RPLeGFIYAVSPFNFT 221
Cdd:PLN02419 189 NMDKLAMNITTeQGKTLKDSHGDIFRGLE-----VVEHACGMATLQMGEYLPNVSNGVDTysirEPL-GVCAGICPFNFP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 222 A-IAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVtDQLLASKEFGGLHFTGSTQVFK 300
Cdd:PLN02419 263 AmIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 301 QLYGKiqtGVVNGlyrdyPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSR-LYIPQSKSEEffRDLI 379
Cdd:PLN02419 342 HIYAR---AAAKG-----KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSWE--DKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 380 GTLQQQKVTpvntaaspiSGGDLHGFMGPVIHEQSYNKLIKVIEEAKTDPELEIIYGGQ-----YDKGEgwFVGPTIIKC 454
Cdd:PLN02419 412 ERAKALKVT---------CGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKGN--FIGPTILSG 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 366986647 455 KDPKHKFMTTEFFGPILSVYEypDNKFSETCDLIDQTSmYGLTGSVFAKDREA 507
Cdd:PLN02419 481 VTPDMECYKEEIFGPVLVCMQ--ANSFDEAISIINKNK-YGNGAAIFTSSGAA 530
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
147-551 |
9.98e-29 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 118.30 E-value: 9.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 147 RYDMLAATMLG-QGKNVYQAEIDcITELSDFFRFNVKYAHDlYNLQPVQSAQGVWNKAEYRPLEGFIYAVSPFNFT--AI 223
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVE-VAFTADYIDYMAEWARR-YEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 224 AANLigAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQL 302
Cdd:PRK10090 89 ARKM--APALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 303 YGKIQTGVVnglyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTL 382
Cdd:PRK10090 167 MAAAAKNIT--------KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 383 QQQKVtpvntaASPISGGDLHgfMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFM 462
Cdd:PRK10090 239 QAVQF------GNPAERNDIA--MGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 463 TTEFFGPILSVYEYpdNKFSETCDLIDQtSMYGLTGSVFAKDREAINLADEKLKFscGNFYINDKCTGAVvaQQWFGGAR 542
Cdd:PRK10090 310 HEETFGPVLPVVAF--DTLEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLKF--GETYINRENFEAM--QGFHAGWR 382
|
410
....*....|..
gi 366986647 543 MS---GTDDKSG 551
Cdd:PRK10090 383 KSgigGADGKHG 394
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
90-553 |
1.06e-27 |
|
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: 116.25 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPACHkQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAV-------FLKAADLIStkyrydmlAATMLGQGKNV 162
Cdd:cd07098 2 DPATG-QHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVlrsllkyILENQEEIC--------RVACRDTGKTM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 163 YQA---EIDCITElsdffRFNVKYAHDLYNLQPVQSAQGV--WNKA---EYRPLeGFIYAVSPFNFTAiaANLIGA--PA 232
Cdd:cd07098 73 VDAslgEILVTCE-----KIRWTLKHGEKALRPESRPGGLlmFYKRarvEYEPL-GVVGAIVSWNYPF--HNLLGPiiAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 233 LM-GNTVIWKPSQSAALSNYLLL----TVLEEAGLPKGVINFVPGDPiLVTDQLLASKEFGGLHFTGSTQVFKqlygKIQ 307
Cdd:cd07098 145 LFaGNAIVVKVSEQVAWSSGFFLsiirECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGK----KVM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 308 TGVVNGLYrdyPRIVgETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEF---FRDLIGTLQQ 384
Cdd:cd07098 220 AAAAESLT---PVVL-ELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLleiLTDRVQALRQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 385 qkvtpvntaaSPISGGDLHgfMGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGEGWFVG----PTIIKCKDPKHK 460
Cdd:cd07098 296 ----------GPPLDGDVD--VGAMISPARFDRLEELVADA-VEKGARLLAGGKRYPHPEYPQGhyfpPTLLVDVTPDMK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 461 FMTTEFFGPILSVYeypdnKFSETCDLID--QTSMYGLTGSVFAKDREAINLADEKLKfsCGNFYINDKCTGAVVAQQWF 538
Cdd:cd07098 363 IAQEEVFGPVMVVM-----KASDDEEAVEiaNSTEYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPF 435
|
490
....*....|....*
gi 366986647 539 GGARMSGTdDKSGGP 553
Cdd:cd07098 436 GGVKGSGF-GRFAGE 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
58-545 |
2.17e-27 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 115.77 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 58 MKFKSSSL-EVPLVINGEriYYNNSNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFL 136
Cdd:PRK11241 1 MQLNDSTLfRQQALINGE--WLDANNGEVIDVTNPA-NGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 137 KAADLISTkyRYDMLAATM-LGQGKNVYQAEIDcITELSDFFRFNVKYAHDLYNlqpvQSAQGvwNKAEYR------PLe 209
Cdd:PRK11241 78 RWFNLMME--HQDDLARLMtLEQGKPLAEAKGE-ISYAASFIEWFAEEGKRIYG----DTIPG--HQADKRlivikqPI- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 210 GFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLLASKEFG 288
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 289 GLHFTGSTQVFKQLYGKIQtgvvnglyRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQ 368
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCA--------KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 369 SKSEEFFRDLIGTLQQQKVTpvntaaspiSGGDLHGFMGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGEGWFVG 448
Cdd:PRK11241 300 GVYDRFAEKLQQAVSKLHIG---------DGLEKGVTIGPLIDEKAVAKVEEHIADA-LEKGARVVCGGKAHELGGNFFQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 449 PTIIKCKDPKHKFMTTEFFGPILSVYeypdnKFSETCDLIDQT--SMYGLTGSVFAKDREAINLADEKLKFscGNFYIND 526
Cdd:PRK11241 370 PTILVDVPANAKVAKEETFGPLAPLF-----RFKDEADVIAQAndTEFGLAAYFYARDLSRVFRVGEALEY--GIVGINT 442
|
490
....*....|....*....
gi 366986647 527 KCTGAVVAQqwFGGARMSG 545
Cdd:PRK11241 443 GIISNEVAP--FGGIKASG 459
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
204-545 |
1.32e-26 |
|
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: 112.62 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 204 EYRPLeGFIYAVSPFNF---TAIAAnLIGAPAlMGNTVIWKPS-QSAALSNyLLLTVLEEAgLPKGVINFVPGDpILVTD 279
Cdd:cd07087 97 IPEPL-GVVLIIGPWNYplqLALAP-LIGAIA-AGNTVVLKPSeLAPATSA-LLAKLIPKY-FDPEAVAVVEGG-VEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 280 QLLASKeFGGLHFTGSTQVfkqlyGKI--------QTGVVngLyrdyprivgETGGKNFHLIHKSANIPNAVFSTIRGAF 351
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAV-----GKIvmeaaakhLTPVT--L---------ELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 352 EFQGQKCSATSRLYIPQSKSEEFfrdlIGTLQQQKVT--PVNTAASPisggDLhgfmGPVIHEQSYNKLIKVIEEAKtdp 429
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDEL----IEELKKAIKEfyGEDPKESP----DY----GRIINERHFDRLASLLDDGK--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 430 eleIIYGGQYDKGEGwFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQTS----MYgltgsVFAKDR 505
Cdd:cd07087 299 ---VVIGGQVDKEER-YIAPTILDDVSPDSPLMQEEIFGPILPILTYDD--LDEAIEFINSRPkplaLY-----LFSEDK 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 366986647 506 EAINLADEKLkfSCGNFYINDkctgaVVAQQW-----FGGARMSG 545
Cdd:cd07087 368 AVQERVLAET--SSGGVCVND-----VLLHAAipnlpFGGVGNSG 405
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
205-545 |
3.13e-26 |
|
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: 111.83 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 205 YRPLeGFIYAVSPFN--FTAIAANLIGAPAlMGNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDpILVTDQLL 282
Cdd:cd07136 98 YEPY-GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGG-VEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 283 ASKeFGGLHFTGSTQVfkqlyGKI--------QTGVVngLyrdyprivgETGGKNFHLIHKSANIPNAVFSTIRGAFEFQ 354
Cdd:cd07136 174 DQK-FDYIFFTGSVRV-----GKIvmeaaakhLTPVT--L---------ELGGKSPCIVDEDANLKLAAKRIVWGKFLNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 355 GQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKvtpvntAASPISGGDlhgfMGPVIHEQSYNKLIKVIEEAKtdpeleII 434
Cdd:cd07136 237 GQTCVAPDYVLVHESVKEKFIKELKEEIKKFY------GEDPLESPD----YGRIINEKHFDRLAGLLDNGK------IV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 435 YGGQYDKgEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYpdNKFSETCDLIDQT----SMYgltgsVFAKDREAINL 510
Cdd:cd07136 301 FGGNTDR-ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKSRpkplALY-----LFSEDKKVEKK 372
|
330 340 350
....*....|....*....|....*....|....*
gi 366986647 511 ADEKLKFSCGnfYINDKCTGAVVAQQWFGGARMSG 545
Cdd:cd07136 373 VLENLSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
217-545 |
5.10e-24 |
|
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: 105.00 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 217 PFNFT------AIAAnligapalmGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVpGDPilVTDQLLASKEFGGL 290
Cdd:cd07134 113 PFNLAfgplvsAIAA---------GNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE-GDA--EVAQALLELPFDHI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 291 HFTGSTQVfkqlyGKIqtgVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSK 370
Cdd:cd07134 181 FFTGSPAV-----GKI---VMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 371 SEEFFRDLIGTLQQQKVTPVNTAASPisggDLhgfmGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGwFVGPT 450
Cdd:cd07134 253 KDAFVEHLKAEIEKFYGKDAARKASP----DL----ARIVNDRHFDRLKGLLDDAVAKGA-KVEFGGQFDAAQR-YIAPT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 451 IIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQT----SMYgltgsVFAKDREAIN--LADEklkfSCGNFYI 524
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYED--LDEVIEYINAKpkplALY-----VFSKDKANVNkvLART----SSGGVVV 391
|
330 340
....*....|....*....|....*..
gi 366986647 525 NDkctgavVAQQW------FGGARMSG 545
Cdd:cd07134 392 ND------VVLHFlnpnlpFGGVNNSG 412
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
87-545 |
3.57e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 102.51 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 87 AQSNPAChKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyrYDMLAATM-LGQGKNVYQA 165
Cdd:PRK09406 4 ATINPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAE--ADQVAALMtLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 166 EIDcITELSDFFRFNVKYAHDLYNLQPVQSAQGVWNKA--EYRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKP 242
Cdd:PRK09406 81 KAE-ALKCAKGFRYYAEHAEALLADEPADAAAVGASRAyvRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 243 SQSAALSNYLLLTVLEEAGLPKGVIN--FVPGDPIlvtDQLLASKEFGGLHFTGSTQVFKQLygkiqtGVVNGlyRDYPR 320
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPAGRAV------AAIAG--DEIKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 321 IVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAASpisg 399
Cdd:PRK09406 228 TVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVgDPTDPDTD---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 400 gdlhgfMGPVIHEQSYNKLIKVIEEAkTDPELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDn 479
Cdd:PRK09406 304 ------VGPLATEQGRDEVEKQVDDA-VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 366986647 480 kFSETCDLIDQTSmYGLTGSVFAKD-REAINLADEklkFSCGNFYINdkctGAVVA--QQWFGGARMSG 545
Cdd:PRK09406 376 -IDEAIEIANATT-FGLGSNAWTRDeAEQERFIDD---LEAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
90-545 |
3.88e-23 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 102.63 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 90 NPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVF--LKAADLISTKYRYDMLAATMlgqGKNVYQA-- 165
Cdd:PRK13968 13 NPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLrdIGKALRARSEEMAQMITREM---GKPINQAra 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 166 EIDCITELSDFFrfnVKYAHDLYNLQP--VQSAQGVwnkAEYRPLeGFIYAVSPFNFtAIAANLIGA-PALM-GNTVIWK 241
Cdd:PRK13968 89 EVAKSANLCDWY---AEHGPAMLKAEPtlVENQQAV---IEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 242 PSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTdQLLASKEFGGLHFTGSTQVFKQLygKIQTGVVnglyrdYPRI 321
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVS-QMINDSRIAAVTVTGSVRAGAAI--GAQAGAA------LKKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 322 VGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggD 401
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKM------GDPR---D 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 402 LHGFMGPV----IHEQSYNKLIKVIEEAKTdpeleIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYP 477
Cdd:PRK13968 303 EENALGPMarfdLRDELHHQVEATLAEGAR-----LLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 478 DnkfSETCDLIDQTSMYGLTGSVF-AKDREAINLADEklkFSCGNFYINDKC-TGAVVAqqwFGGARMSG 545
Cdd:PRK13968 378 D---AEHALELANDSEFGLSATIFtTDETQARQMAAR---LECGGVFINGYCaSDARVA---FGGVKKSG 438
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
81-554 |
8.75e-23 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 101.83 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 81 SNRSVFAQSNPAcHKQVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYRYdMLAATMLGQGK 160
Cdd:PLN02315 31 ANGPLVSSVNPA-NNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDY-LGRLVSLEMGK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 161 NVYQAeIDCITELSDFFRFNVKYAHDLYNL-----QPVQSAQGVWNkaeyrPLeGFIYAVSPFNFTAIAANLIGAPALM- 234
Cdd:PLN02315 109 ILAEG-IGEVQEIIDMCDFAVGLSRQLNGSiipseRPNHMMMEVWN-----PL-GIVGVITAFNFPCAVLGWNACIALVc 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 235 GNTVIWKPSQSAAL----SNYLLLTVLEEAGLPKGVINFVPGDPiLVTDQLLASKEFGGLHFTGSTQVfkqlyGKIQTGV 310
Cdd:PLN02315 182 GNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKV-----GLMVQQT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 311 VNGlyrDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpv 390
Cdd:PLN02315 256 VNA---RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKI--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 391 ntaASPISGGDLhgfMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYDKGEGWFVGPTIIKCKdPKHKFMTTEFFGPI 470
Cdd:PLN02315 330 ---GDPLEKGTL---LGPLHTPESKKNFEKGIEIIKSQGG-KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 471 LSVYEYpdNKFSETCDlIDQTSMYGLTGSVFAKDREAINLADEKLKFSCGNFYINDKCTGAVVAQQwFGGARMSGTDDKS 550
Cdd:PLN02315 402 LYVMKF--KTLEEAIE-INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREA 477
|
....
gi 366986647 551 GGPS 554
Cdd:PLN02315 478 GSDS 481
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
96-545 |
1.03e-22 |
|
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: 101.37 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 96 QVLANVTQATELDVKDAIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKYryDMLA-ATMLGQGKNVYQAEIDCITELS 174
Cdd:cd07116 27 KVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL--EMLAvAETWDNGKPVRETLAADIPLAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 175 DFFRfnvkyahdlYNLQPVQSAQGVWNKAE--------YRPLeGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQS 245
Cdd:cd07116 105 DHFR---------YFAGCIRAQEGSISEIDentvayhfHEPL-GVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 246 AALSNYLLLTVLEEAgLPKGVINFVPGDPILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVVnglyrdyPrIVGET 325
Cdd:cd07116 175 TPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENII-------P-VTLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 326 GGKNfhlihksaniPNAVFSTIRGA--------------FEF-QGQKCSATSRLYIPQSKSEEFFRDLIgtlqqQKVTPV 390
Cdd:cd07116 246 GGKS----------PNIFFADVMDAddaffdkalegfvmFALnQGEVCTCPSRALIQESIYDRFMERAL-----ERVKAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 391 nTAASPIsggDLHGFMGPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQY----DKGEGWFVGPTIIKcKDPKHKFMTTEF 466
Cdd:cd07116 311 -KQGNPL---DTETMIGAQASLEQLEKILSYIDIGKEEGA-EVLTGGERnelgGLLGGGYYVPTTFK-GGNKMRIFQEEI 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 366986647 467 FGPILSVYEYPDnkFSETCDLIDQTsMYGLTGSVFAKDREAINLADEKLKfsCGNFYINdkCTGAVVAQQWFGGARMSG 545
Cdd:cd07116 385 FGPVLAVTTFKD--EEEALEIANDT-LYGLGAGVWTRDGNTAYRMGRGIQ--AGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
200-545 |
1.17e-21 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 98.56 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 200 WNKAEY-------RPLEGFI----YAV----SPFNFTA--IAANLIGAPAlMGNTVIWKPSQ-SAALSNylLLTVLEEAG 261
Cdd:PTZ00381 86 YLKPEKvdtvgvfGPGKSYIipepLGVvlviGAWNYPLnlTLIPLAGAIA-AGNTVVLKPSElSPHTSK--LMAKLLTKY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 262 LPKGVINFVPGDpILVTDQLLaSKEFGGLHFTGSTQVfkqlyGKIqtgVVNGLYRDYPRIVGETGGKNFHLIHKSANIPN 341
Cdd:PTZ00381 163 LDPSYVRVIEGG-VEVTTELL-KEPFDHIFFTGSPRV-----GKL---VMQAAAENLTPCTLELGGKSPVIVDKSCNLKV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 342 AVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFfrdlIGTLQQQKVTpvntaaspisggdlhgFMGP----------VIH 411
Cdd:PTZ00381 233 AARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKF----IEALKEAIKE----------------FFGEdpkksedysrIVN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 412 EQSYNKLIKVIEEAKTDpeleIIYGGQYDKGEGWfVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkFSETCDLIDQT 491
Cdd:PTZ00381 293 EFHTKRLAELIKDHGGK----VVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYEN--IDEVLEFINSR 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 366986647 492 SmYGLTGSVFAKDREAINLADEKLkfSCGNFYINDkCTGAVVAQQW-FGGARMSG 545
Cdd:PTZ00381 366 P-KPLALYYFGEDKRHKELVLENT--SSGAVVIND-CVFHLLNPNLpFGGVGNSG 416
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
112-562 |
1.88e-21 |
|
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: 97.31 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 112 AIQAAKEAKSKWYQLPFYDRAAVFLKAADLISTKyRYDMLAATMLGQGKNVYQAEIDCITELSDFFRFNVKYAHDLY--- 188
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAK-SYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPhep 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 189 ----NLQPVQSAQGvwnkaeYRPLEGFIYAVSPFNFTAIAANLIGAPAL-MGNTVIWKPSQSAALSNYLLLTVLEEAG-L 262
Cdd:cd07084 83 gnhlGQGLKQQSHG------YRWPYGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 263 PKGVINFVPGDPILvTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGvvnglyrdypRIVGETGGKNFHLIHKSANIPNA 342
Cdd:cd07084 157 PPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA----------RIYLELAGFNWKVLGPDAQAVDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 343 VF-STIRGAFEFQGQKCSATSRLYIPQSKS-EEFFRDLIGTLQQQKVtpvntaaspisgGDLhgFMGPVIHEQSYNKlik 420
Cdd:cd07084 226 VAwQCVQDMTACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKL------------EDL--LLGPVQTFTTLAM--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 421 vIEEAKTDPELEIIYGGQYDKGEGW--FVGPTI-------IKCKDPKHKFMTTEFFGPILSVYEYPDNKFSETCDLIDQt 491
Cdd:cd07084 289 -IAHMENLLGSVLLFSGKELKNHSIpsIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLER- 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 366986647 492 sMYG-LTGSVFAKDREAINLADEKLKFSCGNFYINDKCTGAVVAQQWFGGARMSGTDDKSGGPSIL---NRFVSI 562
Cdd:cd07084 367 -MHGsLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIklvWRCHAE 440
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
106-545 |
2.72e-21 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 97.10 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 106 ELDVKDAIQAAKEA-------KSKWyqLPFYDRAAVFLKAADLISTkyRYDMLAATMLGQGKNVYqaeIDCITELSDFFR 178
Cdd:cd07148 16 PTVDWAAIDKALDTahalfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGGKPL---VDAKVEVTRAID 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 179 fNVKYA-HDLYNLQPVQSAQGVWNKAEYR-------PLeGFIYAVSPFNFtaiAANLI---GAPAL-MGNTVIWKPSQSA 246
Cdd:cd07148 89 -GVELAaDELGQLGGREIPMGLTPASAGRiafttrePI-GVVVAISAFNH---PLNLIvhqVAPAIaAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 247 ALSNYLLLTVLEEAGLPKGVINFVPGDpILVTDQLLASKEFGGLHFTGSTQVFKQLYGKIQTGVvnglyrdypRIVGETG 326
Cdd:cd07148 164 PLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT---------RCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 327 GKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVtpvntaASPIsggDLHGFM 406
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVV------GDPT---DPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 407 GPVIHEQSYNKLIKVIEEAKTDPElEIIYGGQYdKGEGWFvGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDNKfsetcD 486
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKR-LSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLD-----E 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 366986647 487 LIDQTSM--YGLTGSVFAKDREAINLADEKLKFSCgnFYINDKCTGAVvaqQW--FGGARMSG 545
Cdd:cd07148 377 AIAQANSlpVAFQAAVFTKDLDVALKAVRRLDATA--VMVNDHTAFRV---DWmpFAGRRQSG 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
206-546 |
1.81e-19 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 91.13 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 206 RPLeGFIYAVSPFNF---TAIAAnLIGAPAlMGNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDpILVTDQLL 282
Cdd:cd07135 107 EPL-GVVLIIGPWNYpvlLALSP-LVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGG-VPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 283 ASKeFGGLHFTGSTQVfkqlyGKI--------QTGVVngLyrdyprivgETGGKNFHLIHKSANIPNAVFSTIRGAFEFQ 354
Cdd:cd07135 182 EQK-FDKIFYTGSGRV-----GRIiaeaaakhLTPVT--L---------ELGGKSPVIVTKNADLELAAKRILWGKFGNA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 355 GQKCSATSRLYIPQSKSEEFFRDLIGTLQqqKVTPVNTAASPIsggdlhgfMGPVIHEQSYNKLIKVIEEAKTDpeleII 434
Cdd:cd07135 245 GQICVAPDYVLVDPSVYDEFVEELKKVLD--EFYPGGANASPD--------YTRIVNPRHFNRLKSLLDTTKGK----VV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 435 YGGQYDKGEGwFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPDnkfSETCDLIDQTSMYGLTGSVFAKDREAINLADEK 514
Cdd:cd07135 311 IGGEMDEATR-FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDD---LDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
|
330 340 350
....*....|....*....|....*....|..
gi 366986647 515 LkfSCGNFYINDKCTGAVVAQQWFGGARMSGT 546
Cdd:cd07135 387 T--RSGGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
51-512 |
5.97e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 87.12 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 51 DLLRASIMKFkssslevplVINGEriYYNNSNRSVFAQSNPACHKqvLANVTQA-TELDVKDAIQAAKEAKSKWYQLPFY 129
Cdd:PLN00412 9 EILDGDVYKY---------YADGE--WRTSSSGKSVAITNPSTRK--TQYKVQAcTQEEVNKAMESAKAAQKAWAKTPLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 130 DRAAVFLKAADLIstKYRYDMLAATMLgqgKNVYQAEIDCITElsdffrfnVKYAHDLYNLQpvqSAQGVWNKAEYR--- 206
Cdd:PLN00412 76 KRAELLHKAAAIL--KEHKAPIAECLV---KEIAKPAKDAVTE--------VVRSGDLISYT---AEEGVRILGEGKflv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 207 ------------------PLeGFIYAVSPFNFTA-IAANLIgAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAGLPKGV 266
Cdd:PLN00412 140 sdsfpgnernkycltskiPL-GVVLAIPPFNYPVnLAVSKI-APALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 267 INFVPGDPILVTDQLLASKEFGGLHFTGStqvfkqlygkiQTGVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFST 346
Cdd:PLN00412 218 ISCVTGKGSEIGDFLTMHPGVNCISFTGG-----------DTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 347 IRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPvntaasPISGGDLhgfmGPVIHEQSYNKLIKVIEEAK 426
Cdd:PLN00412 287 IKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP------PEDDCDI----TPVVSESSANFIEGLVMDAK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 427 tdpELEIIYGGQYdKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYpdNKFSETCDLIDQtSMYGLTGSVFAKD-R 505
Cdd:PLN00412 357 ---EKGATFCQEW-KREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI--NSVEEGIHHCNA-SNFGLQGCVFTRDiN 429
|
....*..
gi 366986647 506 EAINLAD 512
Cdd:PLN00412 430 KAILISD 436
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
227-545 |
1.01e-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: 82.65 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 227 LIGAPAlMGNTVIWKPSQSAALSNYLLLTVLeeaglPKGVIN-----FVPGDPilVTDQLLASKeFGGLHFTGSTQVfkq 301
Cdd:cd07132 121 LVGAIA-AGNCVVIKPSEVSPATAKLLAELI-----PKYLDKecypvVLGGVE--ETTELLKQR-FDYIFYTGSTSV--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 302 lyGKIqtgVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEFQGQKCSATSrlYIPQSKS--EEFFRDLI 379
Cdd:cd07132 189 --GKI---VMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD--YVLCTPEvqEKFVEALK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 380 GTLQQQKVTPVNTaaSPisggDLhgfmGPVIHEQSYNKLIKVIEEAKtdpeleIIYGGQYDKGEGwFVGPTIIKCKDPKH 459
Cdd:cd07132 262 KTLKEFYGEDPKE--SP----DY----GRIINDRHFQRLKKLLSGGK------VAIGGQTDEKER-YIAPTVLTDVKPSD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 460 KFMTTEFFGPILSVyeYPDNKFSETCDLIDQTS----MYgltgsVFAKDREAINLADEKLkfSCGNFYINDKCTGAVVAQ 535
Cdd:cd07132 325 PVMQEEIFGPILPI--VTVNNLDEAIEFINSREkplaLY-----VFSNNKKVINKILSNT--SSGGVCVNDTIMHYTLDS 395
|
330
....*....|
gi 366986647 536 QWFGGARMSG 545
Cdd:cd07132 396 LPFGGVGNSG 405
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
201-478 |
1.29e-11 |
|
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: 66.74 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 201 NKAEYRPLeGFIYAVSPFNF----------TAIAAnligapalmGNTVIWKPSQSAALSNYLLLTVLEEAGLPKgVINFV 270
Cdd:cd07133 95 AEVEYQPL-GVVGIIVPWNYplylalgpliAALAA---------GNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 271 PGDPILvtdqllaSKEFGGL---H--FTGSTQVfkqlyGKI--------QTGVVngLyrdyprivgETGGKNFHLIHKSA 337
Cdd:cd07133 164 TGGADV-------AAAFSSLpfdHllFTGSTAV-----GRHvmraaaenLTPVT--L---------ELGGKSPAIIAPDA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 338 NIPNAVFSTIRGAFEFQGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKVTPVNtaaSPisggDlhgfMGPVIHEQSYNK 417
Cdd:cd07133 221 DLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLAD---NP----D----YTSIINERHYAR 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366986647 418 LIKVIEEAKTD-PELEIIYGGQYDKGEGWFVGPTIIKCKDPKHKFMTTEFFGPILSVYEYPD 478
Cdd:cd07133 290 LQGLLEDARAKgARVIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDS 351
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
207-478 |
3.98e-11 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 65.50 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 207 PLEGFIYAVSPFNFTAIAANLIGAPALM-GNTVIWKPSQSAALSNYLLLTVLEEAG-LPKGVINFVPGDPILVTDQLlas 284
Cdd:PRK11903 147 PTRGVALFINAFNFPAWGLWEKAAPALLaGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHL--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 285 KEFGGLHFTGSTQVFKQLygkiqtgvvnglyRDYPRIVGEtgGKNFHLIHKSAN----IPNAVFSTirGAFEF------- 353
Cdd:PRK11903 224 QPFDVVSFTGSAETAAVL-------------RSHPAVVQR--SVRVNVEADSLNsallGPDAAPGS--EAFDLfvkevvr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 354 -----QGQKCSATSRLYIPQSKSEEFFRDLIGTLQQQKV-TPVNTAASpisggdlhgfMGPVIHEQSYNKLIKVIEEAKT 427
Cdd:PRK11903 287 emtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVgNPRNDGVR----------MGPLVSRAQLAAVRAGLAALRA 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 366986647 428 dpELEIIYGG------QYDKGEGWFVGPTIIKCKDPK--HKFMTTEFFGPILSVYEYPD 478
Cdd:PRK11903 357 --QAEVLFDGggfalvDADPAVAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRD 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
230-506 |
3.55e-10 |
|
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: 62.67 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 230 APALM-GNTVIWKPSQSAALSNYLLLTVLEEAG-LPKGVINFVPGDPILVTDQLLaskEFGGLHFTGSTQVFKQLygkiq 307
Cdd:cd07128 166 APALLaGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLG---EQDVVAFTGSAATAAKL----- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 308 tgvvnglyRDYPRIVGEtgGKNFHLIHKSANI----PNAVfstiRGAFEFQ--------------GQKCSATSRLYIPQS 369
Cdd:cd07128 238 --------RAHPNIVAR--SIRFNAEADSLNAailgPDAT----PGTPEFDlfvkevaremtvkaGQKCTAIRRAFVPEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 370 KSEEFFRDLIGTLQQQKVtpvntaaspisgGD--LHGF-MGPVI-HEQSYN---KLIKVIEEAKT---DPELEIIYGGQY 439
Cdd:cd07128 304 RVDAVIEALKARLAKVVV------------GDprLEGVrMGPLVsREQREDvraAVATLLAEAEVvfgGPDRFEVVGADA 371
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366986647 440 DKGEgwFVGPTIIKCKDPK-----HkfmTTEFFGPILSVYEYPDnkfseTCDLIDQTSMYG--LTGSVFAKDRE 506
Cdd:cd07128 372 EKGA--FFPPTLLLCDDPDaatavH---DVEAFGPVATLMPYDS-----LAEAIELAARGRgsLVASVVTNDPA 435
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
200-546 |
7.52e-10 |
|
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: 61.27 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 200 WNKAEYRPLeGFIYAVSPFNFTAIAA--NLIGAPAlMGNTVIWKPSQSAALSNYLLLTVLEEAgLPKGVINFVPGDPIlV 277
Cdd:cd07137 94 KAEIVSEPL-GVVLVISAWNFPFLLSlePVIGAIA-AGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVP-E 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 278 TDQLLASKeFGGLHFTGSTQVfkqlyGKIqtgVVNGLYRDYPRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFEF-QGQ 356
Cdd:cd07137 170 TTALLEQK-WDKIFFTGSPRV-----GRI---IMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 357 KCSATSRLYIPqsksEEFFRDLIGTLqqQKVTPVNTAASPISGGDlhgfMGPVIHEQSYNKLIKVIEEAKTDPelEIIYG 436
Cdd:cd07137 241 ACIAPDYVLVE----ESFAPTLIDAL--KNTLEKFFGENPKESKD----LSRIVNSHHFQRLSRLLDDPSVAD--KIVHG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 437 GQYDKgEGWFVGPTIIkCKDP-KHKFMTTEFFGPILSVYEYpdNKFSETCDLIDQTSMyGLTGSVFAKDREAIN-LADEk 514
Cdd:cd07137 309 GERDE-KNLYIEPTIL-LDPPlDSSIMTEEIFGPLLPIITV--KKIEESIEIINSRPK-PLAAYVFTKNKELKRrIVAE- 382
|
330 340 350
....*....|....*....|....*....|..
gi 366986647 515 lkFSCGNFYINDKCTGAVVAQQWFGGARMSGT 546
Cdd:cd07137 383 --TSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
205-541 |
1.72e-09 |
|
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: 60.20 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 205 YRPLEGFIYAVSPFNF--TAIAANLIGApALMGNTVIWKPSQSAALSNYLLLTVLEEAGLPKGVINFVPGDPILVTDQLL 282
Cdd:cd07126 139 YRWPYGPVAIITPFNFplEIPALQLMGA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 283 ASkEFGGLHFTGSTQVFKQLygkiqTGVVNGlyrdypRIVGETGGKNFHLIHKS-ANIPNAVFSTIRGAFEFQGQKCSAT 361
Cdd:cd07126 218 EA-NPRMTLFTGSSKVAERL-----ALELHG------KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 362 SRLYIPQSKSEEFFRDLIGTLQQQKvtpvntaaspiSGGDLHgfMGPVIhEQSYNKLIKVIEEAKTDPELEIIYGG---- 437
Cdd:cd07126 286 SILFAHENWVQAGILDKLKALAEQR-----------KLEDLT--IGPVL-TWTTERILDHVDKLLAIPGAKVLFGGkplt 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 438 ------QYDKGEGWFVGPTIIKCKDPKH-KFMTTEFFGPILSVYEYPDNKFS---ETCDLIDQTsmygLTGSVFAKDrea 507
Cdd:cd07126 352 nhsipsIYGAYEPTAVFVPLEEIAIEENfELVTTEVFGPFQVVTEYKDEQLPlvlEALERMHAH----LTAAVVSND--- 424
|
330 340 350
....*....|....*....|....*....|....*..
gi 366986647 508 INLADEKLKFSC-GNFY--INDKCTGAvVAQQWFGGA 541
Cdd:cd07126 425 IRFLQEVLANTVnGTTYagIRARTTGA-PQNHWFGPA 460
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
210-387 |
2.20e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 43.75 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 210 GFIYAVSPFNFTAIAANLIGAPALMGNTVIWKPSQSAALSNYLLLTVLEEA---GLPKGVINFVPGDPILVTDQLLASKE 286
Cdd:cd07077 102 GVTMHILPSTNPLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELLSHPK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366986647 287 FGGLHFTGSTQVFKQLYgKIQTGVvnglyrdypRIVGETGGKNFHLIHKSANIPNAVFSTIRGAFeFQGQKCSATSRLYI 366
Cdd:cd07077 182 IDLIVATGGRDAVDAAV-KHSPHI---------PVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYV 250
|
170 180
....*....|....*....|.
gi 366986647 367 PQSKSEEFFRDLIGTLQQQKV 387
Cdd:cd07077 251 VDDVLDPLYEEFKLKLVVEGL 271
|
|
| |
